Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
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B4P5Q9 | PTK7_DROYA | MTARMISIYGLVLASMMASVLASSSRFQRLPQSQSVVENESVKFECESTDSYSELHYDWLHNGHRIAYDKRVHQIGSNLHIEAVRRTEDVGSYVCIATNLASGAREASPPAKLSVIYIESASVQLLGSNRNELLLKCHVEGASGDSEPLEIEWYRNSEKLSTWRNVQLDQHRLIVRQPGSDDDGLYRCTASNAAGRVMSKQGYVYQSSVKCLPRLARRKSQKVMESWDKQTFLCRGKRGGAAGLEALPAAPEDLRIVQGPIAQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPISGHSFDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEAHVPVSSSPGVLEVIEQLKFVPQPTSKNLELDAVVAKVHCKAQGTPTPQVQWVREGENNTLPDQVEVDANGTLIFRNVNSEHRGNYTCLATNTQGQINATVAINVVVTPKFSVPPVGPIETAELGTVVIHCQAIGDPKPTIQWDKDLKYLSENNTDRERFRFLENGTLEIRNVQVEDEGSYGCTIGNSAGLKREDVQLIVKTTGDGFAPEESGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNDLSTKEAGGDQPDATGNGKGSEQEPCLSKQHNGHSKSRSKSSGDAQKSDDTACSQQSRASKKSAHIYEQLALPRSGLSELIQIGRGEFGDVFVGKLKATLVTSPSDKDADTEKQHSNSENGSGGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQHNQSGLEQLVLVKALNKVKDEQACQEFRRQLDLLRAISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATAGSSSPPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNTLLPIRWLAPECIQEDEYTTKSDIFAYGVVVWELFNQATKLPHEELTNEQVVQRSQAGSLEWSVAESTPDSLREILLSCWVANPKERPSFSQLGAALSKAMQSAEK | null | null | cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147] | PF07679;PF13927;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}. | null | null | null | null | null | FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}. | Drosophila yakuba (Fruit fly) |
B4P6P9 | LIS1_DROYA | MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFGLMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR | null | null | border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496] | axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616] | dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}. | null | null | null | null | null | FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}. | Drosophila yakuba (Fruit fly) |
B4PDM5 | PLK4_DROYA | MLSNRAFGETIEDYEVQHLLGKGGFAIVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSTPGALNMFSQSMESADSGIITFASSESRNSQQIRSVENSGPQQMLPQIQEEFKHHKLTYEQPGLFRQTSTGLAEPNWPGAAKASAFHMEIGMVPTSKPAPVKEDRISVPPLNTKRLLSTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRIIDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYENLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPTEGVKVYDRNGMFLSDHTCSESRSLIEHGNECFTHCININNALEVAQTKDNSCFPVTIGRRPVTDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSVSTISSTRNTTDFGNNCSRLNMLASHQNIPIKRINVPDVGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKDDDLPFPVRDRVGQIPNIQIKLKTAPLLESGRKIDYNNATPKTTTPSYNRMLL | 2.7.11.21 | null | centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}. | Drosophila yakuba (Fruit fly) |
B4PL32 | SPAST_DROYA | MVRTKNQSSSSSASSSSTKSPIKSSSATGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHTYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNRDSDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKQNEQAPSKPQRTREPMLAGMTNEPMKLRVRSSGYGPKATTGAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI | 5.6.1.1 | null | adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331] | centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568] | PF00004;PF17862;PF09336; | 1.10.8.60;3.40.50.300;1.20.58.80; | AAA ATPase family, Spastin subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}. | CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021}; | null | null | null | null | FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}. | Drosophila yakuba (Fruit fly) |
B4PN49 | HH_DROYA | MDNTSSVPWASAASVTCLSLDAKCHSSSAKSTASSISATPESQTMRHIAHTQRCLSRLTSLVALLLIVLPMNFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCREKLNLLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGGAVLTVTPAHLISVWQPESQKLTFVFADRIEEKNQVLVRDSETGELRPQRVIKVGSVRSKGVVAPLTREGTIVVNSVAASCYAVINSQSLAHWGLAPMRLLSTLEAWLPAKEQLHSSPKVVSSAEQQNGIHWYANALYKVKDYVLPQSWRHD | 3.1.-.- | null | Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm development [GO:0007506]; heart formation [GO:0060914]; hindgut morphogenesis [GO:0007442]; imaginal disc-derived wing morphogenesis [GO:0007476]; intein-mediated protein splicing [GO:0016539]; labial disc development [GO:0035217]; morphogenesis of larval imaginal disc epithelium [GO:0016335]; mucosal immune response [GO:0002385]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; negative regulation of proteolysis [GO:0045861]; pole cell migration [GO:0007280]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of protein localization to cell surface [GO:2000010]; progression of morphogenetic furrow involved in compound eye morphogenesis [GO:0007458]; protein autoprocessing [GO:0016540]; regulation of cell proliferation involved in compound eye morphogenesis [GO:2000495]; regulation of epithelial cell migration, open tracheal system [GO:2000274]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; spiracle morphogenesis, open tracheal system [GO:0035277]; terminal cell fate specification, open tracheal system [GO:0035154]; ventral midline development [GO:0007418]; wing disc pattern formation [GO:0035222] | cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233] | PF01085;PF01079; | 3.30.1380.10;2.170.16.10; | Hedgehog family | PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}. | CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226}; | null | null | null | null | FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}. | Drosophila yakuba (Fruit fly) |
B4PUP5 | RAS1_DROYA | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML | 3.6.5.2 | null | border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; eye-antennal disc morphogenesis [GO:0007455]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hemocyte migration [GO:0035099]; imaginal disc-derived wing vein morphogenesis [GO:0008586]; imaginal disc-derived wing vein specification [GO:0007474]; instar larval development [GO:0002168]; intestinal stem cell homeostasis [GO:0036335]; leg disc proximal/distal pattern formation [GO:0007479]; lymph gland crystal cell differentiation [GO:0035170]; lymph gland plasmatocyte differentiation [GO:0035169]; Malpighian tubule development [GO:0072002]; MAPK cascade [GO:0000165]; mesodermal cell fate commitment [GO:0001710]; myoblast fate specification [GO:0048626]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of compound eye retinal cell programmed cell death [GO:0046673]; negative regulation of gene expression [GO:0010629]; negative regulation of macroautophagy [GO:0016242]; ommatidial rotation [GO:0016318]; oocyte axis specification [GO:0007309]; peripheral nervous system development [GO:0007422]; photoreceptor cell fate determination [GO:0043703]; photoreceptor cell morphogenesis [GO:0008594]; positive regulation of cell size [GO:0045793]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of hemocyte proliferation [GO:0035208]; positive regulation of photoreceptor cell differentiation [GO:0046534]; positive regulation of TORC1 signaling [GO:1904263]; R8 cell differentiation [GO:0045465]; Ras protein signal transduction [GO:0007265]; regulation of multicellular organism growth [GO:0040014]; sevenless signaling pathway [GO:0045500]; stem cell fate commitment [GO:0048865]; stem cell proliferation [GO:0072089]; terminal branching, open tracheal system [GO:0007430]; terminal region determination [GO:0007362]; torso signaling pathway [GO:0008293]; trachea development [GO:0060438]; tracheal outgrowth, open tracheal system [GO:0007426]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing, spreading of epidermal cells [GO:0035313] | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112, ECO:0000250|UniProtKB:P08646}. | Drosophila yakuba (Fruit fly) |
B4Q0P3 | SWS_DROYA | MDVLEMLRASASGSYNTIFSDAWCQYVSKQITATMYMYCAFGLMGVLFLAWFMYFKRLARLRLRDELARSISSVTNSYGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPIFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMQAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRYKSVSTMSGPINSQTSQSSRQATANGPPMVINQLNLMQSAASGLGMGMGTGTGSGVSVTVTRPPPSPSRHSREEHTLSDPNPNPDGSVHGTSNLFTEVHGDAPNADLFHQQQQSVGNLSTRRSSITQMTPDGSHTCPQAPGVTTSIDMRLVQSSAVDSLRKELGLSEEDAHIIEPFVELRELEPNVTLITEGNADDVCVWFVMTGTLAVYQSNQDATRAKQDKNDMLIHFVHPGEIVGGLAMLTGEASAYTIRSRSNSRIAFIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITHPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGSMQTRSGSGAPGAPVEANPVTHKYSTVALVPITDEVPLTPFTYELYHSLCAIGPVLRLTSDVVRKQLGPNIFEAANEYRLTSWLAQQEDRNIITLYQCDSSLSAWTQRCMRQADVILIVGLGDRSHLVGKFEREIDRLAMRTQKELVLLYPEATNAKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPVDMVGGVSIGALMGALWCSERNITTVTQKAREWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFENMAKAGRLGRFNQWFNKEPPKRVNHASLNEYTFIDLAQIVCRLPETYAVNTAELFSEDEDCDGYISEPTTLNTDRRRIQVPRAGNSLSFSETEMDSDVELDLKLERKMDKSTQSTPPTSSRASVRGKEEARHMDNWHWSVKHKVETASGATEATNAMIDQEQQHQQQADQGVGAEQLADKDEDKENRSSTYNETKN | 3.1.1.5 | null | ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintenance [GO:0045494]; protein localization to membrane [GO:0072657]; sensory perception of smell [GO:0007608] | endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027;PF01734; | 3.40.1090.10;2.60.120.10; | NTE family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969}; | null | null | null | null | FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}. | Drosophila yakuba (Fruit fly) |
B4Q4M7 | FICD_DROSI | MCMEAEPPSPPAQQQEQVNPPLCKAQNPKPARLYRLVLLFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHIPPGPGDLALLMQRFERWLNSEHSSTLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGDIP | 2.7.7.108; 3.1.4.- | null | detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632] | plasma membrane [GO:0005886] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803] | PF02661; | 1.10.3290.10;1.25.40.10; | Fic family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; | null | null | null | null | FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6}. | Drosophila simulans (Fruit fly) |
B4Q599 | IHOG_DROSI | MTLLTSSLLLFSLLTSRLEAIPVLEKSPAHPAHSAHTAHPAHPSPGVRILRAPESLVAPLGDEVVLECETSLQPERFEWSHRSSRSPGAGFKYLRTGTAKANVSQEAAISRLRVLVRPDTLGEYRCVGWFGPLVVTSTTARLELASTSLVDAQEPESPLQWRVSAGNSVLWSCGQQVQSNPSASWSYFRNGVEIKPEFIGTNGNLFLSNVSSESSGSYSCQATNPASGERIQLPGSLQLQVTPEQRSQSKSPHLLKGQPSSQEITIREGSSLLLLCPGVGSPPPTVVWSSPDVVGAVKNKRSKVFGHALEISNTRVHDAGTYICFQDNGVRPALEHYIKVHVEQPPQIVRPPWADLTNEGDRLKLECEATGVPTPEIYWLLNGHSSIDDTEAELSNNFLILHSVLKRHAGYVQCFARNRLGEHSAGTLLQVNPKQIQEPRESGGTHRPNPNQGSKHKQMYPPTPPNVTRLTDESVMLRWMVPRNDGLPIVIFKVQYRMVGKRKNWQTTNDNIPYGKPKWNSELGKSFTASVTDLKPEHTYRFRILAVYSNNDNKESNTSAKFYLQPGAALDPMPVPELLEIEEYSETAVVLHWSLASDADEHLITGYYAYYRPSSSAGEYFKATIEGAHARSFKIAPLETATMYEFKLQSFSAVSASEFSALKQGRTQRPKTSTTEEPTLQMGDRDTTTPSHNETFNMSPMLTGTIGGGAVLILLLISTCLCVCRRRNSRSRGNNPNKPRMAELRDDFVPLGNCSPTKQRQRTRHIHITLNPLAQQQQQALEEKNDTDQDAPYYQRPSSYDYDPALRRMSSSSLRRSQRTLERAGGSNGSNNGNNNNLNQTAEAGAVENPGKPGRVLMKRPRLSSRSENLSSGSLNSVGV | null | null | compound eye development [GO:0048749]; cuticle pattern formation [GO:0035017]; homotypic cell-cell adhesion [GO:0034109]; maintenance of protein location in extracellular region [GO:0071694]; segment specification [GO:0007379]; smoothened signaling pathway [GO:0007224]; wing disc anterior/posterior pattern formation [GO:0048100] | cell surface [GO:0009986]; cytoneme [GO:0035230]; membrane [GO:0016020]; plasma membrane [GO:0005886] | coreceptor activity [GO:0015026]; hedgehog family protein binding [GO:0097108]; heparin binding [GO:0008201]; patched binding [GO:0005113]; protein homodimerization activity [GO:0042803] | PF00041;PF13895;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, IHOG family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9VM64, ECO:0000255}. | null | null | null | null | null | FUNCTION: Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc). {ECO:0000250|UniProtKB:Q9VM64}. | Drosophila simulans (Fruit fly) |
B4QC63 | PTK7_DROSI | MISIYGLVMALMMASVLASSSRFQRVPQSQSVVENESVKFECESTDSYSELHYDWLHNGHRIAYDKRVHQIGSNLHIEAVRRTEDVGNYVCIATNLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDLEPLEIEWYRNSEKLSTWKNVQLDQHRLIIRQPGSEDDGLYRCTASNAAGRVMSKQGYVYQSSVKCLPRLPRRKNQKMMESWDKQTFLCRGKRGGAAGLEALPAVPEDLRIVQGPIAQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPILGHSFDSGKDALLREDARLVLHKQNGTLSFASIIASDAGQYQCQLQLEAHAPISSSPGILEVIEQLKFVPQPTSKNLELDAVVAKVHCKAQGTPTPQVQWIRDGENTTLPDQVEVDANGTLIFRNVNSEHRGNYTCLATNTQGQINATVAINVVVTPKFSVPPVGPIETSEQGTVVMHCQAIGDPKPTIQWDKDLKYLSENNTDRERFRFLENGTLEIRNVQVEDEGSYGCTIGNSAGLKREDVQLVVKTTGDGFAPEESGGDGFLVTRAVLITMTVALAYIVLVVGLMLWCRYRRQARKARLNDLSTKEAGGDQPDAAGNGKGSEQEPCLSKQHNGHSKSRSKSSGDAQKSDDTACSQQSRASKKSAHIYEQLALPRSGLSELIQIGRGEFGDVFVGKLKATLVTSPSDKDADTEKQHSNSENGSGGSGSGSTTLSTLNEKRRSKTSMDDIEEIKEEEQEQHNQSGLEQLVLVKALNKVKDEQACQEFRRQLDLLRAISHKGVVRLFGLCREKDPHYMVLEYTDWGDLKQFLLATAGKVNTATAGSSSPPPLTTSQVLAVAYQIARGMDAIYRARFTHRDLATRNCVISSEFIVKVSYPALCKDKYSREYHKHRNTLLPIRWLAPECIQEDEYTTKSDIFAYGVVVWELFNQATKLPHEELTNEQVVQRSQAGSLEWSVAEATPDSLREILLSCWVSNPKERPSFSQLGAALSKAMQSAEK | null | null | cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499]; retinal ganglion cell axon guidance [GO:0031290]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147] | PF07679;PF13927;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}. | null | null | null | null | null | FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons (By similarity). {ECO:0000250}. | Drosophila simulans (Fruit fly) |
B4QHG6 | LIS1_DROSI | MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR | null | null | border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle orientation [GO:0000132]; germarium-derived cystoblast division [GO:0048142]; germarium-derived oocyte fate determination [GO:0007294]; intracellular mRNA localization [GO:0008298]; intracellular protein transport [GO:0006886]; kinetochore organization [GO:0051383]; microtubule sliding [GO:0051012]; muscle cell cellular homeostasis [GO:0046716]; mushroom body development [GO:0016319]; neuroblast proliferation [GO:0007405]; nuclear migration along microtubule [GO:0030473]; oocyte nucleus migration involved in oocyte dorsal/ventral axis specification [GO:0007312]; ovarian fusome organization [GO:0030723]; ovarian nurse cell to oocyte transport [GO:0007300]; photoreceptor cell axon guidance [GO:0072499]; positive regulation of axonogenesis [GO:0050772]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein localization to kinetochore [GO:0034501]; regulation of dendrite morphogenesis [GO:0048814]; retrograde axonal transport [GO:0008090]; rhabdomere development [GO:0042052]; spermatogenesis [GO:0007283]; spindle assembly [GO:0051225]; stem cell population maintenance [GO:0019827]; vesicle transport along microtubule [GO:0047496] | axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; spindle pole centrosome [GO:0031616] | dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}. | null | null | null | null | null | FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}. | Drosophila simulans (Fruit fly) |
B4QK53 | PLK4_DROSI | MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTSRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGVHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQPGLFGQASTGLAEPNWPGAAKTSAFRMETGMVPNSKPASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPNKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDHSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPDIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKDDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL | 2.7.11.21 | null | centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm axoneme assembly [GO:0007288]; syncytial blastoderm mitotic cell cycle [GO:0035186] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers (By similarity). {ECO:0000250}. | Drosophila simulans (Fruit fly) |
B4QSF0 | SPAST_DROSI | MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHSYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRLSLKEKQKEEARSKPQKSREPMLAGMTNEPMKLRVRSSGYGPKATTSAQPTASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTARPKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI | 5.6.1.1 | null | adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of synaptic assembly at neuromuscular junction [GO:0045886]; nervous system development [GO:0007399]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of lipid metabolic process [GO:0045834]; positive regulation of microtubule depolymerization [GO:0031117]; positive regulation of neuromuscular synaptic transmission [GO:1900075]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein hexamerization [GO:0034214]; regulation of terminal button organization [GO:2000331] | centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568] | PF00004;PF09336; | 1.10.8.60;3.40.50.300;1.20.58.80; | AAA ATPase family, Spastin subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000255|HAMAP-Rule:MF_03021}. | CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021}; | null | null | null | null | FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. {ECO:0000255|HAMAP-Rule:MF_03021}. | Drosophila simulans (Fruit fly) |
B4R1D8 | HH_DROSI | MDNHSSVPWASAASVTCLSLDAKCHSSSSSCSSKSTASSISASPETQTMRHIAHTQRCLSRLTSLVALLLIVLPMMFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCKEKLNVLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGVRKPLGELSIGDRVLSMTANGQGVYSEVILFMDRNLEQMQNFVQLHTDGGAVLTVTPAHLVSVWQPESQKLTFVFADRIEESTFFLLRDGQSGGGGEKQVQQNGIHWYANALYKVKDYVLPQSWRHD | 3.1.-.- | null | Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm development [GO:0007506]; heart formation [GO:0060914]; hindgut morphogenesis [GO:0007442]; imaginal disc-derived wing morphogenesis [GO:0007476]; intein-mediated protein splicing [GO:0016539]; labial disc development [GO:0035217]; morphogenesis of larval imaginal disc epithelium [GO:0016335]; mucosal immune response [GO:0002385]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; negative regulation of proteolysis [GO:0045861]; pole cell migration [GO:0007280]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of protein localization to cell surface [GO:2000010]; progression of morphogenetic furrow involved in compound eye morphogenesis [GO:0007458]; protein autoprocessing [GO:0016540]; regulation of cell proliferation involved in compound eye morphogenesis [GO:2000495]; regulation of epithelial cell migration, open tracheal system [GO:2000274]; regulation of gene expression [GO:0010468]; regulation of mitotic cell cycle [GO:0007346]; segment polarity determination [GO:0007367]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; spiracle morphogenesis, open tracheal system [GO:0035277]; terminal cell fate specification, open tracheal system [GO:0035154]; ventral midline development [GO:0007418]; wing disc pattern formation [GO:0035222] | cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233] | PF01085;PF01079; | 3.30.1380.10;2.170.16.10; | Hedgehog family | PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). The N-product is the active species in both local and long-range signaling, whereas the C-product has no signaling activity (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. {ECO:0000250|UniProtKB:Q62226}.; PTM: [Protein hedgehog N-product]: N-palmitoylation by Rasp of the hedgehog N-product, within the secretory pathway, is required for the embryonic and larval patterning activities of the hedgehog signal. {ECO:0000250|UniProtKB:Q02936}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane {ECO:0000250|UniProtKB:Q02936}; Lipid-anchor {ECO:0000250|UniProtKB:Q02936}. Note=The N-terminal peptide remains associated with the cell surface. Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation. {ECO:0000250|UniProtKB:Q02936}. | CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226}; | null | null | null | null | FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (By similarity). {ECO:0000250|UniProtKB:Q02936, ECO:0000250|UniProtKB:Q62226}.; FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection. During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh-signaling pathway by mediating the ubiquitination and degradation of cos. {ECO:0000250|UniProtKB:Q02936}. | Drosophila simulans (Fruit fly) |
B4URD7 | M2_I06A0 | MSLLTEVETPIRNEWGCRCNGSSDPLTIAANIIGILHLTLWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/Russia:St.Petersburg/8/2006 H1N1) |
B4USZ0 | CADH2_OTOGA | MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLSVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHSKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESPEIEEIVFPRQLTKHNGYLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAIITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTQAWNAVYRISGGDPAGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHSGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPGTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLAEMYGGGDD | null | null | adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; glial cell differentiation [GO:0010001]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural crest cell development [GO:0014032]; neuronal stem cell population maintenance [GO:0097150]; regulation of axonogenesis [GO:0050770]; regulation of synaptic transmission, glutamatergic [GO:0051966]; synapse assembly [GO:0007416]; synaptic vesicle clustering [GO:0097091]; type B pancreatic cell development [GO:0003323] | adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; sarcolemma [GO:0042383] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa (By similarity). Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence (By similarity). {ECO:0000250|UniProtKB:P15116}.; PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P15116}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (By similarity). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15116}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. {ECO:0000250|UniProtKB:P10288, ECO:0000250|UniProtKB:P15116}. | Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby) |
