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
stringlengths 8
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G5EFY4 | EGL46_CAEEL | MVPMNDFWVKAILSSTNPSPVPSTTSTVSNDENLDKTLDFDCSTQTVFPTLPMFWNPTLVQQMLALYQIQQQQIQFSAKLAPQPLFQEPTIQKEFLPFPHQSRKRPLPIDPKKTKLRKLNEDTVTSSPVSGMFIKEEADVKSVEELQKEADLLDETAAYVEVTEESRQKIDEIPNVIGDCICRLCKVKYEDVFKLAQHKCPRIAHEEYKCPDCDKVFSCPANLASHRRWHKPRNELGGSPPAQSSTIVSCSTCFNSFPTKKMLKLHSSTCQRSPLQDLLSRVIPTM | null | null | axon guidance [GO:0007411]; cell cycle [GO:0007049]; cell fate commitment [GO:0045165]; detection of carbon dioxide [GO:0003031]; detection of oxygen [GO:0003032]; male mating behavior [GO:0060179]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuroblast division [GO:0055057]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; neuron migration [GO:0001764]; neuron projection organization [GO:0106027]; positive regulation of exit from mitosis [GO:0031536]; regulation of cell cycle process [GO:0010564]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468] | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | null | 3.30.160.60; | INSM1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274062, ECO:0000269|PubMed:23946438}. Note=Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts. {ECO:0000269|PubMed:23946438}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:30291162). Represses expression of genes involved in differentiation of touch receptor neurons (TRN), probably acting as a heterodimer with egl-44, perhaps by occupying similar cis-regulatory elements as an unc-86/mec-3 heterodimer (PubMed:30291162). Plays a role in cell fate specification of neurons, including the hook neuron HOB, the gas-sensing neuron BAG and touch receptor neurons (PubMed:12954713, PubMed:25395666, PubMed:30291162). Plays a role in neuron differentiation by repressing the expression of zag-1 in FLP neurons, probably acting as a heterodimer with egl-44; because zag-1 represses expression of egl-46 and egl-44, together these proteins form a bistable, negative-feedback loop that regulates the choice between neuronal fates (PubMed:30291162). Acts downstream of egl-44 to prevent touch cell differentiation in FLP neurons (PubMed:11274062). Involved in male mating behavior, acting in concert with egl-44, via modulation of expression of polycystins lov-1 and pkd-2, homeodomain protein ceh-26, and neuropeptide-like protein nlp-8 (PubMed:12954713). Modulates the expression of a subset of terminal differentiation genes involved in O(2)- and CO(2)-sensing, acting in parallel to ets-5 and egl-13 (PubMed:25395666). May act upstream of RFX transcription factor daf-19 to regulate gene expression specifically in the HOB neuron (PubMed:20923979). Plays a role in specifying commissural dendrites of the PVD nociceptive neurons, acting in concert with egl-44 (PubMed:29031632). In association with egl-44, regulates cell cycle exit in the neuronal Q cell lineage (PubMed:23946438). {ECO:0000269|PubMed:11274062, ECO:0000269|PubMed:12954713, ECO:0000269|PubMed:20923979, ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:25395666, ECO:0000269|PubMed:29031632, ECO:0000269|PubMed:30291162}. | Caenorhabditis elegans |
G5EFY5 | NOB1_CAEEL | MISVMQQMINNDSPEDSKESITSVQQTPFFWPSAAAAIPSIQGESRSERESETGSSPQLAPSSTGMVMPGTAGMYGFGPSRMPTANEFGMMMNPVYTDFYQNPLASTGWYSYGQPYQFTANYSIPSLDGNLSDITIPTTAGSSAATTPNAAMHLPWAISHDGKKKRQPYKKDQISRLEYEYSVNQYLTNKRRSELSAQLMLDEKQVKVWFQNRRMKDKKLRQRHSGPFPHGAPVTPCIERLIN | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; cell differentiation [GO:0030154]; embryonic body morphogenesis [GO:0010172]; embryonic pattern specification [GO:0009880]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of nematode male tail tip morphogenesis [GO:0110039]; programmed cell death [GO:0012501]; regulation of asymmetric cell division [GO:0009786]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | Abd-b homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU000682}. | null | null | null | null | null | FUNCTION: Transcription factor, involved in posterior embryonic patterning, morphogenetic movements of the posterior hypodermis, and cell fate specification (PubMed:10781051, PubMed:16824957, PubMed:20824072, PubMed:21408209). Binds to the 5'-TAGT-3' motif in regulatory elements of genes, including Meis protein psa-3 and microRNA mir-57 (PubMed:16824957, PubMed:20824072). Involved in a negative regulatory loop with mir-57 to specify posterior cell identities (PubMed:20824072). Required for asymmetric division of the T hypodermal cell, acting via the regulation of asymmetric expression of psa-3 in cooperation with ceh-20 and the Wnt-MAPK pathway (PubMed:16824957). Involved in the regulation of the onset of non-apoptotic cell death in the linker cell, acting together with the Wnt signaling pathway (PubMed:27472063). Involved in promoting embryogenesis, in concert with orphan nuclear receptor nhr-25 (PubMed:15314147). May regulate expression of transcription factor dmd-3 (PubMed:21408209). {ECO:0000269|PubMed:10781051, ECO:0000269|PubMed:15314147, ECO:0000269|PubMed:16824957, ECO:0000269|PubMed:20824072, ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:27472063}. | Caenorhabditis elegans |
G5EFY7 | PQM1_CAEEL | MSFLNNDFGSPPATSSPPTTMPKLPTIQDMLNNIGASTVNLMQPNPYLMQNQIPLPVPNLPLNPFLHLNPAISQEIIQQFIAMSFNTPNVLASIANMGDDEGPSCNPKMRRGDLLKSVSMDSTEDPPSITLDNNGDMIVPNNDKEGWCRNKKYIEQTENGYMCTVCRKVYGRYNSVSYHVTIYHRNPPIKCNVPNCQFTTREARYIHFHKNYRHGIPLPESIDQGSRKCPHCRHVSKSPAMLEKHIRRHQIKDGLSNINEAIRERTSTICDEAMEIEPAETEVDPIETKPRSCTL | null | null | cellular lipid metabolic process [GO:0044255]; cellular response to heat [GO:0034605]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; glycogen metabolic process [GO:0005977]; innate immune response [GO:0045087]; intracellular oxygen homeostasis [GO:0032364]; negative regulation of vitellogenesis [GO:1903187]; positive regulation of dauer entry [GO:1905911]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of vitellogenesis [GO:1903188]; protein stabilization [GO:0050821]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hypoxia [GO:0001666] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin insulator sequence binding [GO:0043035]; metal ion binding [GO:0046872] | null | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30956009}. Nucleus {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:29949773, ECO:0000269|PubMed:31532389}. Cytoplasm {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:31532389}. Note=Nuclear localization under normal conditions, cytoplasmic as a result of heat-stress (PubMed:23911329). Nuclear localization declines over normal lifespan (PubMed:23911329). Exposure to Gram-negative bacterium P.aeruginosa enhances nuclear localization (PubMed:31532389). Hypoxic stress enhances nuclear localization (PubMed:33009389). {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:31532389, ECO:0000269|PubMed:33009389}. | null | null | null | null | null | FUNCTION: Zinc finger transcription factor which acts as both a transcriptional activator and repressor (PubMed:23911329, PubMed:30956009). Binds to the promoters of genes that contain the 5'-CTTATCA-3' DNA consensus sequence in their regulatory region (PubMed:23911329, PubMed:31532389). Functions downstream of the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:23911329, PubMed:27401555). Involved in normal development, lifespan, stress response, lipid metabolism, innate immunity and exit from the developmentally arrested larval state known as dauer (PubMed:23911329, PubMed:27401555, PubMed:29949773, PubMed:31532389, PubMed:33009389). Required for stress-induced expression of hsp-90 and resistance to heat stress, perhaps as part of a systemic stress signaling pathway (PubMed:29949773). Involved in maintenance of proteostasis (PubMed:29949773). Under hypoxic stress increases lipid levels by positively regulating fatty acid synthesis via fat-7 expression (PubMed:33009389). Associates with homeobox protein ceh-60 at the promoters of some stress-responsive genes to regulate expression; may require phosphorylation for transcriptional repression activity (PubMed:30956009). Acts downstream of nhr-14 to activate transcription of intestinal metal transporter smf-3, modulating innate immunity and iron uptake (PubMed:31532389). May act downstream of the mTORC2 signaling mediated pathway (PubMed:27401555). May act in a mutually exclusive manner with the FOXO transcription factor daf-16 (PubMed:23911329, PubMed:27401555). {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:27401555, ECO:0000269|PubMed:29949773, ECO:0000269|PubMed:30956009, ECO:0000269|PubMed:31532389, ECO:0000269|PubMed:33009389}. | Caenorhabditis elegans |
G5EFZ1 | GPMI_CAEEL | MFVALGAQIYRQYFGRRGMAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELYLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNRWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNGGLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIMCNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHGNAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVLAIMGLPQPAEMTGVSIVQKI | 5.4.2.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17897734}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17897734}; Note=Binds 2 manganese or magnesium ions per subunit (By similarity). Cobalt and nickel are less efficient (PubMed:17897734). {ECO:0000250|UniProtKB:Q9X519, ECO:0000269|PubMed:17897734}; | carbohydrate metabolic process [GO:0005975]; glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity [GO:0046537]; manganese ion binding [GO:0030145] | PF06415;PF01676; | 3.40.720.10;3.40.1450.10; | BPG-independent phosphoglycerate mutase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.12; Evidence={ECO:0000269|PubMed:15234973, ECO:0000269|PubMed:17897734}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.508 mM for 3-phosphoglycerate {ECO:0000269|PubMed:17897734}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. {ECO:0000305|PubMed:15234973}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:17897734}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. Active between 17 and 32 degrees Celsius. {ECO:0000269|PubMed:17897734}; | FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. {ECO:0000269|PubMed:15234973, ECO:0000269|PubMed:17897734}. | Caenorhabditis elegans |