B4UT09 | PI4KB_OTOGA | MGDTVVEPTPLKPTSESTPGPAGSNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSRNSPLELVNGDGVDNEIRCLDDPPSRIREEEDEMGATVAVGTAKGARRQRQNNSAKQSWLLRLFESKLFDISMAMSYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM | 2.7.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | inner ear development [GO:0048839]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310] | Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867] | 1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524] | PF00454;PF21245; | 1.10.1070.11; | PI3/PI4-kinase family, Type III PI4K subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; | null | null | null | null | FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development. {ECO:0000250|UniProtKB:O08561, ECO:0000250|UniProtKB:Q9UBF8}. | Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby) |
B4XC07 | MANA_CRYAT | MVKLFSFLLLVWVASPAFSSEFLKASGSNFYYGGQKVFLSGVNFAWRSYGSDFGNGQYASNGPALKDWINKVKASGGNTARVWVHVEGQVSPAFDSHGFVTSTDSKKTLINDLSDLLDYANGQNVFLILVLFNGALQNNSNVQNLFWDESKLNSYINNALTPMVNALKSKPSLAAWEVLNEPEGTLQPGSDQNSCYDTSTLAAQGAGWGGKKFPMKQILKTINWISSAIHNADSKALVTVGSWSELTQTDSFGYRNHYKDSCLTGAGGKSNGIINFYQMHTYSHSGKWNQNAPFKVNRWAYNVNDKPLLIGEFASVCSQNEGIQNLYKYAYNNGYNGALTWQFNSGGDCSDTYSNQMYGMQALKGQNDQSGGKGGMVSVNIN | 3.2.1.78 | null | mannan catabolic process [GO:0046355] | extracellular region [GO:0005576] | mannan endo-1,4-beta-mannosidase activity [GO:0016985]; oligosaccharide binding [GO:0070492]; polysaccharide binding [GO:0030247] | null | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:18579426, ECO:0000269|PubMed:22333528, ECO:0000269|PubMed:25082572}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.61 mg/ml for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate) {ECO:0000269|PubMed:25082572}; Vmax=2477.22 mol/min/mg enzyme with 0.5% locust bean gum as substrate (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate) {ECO:0000269|PubMed:25082572}; Note=kcat is 1659.90 sec(-1) for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate). {ECO:0000269|PubMed:25082572}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5. Maintains more than 50% of the maximum activity at pH 2.5-6.0. Not active at a pH above 7.0. {ECO:0000269|PubMed:18579426}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Retains approximately 20-40% of its maximum activity even at 0-5 degrees Celsius. Drastic loss of activity at temperatures above 45 degrees Celsius, at which the half-life of the enzyme activity is less than 10 minutes. {ECO:0000269|PubMed:18579426}; | FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426). {ECO:0000269|PubMed:18579426, ECO:0000269|PubMed:25082572}. | Cryptopygus antarcticus (Antarctic springtail) |
B4XMC6 | DCDA_HELPX | MFNYEELFQTHKTPFYLYDFDKIKQAFLNYKEAFKGRKSLICYALKANSNLSILSLLAHLESGADCVSIGEIQRALKAGIKPYRIVFSGVGKSAFEIEQALKLNILFLNVESFMELKTIETIAQSLGIKARISIRINPNIDAKTHPYISTGLKENKFGVGEKEALEMFLWAKKSAFLEPVSVHFHIGSQLLDLEPIIEASQKVAKIAKSLIALGIDLRFFDVGGGIGVSYENEETIKLYDYAQGILNALQGLDLTIICEPGRSIVAESGELITQVLYEKKAQNKRFVIVDAGMNDFLRPSLYHAKHAIRVITPSKGREISPCDVVGPVCESSDTFLKDAHLPELEPGDKIAIEKVGAYGSSMASQYNSRPKLLELALEDHKIRVIRKREALEDLWRLEEEGLKGV | 4.1.1.20 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:18508763}; | lysine biosynthetic process via diaminopimelate [GO:0009089] | null | diaminopimelate decarboxylase activity [GO:0008836]; pyridoxal phosphate binding [GO:0030170] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, LysA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:18508763}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for meso-2,6-diaminoheptanedioate {ECO:0000269|PubMed:18508763}; Note=kcat is 939 min(-1). {ECO:0000269|PubMed:18508763}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_02120}. | null | null | FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:18508763}. | Helicobacter pylori (Campylobacter pylori) |
B4XT64 | NAL1_ORYSJ | MKPSDDKAQLSGLAQSEESSLDVDHQSFPCSPSIQPVASGCTHTENSAAYFLWPTSNLQHCAAEGRANYFGNLQKGLLPRHPGRLPKGQQANSLLDLMTIRAFHSKILRRFSLGTAVGFRIRKGDLTDIPAILVFVARKVHKKWLNPAQCLPAILEGPGGVWCDVDVVEFSYYGAPAQTPKEQMFSELVDKLCGSDECIGSGSQVASHETFGTLGAIVKRRTGNKQVGFLTNHHVAVDLDYPNQKMFHPLPPNLGPGVYLGAVERATSFITDDVWYGIYAGTNPETFVRADGAFIPFADDFDISTVTTVVRGVGDIGDVKVIDLQCPLNSLIGRQVCKVGRSSGHTTGTVMAYALEYNDEKGICFFTDILVVGENRQTFDLEGDSGSLIILTSQDGEKPRPIGIIWGGTANRGRLKLTSDHGPENWTSGVDLGRLLDRLELDIIITNESLQDAVQQQRFALVAAVTSAVGESSGVPVAIPEEKIEEIFEPLGIQIQQLPRHDVAASGTEGEEASNTVVNVEEHQFISNFVGMSPVRDDQDAPRSITNLNNPSEEELAMSLHLGDREPKRLRSDSGSSLDLEK | null | null | internode patterning [GO:0080006]; leaf vascular tissue pattern formation [GO:0010305]; regulation of leaf development [GO:2000024]; stem vascular tissue pattern formation [GO:0010222] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:18562767}. Cytoplasm {ECO:0000269|PubMed:18562767}. Note=Expressed in discrete structures which appeared similar to nuclear protein bodies. {ECO:0000269|PubMed:18562767}. | null | null | null | null | null | FUNCTION: Involved in the regulation of lateral leaf growth (PubMed:18562767, PubMed:22179305, PubMed:23985993). May be involved in the regulation of basipetal polar auxin transport (PAT) and vascular patterning in leaves (PubMed:18562767). Controls photosynthesis rate by regulating carboxylation efficiency and consequently photosynthesis rate (PubMed:23985993). Controls panicle and spikelet numbers, and grain yield (PubMed:23985993, PubMed:24297875, PubMed:24795339). {ECO:0000269|PubMed:18562767, ECO:0000269|PubMed:22179305, ECO:0000269|PubMed:23985993, ECO:0000269|PubMed:24297875, ECO:0000269|PubMed:24795339}. | Oryza sativa subsp. japonica (Rice) |
B4XXY3 | SREA_AJECA | MTGLLASRLRAEGARSPTKGTDIPMRQPSAEDLDAAHQLVSSARGGRDNVMNFRSDRQEMTGKALDNTQGDGSRNMDSQLQNGHKAPVEQRAGESPPESGANPIDHPTSSKKSPKAQSKEQAFTGHSCSNCGTKRTPLWRRSPTGATICNACGLYLKARNTDRPTHRSRSLLTPYGSSSAQTLDKSRSSTSPTNDGNDPRLTDTWSNYAVKECTPSGSCPGGGSCNGTGGAEGCDGCPAYNNRVYKSAARNAMALHTPRTSPQVSTQGGPGSTEGDAGSSNPETMTLHIACQNCQTTVTPLWRRDENGHPICNACGLYHKLHGAYRPPTMKKSIIKRRKRVVPAMREQSPPSATQSSNGSVSPEASPAALAHNHDSHRQYQNVEHGNGHPPPHTRPLYSHAYHAPPPADFTGYTSNVISLPHHPPSTSQQLRPYDNNHNNGETTNTHRAPMPALHNPKKRTISESSIEDSQRPQASQILTHIPQINPPTPPSSSSASFPNNNPGRFNSISSLLNHPGEAATVTAHDRDDSRVDPALSSAVAPRTQQPQQEHQHASAGSHSPPRFSPSLSPAPPSTTAVPVGGGSGSGAAAVAGVVDHRDAKAERRARLQREAQDMREALKAKERELALLE | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-(G/A)ATC(T/A)GATAA-3' of target promoters in an iron- and zinc-dependent manner (PubMed:18549241, PubMed:22117028). Regulation occurs via direct binding of iron ions (PubMed:18549241). Iron acquisition regulation is critical for survival under both iron-limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity) (PubMed:22117028). SRE1 targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis, presumed ferric reductase activity, iron-responsive transcriptional regulation, oxidative stress response, as well as genes encoding a number of putative oxidoreductases, metabolic and mitochondrial enzymes, superoxide dismutase, and genes previously identified as induced during nitrosative stress (PubMed:22117028). {ECO:0000269|PubMed:18549241, ECO:0000269|PubMed:22117028}. | Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum) |
B4YQU1 | FAH12_CLAPU | MASATPAMSENAVLRHKAASTTGIDYESSAAVSPAESPRTSASSTSLSSLSSLDANEKKDEYAGLLDTYGNAFTPPDFSIKDIRAAIPKHCYERSTIKSYAYVLRDLLCLSTTFYLFHNFVTPENIPSNPLRFVLWSIYTVLQGLFATGLWVIGHECGHCAFSPSPFISDLTGWVIHSALLVPYFSWKFSHSAHHKGIGNMERDMVFLPRTREQQATRLGRAVEELGDLCEETPIYTALHLVGKQLIGWPSYLMTNATGHNFHERQREGRGKGKKNGFGGGVNHFDPRSPIFEARQAKYIVLSDIGLGLAIAALVYLGNRFGWANMAVWYFLPYLWVNHWLVAITFLQHTDPTLPHYNREEWNFVRGGACTIDRDLGFIGRHLFHGIADTHVVHHYVSRIPFYNADEASEAIKPIMGKHYRSDTAHGPVGFLHALWKTARWCQWVEPSADAQGAGKGILFYRNRNKLGTKPISMKTQ | 1.14.-.- | null | fatty acid metabolic process [GO:0006631]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | monooxygenase activity [GO:0004497]; oleate 12-hydroxylase activity [GO:0102517]; omega-3 fatty acid desaturase activity [GO:0042389]; omega-6 fatty acid desaturase activity [GO:0045485]; oxidoreductase activity [GO:0016491]; palmitoleic acid delta 12 desaturase activity [GO:0102987]; phosphatidylcholine 12-monooxygenase activity [GO:0050183] | PF11960;PF00487; | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q41131}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + AH2 + O2 = (12R)-hydroxy-(9Z)-octadecenoate + A + H2O; Xref=Rhea:RHEA:55956, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30823, ChEBI:CHEBI:91295; Evidence={ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951, ECO:0000269|PubMed:27830762}; | null | PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis. {ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951, ECO:0000269|PubMed:27830762}. | null | null | FUNCTION: Oleate hydroxylase involved in the biosynthesis of ricinoleate (PubMed:22370951, PubMed:27830762). Exhibits delta(12) hydroxylase activity on 16C and 18C monounsaturated fatty acids (e.g. oleic and palmitoleic acids), and, to a lower extent, gamma(3) hydroxylase activity on ricinoleic acid (PubMed:18467452, PubMed:27830762). It uses cytochrome b5 as an electron donor. May act on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (By similarity). {ECO:0000250|UniProtKB:Q41131, ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951, ECO:0000269|PubMed:27830762}. | Claviceps purpurea (Ergot fungus) (Sphacelia segetum) |
B5A5T4 | QVR_DROME | MWTQRNAVGNWLLVLTAVIGFLTFIWIPQTSAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLHTNGCQLHLIPIAVAVSWLMGQLLSR | null | null | negative regulation of membrane potential [GO:0045837]; positive regulation of circadian sleep/wake cycle, sleep [GO:0045938]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; regulation of synaptic transmission, cholinergic [GO:0032222]; rhythmic process [GO:0048511]; sleep [GO:0030431] | external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | acetylcholine receptor inhibitor activity [GO:0030550]; GPI anchor binding [GO:0034235]; potassium channel activator activity [GO:0099104] | PF17064; | null | Quiver family | PTM: N-glycosylated probably on Asn-57. {ECO:0000269|PubMed:18635795, ECO:0000269|PubMed:26828958}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18635795}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18635795}; Extracellular side {ECO:0000269|PubMed:26828958}. Membrane raft {ECO:0000269|PubMed:21813698}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18635795}; Extracellular side {ECO:0000269|PubMed:26828958}. | null | null | null | null | null | FUNCTION: Bifunctional regulator of neuronal activity in the mushroom body, and possibly other regions of the brain, that acts as a signaling molecule required for homeostatic regulation of sleep under normal conditions and after sleep deprivation (PubMed:18635795, PubMed:20010822, PubMed:24613312). Reduces neuronal excitability by enhancing Sh/shaker K(+) channel activity; possibly by stabilizing Sh/shaker to increase protein levels, accelerating its activation kinetics, slowing C-type inactivation and enhancing recovery from inactivation (PubMed:10934243, PubMed:18635795, PubMed:20010822, PubMed:20429677, PubMed:21813698, PubMed:24613312). Specifically affects the A-type K(+) current (PubMed:10934243). Antagonizes nicotinic acetylcholine receptors (nAChRs) to reduce synaptic transmission, possibly by preventing their localization to the cell surface (PubMed:24613312, PubMed:26828958). Required for regulation of neuromuscular excitability and plasticity at neuromuscular junctions (PubMed:29117754). {ECO:0000269|PubMed:10934243, ECO:0000269|PubMed:18635795, ECO:0000269|PubMed:20010822, ECO:0000269|PubMed:20429677, ECO:0000269|PubMed:21813698, ECO:0000269|PubMed:24613312, ECO:0000269|PubMed:26828958, ECO:0000269|PubMed:29117754}. | Drosophila melanogaster (Fruit fly) |
B5A7L9 | GTF3_STRPA | MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVAGLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAYYNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERFSFVKEWKYDIPLKVYTWQNVELPQNVHKINYRPDEQLLMEMSQGGFGLVWMDDKDKEYQSLYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELVKNVRSFNPILRKGFFTRRLLTESVFQAICD | 2.4.1.- | COFACTOR: Note=In vitro glycosyltransferase activity is metal-independent. {ECO:0000269|PubMed:21653318}; | protein glycosylation [GO:0006486] | null | nucleotide binding [GO:0000166]; UDP-glucosyltransferase activity [GO:0035251] | null | 3.40.50.2000; | Gtf3 glucosyltransferase family | null | null | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:20164186, ECO:0000269|PubMed:25404702}. | null | null | FUNCTION: Required for polymorphic O-glycosylation of the serine-rich repeat protein Fap1. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Fap1; does not use other sugar nucleotides as substrates. {ECO:0000269|PubMed:20164186, ECO:0000269|PubMed:21653318, ECO:0000269|PubMed:25404702}. | Streptococcus parasanguinis |
B5AR80 | OXLA_BOTPA | MNVFFMFSLLFLAALGSCADDGNPLEECFRETDYEEFLEIAKNGLSATSNPKHVVIVGAGMSGLSAAYVLANAGHQVTVLEASKRAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVRLNVRVIKIQQDVKEVTVTYQTSAKETLSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKEEIQAFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLTAARDVNRASE | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated (Probable). The enzymatic activity is not affected by deglycosylation. {ECO:0000269|PubMed:19135502, ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19135502}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:19135502}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:19135502}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:19135502}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:19135502}; CATALYTIC ACTIVITY: Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:19135502}; | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:19135502). Is highly active on L-Met, L-Leu, L-Phe and L-Ile (PubMed:19135502). Exhibits diverse biological activities, such as antibacterial on both Gram-positive and Gram-negative bacteria and antiparasitic activities, as well as induction of platelet aggregation (PubMed:19135502). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also have activities in hemorrhage, hemolysis, edema, and apoptosis. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:19135502}. | Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis) |
B5BLW5 | ARE_SACSO | MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGETRDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRILSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKIATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRKGYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEYDPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGALLKDIFK | 3.1.1.2; 3.1.8.1 | null | aromatic compound catabolic process [GO:0019439] | null | aryldialkylphosphatase activity [GO:0004063]; arylesterase activity [GO:0004064]; triglyceride lipase activity [GO:0004806] | PF07859; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:18931117}; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:18931117}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for phenyl acetate (PA) {ECO:0000269|PubMed:18931117}; KM=29 uM for alpha-naphthyl acetate (alpha-NA) {ECO:0000269|PubMed:18931117}; KM=224 uM for p-nitrophenyl butyrate (C4) {ECO:0000269|PubMed:18931117}; KM=31 uM for p-nitrophenyl caproate (C6) {ECO:0000269|PubMed:18931117}; KM=28 uM for p-nitrophenyl caprylate (C8) {ECO:0000269|PubMed:18931117}; KM=81 uM for p-nitrophenyl caprate (C10) {ECO:0000269|PubMed:18931117}; KM=122 uM for p-nitrophenyl laurate (C12) {ECO:0000269|PubMed:18931117}; KM=276 uM for p-nitrophenyl palmitate (C16) {ECO:0000269|PubMed:18931117}; KM=234 uM for p-nitrophenyl phosphate {ECO:0000269|PubMed:18931117}; KM=5 uM for paraoxon {ECO:0000269|PubMed:18931117}; KM=246 uM for methyl paraoxon {ECO:0000269|PubMed:18931117}; Note=kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(-1) with p-nitrophenyl caprylate (C8) as substrate. kcat is 341 sec(-1) with p-nitrophenyl caprate (C10) as substrate. kcat is 264 sec(-1) with p-nitrophenyl laurate (C12) as substrate. kcat is 265 sec(-1) with p-nitrophenyl palmitate (C16) as substrate. kcat is 269 sec(-1) with p-nitrophenyl phosphate as substrate. kcat is 597 sec(-1) with paraoxon as substrate. kcat is 342 sec(-1) with methyl paraoxon as substrate. {ECO:0000269|PubMed:18931117}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:18931117}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 94 degrees Celsius. Very thermostable, but rapidly inactivated above 94 degrees Celsius. Most of the activity is retained for 5 days at 50 degrees Celsius, and approximately 70% of the activity is retained after 5 days at 70 degrees Celsius. 52% of the activity is still retained after 50 hours at 90 degrees Celsius, but completely inactivated after 5 days at 90 degrees Celsius. {ECO:0000269|PubMed:18931117}; | FUNCTION: Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro. {ECO:0000269|PubMed:18931117}. | Saccharolobus solfataricus (Sulfolobus solfataricus) |
B5BT18 | BTAF1_ARATH | MAQQQSSRLNRLLTLLDTGSTQATRLTAAKQIGDIAKSHPQDLSSLLRKVLHHLRSKKWDTRVAAAHAIGAIVLNVKHPSLSELLNSLATKLGEAGISDNVDEVVAFRNLQSKILANAPFRSFEMNKVLEFGALLASGGQEYDILNDNSKNPRDRVARQKKNLRRRLGLDMCEQFMDVNEMIRDEDLIEQKSNVPANGVGNRLYANCSPHHIQQFVSRMVPRVNSRRPSARELNLLKRKAKISSKDQAKGSCEVADVEMSSSHVASTSKRILSDSLDSSKADIGNEDDIEPDGDGKWPFHSFVEQLILDMFDPAWEIRHGSVMALREILMLHGGSAGVSTEEFSSDNGFELKDVLNKVTREREIDLNMQVSENELEPLRKRPKIEDPSKSFIDNTVLEVIGGDYDINVKDEDAEFLLPPVKVNGQTDCSSTKLEPQSSMDDSTSHSEINHVAEVNNHFEDKSFIEEPVIPKQQEENLEVLDLVKQARHSWIKNFEFLQDCTIRFLCVLSLDRFGDYISDQVVAPVREACAQALGATFKYMNPSLIYETLNILLQMQRRPEWEIRHGSLLGIKYLVAVRQEMLQDLLGYILPACKAGLEDSDDDVRAVAADALIPAAAAIVSLRGQTLLSIVMLLWDILLELDDLSPSTSSIMNLLAEIYSQDDMTLVMHEELSLGEEQNIELNEMGHIESIGERRDVKESPYALSGLAPRLWPFTRHDITSVRFSAIRTLERLLEAGCRKNISGQSKSSFWPSSILGDTLRIVFQNLLLESTEEILECSERVWRLLVQCPVDDLEDTAKFYMASWIELAATPYGSTLDATKMFWPVAPPRKSHFKAAAKMKAVKLENEASSILGFDYARSSASLEKQEDASARSTKIIVGSDMEMSVTRTRVVTASALGIFASRLREGSMQFVVDPLSSTLTSMSGVQRQVGSIVLISWFRETKCKAPSDGSGSLPGFPSPLKKWLLDLLACADPAFPTKDIFLPYAELSRTYTKMRNEASQLLHTVETCHCFDKLLSTNKLNVESVTADETIDFASTLDLWNKESAGNESLEKQVFEDVESSRQQLLSTAGYLKCVQSNLHITVTSLVAAAVVWMSEFPARLNPIILPLMASIKREQEQILQQIAAEALAELIAYCVDRKPSPNDKLIKNICSLTCMDPSETPQASIISSMDIVDDMDFLSSRSNTGKQKAKVVLASGEDRSKVEGFITRRGSELALKHLSLKFGGSLFDKLPKLWECLTEVLVPEIPSDQQKIDLKIESISDPQVLINNIQVVRSIAPVMEETLKPRLLSLLPCIFKCVRHSHVAVRLAASRCVMTMAKSMTTDVMAAVVESAIPMLGDLTCISGRQGAGMLIGLLVQGLGVELVPYSPLLVVPLLRCMSDVDSSVRQSVTRSFAALVPMLPLARGVPPPVGLSKDLSSNAEDAKFLEQLLDNSHIDDYKLCTELKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTDELDVFPSIIVCPSTLVGHWAFEIEKYIDLSLLSVLQYVGSAQDRVSLREQFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQLKLYEQFSGSSAKQEISSIIKVDGSADSGNADVAPTKASTHVFQALQYLLKLCSHPLLVLGDKVTEPVASDLAAMINGCSDIITELHKVQHSPKLVALQEILEECGIGSDASSSDGTLSVGQHRVLIFAQHKALLDIIEKDLFQAHMKSVTYMRLDGSVVPEKRFEIVKAFNSDPTIDVLLLTTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVINAENASMKTMNTDQLLDLFASAETSKKGGGSSKKGSEDNDQIAGTGKGMKAILGNLEELWDQSQYTEEYNLSQFLTKLNG | 3.6.4.- | null | positive regulation of shoot apical meristem development [GO:1902185] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; TBP-class protein binding [GO:0017025] | PF12054;PF00271;PF00176; | 1.25.10.10;3.40.50.300;3.40.50.10810; | Helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in meristem development. Acts as a positive regulator of the CUC-STM pathway in shoot apical meristem (SAM) neo-formation. {ECO:0000269|PubMed:19054368}. | Arabidopsis thaliana (Mouse-ear cress) |
B5D5N9 | CTR2_RAT | MIPCRAVLTFTRCLIRRKIVTLDSLEDSKLCRCLTTMDLIALGVGSTLGAGVYVLAGEVAKADSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVTVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLNKQIGQFFKTYFKMNYTGLAEYPDFFAVCLVLLLAGLLSFGVKESAWVNKFFTAINILVLLFVMVAGFVKGNVANWKISEEFLKNISASAREPPSENGTSIYGAGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVTSLLVCFMAYFGVSAALTLMMPYYLLDEKSPLPVAFEYVGWGPAKYVVAAGSLCALSTSLLGSMFPLPRILFAMARDGLLFRFLARVSKRQSPVAATMTAGVISAVMAFLFDLKALVDMMSIGTLMAYSLVAACVLILRYQPGLCYEQPKYTPEKDILESCTNATSKSESQVTMLQGQGFSLRTLFNPSALPTRQSASLVSFLVGFLAFLIAGLSILTTYGVQAIARLEAWSLALLALFLVLCAAVILTIWRQPQNQQKVAFMVPFLPFLPAFSILVNIYLMVQLSADTWVRFSIWMVLGFLIYFAYGIRHSLEGNPRDEEEDEDVCPDNVNAAAEEKSAMQANDHHQRNLSLPFILHEKTSEC | null | null | amino acid import across plasma membrane [GO:0089718]; establishment of localization in cell [GO:0051649]; L-alpha-amino acid transmembrane transport [GO:1902475]; L-amino acid transport [GO:0015807]; L-arginine import across plasma membrane [GO:0097638]; L-arginine transmembrane transport [GO:1903826]; L-ornithine transmembrane transport [GO:1903352]; macrophage activation [GO:0042116]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide production involved in inflammatory response [GO:0002537]; regulation of inflammatory response [GO:0050727]; regulation of macrophage activation [GO:0043030] | cell junction [GO:0030054]; membrane [GO:0016020]; plasma membrane [GO:0005886] | amino acid transmembrane transporter activity [GO:0015171]; L-amino acid transmembrane transporter activity [GO:0015179]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064] | PF13520;PF13906; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, Cationic amino acid transporter (CAT) (TC 2.A.3.3) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18581}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18581}. | CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199, ChEBI:CHEBI:46911; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-homoarginine(in) = L-homoarginine(out); Xref=Rhea:RHEA:71203, ChEBI:CHEBI:143006; Evidence={ECO:0000250|UniProtKB:P52569}; | null | null | null | null | FUNCTION: Functions as a permease involved in the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine). The affinity for its substrates differs between isoforms created by alternative splicing (By similarity). May play a role in classical or alternative activation of macrophages via its role in arginine transport (By similarity). {ECO:0000250|UniProtKB:P18581, ECO:0000250|UniProtKB:P52569}. | Rattus norvegicus (Rat) |