G5EFZ3 | ASH2_CAEEL | MRSSKGGRGRQAAPKTAPTTVCYCDGKRELGSVEVVCSTCLKWFHGRCLKEFHELNSNGVPFMICYTFTCKQCRPTAEDWKAKKADLVQMCVTVLATLSAERLKADGKLSAEHVPEDFTYLSLKDEIVPYMNENWYMLTAIKQKKEWHQNLAPTLLKEKNIFVQHNDDDDLFALAEKNLSLLGPLHEAVKLIGKRPIERENREPRHIELPPIEGPKTRGASKRRHAEAPVTGKKQKLAADYSSTAAPNGVQIDIPFSKDNYRYYLTEVDPNVPEDPAWNQNQSSAYVIPSFHYRELLNPTVNVSSNDRAFQLSINGNSITGFEGYSMARASHGVSKGTWYFEVNFDDQPDDSHIRIGWSQSYASLQACVGYNKFSYGWRSKHGTKFHEAKGKKYHFGGFKQGDVLGCLIHLPVDKKLQIPANLPSEKYLPVSHKGFNLISFKANYFFEVQEESADIAKTLVEMPGSYIEFFHNGKSCGKAYENIYAGAYYPSISIFKSATATMNLGPKFRNLPRGATGIHARADEQQHEQTLSDMLYLVSKEVNLDHPPRVKREDDDDVKDIKKEIKQEI | null | null | chromatin organization [GO:0006325]; determination of adult lifespan [GO:0008340]; programmed cell death [GO:0012501] | nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976] | PF21198;PF00622; | 2.60.120.920;3.90.980.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20555324}. | null | null | null | null | null | FUNCTION: Component of the set-2/ash-2 histone methyltransferase (HMT) complex (Probable). Required for the di- and trimethylation at 'Lys-4' of histone H3, a mark associated with epigenetic transcriptional activation (PubMed:20555324, PubMed:21527717). Implicated in the epigenetic inheritance of lifespan over several generations (PubMed:22012258). Functions as a transcriptional regulator (PubMed:28379943). Acts in the germline to limit the longevity of the soma, probably by regulating a lipid metabolism pathway that signals from the germline to the intestine, thereby preventing accumulation of mono-unsaturated fatty acids (PubMed:20555324, PubMed:22012258, PubMed:28379943). {ECO:0000269|PubMed:20555324, ECO:0000269|PubMed:21527717, ECO:0000269|PubMed:22012258, ECO:0000269|PubMed:28379943, ECO:0000305}. | Caenorhabditis elegans |
G5EG11 | FAT4_CAEEL | MVLREQEHEPFFIKIDGKWCQIDDAVLRSHPGGSAITTYKNMDATTVFHTFHTGSKEAYQWLTELKKECPTQEPEIPDIKDDPIKGIDDVNMGTFNISEKRSAQINKSFTDLRMRVRAEGLMDGSPLFYIRKILETIFTILFAFYLQYHTYYLPSAILMGVAWQQLGWLIHEFAHHQLFKNRYYNDLASYFVGNFLQGFSSGGWKEQHNVHHAATNVVGRDGDLDLVPFYATVAEHLNNYSQDSWVMTLFRWQHVHWTFMLPFLRLSWLLQSIIFVSQMPTHYYDYYRNTAIYEQVGLSLHWAWSLGQLYFLPDWSTRIMFFLVSHLVGGFLLSHVVTFNHYSVEKFALSSNIMSNYACLQIMTTRNMRPGRFIDWLWGGLNYQIEHHLFPTMPRHNLNTVMPLVKEFAAANGLPYMVDDYFTGFWLEIEQFRNIANVAAKLTKKIA | 1.14.19.37; 1.14.19.44 | null | lipid metabolic process [GO:0006629]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | acyl-CoA delta5-desaturase activity [GO:0062076]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46524, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:76410, ChEBI:CHEBI:78663; EC=1.14.19.37; Evidence={ECO:0000269|PubMed:9917342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46525; Evidence={ECO:0000305|PubMed:9917342}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46528, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74328, ChEBI:CHEBI:78664; EC=1.14.19.37; Evidence={ECO:0000269|PubMed:9917342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46529; Evidence={ECO:0000305|PubMed:9917342}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46420, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:73862, ChEBI:CHEBI:74265; EC=1.14.19.44; Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:26806391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421; Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:26806391}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57368, ChEBI:CHEBI:74264; EC=1.14.19.44; Evidence={ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9917342, ECO:0000305|PubMed:26806391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425; Evidence={ECO:0000269|PubMed:11972048, ECO:0000305|PubMed:26806391, ECO:0000305|PubMed:9917342}; | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:9845325, ECO:0000269|PubMed:9917342}. | null | null | FUNCTION: Can function as a Delta(5) fatty acid desaturase and behaves as a (8-3) desaturase. Introduces a double bond in the fatty acid chain 5 carbons away from carboxy terminal to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a variety of substrates such as dihomo-gamma-linoleoyl-CoA ((8Z,11Z,14Z)-eicosatrienoyl-CoA, 20:3n-6) to generate arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6). Also acts on a number of other substrates, including fatty acids that do not contain a double bond at the 8 position like (11Z,14Z,17Z)-eicosatrienoyl-CoA (20:3n-3) to produce (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3) (PubMed:11972048, PubMed:26806391, PubMed:9845325, PubMed:9917342). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:26806391, ECO:0000269|PubMed:9845325, ECO:0000269|PubMed:9917342}. | Caenorhabditis elegans |
G5EG14 | CATIN_CAEEL | MGKDSKKHKKERRRERSPSTSDSDEERLQKRLAEQRSLKKDEKRRQKEEMKKNESAEEKRARRMEKKMRKDAKRKDADAEDTLIPPELNYTNLNNPFNDTKLTQTFVWGKKLEREGKSGLTQDEITKQTSQRIRKNLHEAAEFKRIRDSRAAAKEDMEMMKRDADLRAGQISDTKEREFQMDQIKERTRIRIDQGRAKAIDLLSRYARFADENPHTAKIPDFELENPMEYLKASCKSVDDYEDLIEDIKTYREVDGWAKNETWWMDVTRIAEDEIQKKAAQNRGDVHASVQTEVQNMFKNKSIDELLKLEDQMDAKIRGNSGNKGYWQDLDDQLKVFIARKRLREHHGRVLRLQLAIIKEEQKKEIQQQESEELLPVAEVPPQVKIQKEEEEEEEEDEDDEKISKKVRRKIDVQTLDDPELDEPERERKWRALTGDQLDDVTRELYRIGCYSPTYISADDTMPGIEILDEQADVDNLTERRNRNRGTLPSSSAASSGAPQGASSKMMAIAREGMEADESIFGAEEQLAAQRHLWSDKYRPRKPTYLNRVQTGFDWNKYNQTHYDQDNPPPKIVQGYKFNIFYPDLLDMTVAPRFGLTSCEDPDFAIIRFKAGPPYEDIAFKVVNREWETLHKNGYKCQFQNGVFQLWFMFKKYRYRR | null | null | gonad development [GO:0008406]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cell migration [GO:0030335]; regulation of cell migration [GO:0030334]; regulation of gene expression [GO:0010468]; regulation of Wnt signaling pathway [GO:0030111] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | RNA binding [GO:0003723] | PF10312;PF09732; | null | CACTIN family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20188721}. Cytoplasm {ECO:0000269|PubMed:20188721}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Plays a role during early embryonic development (PubMed:20188721). Required for the distal tip cell migration at the end of larval development and for gonad morphogenesis (PubMed:20188721). {ECO:0000250|UniProtKB:Q8WUQ7, ECO:0000269|PubMed:20188721}. | Caenorhabditis elegans |
G5EG17 | SMC6_CAEEL | MGKRDIPSPNENIAPRTIGMRDVDLTAAPAKKAKLDTGERIAVSGRVASVKLTNFMCHANLQIDFKTAQNNCFYIGGPNGSGKSALFAAINLGLGGRGSDNDRGNTVKSYIKDGTTQSKITITLTNAGLNAHPDFDDLISIERTINQASSTYIMKSVKVTSSDNHVERIVSRKKADVDRIVSRFSIHLSNPAFWMSQDRSRSFLANFKPANVYKLYLESTNLENIRLSYIRFADALDECFALIQLKAGEILNEQKKLKRMQEQRDLQAKLDQDRALVASFCWKLLFCKVRDYNDQIELTLKKQEAQKTLQDETKKEYAKNRAARTEVEKKIQEFRDEVEVQDAEIAEAREDLDAKKRKVLEFEEKIRECEQSIRKKTSEKKYMERTIVNAKNEVRILLEKQGNQDLTKRLTKVENDYKDISQQRENMELGGESAKLREKLDTVITDYKRKEEEKYTIQRDINQLRRKIEQDMETMRRSRATKKDAINKFGSHMAEILMEINRSKSRFQTVPKGPLGKYITLIDPKWAFTVEECIGNLANNFLCSSHLDAEILRNIFQSLRIPAQDRPTIIVAKCNGRAYTNLHEPSSDFKSIYRVLKFSDPDVHNVIIDKSNCEQFILIEDKTEAMELMGSNYPPQNAVKAYTLDGSQAYANGPNSQYRFYSGRGGHARGTFGNDQGDVDEGALARLIEDTKSEAMRLETQDLRKQDHELKVIYNERDQTKAAIDEFDRKLSNLRSQELQKERQAKDLRAELAQTANEDQVENLNESIEEMQKKIPLIEDEVKDILKNVADITADMAPVIQERKEAEHTLAEIQKETRDFASKSQKLQNELSKYDDAGEILKIRLDKVKADEGVFFHTEAKLKSERDDAMEMVENDKKNHPMPPGETDPPDLSSFPSTTEAQRKIEEMQKAVDRATVGCDTTITLECVKDFKDKLKRLKYLCRMIEDVLIELKNLHAARVKAYPSLKKFTELKVCNKFQELLAVRGHFIGGLEFDHEKETLNVNVQSSKEKDAMAGRRPEVLEVEEVDEHSYDDDSDDSTGPRRKKSKKSGQKKKRVRDLKGLSGGERSFVTAALVMSLWEVMEQPFRMMDEFDVFMDMMNRKLVMDLLVELATKKFPHNQFIFFTPQGIKELNMVDGLQVFEMNRVRD | null | null | chromosome organization [GO:0051276]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; meiotic cell cycle [GO:0051321] | condensed nuclear chromosome [GO:0000794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; Smc5-Smc6 complex [GO:0030915] | ATP binding [GO:0005524]; damaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697] | PF02463; | 3.40.50.300; | SMC family, SMC6 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20661436}. Chromosome {ECO:0000269|PubMed:20661436}. Note=Nucleoplasmic in the distal gonad arm and localizes on chromosomes during pachytene, diplotene and diakinesis in oocytes. {ECO:0000269|PubMed:20661436}. | null | null | null | null | null | FUNCTION: Core component of the smc-5/smc-6 complex (PubMed:20661436). Involved in DNA double-strand break repair by promoting sister-chromatid homologous recombination during meiosis (PubMed:20661436, PubMed:24939994, PubMed:27010650). Also plays a role in the DNA damage repair of ultraviolet (UV) radiation-induced DNA lesions (PubMed:24424777). Promotes efficient DNA replication (PubMed:24424777). {ECO:0000269|PubMed:20661436, ECO:0000269|PubMed:24424777, ECO:0000269|PubMed:24939994, ECO:0000269|PubMed:27010650}. | Caenorhabditis elegans |
G5EG38 | CDC16_CAEEL | MSAISPDTKSFAIPTLADEGSSSKPASSLDLPKHESIRFKPIKTLASRIDGSEYYDEASMEKVMEMLEIGRTDEAVAYADTLYSNIIDDEQQDIVTIAEYVKILVVLRQWRRISHIIARGNYHQIHIVFAYYAATALFQRKLYEDVAELSVGHLLPSNGQIGPLPVRTLSQVTGRYVEEERMKYSFANMAELDNSSKKLRMVPALMITIAESFLKLMNRDAAMICINYALSLDNTTLHVERLMAKYNLVEPAMWEKYRKVRNEQLKLHEGNHDPRILMERAQRAYEMGRFRETKKITDELFDLFGPHPECIILRIHCLTMLKDSRSLLELGHQLVSDDPHIPLPWYCVAMYYYSIGANSRARNFISKCTMMDSTFAEGWVAFGHILHYEVEHEQSMSCYYRASKLVDKSSEPFLYTSLQYSTHSQKLSKKFMGEAVARAPNDPLIRHEEACVAYTAKSYAEADILFRTVLYMVTETDEIIPIEEVLKKKIDDFWHPMLNNIGHIARRQGRLNEAIMFYQKAIRMEPKFVDAIASTALCYAVLGNIDKATEFFNKALAIDPFNETIRQCLSKMIQASKESYSVDQQTLPPAYNSETYFGAQEILPYCAIRKPRNDGFVVPSIVSSSQPFMSMLRDRLRRQDQLYAQEPDNDAGNQV | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; asymmetric cell division [GO:0008356]; cell division [GO:0051301]; eggshell formation [GO:0030703]; meiotic cell cycle [GO:0051321]; neurotransmitter transport [GO:0006836]; polarity specification of anterior/posterior axis [GO:0009949]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein ubiquitination [GO:0016567]; regulation of meiotic cell cycle [GO:0051445]; regulation of mitotic cell cycle [GO:0007346] | anaphase-promoting complex [GO:0005680]; anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; synapse [GO:0045202] | null | PF14559; | 1.25.40.10; | APC6/CDC16 family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:24321454}. Synapse {ECO:0000269|PubMed:24321454}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By similarity). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells (PubMed:11134076). Required for embryonic anterior-posterior axis formation (PubMed:11832245). Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion (PubMed:15556870). Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons (PubMed:24321454). {ECO:0000250|UniProtKB:Q13042, ECO:0000269|PubMed:11134076, ECO:0000269|PubMed:11832245, ECO:0000269|PubMed:15556870, ECO:0000269|PubMed:24321454}. | Caenorhabditis elegans |
G5EG44 | MDL1_CAEEL | MEQQLNLGHLLTAARLLDIGALDISSLDLGALTSTSSSPGSSSPAMFDLSNESELRSLFCGKLKVDKKQSSCASNASTSSQPYCSSPPARKSSKHSRTAHNELEKTRRANLRGCLETLKMLVPCVSDATRNTTLALLTRARDHIIELQDSNAAQMKKLNDLRDEQDELVAELAQLQADEEVAQATSQACQTLSQSRPESRASSFTSTSSRDSPCYLEYSPSSKPMDSHKPTIIDLYAEGLIPRGPITFPRPLVYPHNVFDLMNLPPTPFDVSQFLPINLQV | null | null | determination of adult lifespan [GO:0008340]; regulation of cell differentiation [GO:0045595]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:27402359}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which binds to the E box motif 5'-CACGTG-3', when in a heterodimeric complex with mxl-1 (PubMed:9764821). Involved in the control of lifespan in response to dietary restriction, the decline in protein homeostasis associated with normal aging, germline signaling and may overlap with the insulin-like signaling pathway (PubMed:24699255, PubMed:27001890). Plays a role in autophagy (PubMed:27001890). Involved in promoting infection by the microsporidian pathogen N.parisii, possibly together with transcription factors pha-4 and zip-10 (PubMed:27402359). {ECO:0000269|PubMed:24699255, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27402359, ECO:0000269|PubMed:9764821}. | Caenorhabditis elegans |