B5DE31 | YBOX1_DANRE | MSSEAETQQPPQPAADAESPSSPAAAATAGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVQGSKYAADRNRYRRYPRRRAPPRDYQENYQSDPEAEPREKREGAESAPEGEMQQQQRRPTYPGRRRYPPYFVRRRYGRRPPYTNSQRGEMTEGGEGEENQGGPDQGNKPMRQNYYRGFRPSRGPSRPRPVRDGEEDKENQSESGQNQEPRQRRYRRNFNYRRRRPQTTKPQDGKDSKAADASADKSAAPEAEQGGAD | null | null | chordate embryonic development [GO:0043009]; egg activation [GO:0007343]; embryonic morphogenesis [GO:0048598]; epidermis development [GO:0008544]; establishment of RNA localization [GO:0051236]; miRNA transport [GO:1990428]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; negative regulation of cellular senescence [GO:2000773]; negative regulation of mRNA processing [GO:0050686]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation [GO:0045947]; oocyte maturation [GO:0001556]; regulation of gene expression [GO:0010468]; RNA splicing [GO:0008380]; RNA transport [GO:0050658]; tRNA transport [GO:0051031] | extracellular exosome [GO:0070062]; messenger ribonucleoprotein complex [GO:1990124]; nucleus [GO:0005634]; P-body [GO:0000932] | C5-methylcytidine-containing RNA reader activity [GO:0062153]; eukaryotic initiation factor 4E binding [GO:0008190]; methyl-CpG binding [GO:0008327]; miRNA binding [GO:0035198]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723] | PF00313; | 2.40.50.140; | YBX1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P67809}. Nucleus {ECO:0000250|UniProtKB:P67809}. Cytoplasmic granule {ECO:0000250|UniProtKB:P67809}. Secreted {ECO:0000250|UniProtKB:P67809}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P67809}. Cytoplasm, P-body {ECO:0000250|UniProtKB:P62960}. | null | null | null | null | null | FUNCTION: DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing and transcription regulation (PubMed:30135188, PubMed:31399345). Binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (PubMed:31399345). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting pabpc1a, thereby preventing mRNA decay (PubMed:31399345). Plays a role in the maternal-to-zygotic transition in early embryo by binding to m5C-containing maternal mRNAs and preventing their degradation (PubMed:31399345). Also promotes maternal-to-zygotic transition in oocytes and embryos by promoting translation repression; molecular mechanisms governing translation repression are unknown (PubMed:30135188). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs. Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (By similarity). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (By similarity). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (By similarity). Also able to bind DNA and regulate transcription. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair. The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (By similarity). {ECO:0000250|UniProtKB:P67809, ECO:0000269|PubMed:30135188, ECO:0000269|PubMed:31399345}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B5DEH0 | LIMD1_RAT | MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGASNNPEFEETRRVFATKMAKIHLQQQQQQQLLQEEALPRAGRSPINGGNRQGVSSKLAADGAAKPPLAVPTVAPGLATTTMAVQSSYPPQEQRTRPSAHGARPGSQNCGSREGPVSSQRPALHGLGPCEDPSCLTHGDYYDNFSLASPQWGDKPEESPSMSLSVGSGWPGCPGNDSLSHRSCGDSHPYHPQLSMCSGRSFESGQDSGIGGHSSEKPTGLWSTASSQRVNLGFSSTGLENGTPAQPKGTTVSAPMVPSSTSQGACLRRDSSLGYEAPGRVFKPLVDTQPWLQDGPKSYLSVSAPLSSTTSKDNAQTGMTAGLDPKLGCVESGTSPKPSPTSNVHPVMSAPSELSCKESPPSWSTDSSLGPVLPESPTPSRVRLPCQTLTPGPELGPSTAELKLEALTQRLEREMDAHPKADYFGACVKCSKGVFGAGQACQAMGDLYHDACFTCAACSRKLRGKAFYFVNGKVFCEEDFLYSGFQQSADRCFLCGHLIMDMILQALGKSYHPGCFRCVICNECLDGVPFTVDSENKIYCVRDYHKVLAPKCAACGLPILPPEGSDETIRVVSMDRDYHVECYHCEDCGLELNDEDGHRCYPLEDHLFCHSCHVKRLEKGPSPASLHQHHF | null | null | cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of hippo signaling [GO:0035331]; negative regulation of osteoblast differentiation [GO:0045668]; osteoblast development [GO:0002076]; P-body assembly [GO:0033962]; phosphorylation [GO:0016310]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; regulation of cell shape [GO:0008360]; regulation of DNA-templated transcription [GO:0006355]; response to hypoxia [GO:0001666] | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; plasma membrane [GO:0005886]; RISC complex [GO:0016442]; transcription regulator complex [GO:0005667] | metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | PTM: Phosphorylated during mitosis. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
B5DEI4 | UBE2W_RAT | MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC | 2.3.2.23; 2.3.2.25 | null | antiviral innate immune response [GO:0140374]; cellular response to misfolded protein [GO:0071218]; DNA repair [GO:0006281]; negative regulation of TORC1 signaling [GO:1904262]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K11-linked ubiquitination [GO:0070979]; protein monoubiquitination [GO:0006513]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated at Met-1. {ECO:0000250|UniProtKB:Q96B02}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96B02}. Note=In the nucleus, colocalizes with FANCL. {ECO:0000250|UniProtKB:Q96B02}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:Q96B02, ECO:0000255|PROSITE-ProRule:PRU00388}; CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].; EC=2.3.2.25; Evidence={ECO:0000250|UniProtKB:Q96B02}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate. {ECO:0000250|UniProtKB:Q96B02}. | Rattus norvegicus (Rat) |
B5DF27 | LOXL2_RAT | MEIPFGSCLYSCLALLVLLPSLSLAQYESWPYQLQYPEYFQQPPPEHHQHQVPSDVVKIQVRLAGQKRKHNEGRVEVYYEGQWGTVCDDDFSIHAAHVVCREVGYVEAKSWTASSSYGPGEGPIWLDNIYCTGKESTLAACSSNGWGVTDCKHPEDVGVVCSEKRIPGFKFDNSLINQIESLNIQVEDIRIRPILSAFRHRKPVTEGYVEVKEGKAWKQICDKHWTAKNSHVVCGMFGFPAEKTYNPKAYKTFASRRKLRYWKFSMNCTGTEAHISSCKLGPPMFRDPVKNATCENGQPAVVSCVPSQIFSPDGPSRFRKAYKPEQPLVRLRGGAQVGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGTAKEAVTGSRLGQGIGPIHLNEVQCTGTEKSIIDCKLNTESQGCNHEEDAGVRCNIPIMGFQKKVRLNGGRNPYEGRVEVLTERNGSLVWGNVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGNIFANKVIMSGVKCSGTELSLAHCRHDEEVVCPEGGVQYGAGVACSETAPDLVLNAEIVQQTAYLEDRPMALLQCAMEENCLSASAVHTDPTRGHRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTYYDLLSLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWIDITDVPPGDYLFQVVINPNYEVPESDFSNNIMKCRSRYDGYRIWMYNCHVGGAFSEETEQKFEHFSGLLNNQLSVQ | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein modification process [GO:0036211]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040] | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.; PTM: N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:21835952}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0}. | Rattus norvegicus (Rat) |
B5DF45 | TRAF6_RAT | MSLLNCENSCASSQSSSDCCAAMANSCSAAMKDDSVSGCVSTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACITKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNKGCVQKMELRHLEDHQVHCEFALVICPQCQRFFQKCQINKHIIEDCPRRQVSCVNCAVPMPYEEKEIHDQSCPLANIICEYCGTILIREQMPNHYDLDCPTAPVPCTFSVFGCHEKMQRNHLARHLQENTQLHMRLLAQAVHNVNLSLRPCDASSPSRGCRPEDPNYEETVKQLEGRLVRQDHQIRELTAKMETQSMHVSELKRTIRSLEDKVAEMEAQQCNGIYIWKIGNFGMHLKSQEEERPVVIHSPGFYTGRPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAVIRQNHEEVMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQGTFIKDDTLLVRCEVSTRFDMGGLRKEGFQPRSTDAGV | 2.3.2.27 | null | animal organ morphogenesis [GO:0009887]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antiviral innate immune response [GO:0140374]; autophagosome assembly [GO:0000045]; bone remodeling [GO:0046849]; bone resorption [GO:0045453]; canonical NF-kappaB signal transduction [GO:0007249]; cell development [GO:0048468]; cellular response to angiotensin [GO:1904385]; cellular response to cytokine stimulus [GO:0071345]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; DNA damage response [GO:0006974]; immune response [GO:0006955]; in utero embryonic development [GO:0001701]; innate immune response [GO:0045087]; interleukin-1-mediated signaling pathway [GO:0070498]; interleukin-17-mediated signaling pathway [GO:0097400]; interleukin-17A-mediated signaling pathway [GO:0038173]; interleukin-33-mediated signaling pathway [GO:0038172]; JNK cascade [GO:0007254]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube closure [GO:0001843]; non-canonical NF-kappaB signal transduction [GO:0038061]; odontogenesis of dentin-containing tooth [GO:0042475]; ossification [GO:0001503]; osteoclast differentiation [GO:0030316]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of immunoglobulin production [GO:0002637]; response to interleukin-1 [GO:0070555]; response to ischemia [GO:0002931]; signal transduction [GO:0007165]; T cell receptor signaling pathway [GO:0050852]; T-helper 1 type immune response [GO:0042088]; toll-like receptor 4 signaling pathway [GO:0034142]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | CD40 receptor complex [GO:0035631]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; lipid droplet [GO:0005811]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; protein kinase B binding [GO:0043422]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-ubiquitin ligase activity [GO:0034450]; zinc ion binding [GO:0008270] | PF21355;PF18048;PF00097;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated on Lys-124 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. LRRC19 induces 'Lys-63' ubiquitination (By similarity). Ubiquitinated at Lys-327 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250|UniProtKB:P70196}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN (By similarity). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (By similarity). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | Rattus norvegicus (Rat) |
B5DF51 | EMC5_RAT | MAPSLWKGLVGVGLFALAHAAFSAAQHRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGIVHIAGEFKDMDATSELKNKTFDTLRNHPSFYVFNHRGRVLFRPSDATNSSNLDALSSNTSLKLRKFDSLRR | null | null | cobalt ion transport [GO:0006824]; copper ion transport [GO:0006825]; iron ion transport [GO:0006826]; magnesium ion transport [GO:0015693]; monoatomic cation transport [GO:0006812]; protein insertion into ER membrane by stop-transfer membrane-anchor sequence [GO:0045050]; tail-anchored membrane protein insertion into ER membrane [GO:0071816] | cytoplasm [GO:0005737]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; EMC complex [GO:0072546]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886] | cobalt ion transmembrane transporter activity [GO:0015087]; ferrous iron transmembrane transporter activity [GO:0015093]; inorganic cation transmembrane transporter activity [GO:0022890]; magnesium ion transmembrane transporter activity [GO:0015095]; membrane insertase activity [GO:0032977] | PF10270; | null | Membrane magnesium transporter (TC 1.A.67) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N4V1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N4V1}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8K273}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N4V1}. Early endosome membrane {ECO:0000250|UniProtKB:Q8K273}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N4V1}. | null | null | null | null | null | FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (By similarity). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. May be involved in Mg(2+) transport (By similarity). {ECO:0000250|UniProtKB:Q8K273, ECO:0000250|UniProtKB:Q8N4V1}. | Rattus norvegicus (Rat) |
B5DF89 | CUL3_RAT | MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLACMYKLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLQESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIESGHIFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; cell projection organization [GO:0030030]; cellular response to amino acid stimulus [GO:0071230]; COPII vesicle coating [GO:0048208]; embryonic cleavage [GO:0040016]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; fibroblast apoptotic process [GO:0044346]; gastrulation [GO:0007369]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; liver morphogenesis [GO:0072576]; mitotic cell cycle [GO:0000278]; mitotic metaphase chromosome alignment [GO:0007080]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type I interferon production [GO:0032480]; nuclear protein quality control by the ubiquitin-proteasome system [GO:0071630]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic cell cycle phase transition [GO:1901992]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of TORC1 signaling [GO:1904263]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein catabolic process [GO:0030163]; protein destabilization [GO:0031648]; protein K48-linked ubiquitination [GO:0070936]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation protein catabolic process at postsynapse [GO:0140252]; stem cell division [GO:0017145]; stress fiber assembly [GO:0043149]; trophectodermal cellular morphogenesis [GO:0001831]; ubiquitin-dependent protein catabolic process [GO:0006511]; Wnt signaling pathway [GO:0016055] | centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; polar microtubule [GO:0005827]; postsynapse [GO:0098794]; sperm flagellum [GO:0036126]; spindle pole [GO:0000922]; synapse [GO:0045202] | cyclin binding [GO:0030332]; identical protein binding [GO:0042802]; Notch binding [GO:0005112]; POZ domain binding [GO:0031208]; ubiquitin ligase complex scaffold activity [GO:0160072]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625] | PF00888;PF10557; | 1.20.1310.10;1.10.10.10; | Cullin family | PTM: Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q13618}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13618}. Golgi apparatus {ECO:0000250|UniProtKB:Q13618}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q13618}. Cytoplasm {ECO:0000250|UniProtKB:Q13618}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q13618}. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q13618}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q13618}. Note=Detected along the length of the sperm flagellum and in the cytoplasm of the germ cells. Predominantly found in the nucleus in interphase cells, found at the centrosome at late G2 or prophase, starts accumulating at the spindle poles in prometaphase and stays on the spindle poles and the mitotic spindle at metaphase. {ECO:0000250|UniProtKB:Q13618}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, MACROH2A1 and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). The BCR(KLHL25) ubiquitin ligase complex is also involved in lipid synthesis by mediating ubiquitination and degradation of ACLY. The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis. The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity. The BCR(KLHL18) E3 ubiquitin ligase complex mediates the ubiquitination of AURKA leading to its activation at the centrosome which is required for initiating mitotic entry. The BCR(KEAP1) E3 ubiquitin ligase complex acts as a key sensor of oxidative and electrophilic stress by mediating ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes. As part of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex functions mediates 'Lys-48' ubiquitination and proteasomal degradation of TIAM1. By controlling the ubiquitination of that RAC1 guanine exchange factors (GEF), regulates RAC1 signal transduction and downstream biological processes including the organization of the cytoskeleton, cell migration and cell proliferation. {ECO:0000250|UniProtKB:Q13618}. | Rattus norvegicus (Rat) |
B5DF91 | ELAV1_RAT | MSNGYEDHMAEDCRDDIGRTNLIVNYLPQNMTQEELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAISTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNMALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGISGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA destabilization [GO:0061157]; mRNA stabilization [GO:0048255]; negative regulation of miRNA-mediated gene silencing [GO:0060965]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of translation [GO:0045727]; post-transcriptional gene silencing [GO:0016441]; protein homooligomerization [GO:0051260]; protein import into nucleus [GO:0006606]; regulation of stem cell population maintenance [GO:2000036] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; postsynapse [GO:0098794]; ribonucleoprotein complex [GO:1990904]; sarcoplasm [GO:0016528] | double-stranded RNA binding [GO:0003725]; lncRNA binding [GO:0106222]; miRNA binding [GO:0035198]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | RRM elav family | PTM: Phosphorylated by MAPKAPK2. Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:Q15717}.; PTM: Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge. {ECO:0000250|UniProtKB:Q15717}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18161049}. Nucleus {ECO:0000250|UniProtKB:Q15717}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P70372}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q15717}. Note=Translocates into the cytoplasm following phosphorylation by MAPKAPK2. Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoskeleton-bound polysomes. Localizes to the stress granules in the presence of PLEKHN1. {ECO:0000250|UniProtKB:Q15717}. | null | null | null | null | null | FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (By similarity). Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). Has also been shown to be capable of binding to m6A-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA (By similarity). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (By similarity). {ECO:0000250|UniProtKB:P70372, ECO:0000250|UniProtKB:Q15717}. | Rattus norvegicus (Rat) |
B5DF94 | SRPX2_RAT | MKTGSLTQRGALLLLLLLAPAVTPTWYAGSGYSPDESYNEVYAEEVPDTRALDYRVPRWCYTLNIQDGEATCYSPRGGNYHSSLGTRCELSCDRGFRLIGRKSVQCLPSRRWSGTAYCRQMRCHTLPFITSGTYTCTNGMLLDSRCDYSCSSGYHLEGDRSRICMEDGRWSGGEPVCVDIDPPKIRCPHSREKIAEPEKLTARVYWDPPLVKDSADGTITRVTLRGPEPGSHFPEGEHVIRYTAYDRAYNRASCKFIVKVQVRRCPILKPPQHGYLTCSSAGDNYGAICEYHCDGGYERQGTPSRVCQSSRQWSGSPPVCTPMKINVNVNSAAGLLDQFYEKQRLLIVSAPDPSNRYYKMQISMLQQSTCGLDLRHVTIIELVGQPPQEVGRIREQQLSAGIIEELRQFQRLTRSYFNMVLIDKQGIDRERYMEPVTPEEIFTFIDDYLLSNQELARRAEQRDVCE | null | null | angiogenesis [GO:0001525]; cell motility [GO:0048870]; cell-cell adhesion [GO:0098609]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of synapse assembly [GO:0051965]; regulation of phosphorylation [GO:0042325]; vocalization behavior [GO:0071625] | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; excitatory synapse [GO:0060076]; extracellular space [GO:0005615]; synaptic membrane [GO:0097060] | hepatocyte growth factor binding [GO:0036458]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102] | PF13778;PF02494;PF00084; | 2.10.70.10; | null | PTM: Contains chondroitin sulfate chains. {ECO:0000250|UniProtKB:O60687}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O60687}. Cytoplasm {ECO:0000250|UniProtKB:O60687}. Cell surface {ECO:0000269|PubMed:24179158}. Synapse {ECO:0000269|PubMed:24179158}. | null | null | null | null | null | FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF (By similarity). Promotes synapse formation. {ECO:0000250|UniProtKB:O60687, ECO:0000250|UniProtKB:Q8R054, ECO:0000269|PubMed:24179158}. | Rattus norvegicus (Rat) |
B5DFG1 | PINK1_RAT | MAVRQALGRGLQLGRALLLRFAPKPGPVSGWGKPGPGAAWGRGERPGRVSSPGAQPRPLGLPLPDRYRFFRQSVAGLAARIQRQFVVRARGGAGPCGRAVFLAFGLGLGLIEEKQAESRRAASACQEIQAIFTQKNKQVSDPLDTRRWQGFRLEDYLIGQAIGKGCNAAVYEATMPTLPQHLEKAKHLGLLGKGPDVVSKGADGEQAPGAPAFPFAIKMMWNISAGSSSEAILSKMSQELVPASRMALDGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADERVGLQLPFNSSSVERGGNGSLMAPEVSTAHSGPHAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPKSVPPETRQLVRSLLQREANKRPSARIAANVLHLSLWGEHLLALKNLKLDKMIAWLLQQSAATLLADRLREKSCVETKLQMLFLANLECEALCQAALLLSSWRAAP | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BXM7}; | catecholamine secretion [GO:0050432]; cellular response to hydrogen sulfide [GO:1904881]; cellular response to hypoxia [GO:0071456]; cellular response to oxidative stress [GO:0034599]; cellular response to toxic substance [GO:0097237]; dopamine secretion [GO:0014046]; establishment of localization in cell [GO:0051649]; establishment of protein localization to mitochondrion [GO:0072655]; hemopoiesis [GO:0030097]; intracellular signal transduction [GO:0035556]; maintenance of protein location in mitochondrion [GO:0072656]; mitochondrial fission [GO:0000266]; mitochondrion organization [GO:0007005]; mitochondrion to lysosome vesicle-mediated transport [GO:0099074]; mitophagy [GO:0000423]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of gene expression [GO:0010629]; negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway [GO:1903384]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:1903751]; negative regulation of macroautophagy [GO:0016242]; negative regulation of mitochondrial fission [GO:0090258]; negative regulation of mitophagy [GO:1901525]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization [GO:1904925]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of catecholamine secretion [GO:0033605]; positive regulation of cristae formation [GO:1903852]; positive regulation of dopamine secretion [GO:0033603]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mitochondrial electron transport, NADH to ubiquinone [GO:1902958]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of mitophagy in response to mitochondrial depolarization [GO:0098779]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of synaptic transmission, dopaminergic [GO:0032226]; positive regulation of translation [GO:0045727]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of hydrogen peroxide metabolic process [GO:0010310]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of mitochondrion organization [GO:0010821]; regulation of neuron apoptotic process [GO:0043523]; regulation of oxidative phosphorylation [GO:0002082]; regulation of protein targeting to mitochondrion [GO:1903214]; regulation of protein ubiquitination [GO:0031396]; regulation of protein-containing complex assembly [GO:0043254]; regulation of reactive oxygen species metabolic process [GO:2000377]; respiratory electron transport chain [GO:0022904]; response to ischemia [GO:0002931]; response to oxidative stress [GO:0006979] | astrocyte projection [GO:0097449]; axon [GO:0030424]; cell body [GO:0044297]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; growth cone [GO:0030426]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; C3HC4-type RING finger domain binding [GO:0055131]; calcium-dependent protein kinase activity [GO:0010857]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]; protein kinase activity [GO:0004672]; protein kinase B binding [GO:0043422]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; TORC2 complex binding [GO:1904841]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into the inner mitochondrial membrane (IMM), where it is proteolytically cleaved by mitochondrial-processing peptidase (MPP) and then undergoes further proteolytic cleavage by PARL or AFG3L2 to give rise to the 52 kDa short form. The 52 kDa short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM). If accumulation at the OMM fails and it is imported into the depolarized mitochondria, it undergoes cleavage by the IMM protease OMA1, promoting its subsequent degradation by the proteasome. {ECO:0000250|UniProtKB:Q9BXM7}.; PTM: Autophosphorylated. Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation. Autophosphorylation at Ser-227 and Ser-401 is sufficient and essential for selective recruitment of PRKN to depolarized mitochondria, via PINK1-dependent phosphorylation of ubiquitin and maybe PRKN. {ECO:0000250|UniProtKB:Q9BXM7}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:31536960}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q99MQ3}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BXM7}. Note=Localizes mostly in mitochondrion and the two smaller proteolytic processed fragments localize mainly in cytosol. When mitochondria lose mitochondrial membrane potential following damage, PINK1 import is arrested, which induces its accumulation in the outer mitochondrial membrane, where it acquires kinase activity. {ECO:0000250|UniProtKB:Q9BXM7}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9BXM7}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9BXM7}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as PRKN and DNM1L, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components. Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy. Mediates the translocation and activation of PRKN at the outer membrane (OMM) of dysfunctional/depolarized mitochondria. At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains at 'Ser-65', the PINK1-phosphorylated polyubiquitin then recruits PRKN from the cytosol to the OMM where PRKN is fully activated by phosphorylation at 'Ser-65' by PINK1. In damaged mitochondria, mediates the decision between mitophagy or preventing apoptosis by promoting PRKN-dependent poly- or monoubiquitination of VDAC1; polyubiquitination of VDAC1 by PRKN promotes mitophagy, while monoubiquitination of VDAC1 by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. When cellular stress results in irreversible mitochondrial damage, functions with PRKN to promote clearance of damaged mitochondria via selective autophagy (mitophagy). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by phosphorylating and thus promoting the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2. This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes. Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L. Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (By similarity). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity). Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity (By similarity). {ECO:0000250|UniProtKB:Q99MQ3, ECO:0000250|UniProtKB:Q9BXM7}. | Rattus norvegicus (Rat) |
B5DFI8 | UBE2S_RAT | MNSNVENLPPHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHPNVGPNGEICVNVLKRDWTAELGIRHVLLTIKCLLIHPNPESALNEEAGRLLLENYEEYAARARLLTEIHGGACSTSSGRAEASRDLASGASASSTDPMTPGVLGGAEGPMAKKHAGERDKKLAAKKKLDKKRALRRL | 2.3.2.23 | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell division [GO:0051301]; exit from mitosis [GO:0010458]; free ubiquitin chain polymerization [GO:0010994]; positive regulation of ubiquitin protein ligase activity [GO:1904668]; protein K11-linked ubiquitination [GO:0070979]; protein K27-linked ubiquitination [GO:0044314]; protein K29-linked ubiquitination [GO:0035519]; protein K6-linked ubiquitination [GO:0085020]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | anaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | anaphase-promoting complex binding [GO:0010997]; ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated by the APC/C complex during G1, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q16763}. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. Also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination. {ECO:0000250|UniProtKB:Q16763}. | Rattus norvegicus (Rat) |
B5DFN2 | SAHH2_RAT | MQEFTKFPTKTGRRSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIYSTQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKKYPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRSQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY | null | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250|UniProtKB:O43865}; Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:O43865}; | angiotensin-activated signaling pathway [GO:0038166]; apoptotic process [GO:0006915]; epithelial fluid transport [GO:0042045]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; one-carbon metabolic process [GO:0006730]; positive regulation of sodium ion transport [GO:0010765]; protein export from nucleus [GO:0006611]; regulation of monoatomic anion transport [GO:0044070]; regulation of mRNA 3'-end processing [GO:0031440]; response to calcium ion [GO:0051592]; S-adenosylmethionine cycle [GO:0033353] | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233] | enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF05221;PF00670; | 3.40.50.1480;3.40.50.720; | Adenosylhomocysteinase family | PTM: Phosphorylated at Ser/Thr residues between Ser-21 and Thr-25 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1. Phosphorylation at Ser-21 by PRKD1 and CAMK4 is required for further phosphorylations by CSNK1A1. Phosphorylation is induced by oxidative stress. Probably phosphorylated by CAMK2A; phosphorylation at Ser-21 may be required for interaction with SLC9A3. Dephosphorylated in response to apoptotic stress conditions which causes translocation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes and promotes apoptosis. {ECO:0000250|UniProtKB:O43865}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q80SW1}. Cytoplasm, cytosol {ECO:0000269|PubMed:20584908}. Apical cell membrane {ECO:0000269|PubMed:20584908}; Peripheral membrane protein {ECO:0000305}. Microsome {ECO:0000250|UniProtKB:Q80SW1}. Note=Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (By similarity). Localization to MAMs is greatly reduced under apoptotic stress conditions (By similarity). {ECO:0000250|UniProtKB:O43865}. | null | null | null | null | null | FUNCTION: Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate, competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. Promotes the formation of contact points between the endoplasmic reticulum (ER) and mitochondria, facilitating transfer of Ca(2+) from the ER to mitochondria (By similarity). Under normal cellular conditions, functions cooperatively with BCL2L10 to limit ITPR1-mediated Ca(2+) release but, under apoptotic stress conditions, dephosphorylated which promotes dissociation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes, inhibits BCL2L10 interaction with ITPR1 and leads to increased Ca(2+) transfer to mitochondria which promotes apoptosis (By similarity). In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (By similarity). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates from ITPR1 to interact with CFTR and SLC26A6, mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (By similarity). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition. May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state. Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (By similarity). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (By similarity). {ECO:0000250|UniProtKB:O43865, ECO:0000250|UniProtKB:Q80SW1, ECO:0000269|PubMed:20584908}. | Rattus norvegicus (Rat) |
B5FXE5 | FSP1_TAEGU | MGSRLSLDGSVRVVVVGGGFGGTAAASLLKSWAVPFVLVDVRDAFHHNVAALRAAVESGFAKKTFISYSVTFGDSFRQGKVVAIDPGRQQVVLSDGEELHYSHLILATGSDGPFPGKFNQVIDMESAIQTYEDMVKEIEKSQRILVVGGGAAGVEMAAEIKTEYPGKEIILIHSKTALADVELLPSVRQVVKEILLRKGVRLLLSEKVSDIENLRPNQFQKDMVVRTEKGTEVVVDMVVLCTGIKINSSAYAAAFGDKMASDGALKVNKHLQLEGYENIYAIGDCADLKEPKMAYHAGLHANVVVTNIINSLTQKPLKTYEPGSLTFLLSMGRNDGVGQVNGYYVGRLLVTIAKSRDLFVSKSWRTMGQTMPS | 1.6.5.- | COFACTOR: Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; Note=Binds 6-hydroxy-FAD non-covalently. {ECO:0000250|UniProtKB:Q9BRQ8}; | apoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]; vitamin K metabolic process [GO:0042373] | lipid droplet [GO:0005811]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655] | PF07992; | 3.50.50.100; | FAD-dependent oxidoreductase family | PTM: N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane. {ECO:0000250|UniProtKB:Q9BRQ8}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9BRQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BRQ8}. Nucleus {ECO:0000250|UniProtKB:Q9BRQ8}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + phylloquinone = NAD(+) + phylloquinol; Xref=Rhea:RHEA:74075, ChEBI:CHEBI:15378, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74076; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menaquinone-4 + NADH = menaquinol-4 + NAD(+); Xref=Rhea:RHEA:74079, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78277, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74080; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADH = menadiol + NAD(+); Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378, ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; | null | null | null | null | FUNCTION: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death. {ECO:0000250|UniProtKB:Q9BRQ8}. | Taeniopygia guttata (Zebra finch) (Poephila guttata) |
B5FYQ0 | ARL3_TAEGU | MGLLSILRKLKSTPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRNYFENTDILIYVIDSADRKRFEETGQELAELLDEEKLSGVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALSGEGVQDGMNWVCKNVSTKKK | null | null | cilium assembly [GO:0060271]; Golgi to plasma membrane transport [GO:0006893]; intraciliary transport [GO:0042073]; kidney development [GO:0001822]; mitotic cytokinesis [GO:0000281]; photoreceptor cell development [GO:0042461]; protein localization to ciliary membrane [GO:1903441]; protein transport [GO:0015031]; small GTPase-mediated signal transduction [GO:0007264]; smoothened signaling pathway [GO:0007224] | axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasmic microtubule [GO:0005881]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; photoreceptor connecting cilium [GO:0032391]; spindle microtubule [GO:0005876] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Note=Detected predominantly in the photoreceptor connecting cilium. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. Present on the mitotic spindle (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the ciliary membrane by releasing myristoylated protein from unc119 cargo adapters into the cilium (By similarity). {ECO:0000250}. | Taeniopygia guttata (Zebra finch) (Poephila guttata) |
B5FZY7 | IF4A3_TAEGU | MAGSAGSAGGSARKRLMKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI | 3.6.4.13 | null | embryonic cranial skeleton morphogenesis [GO:0048701]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of translation [GO:0045727]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000622] | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; exon-exon junction complex [GO:0035145]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; U2-type catalytic step 1 spliceosome [GO:0071006] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, eIF4A subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q3B8Q2}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P38919}; | null | null | null | null | FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions (By similarity). Involved in craniofacial development (By similarity). {ECO:0000250|UniProtKB:P38919, ECO:0000250|UniProtKB:Q7ZVA6}. | Taeniopygia guttata (Zebra finch) (Poephila guttata) |
B5HDJ6 | SEDS_STRE2 | MEPELTVPPLFSPIRQAIHPKHADIDVQTAAWAETFRIGSEELRGKLVTQDIGTFSARILPEGREEVVSLLADFILWLFGVDDGHCEEGELGHRPGDLAGLLHRLIRVAQNPEAPMMQDDPLAAGLRDLRMRVDRFGTAGQTARWVDALREYFFSVVWEAAHRRAGTVPDLNDYTLMRLYDGATSVVLPMLEMGHGYELQPYERDRTAVRAVAEMASFIITWDNDIFSYHKERRGSGYYLNALRVLEQERGLTPAQALDAAISQRDRVMCLFTTVSEQLAEQGSPQLRQYLHSLRCFIRGAQDWGISSVRYTTPDDPANMPSVFTDVPTDDSTEPLDIPAVSWWWDLLAEDARSVRRQVPAQRSA | 4.2.3.181 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24890698}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:24890698}; | terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + selina-4(15),7(11)-diene; Xref=Rhea:RHEA:54112, ChEBI:CHEBI:33019, ChEBI:CHEBI:138051, ChEBI:CHEBI:175763; EC=4.2.3.181; Evidence={ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:24890698}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:23307484}. | null | null | FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene selina-4(15),7(11)-diene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP leading to a (E,E)-germacradienyl cation (PubMed:23307484, PubMed:24890698). The only accepted substrate is (2E,6E)-farnesyl diphosphate (FPP) (PubMed:23307484, PubMed:24890698). {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:24890698}. | Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL 2958 / 5647) |
B5KM66 | SYCE3_MOUSE | MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; ectopic germ cell programmed cell death [GO:0035234]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental process [GO:0051094]; positive regulation of reproductive process [GO:2000243]; reciprocal meiotic recombination [GO:0007131]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | central element [GO:0000801]; chromosome [GO:0005694]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | null | PF15191; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21637789}. Chromosome {ECO:0000269|PubMed:21637789, ECO:0000269|PubMed:30949703}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000269|PubMed:21637789}. | null | null | null | null | null | FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility. May play a role in apoptosis of spermatogenic cells and pathogenesis of cryptorchidism. {ECO:0000269|PubMed:20407872, ECO:0000269|PubMed:21637789}. | Mus musculus (Mouse) |
B5KRH5 | PILR1_LINCY | MGSLNESSKVLVIGGTGYLGKRLVKASLDAGHDTYVMHRPEIGVDIEKVQLLLSFKMQGAHLVSASFDDHRSLVDAVSLVDVVICAISGVHIRSHQILLQLKLVQAIKEAGNVKRFLPSEFGTDPARMGDAMEPGRVTFDDKMVVRRAIEEAAIPFTYVSANCFAGYFLGGLCQPGSILPSRDHVTLLGDGNQKGVYVDENDIAAYTLKAIDDPRTLNKTLYIKPPKNILSQRQVVGIWEKHIGKQLHKTLLSEQDFLAAMKEQDYAEQVGLTHYYHVCYEGCLTNFEVEQDQEASKLYPDVRYTTVEEYLKRYV | 1.23.1.1; 1.23.1.2 | null | (+)-lariciresinol biosynthetic process [GO:1902132]; (+)-lariciresinol catabolic process [GO:1902131]; (+)-pinoresinol catabolic process [GO:1902125]; (-)-secoisolariciresinol biosynthetic process [GO:1902138]; lignan biosynthetic process [GO:0009807] | null | lariciresinol reductase activity [GO:0010284]; pinoresinol reductase activity [GO:0010283] | PF05368; | 3.40.50.720;3.90.25.10; | NmrA-type oxidoreductase family, Isoflavone reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH; Xref=Rhea:RHEA:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1; Evidence={ECO:0000269|PubMed:18489708}; CATALYTIC ACTIVITY: Reaction=(-)-secoisolariciresinol + NADP(+) = (+)-lariciresinol + H(+) + NADPH; Xref=Rhea:RHEA:34423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65004, ChEBI:CHEBI:67246; EC=1.23.1.2; Evidence={ECO:0000269|PubMed:18489708}; | null | null | null | null | FUNCTION: Reductase involved in lignan (-)-hinokinin biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. Has also a low phenylcoumaran benzylic ether reductase activity. {ECO:0000269|PubMed:18489708}. | Linum corymbulosum (Linum) (Linum strictum subsp. corymbulosum) |
B5L3X1 | WFED_SHIBO | MIDNLIKRTPEINRLLENKRVTGVVTFVNPYSYYKIKEYNKISQLDYIYIDGILLLKLFNFVNGTKIKRHSFDYSSIAKTVFNYSIQNKMKIGLIGSKDYEIEQAVKNIRKKHPGIDISYFHSGYFSSLEEKSSVIDSVIKKSDIIICGLGTPAQEELALDIKIKSNEHLIFTCGGFFTQTASRADFYYPWIKRYNLMWLQRIVLYKHVRKRFFIDYPKFIVRFISENLMKIFTRSN | 2.4.1.304 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21057010}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:21057010}; Name=Pb(2+); Xref=ChEBI:CHEBI:49807; Evidence={ECO:0000269|PubMed:21057010}; Note=Divalent metal cation. Mn(2+), Ni(2+), and Pb(2+) enhance the enzyme activity. {ECO:0000269|PubMed:21057010}; | O antigen biosynthetic process [GO:0009243] | null | beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; hexosyltransferase activity [GO:0016758] | PF03808; | null | Glycosyltransferase 26 family | null | null | CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP; Xref=Rhea:RHEA:36751, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:62959, ChEBI:CHEBI:66914, ChEBI:CHEBI:73984; EC=2.4.1.304; Evidence={ECO:0000269|PubMed:21057010}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:21057010}; KM=0.1 mM for N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol {ECO:0000269|PubMed:21057010}; Vmax=40 umol/h/mg enzyme with UDP-alpha-D-galactose as substrate {ECO:0000269|PubMed:21057010}; Vmax=42 umol/h/mg enzyme with N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol as substrate {ECO:0000269|PubMed:21057010}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. | null | null | FUNCTION: Galactosyltransferase that adds one galactose residue in the beta-1-4 linkage to GlcNAc-alpha-pyrophosphate-lipid in the biosynthesis of the O-polysaccharide repeating unit of the O antigen. {ECO:0000269|PubMed:21057010}. | Shigella boydii |
B5LAT8 | CAD1_CAPAN | MGSLEVEKTAIGWAARDPSGILSPYTYTLRNTGPEDVQVKVLYCGLCHSDLHQVKNDLGMSNYPMVPGHEVVGEVVEVGPEVTKFKVGDTVGVGLIVGCCKNCRPCKQDIEQYCAKKIWNCNDVYTDGKPTQGGFSNFMVVEQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLNHFGFNQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKRQEALDHLGADDYLVSSVNEKMQEAADSLDYIIDTIPVNHPLEPYLSLLKVDGKLILMGVINTPLQFVSPMVMLGRKSITGSFIGSMKETEEVLHFCKEKGVTCQIEMVKMDYINTAMERLEKNDVRYRFVVDVAGSKLDQ | 1.1.1.-; 1.1.1.195 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O49482}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O49482}; | lignin biosynthetic process [GO:0009809] | cytoplasm [GO:0005737] | cinnamyl-alcohol dehydrogenase activity [GO:0045551]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:19553373}. | CATALYTIC ACTIVITY: Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:35858994}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394; Evidence={ECO:0000269|PubMed:35858994}; CATALYTIC ACTIVITY: Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:35858994}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446; Evidence={ECO:0000269|PubMed:35858994}; CATALYTIC ACTIVITY: Reaction=(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45704, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64557; EC=1.1.1.195; Evidence={ECO:0000250|UniProtKB:O49482}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706; Evidence={ECO:0000250|UniProtKB:O49482}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45724, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64555; EC=1.1.1.195; Evidence={ECO:0000250|UniProtKB:O49482}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726; Evidence={ECO:0000250|UniProtKB:O49482}; CATALYTIC ACTIVITY: Reaction=(E)-caffeyl alcohol + NADP(+) = (E)-caffeyl aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45728, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323, ChEBI:CHEBI:31334, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:O49482}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730; Evidence={ECO:0000250|UniProtKB:O49482}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + vanillin = 4-hydroxy-3-methoxy-benzenemethanol + NADP(+); Xref=Rhea:RHEA:76611, ChEBI:CHEBI:15378, ChEBI:CHEBI:18346, ChEBI:CHEBI:18353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:35858994}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76612; Evidence={ECO:0000269|PubMed:35858994}; | null | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:35858994}. | null | null | FUNCTION: Involved in the biosynthesis of capsinoids natural products (e.g. capsiate), non-pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of sweet chili pepper fruit acting as repellant on herbivorous mammals (PubMed:19553373, PubMed:35858994). Catalyzes the reduction of vanillin to generate vanillyl alcohol, a precursor of capsiate, a non-pungent component that accumulates mainly in the placenta of mature red fruits, but also in green fruits to lower levels (PubMed:35858994). Involved in lignin biosynthesis (By similarity). Catalyzes the final step specific for the production of lignin monomers (By similarity). Mediates the conversion of cinnamaldehyde and coniferaldehyde to cinnamyl alcohol and coniferyl alcohol, respectively (PubMed:35858994). Catalyzes the NADPH-dependent reduction of 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols (By similarity). {ECO:0000250|UniProtKB:O49482, ECO:0000269|PubMed:35858994, ECO:0000303|PubMed:19553373, ECO:0000303|PubMed:35858994}. | Capsicum annuum (Capsicum pepper) |
B5LUQ7 | FALX3_LITFA | MASLKKSLFLVLFLGLVSLSICEEKKRENEDDAEDENHEEESEEKRGLLDFAKHVIGIASKLGKRSEEKRYHPFGKRSEEKRYFPIPFGKRSEEKRYFPIPIGKRSEEKRYFPIPIGKKKKKK | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | null | PF03032; | null | Frog skin active peptide (FSAP) family, Brevinin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18803332}. | null | null | null | null | null | FUNCTION: Fallaxidin-1.1 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-1.2 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-1.3 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram-positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram-negative bacteria E.cloacae and E.coli. {ECO:0000269|PubMed:18803332}. | Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax) |