G5EG59 | EXOS5_CAEEL | MAGRLREMRCELSFLKNADGSACFSQGATCIWASCSGPGDVHASKASDEAMTLDISYRANCGDNKFNVLNNIIHSTLSNAINLELFPHTTISVTVHGIQDDGSMGAVAINGACFALLDNGMPFETVFCGVLIVRVKDELIIDPTAKQEAASTGRVLFSVCKGSDGHPEVCAMDAIGHWDFIQLEAAWSLAQPSASAIFDFYKTVMKRKLSVDEQ | null | null | apoptotic DNA fragmentation [GO:0006309]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; RNA processing [GO:0006396]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; U4 snRNA 3'-end processing [GO:0034475] | cytoplasmic exosome (RNase complex) [GO:0000177]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730] | 3'-5' exonuclease activity [GO:0008408]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899] | PF01138;PF03725; | 3.30.230.70; | RNase PH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQT4}. Nucleus {ECO:0000250|UniProtKB:Q9NQT4}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). Involved in apoptotic DNA degradation (PubMed:12718884). In vitro, does not bind or digest single-stranded RNA (PubMed:20660080). In vitro, binds to double-stranded DNA without detectable DNase activity (PubMed:20660080). {ECO:0000250|UniProtKB:Q9NQT4, ECO:0000269|PubMed:12718884, ECO:0000269|PubMed:20660080}. | Caenorhabditis elegans |
G5EG78 | PXDN2_CAEEL | MLLEFLLLIGISLSTACPSECRCAGLDVHCEGKNLTAIPGHIPIATTNLYFSNNLLNSLSKSNFQALPNLQYLDLSNNSIRDIEETLLDSFPGLKYLDLSWNKIRYVPKLSTAPNALVSLNLVHNEISRLDNDLVSHSPYMQTFLIQRNRIQSLPHDFFNSRMVPTLKTVKMAGNPWSCDCRMVNVKQFADSLFAHSNQNIFIVGKCFFPKGLRNYVFRNLSIENLECEKPEYSKTDDGMFKMSCPNNEMEGYHYDSIFLENNKEARHTAHFARDKDGSLLSNGQFTRNYQCAFYRQKQSIHMQKKMQASSSTEPPITTTTMEPMTTSTMDSMDTTESVVTMTTMPEIDTKIVFEHKQLDTTSRDGETLELKCEASGEPTPTITWLFEKQKLTESRKHKLTKNGSVLKIFPFLNTDIGQYECVASNGEESKSHIFSVSLKESEQPVIIDAPMDTNATIGQQVTLRCNAKGFPVPDVVWLFEGIRIPRRNTRYTISDNNIELTIEKVTRHDSGVFTCQAVNSVGSAVATANLLVGAELTEKVDKLLDDSTIEKIAKEAKQKVEKALSSTKDQQRMDKIESPNDLSKLFKFAINLKKVDLGKAREIYEESIRLVQMHIDNGLAFESAMISPNVSYEAVLPVSYVQTLMEKSGCQTGQFAESCEDHCFFSKYRSYDGQCNNHEHPWWGVSEMAFMRLLPPRYENGFNTPVGWEKGKRYNGYEVPNARKVSRVLIGTDETTPHSHLSAMTMQWGQFIDHDLTLTAPALTRHSYKEGAFCNRTCENADPCFNIQLEADDPKLHTGLYQKHPCMEFERNGAACGSGETSPIFQRVTYRDQLNLLTSYLDASGIYGNSEEQALELRDLYSDHGLLRFDIVSGANKPYMPFEKDSDMDCRRNFSRENPIKCFLAGDVRANEQLGLMSMHTIFLREHNRIASRLLEVNENWDGETIFQETRKLIGAMLQHITYNAWLPKILGKATYNTIIGEYKGYNPDVNPTIANEFATAALRFAHTLINTHLFRFDKDFKETKQGHLPLHNAFFAPERLVSEGGVDPLLRGLFAAPIKMPRPDQVLNKELTEKLFNRFHEVALDLAALNIQRGRDHGLPSWTEYRKFCNLTVPKTWSDMKNIVQNDTVISKLQSLYGVTENIDLWVGGVTEKRTADALMGPTLACIIADQFKRLRDGDRFWYENEEMFSKAQLRQIKKVTLSKIICTNGDDIDRIQRDIFVYHGNSTQFYEPCESLPEINLNMWTTCCDAMCSSSSTLARNAIGGDEKAKRRKRRHHHSKKSCHDKGKRRKSGDRWNHSNDICVECMCHDGEVWCKTNNFCKSQV | 1.11.2.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; | axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; embryonic body morphogenesis [GO:0010172]; muscle attachment [GO:0016203]; negative regulation of axon regeneration [GO:0048681]; regulation of basement membrane organization [GO:0110011]; response to oxidative stress [GO:0006979] | basement membrane [GO:0005604]; extracellular space [GO:0005615] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098;PF07679;PF13855; | 1.10.640.10;2.60.40.10;3.80.10.10; | Peroxidase family, XPO subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20876652, ECO:0000269|PubMed:25475546}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:20876652}. Note=Localizes to the basement membrane in between the epidermis and muscles. {ECO:0000269|PubMed:20876652}. | CATALYTIC ACTIVITY: Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:29250; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O; Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357; Evidence={ECO:0000250|UniProtKB:Q92626}; | null | null | null | null | FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (By similarity). Required for embryonic morphogenesis playing a role in epidermal elongation at the twofold stage of embryonic development (PubMed:20876652). Required post-embryonically for basement membrane integrity and muscle-epidermal attachments, and specifically in the function of basement membrane components such as the type IV collagens (PubMed:20876652, PubMed:29440357). May have a role in inhibiting axon regeneration (PubMed:20876652). May functionally antagonize the peroxidasin pxn-1 (PubMed:20876652). {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:20876652, ECO:0000269|PubMed:29440357}. | Caenorhabditis elegans |
G5EG86 | BRC2_CAEEL | MGDSSKKVKDSFDTISEPDSFDEPKGVPISMEPVFSTAAGIRIDVKQESIDKSKKMLNSDLKSKSSSKGGFSSPLVRKNNGSSAFVSPFRREGTSSTTTKRPASGGFEDFEAPPAKKSTSSSSKKSKKHSKKEKKKEFKEIHADVLRVSRIYEKDKFRIILQESSSTPLILATCSYNRGSDIKFGDRIHVDAEVCKKSSSGDVTEIYIDRVLKNKENGAKSGIRRHSIAKKPFCIKPRFIHELSDTKIKKTVVQVNLLDLNLDFYAGCSKCKHSLPEAANQCEFCKDSQGKSELSMYSRVRVMDFSGQMFINVTTKNMKKLLDLLGYEGFDNWFRFKDPQERQNYVFRPVMVEIEKSNDEWECTDVAEVDWKDFGSYLKHKEDKKKRRSKKKHP | null | null | DNA strand invasion [GO:0042148]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via single-strand annealing [GO:0045002]; egg-laying behavior [GO:0018991]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic DNA recombinase assembly [GO:0000707]; regulation of protein localization [GO:0032880] | condensed nuclear chromosome [GO:0000794]; nucleus [GO:0005634] | single-stranded DNA binding [GO:0003697] | null | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15798199}. Chromosome {ECO:0000269|PubMed:15798199}. Note=Diffusely localized in the nucleus. Recruited to sites of DNA damage upon induction of DNA double strand breaks by ionizing radiation (IR) or in meiosis. {ECO:0000269|PubMed:15798199}. | null | null | null | null | null | FUNCTION: Required for the homologous recombination repair of DNA double strand breaks, thereby playing a role in chromosome integrity (PubMed:15798199, PubMed:16843491). Acts by targeting rad-51 to sites of DNA damage and stabilizing rad-51-DNA filaments by blocking ATP hydrolysis catalyzed by rad-51 (PubMed:15798199, PubMed:16843491, PubMed:17483448, PubMed:18779660). Promotes rad-51 mediated displacement-loop (D-loop) formation during strand invasion between the invading single-stranded DNA (ssDNA) and the homologous duplex DNA (PubMed:16843491). Also functions independently of rad-51 in DNA double-strand break (DSB) repair by promoting DNA single-strand annealing (SSA) when the homologous recombination (HR) and non-homologous end joining (NHEJ) pathways are compromised (PubMed:15798199, PubMed:16843491). Binds selectively to single-stranded (ssDNA) via its C-terminus (PubMed:15798199). Involved in telomere maintenance and replicative senescence (PubMed:27761361). {ECO:0000269|PubMed:15798199, ECO:0000269|PubMed:16843491, ECO:0000269|PubMed:17483448, ECO:0000269|PubMed:18779660, ECO:0000269|PubMed:27761361}. | Caenorhabditis elegans |
G5EG88 | ACH23_CAEEL | MHRIYTFLIFISQLALGLSNNPDIPIQYELANNIMENYQKGLIPKVRKGSPINVTLSLQLYQIIQVNEPQQYLLLNAWAVERWVDQMLGWDPSEFDNETEIMARHDDIWLPDTTLYNSLEMDDSASKKLTHVKLTTLGKNQGAMVELLYPTIYKISCLLNLKYFPFDTQTCRMTFGSWSFDNSLIDYFPRTFTNGPIGLANFLENDAWSVLGTKVNREEKKYTCCPVNYTLLHYDVVIQRKPLYYVLNLIAPTAVITFISIIGFFTSVNPFTNFCNVSSSVHDLRQEKITLGITTLLSMSIMIFMVSDKMPSTSTCVPLIALFYTLMITIISVGTLAASSVIFVQKLGSIGNPPASKTMKWTHRIAPFVLIQMPLVMKQAYAKRAKEEKHRKRMSRKNSMWTKVYHLARDHSKLMETVPDGAVKFNQISDFKNNDIGNMESPRMAESQTSETFAAPMDTSFTESLHIPELNRVASSNSIQSVLKPTEIQLTPYCTRNIVELEWDWVAAVLERVFLIFFTICFLFSAIGINLYGWYIWYTENHFLF | null | null | null | neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23950710, ECO:0000269|PubMed:24212673}; Multi-pass membrane protein {ECO:0000269|PubMed:24212673, ECO:0000305|PubMed:23950710}. | null | null | null | null | null | FUNCTION: Betaine receptor that functions as a ligand-gated non-selective monovalent cation channel in mechanosensory neurons to maintain basal levels of locomotion. The channel is permeable to Na(+) and K(+) but not to Ba(2+) or Ca(2+) ions. Elicits current in response to betaine, very weak current in response to choline, virtually no current in response to acetylcholine and nicotine, and no current in response to glycine and GABA. {ECO:0000269|PubMed:23950710, ECO:0000269|PubMed:24212673}. | Caenorhabditis elegans |
G5EGA3 | ANKL1_CAEEL | MPPNGAITTTPRSRMPPTTPSSGKSRPKKETLHYLAASSSTTSVDAARTLLERGANVNAIDRDGATPLHYACTHDNVAMAQLLLTFGADPMSADKLGRTAYSIAKGNTLRFLRRYKKSSNRQRLGFFRRFFACHSRNETFFIVRNNQEVAPLRPTALAEAASISFNRGNVLTNSYRCAKKKIRATFHAIRRSRSNSTATLQDVVLTSEGIRTVTTPSRRAPKATVYAKRSMSVSDLLLIPDRRDIKNEDVKTRGSPVKKTRGTGRSRTPEAILNPRKQRTPVNHHKRSKSQETKLVAMPSPNSMAYYNTSRARNAGLRPAPSAPPLSPEPAIAAVKTPKTPTTPKTSKGRSKSPANTTAYFTADESLELLGNNMEKLNIESKSAKSSKLKTPSKPTTSSSTSFSSAEDDKEAEVSTPTTVDDGEIRKIRRLREGELKSELKKFGISPAGPLDARTRRLYEKKLLIERRKITNRGYSPDADVVSCRNSPQLELVLRNGFLPADFASRARKCDENVRSEFSGNGFGYNAFCYLIMDPRILGSNVENLTLETFVRSIFYVGKGSKNRPLAHFIDARNERRDKLDKLKTCEKLKTIDELWTLGFGIPRHEISHGVSDEEAFVREASIIEAVKLKNLRNKKAGEFHGTTKSWDNITKSEYGTFLLDRALSTLKLEGIRLITEDNLPDSLYPYVNNRRGAGGGRTPKTPK | 3.1.-.- | null | cell division [GO:0051301]; cellular response to hydroxyurea [GO:0072711]; cellular response to ionizing radiation [GO:0071479]; DNA catabolic process [GO:0006308]; DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in birth or egg hatching [GO:0009792]; mitotic sister chromatid segregation [GO:0000070]; reproduction [GO:0000003]; resolution of meiotic recombination intermediates [GO:0000712]; response to UV [GO:0009411]; response to UV-C [GO:0010225]; response to X-ray [GO:0010165] | condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; nucleoplasm [GO:0005654]; spindle midzone [GO:0051233] | DNA endonuclease activity [GO:0004520] | PF13637;PF03020; | 1.10.720.40;1.25.40.20; | null | PTM: Phosphorylated. Phosphorylated during telophase when localized at the midbody. {ECO:0000269|PubMed:29463814}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}. Nucleus {ECO:0000269|PubMed:29879106}. Chromosome {ECO:0000269|PubMed:29463814}. Midbody {ECO:0000269|PubMed:29463814}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:29463814}. Note=Localizes to foci-like structures outside the nucleus (PubMed:22383942, PubMed:29463814, PubMed:29879106). In pachytene, localizes to foci both in and outside of the nucleus (PubMed:29879106). Colocalizes with air-2 between dividing nuclei in meiosis II (PubMed:29879106). In mitosis, localizes to the center of chromatin bridges that are formed in response to DNA defects (PubMed:29463814). Forms initially a ring like structure encircling chromatin bridges between two separated daughter cells until in late telophase, localizes to the center of chromatin bridges (PubMed:29463814). Colocalizes with air-2 at the midbody (PubMed:29463814). Midbody localization depends on the formation of the central spindle and the midbody and on air-2 (PubMed:29463814). Colocalizes with the central spindle component zen-4 at the central spindle (PubMed:29463814). {ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}. | null | null | null | null | null | FUNCTION: Endonuclease which, in association with baf-1, plays an essential role during embryogenesis in the DNA repair response following DNA damage probably by ensuring proper chromosome segregation (PubMed:22383942). Also required during postembryonic cell divisions after DNA damage caused by ionizing radiation to ensure normal cell proliferation (PubMed:22383942). Resolves chromatin bridges in late mitosis that result from incomplete DNA replication, defective chromosome condensation or unresolved recombination intermediates (PubMed:29463814). Together with brc-1, contributes to genome integrity by resolving mitotic chromatin bridges that result from incomplete processing of DNA breaks (PubMed:29463814). In parallel to the slx-1/mus-81 pathway, acts in processing early recombination intermediates in meiotic prophase I to prevent illegitimate recombination (PubMed:29879106). Also involved in processing remaining, erroneous recombination intermediates that persist into the second meiotic division (PubMed:29879106). {ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:29463814, ECO:0000269|PubMed:29879106}. | Caenorhabditis elegans |