B5LUQ8 | FALX6_LITFA | MASLKKSLFLVLFLGFVSLSICEEEKRENEGNENEEEDENHEEGSEEKRGLLDLAKHVIGIASKLGKRSEEKRYHPFGKRSEEKRYHPFGKRSEEKRYPPIGK | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | null | PF03032; | null | Frog skin active peptide (FSAP) family, Brevinin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18803332}. | null | null | null | null | null | FUNCTION: Fallaxidin-1.3 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-1.4 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-3.1 shows antibacterial activity against the Gram-positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=100 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram-negative bacteria E.cloacae and E.coli. {ECO:0000269|PubMed:18803332}. | Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax) |
B5LUQ9 | FALX7_LITFA | MASLKKSFFLVLFLGLVSLSMCEEKKRENEDDAEDGNHEEESEEKRGLVDFAKHVIGIASKLGKRSEEKRYHPFGKRSEEKRYFPIPFGKRSEEKRYFPIPIGKRSEEKRYFPIPIGKRSEEKRYFPIPIGK | null | null | defense response [GO:0006952] | extracellular region [GO:0005576] | null | PF03032; | null | Frog skin active peptide (FSAP) family, Brevinin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18803332}. | null | null | null | null | null | FUNCTION: Fallaxidin-1.1 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-1.2 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}.; FUNCTION: Fallaxidin-1.3 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. {ECO:0000269|PubMed:18803332}. | Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax) |
B5RHV8 | PHT14_LOTJA | MALEVLEALDSARTQWYHVTAIVIAGMGFFTDAYDLFCITTVSKLLGRLYYFDPSTGKPGKLPNNVNNLVTGVALVGTLSGQLFFGYLGDKLGRKKVYGVTLILMVACAICSGLSFGASAKSVMGTLCFFRFWLGFGIGGDYPLSATIMSEYANKRTRGAFIAAVFAMQGVGIIFAGLVSMCLSAGFKASYHAPSFHDDPIMSTQPQGDLMWRLVLMIGAVPAAMTYYWRMKMPETGRYTAIIEGNAKQAAADMARVLDIEIQAEQDKLAEFKAANDYPLWSNEFFTRHGRHLIGTMTSWFLLDIAFYSQNLTQKDIFPAMGLIDKDFEMNAIQEVFETSRAMFVIALFGTFPGYWFTVFFIEKLGRYKIQLIGFFMMSVFMFIIGVKYDYLRNENSHMFALLYGLTFFFANFGPNSTTFVLPAELFPTRVRSTCHALSAAAGKAGAMVGAFGIQNYTQKGEQKQIKHAMMILAVTNLIGFFCSFLVTETKGRSLEEISGEDGRESELTPTPPNNRVPTRQEPRSETM | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to phosphate starvation [GO:0016036]; detection of phosphate ion [GO:0010247]; lateral root formation [GO:0010311]; phosphate ion transport [GO:0006817]; response to symbiotic fungus [GO:0009610] | periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | inorganic phosphate transmembrane transporter activity [GO:0005315]; symporter activity [GO:0015293] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Phosphate:H(+) symporter (TC 2.A.1.9) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8GSG4}; Multi-pass membrane protein {ECO:0000255}. Note=Present on the periarbuscular membrane in cells containing arbuscules during arbuscular mycorrhizal (AM) symbiosis with AM fungi. {ECO:0000250|UniProtKB:Q8GSG4}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out); Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q8GSG4}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29941; Evidence={ECO:0000250|UniProtKB:Q8GSG4}; | null | null | null | null | FUNCTION: Low-affinity transporter for external inorganic phosphate (Pi) probably involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi (e.g. Gigaspora margarita and Funnelliformis mosseae) during AM symbiosis; required for propper mycorrhizal arbuscule morphology (PubMed:26476189). Acts as a Pi-sensing machinery at the root tip level, independently of AM fungi, involved in the regulation of early root branching and lateral roots formation (PubMed:26476189). {ECO:0000269|PubMed:26476189}. | Lotus japonicus (Lotus corniculatus var. japonicus) |
B5SY89 | PRIO_BOBOX | MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG | null | null | calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; protein destabilization [GO:0031648]; protein homooligomerization [GO:0051260] | cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | amyloid-beta binding [GO:0001540]; cuprous ion binding [GO:1903136]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; molecular condensate scaffold activity [GO:0140693]; protein-containing complex binding [GO:0044877]; type 5 metabotropic glutamate receptor binding [GO:0031802] | PF00377;PF11587; | 1.10.790.10; | Prion family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}. | null | null | null | null | null | FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). {ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}. | Bos indicus x Bos taurus (Hybrid cattle) |
B5T267 | TLR2_BOSIN | MPRALWTAWVWAVIILSTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITYVSNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTEIHEKDFTGLTFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMSTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFQDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKXGELLLTLENLNSLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLXVMRISRNIINTFSKEQLDSFQQLKTLEAGGNNFICSCDFLSFTQGQQALGRVLVDWPDDYHCDSPSHVRGQRVQDARLSLSECHRAAVVSAACCALFLLLLLMGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDICYDAFVSYSERDSYWVENLMVQELEQFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTIFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPVDETQQEGFWLNLRAAIRS | null | null | cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224] | Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670] | NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497] | PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}. | null | null | null | null | null | FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity). {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}. | Bos indicus (Zebu) |
B5TVM2 | ILDR2_MOUSE | MPAFPTLDLDGKLGKMDRVVLGWTAVFWLTAMVEGLQVTVPDKKKVAMLFQPTVLRCHFSTSSHQPAVVQWKFKSYCQDRMGESLGMSSPRAQALSKRNLEWDPYLDCLDSRRTVRVVASKQGSTVTLGDFYRGREITIVHDADLQIGKLMWGDSGLYYCIITTPDDLEGKNEDSVELLVLGRTGLLADLLPSFAVEIMPEWVFVGLVILGIFLFFVLVGICWCQCCPHSCCCYVRCPCCPDSCCCPQALYEAGKAAKAGYPPSVSGVPGPYSIPSVPLGGAPSSGMLMDKPHPPPLAPSDSTGGSHSVRKGYRIQADKERDSMKVLYYVEKELAQFDPARRMRGRYNNTISELSSLHDDDSNFRQSYHQMRNKQFPMSGDLESNPDYWSGVMGGNSGTNRGPALEYNKEDRESFRHSQQRSKSEMLSRKNFATGVPAVSMDELAAFADSYGQRSRRANGNSHEARAGSRFERSESRAHGAFYQDGSLDEYYGRGRSREPPGDGERGWTYSPAPARRRPPEDAPLPRLVSRTPGTAPKYDHSYLSSVLERQARPESSSRGGSLETPSKLGAQLGPRSASYYAWSPPTTYKAGASEGEDEDDAADEDALPPYSELELSRGELSRGPSYRGRDLSFHSNSEKRRKKEPAKKPGDFPTRMSLVV | null | null | cell differentiation [GO:0030154]; homeostasis of number of cells within a tissue [GO:0048873]; insulin secretion [GO:0030073]; negative regulation of T cell activation [GO:0050868]; pancreas development [GO:0031016]; regulation of RNA splicing [GO:0043484]; response to glucose [GO:0009749] | bicellular tight junction [GO:0005923]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleus [GO:0005634]; tight junction [GO:0070160] | null | PF05624; | 2.60.40.10; | Immunoglobulin superfamily, LISCH7 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23826244}; Single-pass type I membrane protein {ECO:0000269|PubMed:23826244}. Cell junction, tight junction {ECO:0000269|PubMed:23239027}. Nucleus {ECO:0000269|PubMed:28785060}. | null | null | null | null | null | FUNCTION: May be involved in ER stress pathways with effects on lipid homeostasis and insulin secretion (PubMed:23826244, PubMed:33863978). With ILDR1 and LSR, involved in the maintain of the epithelial barrier function through the recruitment of MARVELD2/tricellulin to tricellular tight junctions (PubMed:23239027). Also functions as a B7-like protein family member expressed on immune cells and inflamed tissue and with T-cell inhibitory activity (PubMed:29431694). In the inner ear, may regulate alternative pre-mRNA splicing via binding to TRA2A, TRA2B and SRSF1 (PubMed:28785060). {ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:23826244, ECO:0000269|PubMed:28785060, ECO:0000269|PubMed:29431694, ECO:0000269|PubMed:33863978}. | Mus musculus (Mouse) |
B5X0E4 | ABCB5_MOUSE | MANSERTNGLQETNQRYGPLQEQVPKVGNQAVGPIEIFRFADNLDIVLMTLGILASMINGATVPLMSLVLGEISDHLINGCLVQTNRTKYQNCSQTQEKLNEDIIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPGYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNIFQVIDKKPNIDNFSTAGFVPECIEGNIEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQDIKKVDEQMESRTCSTAGNASYGSLCDVNSAKAPCTDQLEEAVHHQKTSLPEVSLLKIFKLSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLVTMFEDKNKATLKQDAELYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDKENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFIVFTAIAYGAMAIGETLVWAPEYSKAKAGASHLFALLKNKPTINSCSQSGEKPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVAAH | 7.6.2.2 | null | cell differentiation [GO:0030154]; eye development [GO:0001654]; regulation of membrane potential [GO:0042391]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886] | ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; efflux transmembrane transporter activity [GO:0015562] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25030174}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:25030174}. | CATALYTIC ACTIVITY: Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+) + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64677, ChEBI:CHEBI:456216; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:Q2M3G0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148; Evidence={ECO:0000250|UniProtKB:Q2M3G0}; | null | null | null | null | FUNCTION: Energy-dependent efflux transporter responsible for decreased drug accumulation in multidrug-resistant cells (By similarity). Specifically present in limbal stem cells, where it plays a key role in corneal development and repair (PubMed:25030174). {ECO:0000250|UniProtKB:Q2M3G0, ECO:0000269|PubMed:25030174}. | Mus musculus (Mouse) |
B5X0I6 | VIP6_ARATH | MASVYIPVQNSEEEVRVVLDQLPRDASDILDILKAEQAPLDLWLIIAREYFKQGKIEQFRQILEEGSSSDIDEYYADVKYERIAILNALGAYYSYLGKTETKNREKEEQFISATRYYNKASRIDMHEPSTWVGKGQLLLAKGEIDNALQAFKIVLDTAPDNVPALLGQASVEFNRGRFSESLQLYKRALQVFPGCPAAVRLGIGLCRYKLGQLDKARQAFDRVLQLDPDNVEALVALGIMDLQANDSIGMRKGMDRMQQAFEIYPYCASALNYLANHFFFTGQHFLVEQLTETALAVTTHGPTKSHSFYNLARSYHSKGDFEKAGMYYMAAIKETNNNPHEFVFPYFGLGQVQLKLGELKGSVFNFEKVLEVYPDNCETLKALGHLYTQLGQNEKALEYMRKATKLDPRDAQAFVGLGELLISSDTGAALDAFKMARTLMKKGGQEVPIEVLNDIGALHFEREEFESALENFKEALGDGIWISFLDEKENLEQTGVSVLGYKDTGIFHRLIESGHSVDVPWNKVTTLFNLARLLEQIHKTEAATFMYRLILFKYPGYIDAYLRLAASAKAQNNLPLAIELVNEALKVDDKNPNALSLLGELELKNDDWVKAKETFRAANDATDGKDSYAILSLGNWNYFAAMRNEKRNPKLEATHLEKAKELYTKVLTQHNSNMYAANGSGIVLAEKGQFDIAKDVFTQVQEAASGSVFLQMPDVWVNLAHVYFAQGNFALTVKMYQNCLRKFFYNTDSQILLYLARTHYEAEQWQECKKTLLRAIHLTPSNYTFRFDLGAVMQKSSSSTLQKKKRTADEVRSTVAEAENAVRVFTQLSAASDLHVHGFDSKKIQTHVQYCSHLLEAAKVHREAAEQEELQNRQRLEVARQAALAEEARRKAEEQRKYQLEKRKQEEELRRLKQEEEKFQRIKEQWKSSTPGSNKRKDRVEDDDGESKPSERRRKKGGKRRKKDKSSRARHYEDDEEEAATMDDHNEVEDEDANTNYNREDEMTTQEAEEPVDDDAHDLLAAAGLEDPDVDDDEVPTSGVRRRRALSSSDEEGELMEESHPNSSPQKEKEESNGEAGDPNMEEEEEEEEAN | null | null | flower development [GO:0009908]; negative regulation of flower development [GO:0009910]; positive regulation of DNA-templated transcription [GO:0045893]; transcription elongation by RNA polymerase II [GO:0006368] | Cdc73/Paf1 complex [GO:0016593]; nucleus [GO:0005634] | RNA polymerase II complex binding [GO:0000993] | PF13432;PF13181; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20363855}. | null | null | null | null | null | FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time. Required for the expression of the MADS box genes and flowering repressors FLC, AGL27/FLM and AGL31/MAF2 (PubMed:15472079, PubMed:15520273). Required for histone H3 trimethylation on 'Lys-4' H3K4me3 at the FLC and AGL27/FLM loci (PubMed:15520273). Involved in the control of seed dormancy and germination (PubMed:21799800). {ECO:0000269|PubMed:15472079, ECO:0000269|PubMed:15520273, ECO:0000269|PubMed:20363855, ECO:0000269|PubMed:21799800}. | Arabidopsis thaliana (Mouse-ear cress) |
B5X3C4 | LIS1B_SALSA | MVLSQRQRDELNRAIADYLRSNGYEEAYSTFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEITLGGPVAQKRDPKEWIPRPPERYALSGHRSPVTRVIFHPVFSVMVTSSEDATIKVWDYEAGDFERTLKGHTDSVQDISFDQTGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVATGYCVKTFTGHREWVRMVRPNQDGSLIASCSNDQTVRVWVATSKECKAELREHEHVVECIAWAPDTAHPTILEATSSESKKNGKSGPFLLSGSRDKTIKMWDISTGMCLMTLVGHDNWVRGVLVHPGGRFIVSCADDKTLRIWDYKNKRCMKTLCAHEHFVTSLDMHQTAPYVVTGSVDQTVKVWECR | null | null | brain morphogenesis [GO:0048854]; cell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; germ cell development [GO:0007281]; microtubule organizing center organization [GO:0031023]; microtubule sliding [GO:0051012]; nuclear migration [GO:0007097]; reelin-mediated signaling pathway [GO:0038026]; retrograde axonal transport [GO:0008090]; vesicle transport along microtubule [GO:0047496] | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635] | dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]; protein heterodimerization activity [GO:0046982] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}. | null | null | null | null | null | FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. May be required for proliferation of neuronal precursors and neuronal migration. {ECO:0000250|UniProtKB:P43033, ECO:0000255|HAMAP-Rule:MF_03141}. | Salmo salar (Atlantic salmon) |
B5X3Z6 | LIS1A_SALSA | MVLSQRQRDELNRAIADYLRSNGYEEAYSTFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEITLGGPIAQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHTGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVATGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVASKECKAELREHEHVVECISWAPESAHPTILEATGSESKKSGKPGPFLLSGSRDKTIKMWDVSIGMCLMTLVGHDNWVRGMLVHPGGKFILSCADDKTLRIWDYKNKRCMKTLGAHEHFVTSLDFHKNAPYVVTGSVDQTVKVWECR | null | null | brain morphogenesis [GO:0048854]; cell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; germ cell development [GO:0007281]; microtubule organizing center organization [GO:0031023]; microtubule sliding [GO:0051012]; nuclear migration [GO:0007097]; reelin-mediated signaling pathway [GO:0038026]; retrograde axonal transport [GO:0008090]; vesicle transport along microtubule [GO:0047496] | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635] | dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]; protein heterodimerization activity [GO:0046982] | PF08513;PF00400; | 1.20.960.30;2.130.10.10; | WD repeat LIS1/nudF family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}. | null | null | null | null | null | FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. May be required for proliferation of neuronal precursors and neuronal migration. {ECO:0000250|UniProtKB:P43033, ECO:0000255|HAMAP-Rule:MF_03141}. | Salmo salar (Atlantic salmon) |
B5X4Z9 | STU_ARATH | MAVDKVIVKQRNIILVGIPIDESGVEVLKWALEEVAKHGDCVVVVHVCFTYYRALKSKSSLDRYLKPYIEFCSTKKIELKGEVLKGNSVLGVLVKEAKRYNAMSVVVGVKQQSKLSLKIAKGCAKELPSTTDILAIHRGNIVFRRSNHYQLPLAQKISSRPSSELSEGFSDKDLAKTTGQEKRKISGRSLSLPSVEVVDQTPGWPLLRTSTLATPMVQHQTRKISVVNWVMSLPERFPHHPNQTCQQSFCDKQLKDILKDINRWFSYDVLKTATSDFSLENLIGKGGCNEVYKGFLEDGKGVAVKILKPSVKEAVKEFVHEVSIVSSLSHSNISPLIGVCVHYNDLISVYNLSSKGSLEETLQGKHVLRWEERLKIAIGLGEALDYLHNQCSNPVIHRDVKSSNVLLSDEFEPQLSDFGLSMWGSKSCRYTIQRDVVGTFGYLAPEYFMYGKVSDKVDVYAFGVVLLELISGRTSISSDSPRGQESLVMWAKPMIEKGNAKELLDPNIAGTFDEDQFHKMVLAATHCLTRAATYRPNIKEILKLLRGEDDVSKWVKIEEDDEDGFDDEVYPNSNTELHLSLAMVDVEDNDSVSNSSLERSNNSLFSSSSSSSQELQS | 2.7.11.- | null | gibberellic acid mediated signaling pathway [GO:0009740]; gibberellin mediated signaling pathway [GO:0010476]; phosphorylation [GO:0016310]; positive regulation of cell division [GO:0051781]; response to gibberellin [GO:0009739] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 3.40.50.620;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22492352}. | null | null | null | null | null | FUNCTION: Promotes cell proliferation in the gibberellic acid (GA) signaling pathway, acting downstream of RGA, and possibly through a negative regulation of two cyclin-dependent kinase inhibitors SIM and SMR1. {ECO:0000269|PubMed:22492352}. | Arabidopsis thaliana (Mouse-ear cress) |
B5X582 | TWIH_ARATH | MRFLLRLPQIHFRKLSCSMSVLMGSKQFLEFCLLPSFASYPSSPSYSSSRQVSSVSRRFRPVLASRPVSKNSPYYQRTNGLSSYNSIPRVPTPVDTEVEADKRVVLSRLVTLRRKLAEQGVDAENCPPGQHSGLICPTCEGGNSGEKSLSLFIAPDGSSATWNCFRGKCGLKGGVRADGGLASADPIEKVERKITVEGIELEPLCDEIQDYFAARAISRKTLERNRVMQKRIGDEIVIAFTYWQRGELVSCKYRSLTKMFFQERKTRRILYGLDDIEKTSEVIIVEGEIDKLAMEEAGFLNCVSVPDGAPAKVSSKEIPSEDKDTKYKFLWNCNDYLKKASRIVIATDGDGPGQAMAEEIARRLGKERCWRVKWPKKSEDEHFKDANEVLMSKGPHLLKEAILDAEPYPILGLFSFKDFFDEIDAYYDRTHGHEYGVSTGWKNLDNLYSVVPGELTVVTGIPNSGKSEWIDAMLCNLNHSVGWKFALCSMENKVRDHARKLLEKHIKKPFFDADYGRSVQRMSVEEKDEGKKWLNDTFYPIRCEMDSLPSIDWVLERAKAAVLRYGIRGLVIDPYNELDHQRTPRQTETEYVSQMLTKIKRFSQHHSCHVWFVAHPKQLQHWDGGAPNLYDISGSAHFINKCDNGIIVHRNRDENAGPLDLVQIGVRKVRNKVAGQIGDAYLCYDRTTGSYSDSPVTPGMPERRSPKRY | 2.7.7.-; 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds two Mg(2+) per subunit. {ECO:0000250}; | mitochondrial DNA replication [GO:0006264]; ribonucleotide biosynthetic process [GO:0009260] | chloroplast [GO:0009507]; mitochondrion [GO:0005739] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; DNA primase activity [GO:0003896]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697] | PF03796;PF13662; | 3.40.1360.10;3.40.50.300; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305|PubMed:23452619}. Mitochondrion {ECO:0000269|PubMed:19036033, ECO:0000305|PubMed:23452619}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:23452619}; | null | null | null | null | FUNCTION: Has both DNA primase and DNA helicase activities and may be involved in organelle DNA replication. Capable of producing RNA primers of 9 to 18 bases from a single-stranded DNA template. {ECO:0000269|PubMed:23452619}. | Arabidopsis thaliana (Mouse-ear cress) |
B5X8M4 | BRCC3_SALSA | MAVSAVHLESDAFLVCMNHALSTEKEEVMGLCIGEVDTNRIVHIHSVIILRRSDKRKDRVEISPEQLSSAATEAERLAEMTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSVQAQKGSEYERIEIPIHVVPHEAIGKVCLESAVELPRILCQEEQDTYRKIHSLTHLDPITKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNRQSVIELQLEKERLTQELATM | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:E2AXC7}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:E2AXC7}; | cell division [GO:0051301]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of DNA repair [GO:0045739]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; response to ionizing radiation [GO:0010212] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the brca1-bard1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the rnf8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of nlrp3. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination. {ECO:0000250|UniProtKB:P46736, ECO:0000250|UniProtKB:P46737}. | Salmo salar (Atlantic salmon) |
B5XK69 | OLHYD_STRPZ | MYYTSGNYEAFATPRKPEGVDQKSAYIVGTGLAGLAAAVFLIRDGHMAGERIHLFEELPLAGGSLDGIEKPHLGFVTRGGREMENHFECMWDMYRSIPSLEIPGASYLDEFYWLDKDDPNSSNCRLIHKRGNRVDDDGQYTLGKQSKELIHLIMKTEESLGDQTIEEFFSEDFFKSNFWVYWATMFAFEKWHSAVEMRRYAMRFIHHIDGLPDFTSLKFNKYNQYDSMVKPIIAYLESHDVDIQFDTKVTDIQVEQTAGKKVAKTIHMTVSGEAKAIELTPDDLVFVTNGSITESSTYGSHHEVAKPTKALGGSWNLWENLAAQSDDFGHPKVFYQDLPAESWFVSATATIKHPAIEPYIERLTHRDLHDGKVNTGGIITITDSNWMMSFAIHRQPHFKEQKENETTVWIYGLYSNSEGNYVHKKIEECTGQEITEEWLYHLGVPVDKIKDLASQEYINTVPVYMPYITSYFMPRVKGDRPKVIPDGSVNLAFIGNFAESPSRDTVFTTEYSIRTAMEAVYSFLNGERGIPQGFNSAYDIRELLKAFYYLNDKKAIKDMDLPIPALIEKIGHKKIKDTFIEELLKDANLM | 4.2.1.53 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20145247}; Note=Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme. {ECO:0000269|PubMed:20145247}; | fatty acid metabolic process [GO:0006631]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; oleate hydratase activity [GO:0050151]; protein homodimerization activity [GO:0042803] | PF06100; | 3.50.50.60; | Oleate hydratase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O; Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683, ChEBI:CHEBI:30823; EC=4.2.1.53; Evidence={ECO:0000305|PubMed:20145247}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21854; Evidence={ECO:0000305|PubMed:20145247}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + H2O = 10-hydroxyoctadecanoate; Xref=Rhea:RHEA:75751, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:143089; Evidence={ECO:0000269|PubMed:20145247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75752; Evidence={ECO:0000305|PubMed:20145247}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoate + H2O = 10-hydroxyhexadecanoate; Xref=Rhea:RHEA:75767, ChEBI:CHEBI:15377, ChEBI:CHEBI:32372, ChEBI:CHEBI:194446; Evidence={ECO:0000269|PubMed:20145247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75768; Evidence={ECO:0000305|PubMed:20145247}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + H2O = (12Z)-10-hydroxyoctadecenoate; Xref=Rhea:RHEA:76599, ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:195300; Evidence={ECO:0000269|PubMed:20145247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76600; Evidence={ECO:0000305|PubMed:20145247}; CATALYTIC ACTIVITY: Reaction=(12Z)-10-hydroxyoctadecenoate + H2O = 10,13-dihydroxyoctadecanoate; Xref=Rhea:RHEA:76603, ChEBI:CHEBI:15377, ChEBI:CHEBI:195300, ChEBI:CHEBI:195301; Evidence={ECO:0000269|PubMed:20145247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76604; Evidence={ECO:0000305|PubMed:20145247}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + H2O = (12Z,15Z)-10-hydroxyoctadecadienoate; Xref=Rhea:RHEA:76607, ChEBI:CHEBI:15377, ChEBI:CHEBI:32387, ChEBI:CHEBI:195302; Evidence={ECO:0000269|PubMed:20145247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76608; Evidence={ECO:0000305|PubMed:20145247}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for oleate {ECO:0000269|PubMed:20145247}; KM=49 uM for linoleate {ECO:0000269|PubMed:20145247}; Note=kcat is 67 min(-1) and 101 min(-1) with oleate and linoleate as substrate, respectively.; | PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, probably in the (R) configuration, and of linoleate at its cis-9- and cis-12-double bond to yield 10-hydroxy-12-octadecenoate and 10,13-dihydroxyoctadecanoate. Is not active on trans-double bonds and esterified fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of C16 and C18 fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy derivatives. Appears to play a role in oleic acid detoxification and bacterial virulence. {ECO:0000269|PubMed:20145247}. | Streptococcus pyogenes serotype M49 (strain NZ131) |