G5EGA5 | FAT2_CAEEL | MTIATKVNTNKKDLDTIKVPELPSVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGLYFAVPYIEHYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLCDYSVYTFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFGLDNIMHNITNGHVAHHFFFTKIPHYHLLEATPAIKKALEPLKDTQYGYKREVNYNWFFKYLHYNVTLDYLTHKAKGVLQYRSGVEAAKAKKAQ | 1.14.19.-; 1.14.19.6 | null | collagen and cuticulin-based cuticle development [GO:0040002]; fatty acid elongation [GO:0030497]; innate immune response [GO:0045087]; reproduction [GO:0000003]; unsaturated fatty acid biosynthetic process [GO:0006636] | membrane [GO:0016020] | delta12-fatty-acid desaturase activity [GO:0102985]; oxidoreductase activity [GO:0016491]; palmitoleic acid delta 12 desaturase activity [GO:0102987]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF11960;PF00487; | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383, ChEBI:CHEBI:57387; EC=1.14.19.6; Evidence={ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:22041902, ECO:0000269|PubMed:26806391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25857; Evidence={ECO:0000269|PubMed:26806391, ECO:0000305|PubMed:10775428, ECO:0000305|PubMed:11972048, ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:45096, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:61540, ChEBI:CHEBI:76552; EC=1.14.19.6; Evidence={ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45097; Evidence={ECO:0000305|PubMed:10775428, ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:66040, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383, ChEBI:CHEBI:74034; Evidence={ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66041; Evidence={ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(9Z)-heptadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-heptadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:42196, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74308, ChEBI:CHEBI:78690; Evidence={ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42197; Evidence={ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(9Z)-pentadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-pentadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:42192, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74310, ChEBI:CHEBI:78684; Evidence={ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42193; Evidence={ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:42180, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57363, ChEBI:CHEBI:71489; Evidence={ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42181; Evidence={ECO:0000305|PubMed:22041902}; CATALYTIC ACTIVITY: Reaction=(9Z)-tetradecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-tetradecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:42176, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:65060, ChEBI:CHEBI:78680; Evidence={ECO:0000269|PubMed:22041902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42177; Evidence={ECO:0000305|PubMed:22041902}; | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:26806391}. | null | null | FUNCTION: Can function as a Delta(12)/Delta(15) bifunctional desaturase and behaves as a nu +3' desaturase. Introduces a double bond in the fatty acid chain three carbons away from an existing double bond to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a number of substrates like oleoyl-CoA ((9Z)-octadecenoyl-CoA, 18:1n-9), palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA, 16:1n-7), and gamma-linolenoyl-CoA ((6Z,9Z,12Z)-octadecatrienoyl-CoA, 18:3n-6), to generate linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, 18:2n-6), (9Z,12Z)-hexadecadienoyl-CoA (16:2n-4) and (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA (18:4n-3) respectively (PubMed:10775428, PubMed:11972048, PubMed:22041902, PubMed:26806391). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (Probable). {ECO:0000269|PubMed:10775428, ECO:0000269|PubMed:11972048, ECO:0000269|PubMed:22041902, ECO:0000269|PubMed:26806391, ECO:0000305|PubMed:10775428}. | Caenorhabditis elegans |
G5EGB2 | LIN29_CAEEL | MDQTVLDSAFNSPVDSGIAGTTTGSGSTTHFGVGTNFKVSVRSSSRSTDGTDSTDGANSDNVTGSTGSTPAHHSITNLNMALSQHSIDSATAASSTNPFPHFNQADLLNFHQNSLLPHHMFSQFGRYPQFEQKPDVGVLQQQMQMREAKPYKCTQCVKAFANSSYLSQHMRIHLGIKPFGPCNYCGKKFTQLSHLQQHIRTHTGEKPYKCKFTGCDKAFSQLSNLQSHSRCHQTDKPFKCNSCYKCFTDEQSLLDHIPKHKESKHLKIHICPFCGKSYTQQTYLQKHMTKHADRSKASNFGNDVVPADPFDPSLLSWNPMQGMGDNAHDSSSFNISSLTDQFAANTMIGSQSTNYNPAFQNSAFSQLFNIRNNRYLSEYPTSTKNGERAPGFNMITPLENIQRYNGSSSSATAVVTATGSAVVSSTPSSTSSSSAGSSSSQGGVFNPQSLINNMKNHSY | null | null | cell fate specification [GO:0001708]; cell-cell fusion [GO:0140253]; cellular lipid metabolic process [GO:0044255]; collagen biosynthetic process [GO:0032964]; cuticle development [GO:0042335]; cuticle pattern formation [GO:0035017]; exit from mitosis [GO:0010458]; male genitalia morphogenesis [GO:0048808]; molting cycle process [GO:0022404]; negative regulation of dauer larval development [GO:0061067]; positive regulation of gene expression [GO:0010628]; positive regulation of vitellogenesis [GO:1903188]; programmed cell death involved in cell development [GO:0010623]; regulation of basement membrane organization [GO:0110011]; regulation of development, heterochronic [GO:0040034]; regulation of nematode larval development, heterochronic [GO:0090444]; regulation of Notch signaling pathway [GO:0008593]; regulation of programmed cell death [GO:0043067]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of vulval development [GO:0040028] | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32223899, ECO:0000269|PubMed:8756296, ECO:0000269|PubMed:9334281, ECO:0000269|PubMed:9986728}. Note=Accumulates in nuclei of hypodermal cells in a temporally restricted fashion, beginning during the larval L4 stage. {ECO:0000269|PubMed:8756296}. | null | null | null | null | null | FUNCTION: Transcription factor which regulates the expression of various genes, including those involved in cuticle synthesis and maintenance, such as collagens, and in lipid metabolism (PubMed:27401555, PubMed:29604168, PubMed:31974205, PubMed:7671813). Binds to promoter regions of genes, at 5'-[(T/G)TTTTTT(A/T/C/G)]-3' consensus sequences (PubMed:25905672, PubMed:29604168). Heterochronic protein which controls the choice of stage specific cell fates, including at the juvenile to adult transition (PubMed:32223899, PubMed:7671813). Promotes differentiation, together with transcriptional cofactor mab-10, perhaps as part of a transcriptional complex (PubMed:21862562). Required for vulval morphogenesis and egg laying; perhaps by acting in a subset of the lateral seam cells (PubMed:9334281). Involved in the exit of seam cells from the cell cycle (PubMed:32223899). Required for specification of uterine pi-cell fate, acting upstream of lin-12 Notch signaling, perhaps via maintenance of lag-2 expression in the anchor cell (AC) (PubMed:11114514). Involved in morphogenesis of the specialized male tail used in mating (PubMed:9986728). Acts cell non-autonomously from the hypodermis to regulate expression of genes in the intestine, including genes involved in lipid metabolism (PubMed:27401555, PubMed:31974205). May regulate vitellogenesis via the mTORC2 signaling mediated pathway, independently of daf-16 (PubMed:27401555). May promote nuclear accumulation of mab-10 in seam cells post-transcriptionally (PubMed:21862562). Dispensable for seam cell fusion (PubMed:32223899). {ECO:0000269|PubMed:11114514, ECO:0000269|PubMed:21862562, ECO:0000269|PubMed:25905672, ECO:0000269|PubMed:27401555, ECO:0000269|PubMed:29604168, ECO:0000269|PubMed:31974205, ECO:0000269|PubMed:32223899, ECO:0000269|PubMed:7671813, ECO:0000269|PubMed:9334281, ECO:0000269|PubMed:9986728}.; FUNCTION: [Isoform c]: Required for seam cell fusion. {ECO:0000269|PubMed:32223899}. | Caenorhabditis elegans |
G5EGC9 | PES1_CAEEL | MTSSIKSDAPQFLLDLDNCSSLPPTPPKTASPGNSKMKGFNISDLCLDLDSSTSSSCSVSPASSFHTRSESVGQQQSGRNSPVSSSTESPTKRPKYSYNALIAMAIQSSPFKSLRVSEIYKYISSNFSYYKNQKPLQWQNSVRHNLSLHKEFRKVRTLDGKGSYWAMTADLGTDVYISNNCGKLRRQKSKVAKFPPMQQHFPIPQLPTQNIHQLCMQNPQILATLLQNMYLQNMQNLQNIPMVPGFPIIPVPINPTSFHFPKSS | null | null | anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; embryo development ending in birth or egg hatching [GO:0009792]; nematode larval development [GO:0002119]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; 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] | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:8162851}. Cytoplasm {ECO:0000269|PubMed:8162851}. | null | null | null | null | null | FUNCTION: Transcription factor (By similarity). Plays a role in embryogenesis and later development, perhaps acting redundantly with forkhead protein fkh-2 (PubMed:11044397). {ECO:0000250|UniProtKB:Q12952, ECO:0000269|PubMed:11044397}. | Caenorhabditis elegans |