B5XRB0 | FRD_KLEP3 | MTSNERILQPFTLPNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGLAKIAEAIKAQGSKAILQIYHGGRMVDPQLIGGRQPVAPSAIAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDITHKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTSDPTPLIEKYCAMRSETLAQVPVMGVGGVVNVADAELGLDHGYDLIAVGRACIAYPDWAARIAAGEELELFIDSTQREALHIPEPLWRFSLVEAMIRDMSMGDAKFKPGMFVETVQDDANELVINVSLENDHIADIELAASPVQTVEFTTSFEEIRERILTANTPHVDAISGATSQSEAVKKAVAKAMLKSSKALAAEEGGNDAAPKSYDVVVVGSGGAGLAAAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSIDRTHRPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMSGDEVSGVRLVNDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPDLDGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVDQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG | 1.3.1.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24361839}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:24361839}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:24361839}; Note=Binds 2 FMN prosthetic groups per subunit. 1 FMN is bound covalently, while the other is non-covalent. {ECO:0000269|PubMed:24361839}; | steroid metabolic process [GO:0008202] | cytoplasm [GO:0005737]; membrane [GO:0016020] | FMN binding [GO:0010181]; fumarate reductase (NADH) activity [GO:0016156] | PF00890;PF04205;PF00724; | 3.90.1010.20;3.20.20.70;3.50.50.60;3.90.700.10; | FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily | PTM: Is flavinylated on Thr-447 by ApbE2, encoded in a neighboring gene (PubMed:24361839). Flavinylation is essential for catalytic activity (PubMed:31834358). {ECO:0000269|PubMed:24361839, ECO:0000269|PubMed:31834358}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24361839}. | CATALYTIC ACTIVITY: Reaction=NAD(+) + succinate = fumarate + H(+) + NADH; Xref=Rhea:RHEA:18281, ChEBI:CHEBI:15378, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.6; Evidence={ECO:0000269|PubMed:33107907}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18283; Evidence={ECO:0000305|PubMed:33107907}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for NADH {ECO:0000269|PubMed:33107907}; Note=kcat is about 10 sec(-1). {ECO:0000269|PubMed:33107907}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:33107907}; | null | FUNCTION: Catalyzes the anaerobic reduction of fumarate to succinate (PubMed:24361839, PubMed:33107907). Uses NADH as the inherent electron donor in this process (PubMed:33107907). Is involved in anaerobic fumarate respiration in K.pneumoniae (PubMed:33107907). {ECO:0000269|PubMed:24361839, ECO:0000269|PubMed:33107907}. | Klebsiella pneumoniae (strain 342) |
B5YSJ3 | HCHA_ECO5E | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPQKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli O157:H7 (strain EC4115 / EHEC) |
B5ZZ34 | ARAD_RHILW | MKKKAEWPRKLRSQEWYGGTSRDVIYHRGWLKNQGYPHDLFDGRPVIGILNTWSDMTPCNGHLRELAEKVKAGVWEAGGFPLEVPVFSASENTFRPTAMMYRNLAALAVEEAIRGQPMDGCVLLVGCDKTTPSLLMGAASCDLPSIVVTGGPMLNGYFRGERVGSGTHLWKFSEMVKAGEMTQAEFLEAEASMSRSSGTCNTMGTASTMASMAEALGMALSGNAAIPGVDSRRKVMAQLTGRRIVQMVKDDLKPSEIMTKQAFENAIRTNAAIGGSTNAVIHLLAIAGRVGIDLSLDDWDRCGRDVPTIVNLMPSGKYLMEEFFYAGGLPVVLKRLGEAGLLHKDALTVSGETVWDEVKDVVNWNEDVILPAEKALTSSGGIVVLRGNLAPKGAVLKPSAASPHLLVHKGRAVVFEDIDDYKAKINDDNLDIDENCIMVMKNCGPKGYPGMAEVGNMGLPPKVLKKGILDMVRISDARMSGTAYGTVVLHTSPEAAVGGPLAVVKNGDMIELDVPNRRLHLDISDEELARRLAEWQPNHDLPTSGYAFLHQQHVEGADTGADLDFLKGCRGNAVGKDSH | 4.2.1.25; 4.2.1.6; 4.2.1.67 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:28574691, ECO:0000305|PubMed:27102126}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27102126, ECO:0000269|PubMed:28574691}; | arabinose catabolic process [GO:0019568] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; D-fuconate dehydratase activity [GO:0047818]; galactonate dehydratase activity [GO:0008869]; L-arabinonate dehydratase activity [GO:0050020]; metal ion binding [GO:0046872] | PF00920; | 3.50.30.80; | IlvD/Edd family | null | null | CATALYTIC ACTIVITY: Reaction=L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H2O; Xref=Rhea:RHEA:20968, ChEBI:CHEBI:15377, ChEBI:CHEBI:16501, ChEBI:CHEBI:35173; EC=4.2.1.25; Evidence={ECO:0000269|PubMed:27102126}; CATALYTIC ACTIVITY: Reaction=D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O; Xref=Rhea:RHEA:18649, ChEBI:CHEBI:12931, ChEBI:CHEBI:15377, ChEBI:CHEBI:57989; EC=4.2.1.6; Evidence={ECO:0000269|PubMed:27102126}; CATALYTIC ACTIVITY: Reaction=D-fuconate = 2-dehydro-3-deoxy-D-fuconate + H2O; Xref=Rhea:RHEA:12949, ChEBI:CHEBI:15377, ChEBI:CHEBI:35372, ChEBI:CHEBI:58378; EC=4.2.1.67; Evidence={ECO:0000269|PubMed:27102126}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for L-arabinonate {ECO:0000269|PubMed:27102126}; KM=3.8 mM for D-galactonate {ECO:0000269|PubMed:27102126}; KM=1.8 mM for D-fuconate {ECO:0000269|PubMed:27102126}; KM=9.2 mM for D-xylonate {ECO:0000269|PubMed:27102126}; KM=11.9 mM for D-gluconate {ECO:0000269|PubMed:27102126}; Note=kcat is 728 min(-1) with L-arabinonate as substrate. kcat is 1377 min(-1) with D-galactonate as substrate. kcat is 2949 min(-1) with D-fuconate as substrate. kcat is 349 min(-1) with D-xylonate as substrate. kcat is 431 min(-1) with D-gluconate as substrate. {ECO:0000269|PubMed:27102126}; | PATHWAY: Carbohydrate metabolism. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:27102126}; | null | FUNCTION: Catalyzes the dehydration of L-arabinonate to 2-dehydro-3-deoxy-L-arabinonate during L-arabinose degradation. Can also dehydrate D-galactonate and D-fuconate with good catalytic efficiency. Has weak activity with D-xylonate and D-gluconate. {ECO:0000269|PubMed:27102126}. | Rhizobium leguminosarum bv. trifolii (strain WSM2304) |
B6A7Q3 | CDK14_RABIT | MCDLIEPQPAEKIGKMKKLRRTLSESFSRIVLNVISFVFQICVTKMSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPTNQVKRVHSENNACINFKSSSAGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSSKNLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPESGESMRAFGKNSSYGKSLSNSKH | 2.7.11.22 | null | cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; phosphorylation [GO:0016310]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055] | cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity). {ECO:0000250}. | Oryctolagus cuniculus (Rabbit) |
B6A876 | CHI1_YERET | MEKEEKSNLIYDKDPGYVWDNKNECEGAAEETYQELNYEPSISADKLTWTPTRLAKTVFNTYEDDDDFNVLCYFTDWSQYDPRIINKEIRDTGGRSADILRLNTPDGRPFKRLIYSFGGLIGDKKYSADGNASIAVRLGVATDPDDAIANHKGKTIPVDPDGAVLASINCGFTKWEAGDANERYNQEKAKGLLGGFRLLHEADKELEFSLSIGGWSMSGLFSEIAKDEILRTNFVEGIKDFFQRFPMFSHLDIDWEYPGSIGAGNPNSPDDGANFAILIQQITDAKISNLKGISIASSADPAKIDAANIPALMDAGVTGINLMTYDFFTLGDGKLSHHTNIYRDPSDVYSKYSIDDAVTHLIDEKKVDPKAIFIGYAGYTRNAKNATITTSIPSEEALKGTYTDANQTLGSFEYSVLEWTDIICHYMDFEKGEGRNGYKLVHDKVAKADYLYSEATKVFISLDTPRSVRDKGRYVKDKGLGGLFIWSGDQDNGILTNAAHEGLKRRIKNKVIDMTPFYLDSDEELPTYTEPAEPQCEACNIK | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00704; | 3.10.50.10;3.20.20.80; | Glycosyl hydrolase 18 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21278295}. Note=Secreted when grown at 25 degrees Celsius or less, but not when grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000305|PubMed:22108167}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=580 uM for 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside {ECO:0000269|PubMed:22108167}; Note=In the intact toxin complex the combined chitinase activity of Chi1 and Chi2 is slightly reduced. {ECO:0000269|PubMed:22108167}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0, in the intact toxin complex optimum pH is pH 4.0 to pH 8.0. {ECO:0000269|PubMed:22108167}; | null | FUNCTION: Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295). The TC has an endochitinase activity (Probable) (PubMed:21278295, PubMed:22158901). This subunit might aid infection by degradation of the larval peritrophic membrane (Probable). {ECO:0000269|PubMed:21278295, ECO:0000269|PubMed:22158901, ECO:0000305|PubMed:22108167}. | Yersinia entomophaga |
B6A879 | CHI2_YERET | MVNKYTYTSSKAMSDISDVIGEPLAAWDSQVGGRVFNVIFDGKVYTNTYWVERWQVPGIGSSDGNPHNAWKFVRAATADEINKIGNPTTADVKPTENIPSPILVEDKYTEETYSRPDVNFKEDGSQGNLSYTATRVCAPMYNHYVGDKTKPKLSAYITDWCQYDARLDGGGSKEEERGRGFDLATLMQNPATYDRLIFSFLGICGDIGNKSKKVQEVWDGWNAQAPSLGLPQIGKGHIVPLDPYGDLGTARNVGLPPESADTSIESGTFLPYYQQNRAAGLLGGLRELQKKAHAMGHKLDLAFSIGGWSLSSYFSALAENPDERRVFVASVVDFFVRFPMFSCVDIDWEYPGGGGDEGNISSDKDGENYVLLIKELRSALDSRFGYSNRKEISIACSGVKAKLKKSNIDQLVANGLDNIYLMSYDFFGTIWADYIGHHTNLYSPKDPGEQELFDLSAEAAIDYLHNELGIPMEKIHLGYANYGRSAVGGDLTTRQYTKNGPALGTMENGAPEFFDIVKNYMDAEHSLSMGKNGFVLMTDTNADADFLFSEAKGHFISLDTPRTVKQKGEYAAKNKLGGVFSWSGDQDCGLLANAAREGLGYVADSNQETIDMGPLYNPGKEIYLKSISEIKSK | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00704; | 3.10.50.10;3.20.20.80; | Glycosyl hydrolase 18 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21278295}. Note=Secreted when grown at 25 degrees Celsius or less, but not when grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000305|PubMed:22108167}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=230 uM for 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside {ECO:0000269|PubMed:22108167}; Note=In the intact toxin complex the combined chitinase activity of Chi1 and Chi2 is slightly reduced. {ECO:0000269|PubMed:22108167}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0, in the intact toxin complex optimum pH is pH 4.0 to pH 8.0. {ECO:0000269|PubMed:22108167}; | null | FUNCTION: Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295). The TC has an endochitinase activity (Probable) (PubMed:21278295, PubMed:22158901). This subunit might aid infection by degradation of the larval peritrophic membrane (Probable). {ECO:0000269|PubMed:21278295, ECO:0000269|PubMed:22158901, ECO:0000305|PubMed:22108167}. | Yersinia entomophaga |
B6A8C7 | TARM1_HUMAN | MIPKLLSLLCFRLCVGQGDTRGDGSLPKPSLSAWPSSVVPANSNVTLRCWTPARGVSFVLRKGGIILESPKPLDSTEGAAEFHLNNLKVRNAGEYTCEYYRKASPHILSQHSDVLLLLVTGHLSKPFLRTYQRGTVTAGGRVTLQCQKRDQLFVPIMFALLKAGTPSPIQLQSPAGKEIDFSLVDVTAGDAGNYSCMYYQTKSPFWASEPSDQLEILVTVPPGTTSSNYSLGNFVRLGLAAVIVVIMGAFLVEAWYSRNVSPGESEAFKPE | null | null | adaptive immune response [GO:0002250]; innate immune response [GO:0045087]; negative regulation of CD4-positive, alpha-beta T cell activation [GO:2000515] | plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821] | immunoglobulin receptor binding [GO:0034987] | PF13895; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:26311901}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26311901}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May act as receptor (By similarity). Negatively regulates TCR-mediated CD4(+) T cell proliferation and activation, possibly by binding an unknown ligand on the T cell surface (PubMed:26311901). Enhances Toll-like receptor-mediated production of pro-inflammatory cytokines by macrophages and neutrophils (By similarity). {ECO:0000250|UniProtKB:B6A8R8, ECO:0000269|PubMed:26311901}. | Homo sapiens (Human) |
B6BQB2 | TMM_PELS7 | MSKVAIIGAGPCGLSILRAFEHLEKKGEKIPEIVCFEKQESWGGLWNYNWRTGSDQYGDPVPNSMYRYLWSNGPKECLEFADYSFDQHFGKSIPSFPPREVLQDYILGRVSKGNIKNKIKFNTRVINTVYRNDKFEINYQDKVNDKTLSDTFDYLVVSTGHFSVPFIPEYEGMSSFPGRIMHSHDFRDAEEFRGKNVIVLGSSYSAEDVALQCNKYGAKSVTIGYRHNPMGFKWPKGMKEVHYLDKLDGKKAIFKDGTEQDADVVILCTGYLHHFPFLDESLKLKTHNRLYPPKLYKGVVWQDNHKLLYLGMQDQFHTFNMFDCQAWFARDVIMDKIKMPSDDEIDKDINKWVSMEEKLENPDQMIDFQTEYTKELHNISDYPKIDFELIRKHFKEWEHHKVEDILTYRNKSFSSPVTGSVAPVHHTPWEKAMDDSMKTFLNKR | 1.14.13.148 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:34630359}; | null | null | flavin adenine dinucleotide binding [GO:0050660]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FMO family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + O2 + trimethylamine = H2O + NADP(+) + trimethylamine N-oxide; Xref=Rhea:RHEA:31979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15724, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58389; EC=1.14.13.148; Evidence={ECO:0000269|PubMed:22006322, ECO:0000269|PubMed:34630359}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.5 uM for TMA {ECO:0000269|PubMed:22006322}; KM=139 uM for TMA {ECO:0000269|PubMed:34630359}; KM=306.1 uM for DMA {ECO:0000269|PubMed:22006322}; KM=181.4 uM for DMA {ECO:0000269|PubMed:34630359}; KM=26.4 uM for DMS {ECO:0000269|PubMed:22006322}; KM=250.5 uM for DMS {ECO:0000269|PubMed:34630359}; KM=7456 uM for DMSO {ECO:0000269|PubMed:22006322}; KM=116.2 uM for methimazole {ECO:0000269|PubMed:34630359}; KM=12.8 uM for NADPH {ECO:0000269|PubMed:34630359}; Vmax=67.3 nmol/min/mg enzyme with TMA as substrate {ECO:0000269|PubMed:22006322}; Vmax=41.4 nmol/min/mg enzyme with DMA as substrate {ECO:0000269|PubMed:22006322}; Vmax=97.2 nmol/min/mg enzyme with DMS as substrate {ECO:0000269|PubMed:22006322}; Vmax=41.3 nmol/min/mg enzyme with DMSO as substrate {ECO:0000269|PubMed:22006322}; Note=kcat is 22.4 min(-1) with TMA as substrate. kcat is 17.9 min(-1) with DMA as substrate. kcat is 4.5 min(-1) with DMS as substrate. kcat is 5.2 min(-1) with methimazole as substrate. {ECO:0000269|PubMed:34630359}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 with DMS as substrate. {ECO:0000269|PubMed:34630359}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius with DMS as substrate. {ECO:0000269|PubMed:34630359}; | FUNCTION: Catalyzes the oxidation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) (PubMed:22006322, PubMed:34630359). In vitro, has a broad substrate specificity, oxidizing many nitrogen- and sulfur-containing compounds, including dimethylamine (DMA), dimethylsulfide (DMS), dimethylsulfoxide (DMSO) and methimazole (PubMed:22006322, PubMed:34630359). TMA shows the highest affinity (PubMed:34630359). {ECO:0000269|PubMed:22006322, ECO:0000269|PubMed:34630359}. | Pelagibacter sp. (strain HTCC7211) |
B6CHA3 | UHRF1_XENLA | MWIQVRTMDGRDTRRIDSLSKLTKVDDLRDRIQQLFGVALESQRLFYRGKQMENGHTLFDYSVGLNDIVQLLVRQIPDSFPTKHKECELSDASAGCGSGQRDSDSGSGEGAMDVDGQSISIIGENVGTSLYKKNDLVDARDLNMGAWFEAQIVNVSKKVGPYGTLPEVSDTSVTSDAIIYHVKYEDYPENGVVQLTCKDVRLRARTTLPWHEIKVGQVVMVNYNPDEPKERGYWYDAEILRKHESKKIKEIYAKVLLGDAGDSLNDCRIRFVNEIYKIEEPGSTYLNTESPQKRQNGPECKHCKDNPKRACRMCACCICGGKQDPEKQLLCDECDLAFHIYCLKPPLSVIPQDEDWYCPDCRNDASEVVLAGEKLKESKKKARMASANSSSQRDWGKGMACVGRSRECTIVPSNHYGPIPGVPVGTLWKFRVQVSESGVHRPHVAGIHGRSNDGSYSLVLAGGYEDDVDNGNEFTYTGSGGRDLSGNKRTAEQSCDQKLSNMNRALALNCSAPINDKEGSIAKDWRAGKPVRVVRNSKGRKHSKYAPEEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDYEPAPWSKEGKERIKKLGLTMQYPDGYLETLASKEREKENKTEDEPIDSPSKGKRKRNSDNEQTAAKSIPKKMKVASYKLTLEQKTLIKQDVLNAKLWSEVMLFLKEGPKFVNKVEETFLCICCQEVVYEPVTTECHHNICKGCLDRSFKALVHSCPACRHDLGKNYPLNVNKPLQAILSQLFPGYESGR | 2.3.2.27 | null | cell cycle [GO:0007049]; heterochromatin formation [GO:0031507]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | chromatin [GO:0000785]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; replication fork [GO:0005657] | hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00628;PF02182;PF12148;PF00240; | 2.30.30.1150;2.30.30.140;2.30.280.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits dnmt1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins. However, it is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. | Xenopus laevis (African clawed frog) |
B6CJY4 | TRAF6_CERAT | MSLLNCENSCGSSQSESDCCVAMASSCSAATKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALVDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAALVAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSLIPDSGYVSEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSTYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPDLLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDSGV | 2.3.2.27 | null | DNA damage response [GO:0006974]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | cell cortex [GO:0005938]; lipid droplet [GO:0005811]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF21355;PF18048;PF13923;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated on Lys-124 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated on Lys-124; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. LRRC19 induces 'Lys-63' ubiquitination (By similarity). Ubiquitinated at Lys-319 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250|UniProtKB:P70196}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN (By similarity). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (By similarity). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys) |
B6CJY5 | TRAF6_MACMU | MSLLNCENSCGSSQSESDCCVAMASSCSAATKDDSVGGTASTGNLSSSFMEDIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALVDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAALVAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSLIPDSGYVSEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSTYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPDLLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDSGV | 2.3.2.27 | null | DNA damage response [GO:0006974]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF21355;PF18048;PF13923;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated on Lys-124 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. LRRC19 induces 'Lys-63' ubiquitination (By similarity). Ubiquitinated at Lys-319 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250|UniProtKB:P70196}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN (By similarity). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (By similarity). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT (By similarity). {ECO:0000250|UniProtKB:P70196, ECO:0000250|UniProtKB:Q9Y4K3}. | Macaca mulatta (Rhesus macaque) |
B6CQR5 | PA2A2_MACLB | MRTLWIVAVWLTGVEGDLSQFGDMINKKTGTFGLFSYIYYGCYCGWGGKGKPQDATDRCCFVHDCCYGSVNGCDPKLSTYSYSFQNGDIVCGDDDPCLRAVCECDRVAAICSGENMNTYDKKYMLYSLFDCKEESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=882 umol/min/mg enzyme {ECO:0000269|PubMed:19467252}; | null | null | null | FUNCTION: Snake venom phospholipase that inhibits ADP- and collagen-induced human platelet aggregation. This inhibition is completely inhibited by abolition of catalytic activity in case of collagen as inducer and partially inhibited in case of ADP as inducer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:19467252}. | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
B6CVD7 | ERO1A_PIG | MGHRWGFLIVFLGAVGLLGSGYGRQQPSETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDINQCGRRDCAVKPCQSDEIPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPDAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGKSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVVPFFERPDFQLFTGNKVQDAENKMLLLDILHEIKSFPLHFDENSFFAGDKKEANKLKEDFRLHFRNISRIMDCVGCLKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH | 1.8.4.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q96HE7}; | cell redox homeostasis [GO:0045454]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; release of sequestered calcium ion into cytosol [GO:0051209]; response to endoplasmic reticulum stress [GO:0034976] | dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; protein-disulfide reductase activity [GO:0015035]; thiol oxidase activity [GO:0016972] | PF04137; | null | EROs family | PTM: The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on Ser-145 by FAM20C in the Golgi which increases its enzymatic activity (By similarity). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (By similarity). {ECO:0000250|UniProtKB:Q8R180, ECO:0000250|UniProtKB:Q96HE7}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q96HE7}. Secreted {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000250|UniProtKB:Q96HE7}. | null | null | null | null | null | FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000250|UniProtKB:Q96HE7}. | Sus scrofa (Pig) |
B6CZ18 | GRK7B_XENLA | MCDMGGLDNLIANTAYLQARKSSEGDAKELQKRRKSLSLPPPDVSRNEVKETITLDYQSICVEQPIGQRLFKDFLATVPEYKLAEDFLEEVKEWELEEGSAKEQLMEKLVSRRFKEPAEGSLNFLGKDLSSRIQQAQSKDMPELILLAKDSGNAFLMDAPFQDFQNSPFYDRFLQWKAFERQPINQKYFYEFRILGKGGFGEVCAIQVKNTGQMYACKKLDKKRLKKKNGEKMALLEKEILEKVHSPFIVSLAYAYETKTHLCLVMSLMNGGDLKFHIYNVGDKGVEIKRVIFYSAQICCGILHLHSLKIVYRDMKPENVLLDDHGNCRLSDLGLAVKVKEGKAITQRAGTNGYMAPEILTDEDYSYPVDWFAMGCSIFEMIAAYTPFRDPKEKTSKEELKRKTLEDEVVFPLPTFTEEAKDICRLFLAKKPQNRLGSRTNDDDPRKHAFFKSINFQRLEAGMVDPPFVPDPSVVYAKDISDIADFSEVKGIEFDDKDAKLFKRFSTGAVPISWQKEIIDTGLFDELNDPSREVTGGGNSGEKSGVCSIL | 2.7.11.14 | null | phosphorylation [GO:0016310]; regulation of signal transduction [GO:0009966]; signal transduction [GO:0007165]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; membrane [GO:0016020] | ATP binding [GO:0005524]; rhodopsin kinase activity [GO:0050254] | PF00069;PF00615; | 1.10.167.10;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily | PTM: Autophosphorylated in vitro at Ser-487 (By similarity). Phosphorylation at Ser-36 is regulated by light and activated by cAMP. {ECO:0000250, ECO:0000269|PubMed:18803695}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-anchor {ECO:0000250|UniProtKB:Q8WMV0}. | CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596, Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.14; Evidence={ECO:0000250|UniProtKB:Q8WTQ7}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-[rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14; Evidence={ECO:0000250|UniProtKB:Q8WTQ7}; | null | null | null | null | FUNCTION: Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO). {ECO:0000250|UniProtKB:Q8WTQ7}. | Xenopus laevis (African clawed frog) |
B6D434 | CAMP_BUNFA | MEGFFWKTLLVVGALAIAGTSSLPHKPLIYEEAVDLAVSIYNSKSGEDSLYRLLEAVSPPKWDPLSESNQELNFTMKETVCLVAEERSLEECDFQEDGVVMGCTGYYFFGESPPVVVLTCKPVGEEGEQKQEEGNEEEKEVEEEEQEEDEKDQPRRVKRFKKFFRKLKKSVKKRAKEFFKKPRVIGVSIPF | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular space [GO:0005615]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | lipopolysaccharide binding [GO:0001530] | PF00666; | 3.10.450.10; | Cathelicidin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18795096}. Target cell membrane {ECO:0000269|PubMed:18795096}. Note=Forms a helical membrane channel in the prey. | null | null | null | null | null | FUNCTION: Potent antimicrobial peptide against most of Gram-negative bacteria, some Gram-positive bacteria (Bacillus) and some fungi (C.albicans, P.pastoris, A.terreus, A.nidulans, and C.globosum). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells. {ECO:0000269|PubMed:18795096}. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
B6DMK2 | MER3_ORYSJ | MAAMGHLGDPYALRSVADLPPPFRSVFGFRYFNSLQSECFPACFLSDVNMVISAPTGSGKTVLFELCILRLLSRFLSSEWRFNLIKGTLKTIYIAPMKALVQEKLRDWNMKLGSLGISCLEMTGDNEFYNTKSIHDADLILTTPEKFDSVSRHGIRDGGLGFFSDIALVLIDEVHLLNDPRGAALEAIVSRIKMLSRLGTMKIAPLANVRFIAVSATIPNIEDIAEWLAVPSEGIKRFGEEMRPVKLTTKVFGYAPARNDFLFERRLQSFIFDILMQHSRGKSALVFCSTRKGAQEAAQCLSQTASSLGYSNPFMKSMQQYEHLKEAALTCSDKQLQACLVHGVGYHNGGLCLKDRSVVEGLFLKGDIQILCTTNTLAHGINLPAHTVVIKSTQFFNKEKGLYVEYERSMVLQMCGRAGRPPFDDTGTIIIMTRRETVHLYENLLNGCEMVESQLLPCAVEHLNAEIVQLTVSDITLAIEWLKCSYLYIRIKKNPQHYGIKKEIPRELLEKQMKDICVEKIHELGEYGLIWTDEDGFLLKPLEPGRLMTKFYLKFDTMKLIVKASACCTLEDLLHIICHSAEITWIQLRRNEKKLLNEINADKEGRLWFHVVGANGKRKKRIQTREEKIFILANDCLTGDPLVHDLSLNQEMNSICSNGCRVAKCMREYFIYKKNYKSAISSMLLAKCLHQKLWESSPFLLKQLPGIGIVTAKALKTAGIDSFESLATADARKIESVTGRNYPFGDSIKSYLPSLGPKIDINIEDAGNRQGKSTIIVTLTRLSQAVGSSKQNYADMVVGSEEDNAILFHEKIKTQEFSSPYSVKLYVPCPPNARATLKVDVIFEEYVGLDIHKKHVVSREDFHVTKVFGIKKAEPLYNLPAESCLVSSKTTRTNQSKYHNGQNPLSKEVCVIEDDFRAKAPDKDDNDLEILGTREYNNLASLEAPSFTLLHEEDYEDVPDVLASEPVEAECKSATNNTIFDHIRKKSRDFPNLMLSKSMDSSYEPLILKKMKTSGDQFGLDQSSLHAYEVTPMVFDRTEARVSPNNTDERCRNILTRTAETRSFQFTGKMDSISQKSEILNRTQGKNSTQLAGKKAFEKSKTPDENSLHFVGKRDSSSEKSKALSKTPDENSLQFLGKMDSSSEKSKFCFSSPLADFQPMQCTKQVAASVQPLTIQDYCKDILASAKSSGTGASFLDVKSVFSFL | 3.6.4.12 | null | reciprocal meiotic recombination [GO:0007131]; resolution of meiotic recombination intermediates [GO:0000712] | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678] | PF00270;PF00271;PF14520;PF02889; | 1.10.150.20;3.40.50.300;1.10.3380.10;1.10.10.10; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22393242}. Chromosome {ECO:0000269|PubMed:22393242}. Note=Detected in punctuate foci onto the chromosomes in prophase I meiocytes. {ECO:0000269|PubMed:22393242}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: DNA helicase required for crossover formation, complete synapsis of homologous chromosomes and bivalent formation during meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover) (PubMed:19417775, PubMed:19470578). Works cooperatively with ZIP4 to promote crossovers (PubMed:22393242). {ECO:0000269|PubMed:19417775, ECO:0000269|PubMed:19470578, ECO:0000269|PubMed:22393242}. | Oryza sativa subsp. japonica (Rice) |
B6E2X2 | MCAL_RHOCA | MSFRTQPPAPARLNRCQLFGPGSRPAIFEKMAQSAADVINLDLEDSVAPDDKPQARRNIIEASHNIDWGNKYLSVRINGLDTPFWYRDVVELLEDGSERIDQIMIPKVGCAADVYAVDALVTAIEAAKGRKKRISLEVIIESAAGIAHVEEIAAASPRLQAMSLGAADFAASMGMATTGIGGTQENYYMLHAGVKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQALRSATLGMVGKWAIHPKQVALANEVFTPSDAAVAEAREILAAMEKAKAEGAGATVYKGRLVDIASIRQAEVIVRQAEMAKV | 4.1.3.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15687206}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15687206}; Note=Divalent cations such as magnesium or manganese. {ECO:0000269|PubMed:15687206}; | oxaloacetate metabolic process [GO:0006107] | null | L-erythro-3-methylmalyl-CoA lyase activity [GO:0043959]; magnesium ion binding [GO:0000287]; malyl-CoA lyase activity [GO:0050083]; metal ion binding [GO:0046872] | PF03328; | 3.20.20.60; | HpcH/HpaI aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malyl-CoA = acetyl-CoA + glyoxylate; Xref=Rhea:RHEA:16629, ChEBI:CHEBI:36655, ChEBI:CHEBI:57288, ChEBI:CHEBI:57317; EC=4.1.3.24; Evidence={ECO:0000269|PubMed:15687206}; CATALYTIC ACTIVITY: Reaction=(2R,3S)-beta-methylmalyl-CoA = glyoxylate + propanoyl-CoA; Xref=Rhea:RHEA:38259, ChEBI:CHEBI:36655, ChEBI:CHEBI:57392, ChEBI:CHEBI:75634; EC=4.1.3.24; Evidence={ECO:0000269|PubMed:15687206}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for L-malyl-CoA {ECO:0000269|PubMed:15687206}; KM=21 uM for beta-methylmalyl-CoA {ECO:0000269|PubMed:15687206}; KM=0.14 mM for acetyl-CoA {ECO:0000269|PubMed:15687206}; KM=1.2 mM for glyoxylate {ECO:0000269|PubMed:15687206}; | null | null | null | FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA. {ECO:0000269|PubMed:15687206}. | Rhodobacter capsulatus (Rhodopseudomonas capsulata) |
B6ECN9 | AADH2_SOLLC | MAIPNIRIPCRQLFIDGEWREPLKKNRLPIINPANEEIIGYIPAATEEDVDMAVKAARSALRRDDWGSTTGAQRAKYLRAIAAKVLEKKPELATLETIDNGKPWFEAASDIDDVVACFEYYADLAEALDSKKQTEVKLHLDSFKTHVLREPLGVVGLITPWNYPLLMTTWKVAPALAAGCAAILKPSELASITSLELGEICREVGLPPGALSILTGLGHEAGSPLVSHPDVDKIAFTGSGPTGVKIMTAAAQLVKPVTLELGGKSPIVVFDDIHNLDTAVEWTLFGCFWTNGQICSATSRLIIQETIAPQFLARLLEWTKNIKISDPLEEDCKLGPVISRGQYEKILKFISTAKDEGATILYGGDRPEHLKKGYYIQPTIITDVDTSMEIWKEEVFGPVLCVKTFKIEEEAIELANDTKFGLGAAILSKDLERCERFTKAFQSGIVWINCSQPCFWQPPWGGKKRSGFGRELGEWSLENYLNIKQVTQYVTPDEPWAFYKSPSKL | 1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.54 | null | cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | null | 1-pyrroline dehydrogenase activity [GO:0033737]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; gamma-guanidinobutyraldehyde dehydrogenase activity [GO:0047107]; protein homodimerization activity [GO:0042803]; sodium ion binding [GO:0031402] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244, ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540, ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382; Evidence={ECO:0000269|PubMed:23408433}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; KM=9 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; KM=141 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; KM=22 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; KM=89 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:23408433}; | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433). {ECO:0000269|PubMed:23408433, ECO:0000305}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
B6EU02 | JBP2_LEITA | MLNGLTRVSTSSELESILDIVQSSGEIAVVFISPSIGDLETITSETQRRQLRIAGIPRGGYTILPAIPLYDDELLQMCERYTAANDYEKAQIRDSLFMREYPLFAYSVRNHKALFHPADYVSRILQFCSYYVQAPDADVLSLLDRSPFLHISPIKEICTHIRLIARGTPLAPEDSESPAPEQLRFHAESDAEKLAAERAGAMSIATSSGGASETEQLSLFSGVVPSALFQKDAVEEVDKDTEETMVDLTGEETVDAVHSFQAEYLTLDGLELVTKAAIFYDREGEGQRIVAVYIPGGVPEDTCRAAAAVLEPAATKKNLRALTNGGLPPDTGLVGYYDYLTNPTRHKCRETEFSRRNWGLLAQSEPLLKHLDKLYSQLAPMHHHLQKVAIPSQYQLCGTVFSTITVNRNFRTAVHTDKGDFRSGLGVLSVINGEFEGCHLAIKKLKKAFQLKVGDVLLFDTSLEHGNTEVINPEIHWQRTSIVCYLRTGLMSSVCEMERRKHLNRLILQQLRNTEVLNTTVNINGADSSLPPLFVPTRLASHLAPVQLAALGFIVERTEKQSGCVVAMTMGLGKTLVALTLCFSQLHLAPQADILILTPKPIISHWVDEKNKWAMHGLHFPHFVASDGLNSLEFEQQLLEYERQKNNEKPKLGHVFVINGEYLAGFLRRFKRFTPLLIIVDEGHRVAAKGNKLTESLDRLRCNLRIVLSGTPLQNDASELYRLVGWVNKGVGRVLPPKRFQELANDINQFVEGDDGAFYNAVMAQEYIQDWMRGFVFREMENDLPPLHDYLLICGSSDVQREYEEKLGLTETTMTALKATEHRPHHLSTHPACYLAFISDSYQSMVSGWTVRAQANTSRMRVSQLEEIDTMRLEHYVQMVENEQLDTFIDLSGKMRVLVDIVLRVQARKEKLIIFSLYVGSQDLIHRTLTALRVCTFTVRGRDSQDRRRRAMQEFSENKDLIVLVLSTKIAAYGLDFTAANHVVLFDSWWNPQVDAQAIARAYRRNQRKPVTVYRLISATENKFVLSSQTRKIALFKCILHERTSRQALPDELEDCAANEKDEERRSFWAKLKTTLLAGGTRALLNVYRYQESVRESE | 1.14.11.6; 3.6.4.12 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; | base J metabolic process [GO:0070580]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; reciprocal meiotic recombination [GO:0007131]; transcription-coupled nucleotide-excision repair [GO:0006283] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; thymine dioxygenase activity [GO:0050341] | PF00271;PF00176;PF12851; | 3.60.130.30;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family; TET family, JBP2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19114062}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000305|PubMed:19114062}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + thymine = 5-hydroxymethyluracil + CO2 + succinate; Xref=Rhea:RHEA:10316, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16964, ChEBI:CHEBI:17821, ChEBI:CHEBI:30031; EC=1.14.11.6; Evidence={ECO:0000305|PubMed:19114062}; | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin. {ECO:0000269|PubMed:19114062}. | Leishmania tarentolae (Sauroleishmania tarentolae) |
B6EUA9 | PR40A_ARATH | MANNPPQSSGTQFRPMVPGQQGQHFVPAASQPFHPYGHVPPNVQSQPPQYSQPIQQQQLFPVRPGQPVHITSSSQAVSVPYIQTNKILTSGSTQPQPNAPPMTGFATSGPPFSSPYTFVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLAVSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTPTSGAISDTEATTIKGDNLSSRGADDSNDGATAQNNEAENKEMSVNGKANLSPAGDKANVEEPMVYATKQEAKAAFKSLLESVNVHSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYIKAGTQWRKIQDRLEDDDRCSCLEKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASNTSGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISEDLSTQQISDINLKLIYDDLVGRVKEKEEKEARKLQRLAEEFTNLLHTFKEITVASNWEDSKQLVEESQEYRSIGDESVSQGLFEEYITSLQEKAKEKERKRDEEKVRKEKERDEKEKRKDKDKERREKEREREKEKGKERSKREESDGETAMDVSEGHKDEKRKGKDRDRKHRRRHHNNSDEDVSSDRDDRDESKKSSRKHGNDRKKSRKHANSPESESENRHKRQKKESSRRSGNDELEDGEVGE | null | null | mRNA cis splicing, via spliceosome [GO:0045292]; RNA splicing [GO:0008380] | mediator complex [GO:0016592]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004] | RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063] | PF01846;PF00397; | 2.20.70.10;1.10.10.440; | PRPF40 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries (Probable). May be involved in pre-mRNA splicing (Probable). {ECO:0000305|PubMed:19467629}. | Arabidopsis thaliana (Mouse-ear cress) |
B6EUB3 | PDS5A_ARATH | MAQKPEEQLKELGSKLDLAPVSKDSLLKLLKEAAVCLSELEQSPPPAVLKSIQPFLDAVIKPEILNHQDKDVKLLVASCVSEITRITAPEAPYSDNIMKDIFQLIVSAFAGLNDVSGPSFGRRVLILETVAKYRSCVVMLDLECDDLVKEVFTTFLDVARDDHPEIVFSSMQNIMIVLLEESEDVQEHLLLILLSKLGRNRSDVRDAARRLAMKVIEHCAPKVESDIKQFLISSMSGDSRFSSSQIDYHEVIYDLYRCAPQALSGVAPYLTGELLADKLETRLKVVGLVGELFSLPGRVISEEFDSIFLEFLKRLTDRVVEVRMAILDHIKDCLLSDPLRAEASQIISALCDRLLDYDENIRKQVVAVICDVSVSALTSIPVDTMKLVAERLRDKAILVKTYTMERLTELFRVYCLRCADGKVDTGDFNWIPGKILRCLYDKDFRSDTIEYILCSSLFPSDFSVRDKVKHWIQIFSGFDKVETKAFEKILEQRQRIQQEMQRYLSIKQTQQTADAPEIQKKILFGFRVMSRAFSDPPKTEQNFLILDQLKDANIWKILTNLLDPNTSITQASRIRDDMLKILSEKHSLYDFLSTLSIKCSYLLFSKEYVKEILAEVSVRKSSKNTLGIQPCMDFLGLLACFCPSLFDGAEEELISFLKDDDEMMKEGTLKILAKAGGTIRENLIVLASSVDLLLERICVEGNRKQAKYAVHALASITKDDGLKSLSVLYKRLVDMLEDKRYQPAVLQCLGCIAQIAMPVYETRESEVVEFIRSKILKLKSETVDDKKLSWDDKSEICQLKIYGIKTLVKSYLPFKDAQLRAGVDDLLGILKNILSFGEVSEDLESSSVDKAHLRLAAAKAVLRLSRHWDDKIPIEIFHLTLKTPEIPFPTAKKIFLGKVHQYVKDRVLEMKYACSFLFDITGSNVLESEEDKHNLADIIQHSYQTKVRKISAQTDANSVTLYPHHILPYLVHALAHHSCPDVEKCKDVKEYEMIYRQLYLIISMLLHKEEDGKTEDIDKEREYVPTIILIFHSIKQSEDVTDATKSKNSHAICELGLSIINHLTQKEPDLQGEITPVSLPPTLYKPSEKVEGDKSQVGEEKLWLADETVLLHFRALKLESHADASVIPQTSENEVMIDGESDGNEIPLGKIVERLRAQGTKTRKGKKNKSVPAEDENGKNDVDVLKMVREINLDHLQMLDKFESSNGHKHSPSERAEICQRDQKGNKRNVGDATSVVSVPKRRRSSSGHSPYKFSNSGPKVQLKASEDELHLESDMDKNVSLDSHDENSDQEKMLESISPRKRKKSLSSKLKITESDWALTDVERSRSAGGGDSKLKSASGSMKKRKNVSGLAKCSTKENKLVNDELIGCRIEVWWPMDKRFYEGTVKSYDSTKQRHVILYEDGDVEVLNLKKEQWELIDTGGKTAKKSRTSKGNSKKKRSSGSKPKNPDGVQRDEDPVTTTPKGKRTPKKNLKQLHPKDTPKSLSLEHEKVESRNKKRRSSALPKTEYSGEAGEEKSESEGKSLKEGEDDEEVVNKEEDLQEAKTESSGDAEGKEAEHDDSDTEGKQENNEMEREAEENAETSDNETLGAWKSKVGKSISRTAI | null | null | cell division [GO:0051301]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; homologous recombination [GO:0035825]; microsporogenesis [GO:0009556]; mitotic sister chromatid cohesion [GO:0007064] | chromatin [GO:0000785]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plastid [GO:0009536] | null | PF20168; | 2.30.30.140;1.25.10.10; | PDS5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | null | null | null | null | null | FUNCTION: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex (PubMed:26648949). Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin (PubMed:26648949). May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (PubMed:26648949). {ECO:0000250|UniProtKB:Q29RF7, ECO:0000269|PubMed:26648949}. | Arabidopsis thaliana (Mouse-ear cress) |
B6F209 | CPAS_ASPOZ | MKTPIAVVGTACRFPGDISSPSQLWELLSNPKDVLRDLNPKRLNLTGFNHHNAEHHGATNVPNKSYILDDDVYRFDAAFFNISAAEAEAMDPQQRLLLETTYEALESAGYTLKQMRGSSTSVFIGAMTSDYHDIQARDLDTISRWHATGTSPSILSNRISYFFDLKGPSMTVNTACSSSLVALHQAVQSLRNGDCTAAIVGGVNLLLDPEVYISHSNLHMLSPTSRCRMWDRDADGYARGEGCTSIMIKTLDQALKDGDDVECIIRETAVNSDGRSAGITMPSPEAQATLIRETYERSGLDPVRDRCQYFECHGTGTQAGDPVEAQAIQQTFYPKNAVFSPDDKLYVGSIKTLIGHLEGCAGLAGVMKAIMCLKNRTITPNMFFDNLNPNISPFYDHLRIPTNTVPWPPVAHGCPLRASVNSFGFGGTNAHAIIESYVPSQPKRQASYCKESNRQKYTNSGPFVFSAHTQESLYSNIERTARYVRSNEALDLGHLAWTLAKRTVLPFKVAITALSREELLGNIDKAIVEYKASKASAQGPSPWKHPPEPHRIMGIFTGQGAQWAGMGRELLLASTVFRKSIERCEHALATLHDGPSWSLQEELLADKPSSRLSNPAISQPVTTAIEIAAYDLLCTSGVNVDVVVGHSSGEIVAAYALSIISAEDAMKIAYYRGLHTKPARSGRMLAVSLSFHDARELCSWPSFSGRVVVAASNGPASTTLSGDYDAILEVKALLDRKKTFARTLQVDVAYHSHHMVPCSAAYLESLRACNIQVKSPRSGCTWISSVTGRNAILDGDIQSFSATYWVDNMVKPVLFSQALDKSLCGTQDLGVCIEFGPHPALRGPVLDTLKSKGTSSVHYTSLLRRGQNDLNAASSAVGYLWERMADRVDLASFLQGFRSQALQLIKGLPGYSWDHGRRYWRESRISRRYRLEGTQLHPLLGRRSADEFPNEFCWKNMLHLKEMPWAQGYKEEGRVVLSAAFYLCSLLSAASSAAVCQRLVVLELNNFVVMEPITLEEYGNGVEYITTIRFDNEDFRTISSTILHAEASCHACKSDESVLTKVCTARLTLHLGDARGPDCDCLPPRGQRNDLLAPVDVADLYDSFEQAGMSYTGPFRSITSIQRSLGEATASVAWAVDTTMPESVLNPAMVEASFQAIMCAFASPLTEELRTPFHAKEIRRVLVTPRLALGGVSCDIDAFVTGVDCGGVEGDVSLYKPDGNAMIQIEGLVMKSVPQPDTSSDRNLFSHVVWESDPFGYSLISYPTPNEDMGWKRAADIVALYHLRRTVEEIDPLESAGFTPHHQLLYREISHIAAAGRGSEYYITHPDCAQTSEEIILAMIDKYAGIVDLQSLHSFGKALPAILRGELDLHNTPNEPDTLEGFTHDAAMFSQLSKDICSIVRRIVHKHPHMNVLGLDPGPSVITHQILEALDDKHTSYCLGSADPVILNKTLARLSAQHRNLYSKVIDLTTVNAGEHGSDKYDMVIAANPLHGTDTSANLFEVCRAMLKPGGYLVFVRVTGRVSMSLLCTCGWLPQWWQGYDQDARSWTDMSTVRYDSHLRSKGFSGIDHIFHDSMNSNGDGLSVMVTQAVNDTVMMLREPMNSTGLAPLTETVVFVGGKTLSVARLLQSIRRIVAASGTATTVVEDIDRLEMNGLTKQHSIISLVELDEPFFSRGAFHERLLAFKELVARSKHVLWLTTRNMTSISVAIGRAMRSERGADISLQFLGLSTVANISPSAVVEVFLRLTWSFVPVLTDGEVLWTNEPELQWDGSTLRIPRLVWDHKRNKRYNYRHRQGRPEAGLPQTAVPLSPRVSTNSVAVQIKYSCLVCTDVYLWVGARIDGQGNVVGISDHVSFVIHARLDHVHNLSDEHDLSPDALRATASFTLAYLLIKSLSGPILLYEPDELLAAAVEQDREPEQTVYFVTSKYNDCSRGWITVHPHASRRMVERMLPRKVSAFVDLSSSDDHVVTTLRDIYSHARIQAVELYRRAFAASPGQLIADSYTQACTSLSILSHTALEVTSSTEASTNIASVAYPKVVNWTSPAPIASPGDMISATTMFSSSGTYFMIDMATPLGLSILKWMATNGARKFVLAGRNPRMHEAWLEEMSRLGATVKPLKMDVSNKESILSAFTQIKEALPPIVGVCYAPLALSDQGFEYTVEDAGGLAATAMINAAKYLDELFPTPTLDFFVILTSLVSVIGTPKQVAYHAPSLFMTDLIQRRRLRGLVGSVMALGMVVDAGYFSRQGKEVIQRMMHHGYAPLSESDLHHAFGEVVAAGVPEAEGNAEIFFGLQLIDSQIDQSRESTSVSNHLLSHFITSRSGTKEGQYAEQEDSPSLLVPDEQLQESGPGRNKYDDLLARLSGKVRSILRLGDQALDVHTPLLDLGCDSLLAVDIQAWVAKEFDIDITPMDALLDTVAGLCEKAVPKPNAPGFVVEKEEQLVKELDFIDVATTASRSEHSSSVQDIPLDSTSSESSCVLCPSDSGFEQVRNDLEPRFTRIEKMSPHQSQIWFAGHWMRDPTQYNVVISYNVEGRFPVDRFKEALEHAVSMHESLRTAFFSDPNNGDLLQGVLKVPPPFLEHVRTPSAASVSQEFDKLASYQWRLEDGEVMRVTVVSIGKDQHTVIFGYHHIVMDGASWSTFLHDLKCIYEQRPRREVAQYVDYSLMLNRDIHNGTFAKELEFWKSELLPPPEMMPVLPLAKEKTRIPTDNFKVHTSTRHISIEATERIKQASRSLRGTPFHFYLATLQVFLAGLLKIESLCIGMSDANRKHQQFTGTVGYFLNMLPLRFEVQQTDSFANVFQKTSSKVLTALLNSSIPSNLVVDALNIPRVSNVTPLFQVAINYRVGEITRMSVDDFALNYDRSVMGNAPYDISFHVTPCANGTSIVEVNCRDYLYSPKATERIIDEYVRLLEIMSSNPLISVQSSVATSAPINEDGLSVQRGPRISHGWPATLPERFQDMVDQYGDRIAITDQGRDFSYLQLQAQSTRIGEALLQKGVRSGDTVAVLCPPSMNSVASMLAILRISAVYVPLDLSLPAARHKAMILASPVRALVCVSSTVEKVLELGVSTILNLSEIPDIRAPSTRFTNSAKGDSLAILLYTSGSTGQPKGVCLPQSGFINYLAAKRKELGLDSSTVVLQQSSLGFDMGLAQTLNAIMNGGKLVIVPQELRGDSIEIARIIRDQKVTFTLATPSEYLVMLQHGREYLHNYAGWRHACLGGEPFTDQLKREFVRLGKNCPVVQDSYGVTEISACTTFETMTASQLEEARSVGRTIPNTSLYIVDADCNLVATGEPGEICISGAGVALGYLNEEQTRLKFVQDPFALPDDIARGWTRVYRTGDKAKLLDDGSLILLGRMDGNTEVKVRGLRIDLEDVASTMVNCHPDLLSSAIVCVKGQGVSETLVAFVAMMPGQTASDVELQHLACNLPLPQYMRPSTVICLDELPRNANGKIDRKRIDAMPWTAPTTLSQSSKRLTLGEGELKLLWQVLLPGKHIQPESDFFLLGGNSTLLVRLQGAIRTSIGVSLTLREMYGASTLAQMALKVDARKAESPSMTINWLAETAIPQHILDRASSTSNLNLPKHCQGSGCQILLTGSTSFLGRVLVQLLLQVPEVERVHCIAVEKEQEHVPPTSDKVSLYYGSLLDPNLGLSTAEWASLQDRVDVVIHNGSNGHCLNTYNSLKGPNLGSTHRLAEFALQSQVPLHYISSGRVILQSGQTALGPTSVSFHPPPLDGSDGLTATKWAGEVFLERLAEHTDISISIHRPCTPIGDQAPAQDALNSLLRYSVNLGATPRLTRMEGYLDFQKVEIIAEEIATLVTSRFTKRSNTSSFTTRGVSFFHHSSNIKVPVKSFKEYMEKVHGRPFQELNLREWSSLALEQGIEPLIPSFLEAVDDNEETLRYPYLGN | 2.3.1.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolite biosynthetic process [GO:0044550] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-tryptophan + malonyl-CoA = CO2 + 2 CoA + cyclo-acetoacetyl-L-tryptophan + H2O; Xref=Rhea:RHEA:66900, ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57912, ChEBI:CHEBI:167552; Evidence={ECO:0000269|PubMed:19663400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66901; Evidence={ECO:0000269|PubMed:19663400}; | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:18854220, ECO:0000269|PubMed:19663400, ECO:0000269|PubMed:21608094}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole tetramic acid scaffold (PubMed:18854220, PubMed:19663400, PubMed:21608094). The hybrid two module polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) cpaS incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway. CpaS catalyzes a Dieckmann-type cyclization on the N-acetoacetyl-Trp intermediate bound in thioester linkage to the phosphopantetheinyl arm of the T domain to form and release c-AATrp (PubMed:18854220, PubMed:19663400, PubMed:21608094). CpaD then regiospecifically dimethylallylates c-AATrp to form beta-cyclopiazonic acid. CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid (PubMed:19877600). The beta-cyclopiazonate dehydrogenase cpaO then carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate (PubMed:21608094). Finally, the cytochrome P450 monooxygenase cpaH mediates the conversion of CPA into the less toxic 2-oxocyclopiazonic acid, the end product of the CPA pathway in A.oryza (PubMed:21608094). {ECO:0000269|PubMed:18854220, ECO:0000269|PubMed:19663400, ECO:0000269|PubMed:19877600, ECO:0000269|PubMed:21608094}. | Aspergillus oryzae (Yellow koji mold) |
B6HAA7 | ARO1_PENRW | MSEPTKISILGRESIVADFGLWRNFVAKDLISDLSSTTYVLVTDTNLGSLYTPTFQKTFEAAAASITPAPRLLIHHVAPGESSKSRQTKADIEDWMLSQNPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGSIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNADLILAAVRSEPKAGQGRFGGIRDILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARVVKCISAYGLPTSMKDARVRKLTAGKHCSVDQLLFNMALDKKNDGPKKKVVLLSAIGRTHEPKASVVSNDDIGVVLAPSVEVHPGVPKSLNVTCAPPGSKSISNRALVLAALGSGTCRVKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGKIIASPTPLYLGNAGTASRFLTTVATLATPSSVDSSVLTGNNRMKQRPIGDLVDALTVNGAGVEYMESKGCLPLKIAASGGFAGGKINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGHYVNPAEYIVESDASSATYPLAIAAVTGTTCTVPNIGSKSLQGDARFAVDVLRPMGCSVVQTDTSTTVTGPTDGVLQPLPDVDMEPMTDAFLTASVLAAVAQGKGANHTTRIYGIANQRVKECNRIKAMKDELAKFGVICREHDDGLEIDGIERSSLRQPSGGVFCYDDHRVAFSFSVLSLIAPQSTLILEKECVGKTWPGWWDALKQMFSVNLNGKELAEAEHAASSDEKRSSASVFIIGMRGAGKTTTGNWVAKALDRRFIDLDTELETSEGMTIPDIIKTRGWEGFRDAELAVLKRVLKDHPTGYVFACGGGVVEMPEARKLLTDYHKSKGNVLLIMRDIKLVMDFLQIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHSTSTELALASEDFTRFMRVVTGQVDSLSLIKKKKHSFFVSLTLPDVEPSGDIITEACVGSDAVELRVDLLKDPAVDGDIPSIDYVNEQMSLLRRRTTLPVIFTIRTKSQGGRFPDDAHDAAMQLYRLAFRCGCEFVDLEIAFPDAMLRAVTEMKGYSKIIASHHDPKGTLSWANMSWIPSYNRALEYGDVIKLVGVANTLDDNNALRKFKTWAEEAHDVPLIAINMGDSGQLSRILNGFMTPVSHPSLPFKAAPGQLSAAEIRRGLSLMGEIKAQKFAIFGSPVSGSRSPALHNTLFAKMGLPHDYSRLETTKVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEVAQEAEIIGAVNTIVRVSNGNNPPRLIGYNTDWQGMIRCMRNAGVYGSTGSQSAVVIGGGGTARAAIFALHNMGFSPIYVVGRTASKLESMVSTFPTNYNIRVVDNRAQLDTVPQVAIGTIPADRPIDPVMRETLCHMFERAQEIDGTLIGKSSDTSKHRVLLEMAYKPAVTALMQLASDAGWSTIPGLEVLVGQGVHQFVHWTGITPLYHEARVSKHLDYFLSF | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