G5EGD2 | HIF1_CAEEL | MEDNRKRNMERRRETSRHAARDRRSKESDIFDDLKMCVPIVEEGTVTHLDRIALLRVAATICRLRKTAGNVLENNLDNEITNEVWTEDTIAECLDGFVMIVDSDSSILYVTESVAMYLGLTQTDLTGRALRDFLHPSDYDEFDKQSKMLHKPRGEDTDTTGINMVLRMKTVISPRGRCLNLKSALYKSVSFLVHSKVSTGGHVSFMQGITIPAGQGTTNANASAMTKYTESPMGAFTTRHTCDMRITFVSDKFNYILKSELKTLMGTSFYELVHPADMMIVSKSMKELFAKGHIRTPYYRLIAANDTLAWIQTEATTITHTTKGQKGQYVICVHYVLGIQGAEESLVVCTDSMPAGMQVDIKKEVDDTRDYIGRQPEIVECVDFTPLIEPEDPFDTVIEPVVGGEEPVKQADMGARKNSYDDVLQWLFRDQPSSPPPARYRSADRFRTTEPSNFGSALASPDFMDSSSRTSRPKTSYGRRAQSQGSRTTGSSSTSASATLPHSANYSPLAEGISQCGLNSPPSIKSGQVVYGDARSMGRSCDPSDSSRRFSALSPSDTLNVSSTRGINPVIGSNDVFSTMPFADSIAIAERIDSSPTLTSGEPILCDDLQWEEPDLSCLAPFVDTYDMMQMDEGLPPELQALYDLPDFTPAVPQAPAARPVHIDRSPPAKRMHQSGPSDLDFMYTQHYQPFQQDETYWQGQQQQNEQQPSSYSPFPMLS | null | null | apoptotic process [GO:0006915]; cellular response to caloric restriction [GO:0061433]; cellular response to hypoxia [GO:0071456]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; negative regulation of apoptotic process [GO:0043066]; phosphorelay signal transduction system [GO:0000160]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to axon injury [GO:0048678]; response to hypoxia [GO:0001666] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF00989;PF14598; | 3.30.450.20; | null | PTM: Hydroxylation on Pro-621 by egl-9 during normoxia conditions is required for vhl-1-mediated proteasomal degradation. {ECO:0000269|PubMed:11595184}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:19889840}. | null | null | null | null | null | FUNCTION: A transcription factor which is a key regulator in various cellular processes; including environment stress resistance (oxygen levels, hydrogen sulfide and cyanide levels and heat), negative regulation of cell apoptosis in ASJ neurons by inhibition of cep-1 via transcriptional activation of tyr-2, resistance/susceptibility to pathogenic bacteria, lifespan and brood size (PubMed:11427734, PubMed:12006646, PubMed:12686697, PubMed:15781453, PubMed:18477695, PubMed:19461873, PubMed:19889840, PubMed:20400959, PubMed:20520707, PubMed:21093262). Involved in mediating susceptibility to enteropathogenic E.coli (PubMed:16091039). Increased levels of hif-1 activity confer resistance to P.aeruginosa-mediated death but also confer susceptibility to S.aureus infection (PubMed:20865124, PubMed:22792069). Required for aha-1 nuclear localization (PubMed:11427734). Following hypoxic stress, up-regulates serotonin levels through activation of tph-1 expression (PubMed:20400959). Role in life span extension is dependent of temperature (PubMed:21241450). Not required for survival in anoxic conditions (PubMed:11427734). Involved in iron homeostasis by repressing transcription of ferritin ftn-1 and ftn-2, and divalent metal transporter smf-3 (PubMed:22194696, PubMed:22396654). May be involved in manganese homeostasis by repressing divalent metal transporter smf-3 (PubMed:22194696). {ECO:0000269|PubMed:11427734, ECO:0000269|PubMed:12006646, ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:15781453, ECO:0000269|PubMed:16091039, ECO:0000269|PubMed:18477695, ECO:0000269|PubMed:19461873, ECO:0000269|PubMed:19889840, ECO:0000269|PubMed:20400959, ECO:0000269|PubMed:20520707, ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:21093262, ECO:0000269|PubMed:21241450, ECO:0000269|PubMed:22194696, ECO:0000269|PubMed:22396654, ECO:0000269|PubMed:22792069}. | Caenorhabditis elegans |
G5EGE9 | DPY26_CAEEL | MDVPSSSNVTGRRKRQVLDDDEDDGFRSTPLRKVRGTKKIRPADVVPETIMTKIGAHIDDIVNKKKVGELNCFEYKSPLEIHTIEDMIKAKASIQEMAVVLEGAQCIIGYRVDRLHHDVRQIDSALSSGTVMRDSNGEEIHLTLESRKAKKKMAVVDGMNGMLDFLNNMDDALTTTELDADNDKNWKEDEENIAGEPRIDFKANSKDVDAFLQRDIFPEKLIYALSIKRATDLRADLLSDVSNYISADDTAHDLKDANIDWLRANPTFQKATKGSVCNSSNSFHSLNYYGIHSPDGRTLMLHNRIADKNADDRFFTSDVSVSLVKNTRALLTNSLDKKPRILDNYLMLEVKDRPVIGRYKIMSKDVKKSTLPLAESSREKDLANLTFAEMNHRPSNLDMTVAGASDMSMLPGNQGLPLAQGENDETIALDRLTPPLQSSVSQKASDEYVLPPLEANDLDEHLIGKLPIEPNEMDQTLANMFDKKLEVFNTSDTLESKVWKNGIRAEEWGEDDEAIMKNDTKHPRQAGIEGWIKATDAWTNYDVVKMNVNREARSQLDENAIDEQESYRNMVPEIGKNLFLVKSDDYMNNYPGDRPADFTVNDEVSDVMKMWSGEDSTAEDDVPLEQIQQEIREQVQQQDVDMEPIEEMDYDAGGAAFDVDFDDRLAAPVEVEEMEGDNNRNDGRVADILFNEQMDETEVEERNEQDVQRELEDIALAADEVAELMTSAPPPQLVGPSAEMREEIQNIGKNDNAHWVPPVVGDQERQAAVTAQRKRREKKAKSRKATVEDFVHYFRDIPDDEIEREITAAKCSKIADEKSTFLSEQQLYLPTLGIENKPHVAFEMGLLGNSGMFFKKSYGKIRLERVKNQKAEQDLFIDEARGNKDSDCLNWLLSFSGFRCMENPEPITGSDSDENLRTAVEQPFDDDFANDYYDEDRYDPNYEQQLAAAQMGPDMQRKLALTASHINQMFPNIHSKRYGGEYGDSDDEFDDSFDRQSIQAKNLDAAKHKKCLAEILKTDSLSMPSIQYVLEQLTSNQTLRMNNTTIRAADDRNETGRPATPTMEADKTLTSVFDYRSPNKSNHDVNETMKALTEMPDYQAADERPNNQPTTSTYGTANTENRKVHINGCHTLLSLALSMPSRMGETVRPSSIVSFLLHIANENNLQIVQDRSKRSWMSDFIVLNSSESLPRGLKMGRIEDQDEFWKRTQDPDAIEGTASDANNVFSNLMRRPKAVPVRKGRGAGGQPTTSDLGAIVEEEEMEE | null | null | cell division [GO:0051301]; chromosome condensation [GO:0030261]; dosage compensation by hypoactivation of X chromosome [GO:0042464]; meiotic chromosome segregation [GO:0045132]; meiotic sister chromatid segregation [GO:0045144]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of gene expression [GO:0010629] | condensed nuclear chromosome [GO:0000794]; condensin complex [GO:0000796]; dosage compensation complex [GO:0046536]; nuclear chromosome [GO:0000228]; X chromosome [GO:0000805] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. Chromosome {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. Note=During meiosis and mitosis, localizes to condensed chromosomes (PubMed:8939869). In interphase cells, diffusely distributed in nuclei of hermaphrodite embryos prior to the onset of dosage compensation (PubMed:8939869). Localizes to the X chromosome after the 40-cell stage when dosage compensation is initiated in hermaphrodite (XX) but not in male (X0) embryos, where it remains diffusely nuclear (PubMed:18198337, PubMed:8939869). {ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. | null | null | null | null | null | FUNCTION: Required for both chromosome condensation and segregation and for X-chromosome dosage compensation depending on its binding partners (PubMed:19119011, PubMed:19781752, PubMed:2917714, PubMed:8939869, PubMed:8939870). Member of the condensin I complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes and for proper chromosome segregation in mitosis and meiosis (PubMed:19119011, PubMed:19781752). As a member of the condensin I complex, further controls the crossover number and distribution in meiosis by restricting double strand break formation, probably by influencing higher-order chromosome structure (PubMed:18198337, PubMed:19781752). Plays a role in robust cytokinesis upon presence of chromatin obstructions (PubMed:23684975). Also a member of the condensin I-like dosage compensation complex that associates specifically with hermaphrodite X chromosomes to reduce their gene transcription during interphase, possibly through chromatin reorganization (PubMed:19119011, PubMed:19781752, PubMed:2917714, PubMed:8939870). As a member of the dosage compensation complex, also binds to regulatory regions of the autosomal her-1 gene, required for male development, possibly contributing to its repression in hermaphrodites (PubMed:11937488). {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:2917714, ECO:0000269|PubMed:8939869, ECO:0000269|PubMed:8939870}. | Caenorhabditis elegans |
G5EGF4 | EGL18_CAEEL | MSISIMTETRPESAEQQHHEVLQRPSDEPCSGCKQLQKDVAKTISMVMERMDKLQYRLDELLKENNELKSSSVSSGKASPSPAESRSSPKLVETVVAPVSGARKRKPKERSPPAAASPLPDFSNLMNGFMFDPLNMSNPNGMMQLLSMVQQQQQQQQHHQHIENQQSVSPPQSKSVKIEDPMDQDVKQEESERSDIPTATEAQNLLDALTAQFSSNGQATSTTSPPSSSSQVQAVIEAVATPSSQSQDSSMFEKTETSGDPNAARCSNCRTDKTTAWRRDAEGKLVCNPCGLYYRLHKVRRPIEMRKNHIQQRYRRKNKEKESSAATQIFNQLLTQMPTMATGGVSTDGAINTFNLLEQISQFTQAQELMNSSATF | null | null | cell fate commitment [GO:0045165]; cell fate specification [GO:0001708]; membrane fusion [GO:0061025]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode larval development [GO:0002119]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; 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: Probable transcription factor (PubMed:11532911, PubMed:24885717). Involved in embryonic development and in vulval development in larvae, acting redundantly, at least in part, with elt-6 (PubMed:11532911, PubMed:12399309, PubMed:14975731, PubMed:24885717). Perhaps acting together with elt-6, may form a positive feedback loop to initiate and maintain lin-39 gene expression to ensure proper vulval precursor cell (VPC) fate specification (PubMed:24885717). Together with elt-6, acts as a downstream target of the Wnt/beta-catenin asymmetry pathway, required to adopt or maintain the seam cell fate (PubMed:23633508). Required in seam cells, acting redundantly with elt-6, to promote production of alae, expression of several seam-specific genes and maintenance of seam cells in an unfused state (PubMed:11532911, PubMed:23633508). Plays a role in longevity (PubMed:18662544). May form a transcriptional circuit with GATA factors elt-3 and elt-6 (PubMed:18662544). {ECO:0000269|PubMed:11532911, ECO:0000269|PubMed:12399309, ECO:0000269|PubMed:14975731, ECO:0000269|PubMed:18662544, ECO:0000269|PubMed:23633508, ECO:0000303|PubMed:11532911}. | Caenorhabditis elegans |
G5EGH6 | FAT7_CAEEL | MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFISRQVANHGSEESRKKSIM | 1.14.19.-; 1.14.19.1 | null | fatty acid biosynthetic process [GO:0006633]; intracellular oxygen homeostasis [GO:0032364]; post-embryonic development [GO:0009791]; response to hypoxia [GO:0001666]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum membrane [GO:0005789] | 16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; iron ion binding [GO:0005506]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932; Evidence={ECO:0000269|PubMed:16839188, ECO:0000305|PubMed:10872837}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + heptadecanoyl-CoA + O2 = (9Z)-heptadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36951, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74307, ChEBI:CHEBI:74308; Evidence={ECO:0000269|PubMed:10872837}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36952; Evidence={ECO:0000305|PubMed:10872837}; CATALYTIC ACTIVITY: Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36935, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296, ChEBI:CHEBI:74297; Evidence={ECO:0000269|PubMed:10872837}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36936; Evidence={ECO:0000305|PubMed:10872837}; | null | PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}. | null | null | FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols (PubMed:10872837, PubMed:16839188, PubMed:29237573). Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used by several other desaturases and elongases as substrates to synthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes) (PubMed:10872837, PubMed:16839188, PubMed:29237573). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). Partially inhibits expression of genes involved in beta-oxidation, such as ech-1 and acs-2, perhaps signaling via the actions of one of its fatty acid products (PubMed:15719061). May form part of a negative feedback loop with the transcription factor nhr-49 to limit beta-oxidation, in which nhr-49 stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation (PubMed:15719061). {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:15719061, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}. | Caenorhabditis elegans |
G5EGJ5 | IDA1_CAEEL | MRFFHSIIVLLFSISTGSAFLLYGCNLSENLCDNDESCYPDGVFGQCYSSESGSPEPTVLDNLDDTQLELLKLELTRLAAKDKDWGDEETQCVLAYFKMSMFYQLQYDPDFCQVRKPANVWALIQLIDTGLTEDPTILDEDVNPENVTDEDMAQIIEQLKEPSLPTEEDIEEALNAQNEDVDDEILDQYVQAVVNNENPDFSELSDGQLNILIGRLVDLKKNVENEEAQLLTGDGEQEMAVPLDDLEERGEQAILKKDIEQVGEINQGLDNTEHKIVKGRKDQVVTRVDANRVYLKVHLKNEDQLMPLIEFLQNTIAIPNNLYFDDFQFENGQLSMRISRFEGAKPKADKRIDSVEGVASAVYKRRKDIARLSGADVRETGIGSGEDGSLPVESSERDWLLMPVLFVCAFTVTALGLVAAVQIARSRRHYKDNIQQIAEQLDGKNSFAYQDLCRQRADGGRASKSSSTSSWCEETAVPTIDISTGHVVLNFLQEYLSEPTKIEAQWNGIKDYRNEERTKTKAEKFASQNRTILPFDDNIVDIDGKTAENEDFYLNASFIYDDDPRQAVYIAAQTPASSQIAAFWQTIWQHGVCLVVNLSTPEECKQEKNYWPDTGSEVHGAFEIHLVSEHIWSDDYLVRSFYLKNLQNSQTRTITQFHYLSWQKESTPTSAKSILEFRRKVNKSYRGRSSAVLVHSWDGSGRTGVYCAVDVLCARLLRGIRQIDVVATVEHLRDQRDGMVATGDQFKLVYGCVAQEVNHLLKSIATK | null | null | dephosphorylation [GO:0016311]; exocytosis [GO:0006887]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; positive regulation of anterior/posterior axon guidance [GO:1905488]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of secretion [GO:0051046]; ventral cord development [GO:0007419] | axon [GO:0030424]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dense core granule [GO:0031045]; perikaryon [GO:0043204]; secretory granule [GO:0030141]; synapse [GO:0045202]; trans-Golgi network transport vesicle [GO:0030140] | transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 8 subfamily | PTM: Proteolytically cleaved probably at a dibasic consensus sequence by egl-3. {ECO:0000269|PubMed:15180830}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:15180830, ECO:0000305|PubMed:15044551}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell projection, axon {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell projection, dendrite {ECO:0000269|PubMed:15180830}. Note=Localizes to dense-core vesicles along axons. {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. | null | null | null | null | null | FUNCTION: Regulates dense-core vesicle (DCV) trafficking and/or secretion (PubMed:19343207). Probably by controlling DCV trafficking, plays a role in the AVG neuron-mediated formation of the right axon tract of the ventral nerve cord (PubMed:27116976). Involved in locomotion by regulating acetylcholine release (PubMed:15044551). Probably by controlling the secretion of FLP neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Plays a role in preventing dauer formation (PubMed:15044551). {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:19343207, ECO:0000269|PubMed:27116976}. | Caenorhabditis elegans |
G5EGJ9 | DEP1_CAEEL | MIRWKYELHSLIWLFLVLHLSKCQSDSLTTSAEQHELFAIKKDSLSPWSQILVSLPRRHPLYQSFAAKIQDVTENISDEVRDSNKTFVSSDDAPYSIRIHALRAGHRYSIAIHGQKDGSTSLIKEESVVMDPRAPDFRSMDSDIQVAEHNITMRTIKNDSYLQDSFSIEYRQINPDKKFPVLQILDIPEQKNLEFYLGNLNSGFDYSVRVIAHKDGMSSRPWISTLTTKPSPLKEVNINQNAGSCVEVSWQNDEFSGADFYTIQYSLQSTPNNSTNMTIPSTESSISICDSMLQGEAYQIIATVQKGGQVSEPLITKFQLRPLPPIDFRVRADLKRGKYKLLAELPTSSKIDKCQITVAGDEAERSVNYANIEQTKSGHKICWFNFALSPGERFDFSISSMANESASQKLQKSIVLTPAFDFNAFGLTLQESNGGIELIWPKSEVFMTRVKDIWNKVVGAESLLNMRITPIGNNDETDKTLKFETSPKNIDPVFAKNLVKGACYRVQLFTVTKTGIISETRHNETIRMSSPAVNVSLESVTRSSATLRIVFSTHHDSTSISNCQMHIVVRDMNGKSVFDKRMQLTATFAPLLNLDGLSPFHKYTVNTQIICGSGSSETPQCPAATRTMRQLSFSTRQDKPAAVQDLKVEPLNSYSVMLTWLPPALPNGILTHYAVNVTKIGSDETRTIDVGVSSNRSDHTVQVVIDELFGGHTYSFSVRAVTEAGFGENSPVVPTVSMPLMAPPVPTVAPMIMKESVGSHNMIVRFPTTMFDNRNGEIKQFAIIVSETTADESINRWIESDNGTYTWQQVQRFDVWPSYVAKLQDIQKVKQDVDVSIFEELGEDETCLEVRADRICNGPLRSASKYRVRIRLFTSPTLFTDSPPSQVMTTGSATPAIPLLTVVAVLIVIAFVGIVGTIFLFFWNRTKKARLAAAAFKNGPSKEKESQWEALKMMMAERAADCLAKLGLDATTPPPSSTTSSNSPTSTSTTMTDCGSNPHLGAPNAGGHRRTRSLRERTGVEHRLERLSSGPVHRTPLYTVVTGANTNKSRPVRIEDFADHVRLMSADSDFRFSEEYDMMRNVGVGQSVAASELPINRPKNRFTNIPSYDHSRVKLSNPNNIEGGDYINANYVPGFSSRREFIAAQGPLPTTRDHFWQMTWEQQCPAIIALTKCVEKGRDKCHQYWPDHENVPVLYGDIEVTIVAEKEFDEFVIRDIRLEKSGPDGRVTRFVRHWHYMAWPDFGAPSHPNGIIQFSRMFRHHLPHSPHNAPTIVHCSAGVGRSGTFISIDRLLQSSSFGDPIDVFGTVCEMRYERCQMVQNEQQYIFIHYCILQVLQGSSPSPTSTSTGAHHNAGFVQDGQMIVESGF | 3.1.3.48 | null | positive regulation of vulval development [GO:0040026]; protein dephosphorylation [GO:0006470]; vulval cell fate specification [GO:0072327] | membrane [GO:0016020]; receptor complex [GO:0043235] | phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725] | PF00041;PF18861;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 3 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes in intracellular punctate structures in vulva cell precursors which partially colocalize with let-23. {ECO:0000269|PubMed:15901674}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:28135265}; | null | null | null | null | FUNCTION: Phosphatase which may dephosphorylate receptor let-23 and thereby regulate cell fate during the development of the vulva and the excretory system (PubMed:15901674). By inhibiting let-23 signaling prevents the establishment of a primary cell fate in the descendants of vulva precursor cells P5.p and P7.p (PubMed:15901674). Similarly, may prevent duct cell fate in ABpr precursor (PubMed:15901674). Also dephosphorylates the beta-integrin subunit pat-3, probably within the alpha pat-2/beta pat-3 integrin receptor complex, which leads to down-stream effects including the negative regulation of let-23 signaling and vulval induction (PubMed:28135265). In particular, by dephosphorylating pat-3, promotes the recruitment (by unphosphorylated pat-3) of the cytoplasmic adapter protein tln-1 to the plasma membrane of secondary vulval precursor cells (PubMed:28135265). This promotes the linking of focal adhesion sites to the F-actin cytoskeleton, and also acts to restrict the mobility of the let-23 receptor on the plasma membrane of vulval cells thereby attenuating let-23 signaling (PubMed:28135265). {ECO:0000269|PubMed:15901674, ECO:0000269|PubMed:28135265}. | Caenorhabditis elegans |
G5EGK5 | CAM1_CAEEL | MSPRPEDDDLVIEPADDEGLHYGNASMEGTSTGQRPYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNVPDAVKLSQKKGSHHSTKHIAFDEYEDYEMMDRGRLPDEEDADLYRVPDSAAGSNYAPVAVSERWLDGIKYRVGDCVQYRGEACRQYLSNKFVMMTNESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNNQIVSICKHDCDVIQNDECPSELALAAQHELVGDTPKALFPLCSRLSSTSNCIPVMSTALQSSPVAEVNRGHLTHWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTSRDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQEEYCDVPQCPSDMYPHLNDKKVEGSTKGGVSESVTALWDSLDPTMQVALVGGGVFFSLLLLLLFCCACCCRAKKKSQKTRHQNAHCSSAPSVINSAANSAYYRKLNGTSTPIMGRVPPHVEMTSLLPSAQHLGPPPYPMDQHLQQARRFPSQEPIDDNSYKVFEITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASPAHSILQQHNNRAGSHSGSSGAGRPPTHQRGYPSQKLHRRVEGASPLMKRHDANYAYSEDGDSD | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25029443}; Note=Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305}; | axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of neuroblast polarity [GO:0045200]; interneuron migration [GO:1904936]; motor neuron migration [GO:0097475]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; phosphorylation [GO:0016310]; positive regulation of neuron projection development [GO:0010976]; sensory neuron migration [GO:1904937]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; Wnt signaling pathway [GO:0016055] | axon [GO:0030424]; cell projection [GO:0042995]; dendrite [GO:0030425]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; frizzled binding [GO:0005109]; metal ion binding [GO:0046872]; neurotrophin binding [GO:0043121]; neurotrophin receptor activity [GO:0005030]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147] | PF07679;PF00051;PF07714; | 1.10.2000.10;2.60.40.10;2.40.20.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ROR subfamily | PTM: Autophosphorylated at tyrosine residues which are probably located in the activation loop (residues 724-732). Autophosphorylation does not increase kinase activity in vitro. {ECO:0000269|PubMed:25029443}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:15944127}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}. Cell projection, dendrite {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}. Perikaryon {ECO:0000269|PubMed:15944127}. Synapse {ECO:0000269|PubMed:15944127}. Note=Localizes in punctate structures along neuronal processes where it partially colocalizes with synaptic vesicle marker snb-1 (PubMed:15944127). Localizes in punctate structures in the axons forming the nerve ring and in proximal AIM neurites destined for elimination (PubMed:19561603). Enriched at the distal tips of muscle arms where they interact with ventral nerve cord (PubMed:15944127). {ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}.; SUBCELLULAR LOCATION: [Isoform b]: Cell membrane {ECO:0000269|PubMed:10556063}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:10556063}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PIRNR:PIRNR000624, ECO:0000269|PubMed:25029443}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.53 mM for ATP (in the presence of Mg(2+) at 20 degrees Celsius) {ECO:0000269|PubMed:25029443}; KM=0.45 mM for ATP (in the presence of Mn(2+) at 20 degrees Celsius) {ECO:0000269|PubMed:25029443}; Note=Autophosphorylation gives similar KM values for ATP. {ECO:0000269|PubMed:25029443}; | null | null | null | FUNCTION: Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-2 and cwn-1 (PubMed:17942487, PubMed:25029443). Involved in the final positioning of migrating ALM, CAN, BDU and HSN neurons during development (PubMed:10476968, PubMed:14651925, PubMed:9165130, PubMed:9475729). Involved in the anterior-posterior migration of QR neuroblast descendants, QR.p and QR.pa, by maintaining QR.p cell polarization, probably through mig-2 (PubMed:25373777). In addition, plays a role in ASI sensory neuron positioning and functions (PubMed:10556063). Regulates asymmetric division of V cells (seam cells) and CA/CP neuroblast, and axon outgrowth (PubMed:10476968, PubMed:14651925). Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring by controlling axon guidance of SIA and SIB neurons (PubMed:19855022). Involved in synapse plasticity by regulating delivery and/or stabilization of acetylcholine receptor acr-16 at post-synaptic membrane sites and the distribution of synaptic vesicles at pre-synaptic release sites (PubMed:15944127). Probably by acting as a receptor for Wnt ligands cwn-1 and cwn-2, negatively regulates developmental neurite pruning of AIM neurons (PubMed:19561603). Plays a role in ALM neuron polarity (PubMed:25917219). By binding Wnt ligands mom-2, cwn-1 and egl-20 and thereby restricting their availability, negatively regulates Wnt signaling. This mechanism is involved in HSN neuron and QR neuronal descendent migration, and in vulva development (PubMed:15371357, PubMed:17942487). Involved in dauer formation, locomotion, tail morphology and egg-laying (PubMed:10556063, PubMed:14504222, PubMed:9475729). May be involved in distal tip cell (DTC) migration during the development of the posterior gonad (PubMed:10556063). {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:10556063, ECO:0000269|PubMed:14504222, ECO:0000269|PubMed:14651925, ECO:0000269|PubMed:15371357, ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:17942487, ECO:0000269|PubMed:19561603, ECO:0000269|PubMed:19855022, ECO:0000269|PubMed:25029443, ECO:0000269|PubMed:25373777, ECO:0000269|PubMed:25917219, ECO:0000269|PubMed:9165130, ECO:0000269|PubMed:9475729}.; FUNCTION: [Isoform a]: Involved in the positioning of the nerve ring. {ECO:0000269|PubMed:19855022}.; FUNCTION: [Isoform b]: Involved in the positioning of the nerve ring. {ECO:0000269|PubMed:19855022}. | Caenorhabditis elegans |