B6HLU1 | ACVA_PENRW | MGPSNPAMAYFKPSTRDTMDPCSGNAADGSIRVRFRGGIERWKECVNQVPERCDLSGLTTDSTRYQLASTGFGDASAAYQERLMTVPVDVHAALQELCLERRVSVGSVINFSVHQMLKGFGNGTHTITASLHREQNLQNSSPSWVVSPTIVTHENRDGWSVAQAVESIEAGRGSEKESVTAIDSGSSLVKMGLFDLLVSFVDADDARIPCFDFPLAVIVRECDANLSLTLRFSDCLFNEETICNFTDALNILLAEAVIGRVTPVADIELLSAEQKQQLEEWNNTDGEYPSSKRLHHLIEEVVERHEDKIAVVCDERELTYGELNAQGNSLARYLRSIGILPEQLVALFLDKSEKLIVTILGVWKSGAAYVPIDPTYPDERVRFVLDDTKARAIIASNQHVERLQREVIGDRNLCIIRLEPLLASLAQDSSKFPAHNLDDLPLTSQQLAYVTYTSGTTGFPKGIFKQHTNVVNSITDLSARYGVAGQHHEAILLFSACVFEPFVRQTLMALVNGHLLAVINDVEKYDADTLLPFIRRHSITYLNGTASVLQEYDFSDCPSLNRIILVGENLTEARYLALRQRFKNRILNEYGFTESAFVTALKIFDPESTRKDTSLGRPVRNVKCYILNPSLKRVPIGATGELHIGGLGISKGYLNRPELTPHRFIPNPFQTDCEKQLGINSLMYKTGDLARWLPNGEVEYLGRADFQIKLRGIRIEPGEIETMLAMYPRVRTSLVVSKKLRNGPEETTNEHLVGYYVCDSASVSEADLLSFLEKKLPRYMIPTRLVQLSQIPVNVNGKADLRALPAVDISNSTEVRSDLRGDTEIALGEIWADVLGARQRSVSRNDNFFRLGGHSITCIQLIARIRQRLSVSISVEDVFATRTLERMADLLQNKQQEKCDKPHEAPTELLEENAATDNIYLANSLQQGFVYHYLKSMEQSDAYVMQSVLRYNTTLSPDLFQRAWKHAQQSFPALRLRFSWEKEVFQLLDQDPPLDWRFLYFTDVAAGAVEDRKLEDLRRQDLTERFKLDVGRLFRVYLIKHSENRFTCLFSCHHAILDGWSLPLLFEKVHETYLQLLHGDNLTSSMDDPYTRTQRYLHAHREDHLDFWAGVVQKINERCDMNALLNERSRYKVQLADYDQVQEQRQLTIALSGDAWLADLRQTCSAQGITLHSILQFVWHAVLHAYGGGTHTITGTTISGRNLPILGIERAVGPYINTLPLVLDHSTFKDKTIMEAIEDVQAKVNVMNSRGNVELGRLHKTDLKHGLFDSLFVLENYPNLDKSRTLEHQTELGYSIEGGTEKLNYPLAVIAREVETTGGFTVSICYASELFEEVMISELLHMVQDTLMQVARGLNEPVGSLEYLSSIQLEQLAAWNATEAEFPDTTLHEMFENEASQKPDKIAVVYEETSLTYRELNERANRMAHQLRSDVSPNPNEVIALVMDKSEHMIVNILAVWKSGGAYVPIDPGYPNDRIQYILEDTQALAVIADSCYLPRIKGMAASGTLLYPSVLPANPDSKWSVSNPSPLSRSTDLAYIIYTSGTTGRPKGVTVEHHGVVNLQVSLSKVFGLRDTDDEVILSFSNYVFDHFVEQMTDAILNGQTLLVLNDGMRGDKERLYRYIEKNRVTYLSGTPSVVSMYEFSRFKDHLRRVDCVGEAFSEPVFDKIRETFHGLVINGYGPTEVSITTHKRLYPFPERRMDKSIGQQVHNSTSYVLNEDMKRTPIGSVGELYLGGEGVVRGYHNRADVTAERFIPNPFQSEEDKREGRNSRLYKTGDLVRWIPGSSGEVEYLGRNDFQVKIRGLRIELGEIEAILSSYHGIKQSVVIAKDCREGAQKFLVGYYVADAALPSAAIRRFMQSRLPGYMVPSRLILVSKFPVTPSGKLDTKALPPAEEESEIDVVPPRSEIERSLCDIWAELLEMHPEEIGIYSDFFSLGGDSLKSTKLSFMIHESFNRAVSVSALFCHRTVEAQTHLILNDAADVHEITPIDCNDTQMIPVSRAQERLLFIHEFENGSNAYNIDAAFELPGSVDASLLEQALRGNLARHEALRTLLVKDHATGIYLQKVLSPDEAQGMFSVNVDTAKQVERLDQEIASLSQHVFRLDDELPWEARILKLESGGLYLILAFHHTCFDAWSLKVFEQELRALYAALQKTKSAANLPALKAQYKEYALYHRRQLSGDRMRNLSDFWLRKLIGLEPLQLITDRPRPVQFKYDGDDLSIELSKKETENLRGVAKRCKSSLYVVLVSVYCVMLASYANQSDVSVGIPVSHRTHPQFQSVIGFFVNLVVLRVDISQSAICGLIRRVMKELVDAQLHQDMPFQEVTKLLQVDNDPSRHPLVQNVFNFESRANGEHDARSEDEGSLAFNQYRPVQPVDSVAKFDLNATVTELESGLRVNFNYATSLFNKSTIQGFLHTYEYLLRQLSELSAEGINEDTQLSLVRPTENGDLHLPLAQSPLATTAEEQKVASLNQAFEREAFLAAEKIAVVQGDRALSYADLNGQANQLARYIQSVSCIGADDGIALMLEKSIDTIICILAIWKAGAAYVPLDPTYPPGRVQLILEEIKAKAVLVHSSHASKCERHGAKVIAVDSPAIETAVSQQSAADLPTIASLGNLAYIIFTSGTSGKPKGVLVEQKAVLLLRDALRERYFGRDCTKHHGVLFLSNYVFDFSVEQLVLSVLSGHKLIVPPAEFVADDEFYRMASTHGLSYLSGTPSLLQKIDLARLDHLQVVTAAGEELHATQYEKMRRRFNGPIYNAYGVTETTVYNIIAEFTTNSIFENALREVLPGTRAYVLNAALQPVPFDAVGELYLAGDSVTRGYLNQPLLTDQRFIPNPFCKEEDIAMGRFARLYKTGDLVRSRFNRQQQPQLEYLGRGDLQIKMRGYRIEISEVQNVLTSSPGVREGAVVAKYENNDTYSRTAHSLVGYYTTDNETVSEADILTFMKARLPTYMVPSHLCCLEGALPVTINGKLDVRRLPEIINDSAQSSYSPPRNIIEAKMCRLWESALGMERCGIDDDLFKLGGDSITSLHLVAQIHNQVGCKITVRDIFEHRTARALHDHVFMKDSDRSNVTQFRTEQGPVIGEAPLLPIQDWFLSKALQHPMYWNHTFYVRTPELDVDSLSAAVRDLQQYHDVFRMRLKREEVGFVQSFAEDFSPAQLRVLNVKDVDGSAAVNEILDGWQSGFNLENGPIGSIGYLHGYEDRSARVWFSVHHMAIDTVSWQILVRDLQTLYRNGSLGSKGSSFRQWAEAIQNYKASDSERNHWNKLVMETASSISALPTSTGSRVRLSRSLSPEKTASLIQGGIDRQDVSVYDSLLTSVGLALQHIAPTGPSMVTIEGHGREEVDQTLDVSRTMGWFTTMYPFEIPRLSTENIVQGVVAVSERFRQVPARGVGYGTLYGYTQHPLPQVTVNYLGQLARKQSKPKEWVLAVGDNEFEYGLMTSPEDKDRSSSAVDVTAVCIDGTMIIDVDSAWSLEESEQFISSIEEGLNKILDGRASQQTSRFPDVPQPAETYTPYFEYLEPPRQGPTLFLLPPGEGGAESYFNNIVKRLRQTNMVVFNNYYLHSKRLRTFEELAEMYLDQVRGIQPHGPYHFIGWSFGGILAMEMSRRLVASDEKIGFLGIIDTYFNVRGATRTIGLGDTEILDPIHHIYNPDPANFQRLPSATDRIVLFKAMRPNNKYESENQRRLYEYYDGTRLNGLDSLLPSDSDVQLVPLTDDTHFSWVGNPQQVEQMCATIKEHLARY | 6.3.2.26 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Note=Binds 3 phosphopantetheines covalently. {ECO:0000255}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9355751}; | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; penicillin biosynthetic process [GO:0042318] | cytosol [GO:0005829]; vacuolar membrane [GO:0005774] | ATP binding [GO:0005524]; ligase activity [GO:0016874]; phosphopantetheine binding [GO:0031177] | PF00501;PF13193;PF00668;PF00550;PF00975; | 3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12223189}. Vacuole membrane {ECO:0000269|PubMed:1899377, ECO:0000269|PubMed:8416970}; Peripheral membrane protein {ECO:0000269|PubMed:8416970}. Note=Loosely attached to the vacuoles. {ECO:0000269|PubMed:8416970}. | CATALYTIC ACTIVITY: Reaction=3 ATP + H2O + L-2-aminoadipate + L-cysteine + L-valine = 3 AMP + 3 diphosphate + 3 H(+) + N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine; Xref=Rhea:RHEA:23196, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:57762, ChEBI:CHEBI:58572, ChEBI:CHEBI:58672, ChEBI:CHEBI:456215; EC=6.3.2.26; Evidence={ECO:0000269|PubMed:1368505, ECO:0000269|PubMed:19686863, ECO:0000269|PubMed:21889568, ECO:0000269|PubMed:9266851, ECO:0000269|PubMed:9355751}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23197; Evidence={ECO:0000269|PubMed:1368505, ECO:0000269|PubMed:19686863, ECO:0000269|PubMed:21889568, ECO:0000269|PubMed:9266851, ECO:0000269|PubMed:9355751}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for L-2-aminoadipate {ECO:0000269|PubMed:9355751}; KM=80 uM for L-cysteine {ECO:0000269|PubMed:9355751}; KM=83 uM for L-valine {ECO:0000269|PubMed:9355751}; | PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 1/3. {ECO:0000269|PubMed:1368505, ECO:0000269|PubMed:19686863, ECO:0000269|PubMed:21889568, ECO:0000269|PubMed:9266851, ECO:0000269|PubMed:9355751}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. {ECO:0000269|PubMed:9355751}; | null | FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:1368505, PubMed:21889568, PubMed:9266851). The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine (PubMed:19686863, PubMed:21889568, PubMed:9266851, PubMed:9355751). The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV (PubMed:22777282, PubMed:8416970). Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates (PubMed:21889568, PubMed:9266851). The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus (PubMed:1368505, PubMed:1369045, PubMed:1588566). Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin (PubMed:1368505, PubMed:2110531, PubMed:2120195). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (PubMed:23053082). {ECO:0000269|PubMed:1368505, ECO:0000269|PubMed:1369045, ECO:0000269|PubMed:1588566, ECO:0000269|PubMed:19686863, ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195, ECO:0000269|PubMed:21889568, ECO:0000269|PubMed:22777282, ECO:0000269|PubMed:23053082, ECO:0000269|PubMed:8416970, ECO:0000269|PubMed:9266851, ECO:0000269|PubMed:9355751}. | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
B6I112 | HCHA_ECOSE | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli (strain SE11) |
B6JVD0 | ARO1_SCHJY | MSQDTDVVSVPILGKEAVFVGFNLERRVCDFLIENAKSSAYVIVTDTNIAPHYLEKYTTALSEAAKRHGVAPRILTRVIPPGETSKCRSMKAEIEDWMLSQSCTRDTVLVAMGGGVIGDMAGYVAATFMRGIRFIQLPTTLLAMVDSSIGGKTAIDTPNGKNLVGAFWQPLAVFADLNFLETLEPRQFINGMGEVIKTAAMWNEKDFCLLEQNPTVILEAVHRPRVPGQFKFENIRNLLQKIILASVRTKCEVVTLDEREGGLRNLLNFGHSIGHAYEAILFPQILHGECVSIGMVKELELSRYLGILKPNAVGRVTKCLMSYTLPVSVHDAHIKKYAGYKKCPVDKLIRIMAVDKKNQGLQKRVVILKAVGETYEKHATVVSDEDIRVVLSHDIQVSPFDNSVSDVVVTPPGSKSISNRALILAAMAKGTTKLTNMLHSDDTQVMMAALEELGAATFSWEDNGETLVVNGGGKFKTPSKELYLSNAGTAARFLTTVAALVGENEQGGEVVLTGNHRMKVRPIGPLVDALRANGCSISYLEREGSLPLKMIPQNGLRGGVIELAATVSSQYVSSILMCAPYAQEPVTLKLVGGKPISQLYVDMTIAMMKGFGVNVVKSETEAYTYHIPKANYTSPGDYEIESDASSATYPLAFAAITGTKCTVPNIGSASLQGDARFARDVLAPMGCTVEQTPTSTTVQGPPMGQLKPLESVDMETMTDAFLTATALAAVACNSSGNEHITRITGIANQRVKECNRIAAMVHELAKFGVKAGELEDGIFIHGQSYKDLKTPEEGIYTYDDHRVAMAFSILTLVTPKPTVILDKACVVKTWPYWWDVLRNSFKIKLAGVESKETVKSVKLTRSRASVILIGMRGAGKTTIGSIIAGQLNMKFLDLDQELEKKLNTTIPDLVNTRGWDDFRQEELQVLQEFIDTKSSDFVAACGGGIVETPAARELLCKYVKEGGIVLHIHRNLDQVLSYLSIDKSRPAYADRESTKNVYLRRHQWYLDCRSHDFVSPTIESGNVQSKLETSMSRFLRVVTGKSTWFEKAIQKPHSFFLSLTFPNINDAISFLPEAIIGCDAVELRADLLEDPNSTTGYPSVEFVAEQFATLRAAIDLPIIFTVRSKDQGGRFPNANESEAVELMLAALRWGVDVLDLELGWSTESLQAIYARKENTKIITSWHDTAQRCSWAQPDEWLQKLDMATAFGDVVKFVGIAKSMQDNFDLEKFRKSFKGYTNKPLIAINMGTVGQLSRVFNNVLTPVTSPALPYKAAPGQLSVRQIITALSLMGSISPKKFYLFGTPIQHSKSPILHKTCYDLTGLPYTYDLFETESVEGVKDVLSQPDFGGANVTIPYKLDILQYLDELSDEARFLGAVNTVVPISENGKRKLRGDNTDWRGIVRTFVRAGANNLNGKNALVIGAGGTSRAAIFAMHKLGAKNIYLLNRTLVNAEKVKAVFPEEYNVKVIDHTKQSEISEWTKLQVAAVVSTVPADRPLPESVSKVIDALLSEIPAQKKEQYVFLDMAYKPLNTPLMSVASKHGYTCINGLEVLLQQGLASFEIWTGLAVPFEHVFGLYMVLCAKEHN | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast) |
B6JYI7 | FEN1_SCHJY | MGIKGLSQVIADNCPSAVRHNDIKNYFGRKVAIDASMSLYQFLIQVRGQDGQQLMNDQGETTSHLMGMFYRTLRMVDNGLKPCYVFDGKPPTLKSGELAKRASRQQKAREEREEAKEVGTAEMVDKFAKRTVRVTRQHNDEAKKLLELMGIPYVNAPCEAEAQCAALARAGKVYAAASEDMDTMCFQAPILLRHLTFSEQRKEPISEYSFEKTIEGLNFTIEQFVDLCILLGCDYCDPIRGVGPARAVELIRQHGNLDNFVKDADKKKFPIPEDWPYQDARRLFLEAEVQEAKDIELKWRAPDEQGIIKFLVEEKGFNEDRVRVGINRLVKASKTIPQGRLDSFFKVLPSTKKEKEKPKAAAKRKRDTKSSAPKKKR | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03140}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000255|HAMAP-Rule:MF_03140}; | base-excision repair [GO:0006284]; DNA replication, removal of RNA primer [GO:0043137]; mitochondrial DNA metabolic process [GO:0032042]; UV-damage excision repair [GO:0070914] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | 5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; DNA binding [GO:0003677]; double-stranded DNA 5'-3' DNA exonuclease activity [GO:0051908]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; single-stranded DNA 5'-3' DNA exonuclease activity [GO:0045145] | PF00867;PF00752; | 1.10.150.20;3.40.50.1010; | XPG/RAD2 endonuclease family, FEN1 subfamily | PTM: Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. {ECO:0000255|HAMAP-Rule:MF_03140}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}. | null | null | null | null | null | FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140}. | Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast) |
B6KAM0 | AMA1_TOXGV | MICSIMGGLRSLRAARPYSHQSNTETKHMGLVGVASLLVLVADCTIFASGLSSSTRSRESQTLSASTSGNPFQANVEMKTFMERFNLTHHHQSGIYVDLGQDKEVDGTLYREPAGLCPIWGKHIELQQPDRPPYRNNFLEDVPTEKEYKQSGNPLPGGFNLNFVTPSGQRISPFPMELLEKNSNIKASTDLGRCAEFAFKTVAMDKNNKATKYRYPFVYDSKKRLCHILYVSMQLMEGKKYCSVKGEPPDLTWYCFKPRKSVTENHHLIYGSAYVGENPDAFISKCPNQALRGYRFGVWKKGRCLDYTELTDTVIERVESKAQCWVKTFENDGVASDQPHTYPLTSQASWNDWWPLHQSDQPHSGGVGRNYGFYYVDTTGEGKCALSDQVPDCLVSDSAAVSYTAAGSLSEETPNFIIPSNPSVTPPTPETALQCTADKFPDSFGACDVQACKRQKTSCVGGQIQSTSVDCTADEQNECGSNTALIAGLAVGGVLLLALLGGGCYFAKRLDRNKGVQAAHHEHEFQSDRGARKKRPSDLMQEAEPSFWDEAEENIEQDGETHVMVEGDY | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | null | PF02430; | 2.10.70.70;3.50.4.10; | Apicomplexan parasites AMA1 family | PTM: Proteolytically cleaved during invasion within its transmembrane domain, releasing a soluble form from the tachyzoite surface. The cytosolic tail generated by ROM4 cleavage during invasion may trigger parasite replication within the parasitophorous vacuole. {ECO:0000269|PubMed:16102004, ECO:0000269|PubMed:20421941}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11083833, ECO:0000269|PubMed:11087913, ECO:0000269|PubMed:16102004, ECO:0000269|PubMed:16244709}. Note=Initially localizes to micronemes, specialized secretory organelles of apicomplexan parasites important for host cell invasion. Relocalizes to the surface membrane upon host invasion by tachyzoites. Found predominantly on the apical end of the parasite surface. A cleavage product of the large ectodomain is released into the medium by extracellular parasites. | null | null | null | null | null | FUNCTION: Essential microneme protein that plays an important role in host cell invasion. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV). {ECO:0000269|PubMed:11083833, ECO:0000269|PubMed:11087913, ECO:0000269|PubMed:16000372, ECO:0000269|PubMed:16102004, ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:19247437, ECO:0000269|PubMed:20421941, ECO:0000269|PubMed:21205639, ECO:0000269|PubMed:22523242}. | Toxoplasma gondii (strain ATCC 50861 / VEG) |
B6KV60 | RON2_TOXGM | MTKRAGLPLGRAFLVLILLSAADSLFFSSFPRSALQLFSSVLFTDAAEPDSDATPGLRPQPSPRTFRPTGYQRIEVKTVDEELPEDLKVYTASTRGSSSRTFEVRNAGGRQEGFTLSVLTAGGPLPHGSWSWSGTPPEVQTTGGSQISFGWVPDTETPSLPERNLLQLKRMLRDEGLIEAVQLRAAEKGCPVAVLHNLRQLPVNFREVLHEEYESRSNPAKMYEVANSYVQQRGSDAARWSVSQSVELSLLEMHATSTTDPRGSSAVPSFLETGPQVRVAMTDAVPSGIRVYATPPAPRPVPVQSNQTEKERSPTSKRLVGMQLGLYLICKLAALFGHPTLFLNPYYTEQQLLEAVAQALGIAPPHRGDFENEGNEAQATANQHNGSADQLLAAIEIFRLGPNPYTIGHVLTLMIAYLDYESFFGASPSKPFHSWVSLAASAGNNTGFAMLDEMCDNHRGPKRRGQKHWYQTGGARKHKNRDMLPLHRQLCDALELVLNGVQQIQIDLMDELGKYKTGVEPLVDPATNSARIHTRTCRGLSPVCDYEATILAPVRALEPHEQQDSLRTKKAFNLVTGYGSGHVGQITGSIAEPFSHSWRTRWGKVVADPTAYGEIFERTLWFDDRELMAKSSGALFRQYDRIAKDSMSFGVFMNVENGLLKKDMRSKLEAYISQRKSFVEKRQQSRFAKLRKKIPENDPYALRAAIFLALNSRTFCAQPTSFLSSFRTFLTNQYHKLSQGRNLPRSQRSLMAFMRTGQVKFFQEWCSFDPLAVNALFLFRFAVSGTDPAALHDRQHTRVSRNKKTMRILNSKWTPAVLKKLMRKVNHKHMAREAKALLLRSLDPTVLSSIVTAFDFITHTQANLEVNQNAFMYHEVRAREVSRQSAAEKGSHRLHERGLVRETDDMIKRWAEHGIPGDIKRRLARGEKLPEGMSFGGIPIPNLTNWDAQLNSKWLEAYNAYLRHPYGRAALNARDPVALLVKDSRDRLQAEAEGTIFLGRIAKRVHQSKNLLRRAGRALKTFFLSLLRENERSEYAVWFGVKVDMRQVIQTCRQINSVAEVVKNDRLYDFITDGWMELVKDVVAGYTKASVRVPGFDTISAANEQLRKEGVAAATARNQGFLSIHYDYANLPEEERKKEFQRSMCMEQCEALWKLVMAFVMPNLQNPKKLKGYEKDFSGAKEIEKLNSPHHVNAFRFSLSVQIDFFDNMLDKTSKKNLKAMKFGASTWFTYAMKLAGQVNSEMGNPNLGTALYMQAAYYGNYIRKWMEQRRKSRKQAIIGVLTLGMMGLYALLNVADIVQHMEDIGGAPPVSCVTNEILGVTCAPQAIAKATTSAARVATQDFLKVGLFAGMAPYLMLPMAVVSVWNILKSEIKVLLQFEMALKHTFTRLKRWLAAPFKNWWAKRGRLKDALFRRASQTYRKTEQETKQPPRPRNLHNPSSWGDTELDSLGVPPEPFVQDFEIKYTTPVFPMSAPLIKA | null | null | null | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | null | null | null | Apicomplexan parasites RON2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21347343}. Cytoplasm {ECO:0000269|PubMed:21347343}. Host cell membrane {ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:19247437, ECO:0000269|PubMed:21347343}; Single-pass type I membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:21347343}. Note=Initially localizes to rhoptries, specialized secretory organelles of apicomplexan parasites important for host cell invasion (PubMed:16002398, PubMed:16244709). Upon host invasion by tachyzoites, the protein is injected into the host cell, where it spans the host cell membrane (PubMed:21347343). {ECO:0000269|PubMed:16002398, ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:21347343}. | null | null | null | null | null | FUNCTION: Essential rhoptry neck protein that plays an important role in host cell invasion. Upon host invasion by tachyzoites, the protein is injected into the host cell where it functions as a receptor for apical membrane antigen 1 (AMA1) on the parasite. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV). {ECO:0000269|PubMed:16244709, ECO:0000269|PubMed:19247437, ECO:0000269|PubMed:21347343, ECO:0000269|PubMed:21347354}. | Toxoplasma gondii (strain ATCC 50611 / Me49) |
B6QCA7 | ARO12_TALMQ | MAEPTKISILGRESIVAEYGIWGTYIVQDLLTNLPSTTYVLVTDTNLGSIYREKFAKVFNEAAAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVASTYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAARSKAGKGRFDSVRQVLKDRIVASARHKAYVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELELARYLGILKPIAVSRMVKCLSKYGLPTSLKDARVRKHTAGKHCSLEQLMANMALDKKNDGPKKKVVLLSAIGKTYEPKASVVSNEDIRVVLAPSIEVIPGVPKNLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDYNILTGNNRMKQRPIGDLVDALTVNGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQGSYTNPPEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVEVLRPMGCNVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGKGGNNTTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGINRSSLRHPAGGVFCYDDHRVAFSFSILSLVAPTSTLILEKECVGKTWPTYWDALKQKFGVQLEGKELAESEVTHGSADRSNASIIIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALAERPTGHVFACGGGIVEIAEARKILVDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRQPWYQECSNVQYYSRHSSSPELALAMDDFGRFIQFVSGQTDYLAAIRKKHLSFFVSLTLPDLRESGDLLRTVASGSDAVELRVDLLKDPSSDSVIPSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPDDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVTESKAHAKIIASHHDPRGKLNWANGSWIQYYNKALQYGDIIKLVGVAETLKDNTSLKDFKDWAEQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRRGLSIMGEIPAKKFAVLGKPVSASRSPPMHNTLFEQNGLPHVYTRLETDKAQDVKEFIRSPDFGGASVTIPLKLDIIPLIDEILNEAEIIGAVNTIIPVEGKDGSTRLVGRNTDWSGIVRCLREAGAHSNEGKSSALVIGGGGTARAAIYALHHMGFSTIYVLGRSPEKIQNMASTFPTGFDIRVLEHANDVESIPRVAVGTIPGDKPIESNIREILCTIFQRSGSAGDESGVLLEMAYKPSVTPLIQLASDYGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTNETK | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei) |
B6QWH9 | ARO11_TALMQ | MAEPTKISILGRESIVADCGIWGTYIVQDLLTNLPSTTYVLVTDTNLGSIYREKFAKIFNEAAAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAARSKPGKGRFDLVRQVVKDRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSRVRKHTAGKHCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEPKASVVSNEDIRAVLAPSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDYNILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQGSYNNPPEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVEVLRPMGCKVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGEGGNHATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAGGVFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDALKQKFGVSLKGKELAESEITHGPADRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERPTGHVFACGGGIVEIAEARNILIDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRFIQFVSGKTDYLAAIRRKRLSFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSGNGIPSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAESKAHAKIIASHHDPQGKLNWANGSWIQYYNKALQYGDIIKLVGVAETLKDNTALREFKDWAEQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKDGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIPGDRPIEANMREILCTIFERSGRAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTDETK | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei) |
B6RAL1 | PATM_PENEN | MVDNYHSSLDVAKTPIQSDADAQKSEAETEGPSSKSSQIAAGESIADSVRNFLELRQGGIPDDTGVVFDKISAVGSGTGSQDAPTVTSAAQSAFGLLSPLQNRQRKQYSRPILSGFSGTINPGEMLLVLGKPGSGCTTFLKTLSGLWDEYKEIQGELTLGGHPLLDVMKQRPQDILFCAESDDHFPTLTVAETLRFATRARCGPQVSAREIDTMVTQLAKLVGLGNVLNTKVGDAKIRGVSGGERRRVSLAEALATCARLICLDNPTHGLDSSTAVEFMEMMREWTTQSRCVAAMSVYQASDAIVSYFDKVLIINSGRQIYYGPVRDAKAYFEDLGFECLSTTTVADFLNVMSADPDVRRAQENRENQVPRTAEEFERAFSASPIYQEMQKSVQVAKERFQTNPSPLVKTSAFALPIWHQIWYCAGRQFRIVTSDYSLWAVELATIVVQSLVLGTLFRNQQRTTSSLFIFASALFYSVLVPALQSMAEFGNGFAQRPLILKQKRYQISRPIAYALGLVTTDVVWKVAAICYNIPLYFLTGFQRTAGNFFTWFLIIYLEHLALSMFFRSVAIFSPNMHRAVLPVGIFFNMYVLYTGLYVPAPQMQVWLGWLRYLNPLYYAFESVMVNEFRDLSYQCSASDPVPSGLGYNDMAHQVCAVVGSEPGDRLLSGASYIHAQYGFKTSHLWRNVGINAALFVFFALCSGIGMEMLKTPAGQLATVFYKSSPGVTHRRDKIDSETGQDQGNESSEMSAGQSNDALRLQEHQGPDKSHNLAWTNLCLDIKTKEGDQRLLNNLSGSVKSGQLKALMGVSGAGKTTLLNALAGRSTIGNLTGTLALNGQVLPTFFRSRMGYVQQQDIHLPTQTVREALQMTARLRRPESISVADKNAYVEKVIEWLSMEHIADALVGVPGAGLNLEQRKKVSIGVEMASKPEILFLDEPTSGLDGQSAMLIARLLRRLADSGQAILCTIHQPAAELIDQFDKLYLLSRGGNLVYDGSLGTRCHEAIQYFQPRSRPCGPEENPAEYFLAVIGAGSRNDAHMDWASLWNDSEQGKEREKAEESLVPAAEQAPQLEQQSLYSVPFHVQLWVVVQRTWLYYWREPDYVNSKLWMSVGNSLLNSLTHLQSPNTERGAYNRVFSAFMSLIVGPPLGLQVQPRFVTLRDIFVHRERESLTYHWLAFVLSAFIVELPFTFLSSLVYWLLWYFPVGYFNAPSRAGYSFLMYELFGVFATSLAQLCASLMPNIEAAFAANGFFFMFCNTFAGTLSPKPVTPSGWRWFYNISPLFYLGEGVTVDVLQDLPIRCEESEVSIFYAVNGTTCGQYAQDFLKTATGYLLNPASTTECQYCRYRDGQSYFQQYGYEFAHRHRNIGVFICFIAFNFTMVLVMTYLTKTRRH | null | null | patulin biosynthetic process [GO:0140723] | plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF00005;PF06422; | 3.40.50.300; | ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein {ECO:0000269|PubMed:30680886}. Cell membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein {ECO:0000269|PubMed:30680886}. | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FUNCTION: ABC transporter; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (Probable) (PubMed:30680886). May be involved in the secretion of E-ascladiol to be converted to patulin by the secreted patulin synthase patE (Probable). {ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:25625822, ECO:0000305|PubMed:27528575, ECO:0000305|PubMed:30680886, ECO:0000305|Ref.1}. | Penicillium expansum (Blue mold rot fungus) |
B6T5Z6 | ERB46_MAIZE | MTENLHSRKMVQPKKFRGVRQRHWGSWVSEIRHPLLKRRVWLGTFETAEEAARAYDEAAVLMSGRNAKTNFPIQRSSTGEPTPAAGRDARSNFSSGSSTTNLSQILSAKLRKCCKAPSPSLTCLRLDPEKSHIGVWQKRAGARADSNWVMTVELNKDAASTDAASQSTSATTAPPATPMDEEERIALQMIEELLSSSSPASPSNGDDQGRFII | null | null | abscisic acid-activated signaling pathway [GO:0009738]; cuticle development [GO:0042335]; ethylene-activated signaling pathway [GO:0009873]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of response to water deprivation [GO:1902584]; positive regulation of wax biosynthetic process [GO:1904278]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to water deprivation [GO:0009414] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF00847; | 3.30.730.10; | AP2/ERF transcription factor family, ERF subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}. | null | null | null | null | null | FUNCTION: Promotes cuticle formation by inducing the expression of enzymes involved in wax biosynthesis, particularly promoting very-long-chain waxes formation (PubMed:35696901). Confers drought resistance (PubMed:35696901). Acts as a transcriptional activator binding directly to promoter regions of CER2, CER3.2 and KCS1, wax biosynthesis-related genes (PubMed:35696901). Binds to the GCC-box pathogenesis-related promoter element (By similarity). May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). {ECO:0000250|UniProtKB:Q9XI33, ECO:0000269|PubMed:35696901}. | Zea mays (Maize) |
B6TNK6 | MOC31_MAIZE | MGGRREAIERELKKLRAEREELDGRIRLLESQLEAGPAGFNGAAAGKGVGDDACGGSGACQSRVGNEFAPDGSLPADMIYRYSRHLLLPDFGVEGQRKLSQSSILVVGAGGLGSPLALYLAACGVGRLGIVDGDDVELNNLHRQIIHKEAYVGQSKVKSAADACREINSSIKVVEYHHTLKPCNALEVARKYDIVVDATDNLPTRYMISDCCVLLNKPLVSGAALGLEGQLTVYHHNGSPCYRCLFPTPPPVAACQRCSDSGVLGVVPGVIGCLQALEAIKVATGVGEPLCGRMLLFDALSARIRVVKLRGSSPDCTHCGENSVFTEEDFQKFDYESFTQSPMSDKAAPSVNVLPESARITCREYKKLADDGEPHLLLDVRPAHHFQIASISPSHNIPLSMLEEKLPALEASLKEAGEGSALVVLCRRGNDSQRAVQLLREKGFTSAKDIIGGLQAWGRDVDPDFPVY | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; tRNA wobble position uridine thiolation [GO:0002143] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292] | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}. | Zea mays (Maize) |
B6ULW4 | BTDA_PAPAN | MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQPGADDQGMAHSFTWPENAALPLSESAKGLRCVCTRGFCRLL | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; innate immune response in mucosa [GO:0002227]; killing of cells of another organism [GO:0031640] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | null | PF00879; | null | Alpha-defensin family, Theta subfamily | PTM: Forms a cyclic peptide with subunit B (BTD-1), subunit A (BTD-3), subunit C (BTD-4), or subunit D (BTD-7). An additional intersubunit disulfide bond is formed. {ECO:0000269|PubMed:18852242}. | null | null | null | null | null | null | FUNCTION: BTD-1, BTD-3, BTD-4 and BTD-7 have antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. BTD-3 is more effective against E.coli than BTD-1, BTD-4 and BTD-7. {ECO:0000269|PubMed:18852242}. | Papio anubis (Olive baboon) |
B6ULW5 | BTDB_PAPAN | MRTFALLTAMLLLVALQPQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESAKGLRCVCRRGVCQLL | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; innate immune response in mucosa [GO:0002227]; killing of cells of another organism [GO:0031640] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | null | PF00879; | null | Alpha-defensin family, Theta subfamily | PTM: Forms a cyclic peptide with subunit A (BTD-1), or subunit B (BTD-2). An additional intersubunit disulfide bond is formed. {ECO:0000269|PubMed:18852242}. | null | null | null | null | null | null | FUNCTION: BTD-1 and BTD-2 have antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. BTD-2 is more effective against E.coli than BTD-1. {ECO:0000269|PubMed:18852242}. | Papio anubis (Olive baboon) |
B6ULW6 | BTDC_PAPAN | MRTFAFLTAMLLLVALHAQAEARQARADEAAIQEQPGADDQGMAHSFTRNESAVLPLSESERGLRCICLLGICRLL | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; innate immune response in mucosa [GO:0002227]; killing of cells of another organism [GO:0031640] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | null | PF00879; | null | Alpha-defensin family, Theta subfamily | PTM: Forms a cyclic peptide with subunit A (BTD-4). An additional intersubunit disulfide bond is formed. {ECO:0000269|PubMed:18852242}. | null | null | null | null | null | null | FUNCTION: BTD-4 has antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. {ECO:0000269|PubMed:18852242}. | Papio anubis (Olive baboon) |
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