G5EGK6 | DIN1_CAEEL | MVQVPSTNTVKESRHVAISGLPSTLPDDRLQLHFTKFGEIQRLVRQHGNPEIVLVSYMDARGALRARSTKPQFEDSIEYKISAYIPEPTQNSSMASMSSTPSSGQSSSPRNAELSPQRYGDTRGAEVKSPSFRNQMEARRGGPHLSVQSQQRHSREYWPIPEFPSESTACVVYEIQSGSTPERDLFELVKKHSKRSGVPIDIQLESTTEPGWKKARVHYYRLDTDGLKADKSLILGRPPKFRVYYPTSGEQKHPQCHPSTSYAIPKLKGDHLLKASCSVHVPHLDRHSPDHYRRRFESYGQVIDVDMVKSNDNKAFAVVQFTNIDDAQKALQDTNIPKPMSYQSRPSHRIIIFYLPIECTNEEIMLIIRSLSDRIVDICVDWWDRSAVITLDDMEPANLLLKRMKLVGRNNFGEHKVAVDFCSDRFNLYFINRKKENIEVAARSSSPTSKSENDQGSSSPSSSRDRQNLHDPLQTRSSVEHHTNQEDQENNASGSDSSSDSDSEEGSSSSNEDSDEQNDVDEEDDEDVVSEEKRHEPEEGKSSSPGNGHRDESNGDKDHEDSSERFSQPSTSSHHETSHSPEKDSEAYQSRSFSPLNYQSQSPGYEFLESKEIKQEFSPTTSSASSSDLELDMEMPDNPLTRMLERMHWRPFIDVSSFVNRIDEIVELNQKARASYEKFTGRPFPKCNNDEVLSIQKIVFHEPRDYYYYENPCSELEVRIRDWRKLSDTADLDDFRATDSKELGRDQPAGGRTSGRPSLDESRTNRLSFDSTHHPAELAQRSHSLCIGPMTPSTPFPTSQPLLVNTTHLPGTSQPSTSGGITTPRSSQPPPLMSPVSRHNSMSSTGRPASIQTLRHQSVMFPPDVSIPPPPIPPTHDEMMAPRGTPPSRRSSETMVPLRSPPFGTPIQNLLTMPIVPPPHLIAATSTGTHSVSSSAHSTPRHSISGTPVHCEPSNSKTSQPPTPKSRPEKVQIRHDTISKSGPSNAINALQARSQSMTSGDPKKSAPSTPVVRDAGSDLVAQIMSNQPNLGLRKLPRIEKKSSALQNIQNHQPPHSNANSTPSTPSTSTHQAMFKDKEKERKKKEKEKEEREREARREMKRKETKEERNKRKEMERAKRLEDERQERKREKKKERDERKKEKEKVRKKAEKEKLKKKKHRKGDSSDESDSDSNDELDLDVRKSTKEMTQEEKDHQLALLLSKGGIIENLKSRRRSDKRAHDSFEKMQQKSQQRRVLIESSDDEGGKDGDKGNSSNGEESDSEKADLPPPPAPPSLSESADQRLKVLKEREKGELTTSSDDEDHNDAGEIHQQRLTEDRENRKRQKSLTAYSSDEQGERKNVPKRMRRDDSEDAAAKHPGWSAKDDQKQRKRKLEHRRSSEDESKKNAKRDFRDIPHEDVSDEEETEDGSRSRRQSTSSTISNVTAKERKEKSGKTPLRIVPEPTGTPLLSPKILSPKHLSPKTSTSSTKRSSISDHENLISPRQRNRTTSSTSTATTSSKHEALSIPEKPLSPPVTAKSSVSSIDDPSIRDEFSMNSAADSPMSTTGRPMVLTKAAMKAFNSTPPKKKNSSSGQHDSSSGSSSDSSSSDGSTSSDDSSDDEVPKQTEPVTSIPVVASDNGSPENVVVETPSIVSQTPREPEPFTISEQSSESEPEAVPECPEASVEPQMETSQNVEPVSEEHEDSHEHGDSEVAVESQQQPLEHQEEKEELENKILDVAAEHHEEQVQGDEDSVESSIPAPSDEPDPVTQAQEKSAHTLISDQETDQAVQSIFDEEEADEFPQYPDFGISTNEKEVSGKDPHNIKPTEPLNNGHTDLLFSPSSSAHASEKQSTKSEDDMEEDSELVVMEKEVPMEQVIAQEVHVPSEPSPMEEEVKLETSPVPKEEPIKMEESPEQTPTPDLISNNESQDTPGAVNNHLHENHDAVQTPIQLQPASQHQVAQPSPRPAVAPDSQQNGPVLVSQQSQPSPMSSQQSDMAQNLILSSKDINDLAAKLHKNPEALAQATRGDCSGIFQHLLLHAQGNGQNMTPEMLQLKAAFFAQQQENEANQMMQAKMKQQTINKDRIKEQERVKRMYEENERKVEEDRREKQRKEEERQRLAAATAAATMATQKAAEALKQKQEVPRHGFQHVLSMMTPEARSLYEQFPGLSSYINRDSIGATNGVLHLPTQSIQRPSSTASTSSNPPKAPLQPSASVNQNTIDPAEIEEIRVQRWFYKHFPMVWTGRLALKSTEAMINLHLINGSETFLNDVLGRQVTEENPRRDSVKILQRLRLDNGQVEHIYRILTNPEYACCLALSSVNNIENLKENDTNLKSHFIDYLINKKIAGISSLGEVETKFKSARVHVFAPGEIVNRYLSELATSLHDYLQNTDTRYLLIVFTNDKADPNMTGPPSVASLAVPPVSST | null | null | protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634] | RNA binding [GO:0003723]; ubiquitin protein ligase activity [GO:0061630] | PF00076;PF07744; | 2.40.290.10;3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314028}. | null | null | null | null | null | FUNCTION: [Isoform d]: Probable transcriptional corepressor which modulates activity of the nuclear hormone receptor daf-12 to regulate the dauer diapause. {ECO:0000269|PubMed:15314028}. | Caenorhabditis elegans |
G5EGK8 | PP2A_CAEEL | MAAAPPSADPLDKALIVDVDQWIEQLYECKPLSENQVKTLCEKAKEILEKEPNVQEVRCPVTVCGDVHGQFHDLMELFKMGGKSPDTNYLFMGDYVDRGYYSVETVSLLVCLKIRYKDRVTLLRGNHESRQITQVYGFYDECLRKYGNSNVWKYFTDLFDCFPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHSNGLTLISRAHQLVMEGYNWSHDRNVVTVFSAPNYCYRCGNQAAMVELDDDLKYSFLQFDPAPRRGEPHVTRRTPDYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P36873}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:P36873}; | centriole assembly [GO:0098534]; centrosome separation [GO:0051299]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic spindle disassembly [GO:0051229]; mitotic cell cycle [GO:0000278]; mitotic centrosome separation [GO:0007100]; mitotic nuclear membrane reassembly [GO:0007084]; mitotic spindle organization [GO:0007052]; negative regulation of insulin receptor signaling pathway [GO:0046627]; pronuclear envelope synthesis [GO:0018985]; regulation of vulval development [GO:0040028] | axon [GO:0030424]; axonal growth cone [GO:0044295]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein phosphatase type 2A complex [GO:0000159] | DEAD/H-box RNA helicase binding [GO:0017151]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-1 subfamily | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:20392746}. Cell projection, axon {ECO:0000269|PubMed:20392746}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259}. Cytoplasm {ECO:0000269|PubMed:17218259}. Note=Localizes to the margins of VD neuron growth cones and to small transport vesicles (PubMed:20392746). During mitosis, localizes around chromatin after the nuclear envelope breakdown (PubMed:17218259). {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:20392746}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|RuleBase:RU004273}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|RuleBase:RU004273}; | null | null | null | null | FUNCTION: Protein phosphatase which plays an essential role in early embryonic cell division (PubMed:17218259, PubMed:20392746, PubMed:21497766). Probably together with constant regulatory subunit paa-1 and regulatory subunit sur-6, positively regulates centriole duplication by preventing the degradation of sas-5 and kinase zyg-1 (PubMed:21497766). In addition, plays a role in the recruitment of sas-6 and maybe sas-5 to centrioles and may dephosphorylate sas-5 and zyg-1 negative regulator szy-20 (PubMed:21497766). During vulva development, may play a role with regulatory subunits paa-1 and sur-6 in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 activation (PubMed:10521400). In association with regulatory subunit rsa-1 and probably paa-1, regulates microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules (PubMed:17218259). Plays a negative role in axon guidance probably by dephosphorylating unc-51, unc-14 and vab-8 (PubMed:20392746). {ECO:0000269|PubMed:10521400, ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:20392746, ECO:0000269|PubMed:21497766}. | Caenorhabditis elegans |
G5EGL9 | AFF1_CAEEL | MRLWQWSIAVAICLVMVTEARLRRHHRKRRFVSSNFDEFYCGESAHAQSQFEEERESNSSKVSSVHSTQFNWGLDNTICIKLQNVVHVLKYERLEQRYPIENSYTFSVPLIDTNCKCHCYGFGTNDVCNVEKYADDRNCTTSSEFPTCYTKYHPAVEPLDCPVTSIPAKACCDIKLKPRDGRMFRAVKLQQPINDMIISHSIFANNSGKMMKVLGPDEFRINLLKGKEQFELTEYHRISVQLVASSPQQQLREGMYYFPEENHNDLREGKINEITESDLDKLGWYRRVGNDWQVATSGLLLRNAHKVVIKNCKGQVHMDQFSGTKNFVLRGTQYNDTYNERRVSDNNFVRSVKVDESSREITIVHEHGTAAQVSLKTDTRPNLTKSQSLLANFTGSITLDHDGNRMLNVTFFGVKGTVHIKMYVNDRKLIATFACTAQFGTSLKDDGSRISLPSTINQAQWVCILPDEQPTKSEICKWIPYEEKAMRTPRQEQSWSKGHSPCSQAECNSLKSGVSDLFPWIMNFDYFMAHGGDFTEWLKIGIHIVIAVGLLLLLILLFTKCLVPLACCSLSIPFKNRNKKKKKKNSSDY | null | null | regulation of egg-laying behavior [GO:0046662]; syncytium formation by plasma membrane fusion [GO:0000768] | apical plasma membrane [GO:0016324]; cell-cell contact zone [GO:0044291]; intracellular organelle [GO:0043229]; plasma membrane [GO:0005886] | null | PF14884; | 2.60.40.3980; | EFF/AFF cell fusogen family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17488621}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:21350017}. | null | null | null | null | null | FUNCTION: Required for cell fusion events during development including the fusion of anchor cells (AC), vulval A and vulval D rings, and late epidermal seam cells (PubMed:17488621). Required for amphid sheath cell fusion induced by entry into dauer stage (PubMed:21350017). {ECO:0000269|PubMed:17488621, ECO:0000269|PubMed:21350017}. | Caenorhabditis elegans |
G5EGM1 | MMPA_CAEEL | MFTGLHDILIILFLLVTLKIAQNVDHTKFLQKYGYLTSGDNQLSSESLSDALKNMQRMAGLEETGELDERTIQMMERPRCGHPDVEDHQKSRGKRYAPPQFKWKEKIITYGCKAVGTSTRISLDDLRRTMHQAASQWSELADVEIVESSVKNPMMVISAGRENHYPCTVRFDTKTLAHAFFPTNGQIHINDRVQFAMTNYTERMGANSLYSVVAHEMGHALGFSHSPDIDSVMFAYDTPRKWKFTSMDKYNMRSYYGAKASKKENEEEERKTENEDKRRKTEKDRGRTREHESDDIRPNECRVENPIVVQYRGEYLIFKSQWVWRVSSDWKRLIIKAVPINQLFPGLPNPIDAAVTVGHNLWVFVGEMIYVIYGNHMVHAPLRLSDIGINEKYVDLAYEWHYFNPPAVYIWKGSRYWKLDEKMYHRRVDERYPKDTDLNWARVPKGVHSAFTYEKEIHLLRGNQVFRMNSSRSVFDIADGYPQPLQSFFGFCPRNEKLVLNSSSSHFSLIYATITILILIF | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O60882}; | basement membrane disassembly [GO:0034769]; collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270] | PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15960981}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:15960981}. Note=Localizes to puncta on the cell surface that are often concentrated at the invasive basolateral membrane of the anchor cell. {ECO:0000269|PubMed:15960981}. | null | null | null | null | null | FUNCTION: Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium. {ECO:0000269|PubMed:15960981}. | Caenorhabditis elegans |
G5EGM3 | TAF1_CAEEL | MNNTHHHTNGYRTEKPKNEEDLEDPYANLSDFYKNHPAARNEACSSASNGGSKSVKMEPKVEKNEEFEEYIGDPVRLEDMEPFARPSLRDDAPLSSILHPDLDGIDPRIFFKDFNPNKTLRFSRLFAQNIKHTSRAEIWWASRTFSKHQRKKEPEEPLADDVIVGAKKLKLNIIEKVPRVMLADDEEERMRRPILTDAEEMAKKNEEGTVVQPWRTGPAKIWYDMMNLPMTSQAVNYGFKLKKSPQKVSIRSGKPLNYRTPDDLPSTSSGPAPNSAPFLDKVEVIDKSCEASTSEDILLPYQVIEWENDVILDGEEVKDQLLEEFSNGRGCGWIPTQYTRTYEHFVYAANNNAFEQMFDGKSAPINLTGPDSAILPTPGHSIFPSAPCDLDILPWETNIIWDADAMPSTLEPIDFLVDFQDDPLIYGMPEDRRHDEGPDHHHHHHHHRKDGQYTKKSKMILGQVQQRQKQEEDEQMESTMAQFTDNDPFNLSNDDYYVPKATSKTLSNNSLLIQHSTPATNIATHFFPTHPSAFRLRYWHRTPFTRRIVRHWQPMRFQPIQTPVKHQQRVAAMREAMRQAQGGGEVFYMRDVQDLSGKDETLVMIEYSEEHPVILSQPGMASKMKNYFKRRQANDSEPTFTFGELAFSHQIPFLGQLQPGQSLQSIENMLYRAPIYLHKRQNTDFLLIRSMNQWYIRPLPSIFVAGQQCPLYEVPSPNSKRATVFVRDFLFAFIYRLFWASDSSPRRLKMDDVRNAFPHYAESNIRKRLKMCSTFVRQGSETYWSLKPDFRLPSKEEVLSMVTPEMCCAQYSMMAAEQRLKDAGYGEKYFFTPENDEGSEDEVTIEDEIKCAPWNTTRAFLASQREKCLLDQTGIADPTGCGQGFSYVRVSQKPHKDENATPVPKKLVTGTNADLRKLPLKEAKQICRGYGVKEEEISALTRWEIIDVIRTLSTQAAKATKDGEIIAVSGMARFARGNTRFSSADMQEKYRKHCQRIFDQQNQTLANTDPISTDDDSTDADSDNEELASRLESMLEANKGKKNISMSEKAKIDFETEEKEREDLKRMIHGTTNQVEKGEKKEEGEVTAEEKKSASQFGEDVAMSASKISGITANQQLKIYRTCKGPDGKDVTRIEIVTRPQLIEAYTRIRMTRDDTFIQVYAQMDEQYKEEKRKKKRRLQDQIRRMKKNEEKAAHKVQKMTEKKVKPIKPPNPNLQKMRCSACHAYGHMKTNRNCPLYGKDPLTPLKEEDEGSTIMTSVSSASLVAPDAVQVDGTKVKFNLNFAEIRKEQNREEKLKRKLAKMAEAAVRERQMAHLMEYGGGASSSGGAGGGGSGIGGSTGGGITDNDDDDRFSQISGTSSFLNGPPGAIRGGNRNSSVSGSKRRSSMMPEEDYLQGPLKVAHRARADPKVVMSSMLTDIVNELKMISGSDAFVTPVNSKKVVDYYNIIKNPISLQEIKKKISEQSYLLRKDFLDDIKLMFDNSRMYNGDNNILTLTAQQMLQLAGKRMIEREQKFIGLEKQINPLLDTNDLIGFSYLLGEIVQKMKNIPKSALFHTRVDPKKIPAYYLKISDPMDLSIMEQKSKSQEYKSIDEFLKDAEKIYTNSVVFNGAESVYSLKAKEMFEMAEMLVKDQMDTLGELERNINPSAINDAAAAQRGLAMDSDDHMDEMEDHPTEEEEEDDDDEIMDDDMDIDATGYSYDHDDNVAVGQIFNDLAMSDSDEDERAEDVKRPANGDDNLLDSF | null | null | embryo development ending in birth or egg hatching [GO:0009792]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription initiation at RNA polymerase II promoter [GO:0006367] | nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669] | DNA binding [GO:0003677]; histone acetyltransferase activity [GO:0004402]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase II general transcription initiation factor binding [GO:0001091]; TBP-class protein binding [GO:0017025] | PF00439;PF12157;PF15288; | 1.20.920.10; | TAF1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14726532}. | null | null | null | null | null | FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-1 (By similarity). May regulate RNA polymerase II activity and thereby may control transcription initiation by RNA polymerase II (PubMed:14726532). Required for early embryonic development (PubMed:14726532). Essential for embryonic transcription of several genes (PubMed:14726532). {ECO:0000250|UniProtKB:P21675, ECO:0000269|PubMed:14726532}. | Caenorhabditis elegans |
G5EGN2 | FAT6_CAEEL | MTVKTRSNIAKKIEKDGGPETQYLAVDPNEIIQLQEESKKIPYKMEIVWRNVALFAALHFAAAIGLYQLIFEAKWQTVIFTFLLYVFGGFGITAGAHRLWSHKSYKATTPMRIFLMILNNIALQNDVIEWARDHRCHHKWTDTDADPHNTTRGFFFAHMGWLLVRKHPQVKEQGAKLDMSDLLSDPVLVFQRKHYFPLVILCCFILPTIIPVYFWKETAFIAFYTAGTFRYCFTLHATWCINSAAHYFGWKPYDSSITPVENVFTTIAAVGEGGHNFHHTFPQDYRTSEYSLKYNWTRVLIDTAAALGLVYDRKTACDEIIGRQVSNHGCDIQRGKSIM | 1.14.19.-; 1.14.19.1 | null | innate immune response [GO:0045087]; long-chain fatty acid biosynthetic process [GO:0042759]; post-embryonic development [GO:0009791]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum membrane [GO:0005789] | 16:0 monogalactosyldiacylglycerol desaturase activity [GO:0009979]; iron ion binding [GO:0005506]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387, ChEBI:CHEBI:57394; EC=1.14.19.1; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932; Evidence={ECO:0000269|PubMed:16839188, ECO:0000305|PubMed:10872837}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + heptadecanoyl-CoA + O2 = (9Z)-heptadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36951, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74307, ChEBI:CHEBI:74308; Evidence={ECO:0000269|PubMed:10872837}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36952; Evidence={ECO:0000305|PubMed:10872837}; CATALYTIC ACTIVITY: Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36935, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296, ChEBI:CHEBI:74297; Evidence={ECO:0000269|PubMed:10872837}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36936; Evidence={ECO:0000305|PubMed:10872837}; | null | PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16839188, ECO:0000305|PubMed:29237573}. | null | null | FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases (PubMed:10872837, PubMed:16839188, PubMed:29237573). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). {ECO:0000250|UniProtKB:G5EGA5, ECO:0000269|PubMed:10872837, ECO:0000269|PubMed:16839188, ECO:0000269|PubMed:29237573}. | Caenorhabditis elegans |
G5EGP4 | VPP3_CAEEL | MGSIYRSEHMKLCQIFFQSESAYQCVAELGELGMAQFIDLNEEQNAYTRKFVNEVRRCDEMERKINFVEDEITKDLVPIPDYDEHIPAPQPKHMGEMEANLEKLEEELVQINKNCKVLKNNHVQLLEMKAVLEHVTSLLDPHSKREAAMSISEAARGEAGPISFGMKDEFDKPVKDEKELKFVTGVVKRSKAIAFERFLWRLSRAKVFAKFIQIQEQTELFSNEFEDKCVFILFFSGEQLRAKVKKICDGFQAKCYTVPENPAERTKLLLNIKVQTTDMKAVIEKTLDYRSKCIHAAATNLRKWGIMLLKLKSIFHTLNMFSVDVTQKCLIAECWVPEADIGQVKNSLHMGTIHSGSTVPAILNEMETDKYPPTYFKLNKFTQGFQNIVDAYGIANYREVNPAPWTIISFPFLFAVMFGDAGHGIIMLIAASAFVIFEKKLISMKIKDEIFNTFFGGRYVVLLMGMFAIYTGFIYNDFYSKSVNIFGSSWVNPYNQTLLANMDAQGADSNTDLSLTFPPEIAFNHDYGPYPFGVDPVWNLAINRLNFLNPMKMKTSILLGISQMAFGIMLSLMNHIGNRSVVDIVFVFIPQCLFLGCIFVYLCLQVLMKWIFFYVKPAYIFGRLYPGSNCAPSLLIGLINMFMVKSRDASFAHDVGTAAGKEWVIVNGQNVTYTINDQCYLQQWYPNQSLVELILLLIAVVSVPVMLLVKPFYIRWRHSRGLHIDLGHGPDEHGEFNFGDIMVHQAIHTIEFVLGCVSHTASYLRLWALSLAHAQLSDVLWTMVLRMSLTMGGWGGSAAITILFYFIFSILSVCILILMEGLSAFLHAIRLHWVEFQSKFYGGTGIQFEPFCFTKIIRVYEGLDQ | null | null | nematode larval development [GO:0002119]; vacuolar acidification [GO:0007035] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220] | ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF01496; | null | V-ATPase 116 kDa subunit family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:19741196}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical surface of intestinal cells (PubMed:11441002). Localizes to dot-like structures, possibly P granules, in P2 cells of 4-cell stage embryos (PubMed:11441002). {ECO:0000269|PubMed:11441002}. | null | null | null | null | null | FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:19741196). In the intestine, required for the rhythmic defecation behavior by promoting acidification in the gut lumen following defecation (PubMed:19741196). Also, luminal acidification is required for nutrient uptake (PubMed:19741196). {ECO:0000250|UniProtKB:Q29466, ECO:0000269|PubMed:19741196}. | Caenorhabditis elegans |
G5EGP8 | CATZ1_CAEEL | MRTFVLLLALCAICILASSAYGKVRKYSNRNRYNLKGCYKQTGRVFEHKRYDRIYETEDFDSEDLPKTWDWRDANGINYASADRNQHIPQYCGSCWAFGATSALADRINIKRKNAWPQAYLSVQEVIDCSGAGTCVMGGEPGGVYKYAHEHGIPHETCNNYQARDGKCDPYNRCGSCWPGECFSIKNYTLYKVSEYGTVHGYEKMKAEIYHKGPIACGIAATKAFETYAGGIYKEVTDEDIDHIISVHGWGVDHESGVEYWIGRNSWGEPWGEHGWFKIVTSQYKNAGSKYNLKIEEDCVWADPIV | 3.4.18.1 | null | ecdysis, collagen and cuticulin-based cuticle [GO:0042395]; embryo development ending in birth or egg hatching [GO:0009792]; gonad morphogenesis [GO:0035262]; post-embryonic body morphogenesis [GO:0040032]; proteolysis involved in protein catabolic process [GO:0051603]; vulval development [GO:0040025] | collagen and cuticulin-based cuticle extracellular matrix [GO:0060102]; extracellular space [GO:0005615]; lysosome [GO:0005764]; yolk granule [GO:0042718] | cysteine-type endopeptidase activity [GO:0004197] | PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=In molting larvae, localizes in both the new and old cuticles, specifically at the interface where the old cuticle is being degraded before ecdysis (PubMed:14630920). Localizes to yolk granules in the developing oocyte (PubMed:16857685). {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. | CATALYTIC ACTIVITY: Reaction=Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.; EC=3.4.18.1; Evidence={ECO:0000250|UniProtKB:Q9UBR2}; | null | null | null | null | FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:14630920). Probably, required for the degradation of the old cuticle (PubMed:14630920). {ECO:0000250|UniProtKB:Q9UBR2, ECO:0000269|PubMed:14630920}. | Caenorhabditis elegans |
G5EGQ3 | MAX2_CAEEL | MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSVGDKNGNTTTNKTTVEPPPPEEPPVRVRASHREKLSDSEVLNQLREIVNPSNPLGKYEMKKQIGVGASGTVFVANVAGSTDVVAVKRMAFKTQPKKEMLLTEIKVMKQYRHPNLVNYIESYLVDADDLWVVMDYLEGGNLTDVVVKTELDEGQIAAVLQECLKALHFLHRHSIVHRDIKSDNVLLGMNGEVKLTDMGFCAQIQPGSKRDTVVGTPYWMSPEILNKKQYNYKVDIWSLGIMALEMIDGEPPYLRETPLKAIYLIAQNGKPEIKQRDRLSSEFNNFLDKCLVVDPDQRADTTELLAHPFLKKAKPLSSLIPYIRAVREK | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20008556}; | cell migration [GO:0016477]; gonad morphogenesis [GO:0035262]; gonadal mesoderm development [GO:0007506]; inductive cell migration [GO:0040039]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; motor neuron axon guidance [GO:0008045]; netrin-activated signaling pathway [GO:0038007]; phosphorylation [GO:0016310]; regulation of axonogenesis [GO:0050770]; regulation of MAPK cascade [GO:0043408]; response to copper ion [GO:0046688] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF00786;PF00069; | 3.90.810.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17050621}. Cell projection, dendrite {ECO:0000269|PubMed:17050621}. Cytoplasm {ECO:0000269|PubMed:19023419}. | 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:0000269|PubMed:20008556}; 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:0000269|PubMed:20008556}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway (PubMed:20008556). In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons (PubMed:18499456). Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases (PubMed:17050621, PubMed:19023419, PubMed:23390595). In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis (PubMed:23390595). {ECO:0000269|PubMed:17050621, ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:19023419, ECO:0000269|PubMed:20008556, ECO:0000269|PubMed:23390595}. | Caenorhabditis elegans |
G5EGQ6 | TEN1_CAEEL | MFQHRTTNAQGPPPNRPMPRPPAGMPMMTSSHEHDYTNDYEDPEEMARSRGEGFSNHLLIKTTPPPQPHPNFNSYEMSMSQQRRSQQHQQPMAPPLSDCWGSGVHDSGVLHKNADGAYYIPSGSLRTTSSTLSPASGQRYLDQPHTSGGAPNPTYSDASTTLLKYPLAAGTNQNRRRQQVGTMNNGDPVAGGPMALSKKKKKFDDDSDTCSRWPSKWNILLAAALLVALFVICILLFRAPNYVYTQPAPSSDATSSAAAAASRYQDLGLRALPPAISLGERVDVEFFPKSMATTELTVTKPSRIRFNATVGSGAQLVLLMSAGVHPSLSLHDALFPIRADRIRDSKSPTHIVEEFGSRSRRSLGASSSRHRNIEILSPRSATFEQFVLEGRHYLTFINERSRVEPISFVAEELQRPTTPPKTSSSGTSGAKEHPLASVLVCESNCNQRGECVHGKCHCAPGFTGRTCDEAVCPVVCSGNGVFSGGICVCKSGFKGKECEMRHNWCEVADCNGRGRCDTDGRCRCNPGWTGEACELRACPHASCHDRGVCVNGTCYCMDGWRGNDCSVFADAIVHVPQAQSPPRRGQEPTESSKTRKAQVKPTPTSEKKKESRELQKPIIATVQVPTESSHPCSAHGQLIDDICQCESGWDSVDCSQQACQCVNGDCLDDGSCQCWKGWRGSNCTDKKCAIGCEDRGKCASDGSCKCSSGWNGENCAIDGCPNQCSGKGECGMDRRSSEWSCRCQAGSTGVDCSVSVEMHCDDGLDNDSDGLIDCDDPECCSSSSCSSESVCSTAASPIEVLMRMPPIFNANFAQRVGFLIMEKSVQSYTDSSQFNENLISVIRGRVMWGGSPTGSDDLSTYSNKSTVPLVGVRVSDAAHPLYGFTLTREDGYFDLTVNGARSVTLQFLRTQFQSVKKSVFVSPRQIIHIDDIVLYRQSGGSPPAISMAPARAKCSPTLRRIPDVVLISNWQYTSDGIETDETSDSSRIVVDSRSIFESLPIQGTDVRLVYDSARSPAAPSTMLIGLLYDRVDKELRKVHINIRIAGRRFDRVLAPRTNLTYVFAWDKMNAYRQSESGLVPVTVRVGYEYQGCDRTSERVWQTRRSQMMGATARKMIGTMWTLDIHHHLDIVNNVVEMGNGGYRLITESEPRVSTFAGLDGVKRDVECLKCEGKVDSISLFRPTTVVYAQDGSLIIGDHNMIRRVSQDGQVSTILTLGLADTSHSYYIAVSPVDGTIAISLPLHKQVWRISSLEPQDSRNNYDVLAGDGTVCASAVDSCGDGALAQNAQLIFPKGISFDKMGNLYLADSRRIRVIDTTGHIRSIGETTPDQHPIRTCAQITKLVDLQMEWPTSLTIDPITGSVLVLDTNVVYEIDVVHDVVTIALGSPTTCDLANATSSASAKSLDHRRHLIQNARDITVGTDGAIYVVESDGRRLNQVRKLSSDRSTFSILTGGKSPCSCDVAACGCDDAVSLRDVAASQAHLSSPYAVCVSPSGDVIIADSGNSKIKKVSARMAKYDGRSRTYEVTDAERQEKYTFNRHGQHSSTVSLITGRTFFNFSYQVDSPISMISEIRAASGVVLRVLKRNDSLFDLETTLGQRTTLTMSAYDGTLEQVSKRDSATSRDATKLFYKKGLLTSRIDVATAVGFEYDEYGRAIGLKRDREYWRLGEETISMGSVNTEVLLNGQRFQQVRLGEGNLAVHSTNGATTRLISLRNEGYSLASPLGTSTLYDKSSSIPDSNGEPLISRRRTKVPAIGNPQRRELTTRWDWRHVARRGDDSDGSLGRRKVAEINGVNMFSMEYDVKSNQDTLRLGSTTDDAQALLFIDYTSSGRIRRISAPEDSQMAEMNITWDGAGRKSEVTWGSWKIRLTYDNSNRLTEHAIDGARVPIKMSYAGASRRPNEIQHDGAKWNIQYDNYDRIKEVISKSQEATSFSSIALGGDEWVLKRRTSLNSKPSLVRLSREGKVLESTTPDENHYWLERKDPITGRTTEILNDEETTVVTCWSPEGAPMCSRSRNLQENTTMQGHLVARKSVTIMTPTSSEPSITSSFTYEYDDMLRVTTIQPVIEQSVLESIQLSYDERRGHVAAINGFKWARDASTSRCQGHGLMYETSKANDHRQVVERKLIFGDARASIKIIRDKAGRASESHLEISSSGTQRNQKITRTFDAAGRVASVEQNDQEPVRIIWNSDARVEKINDRVVEWNRGGALKTFQDISYQVDSIGWVVKRDNTTVFGYDGKGRLVSARSSQLRINIFYDREDRVVQIQNSKDFIHFYYGYIDTPKLVSHFSKNGKISTLFYDDDSVPFAMQSDDGTRYALLTDETSTIKAIIGDSNVLRIIDRSVFGALLPSSSSSHPFLPIGYLGGIEISEISVSILNNGRPLDLYSERYMSISPEAVVRLELNEKFSNSIDLMALEIDRQPFRVENVPEDFETWFSLAGLSPNLLPSAHLGLPASSAIVHRLLSSFPRKLRPLTHLTTVLPTRLASDISLTSPTSETSWSIDDVGFSNLLILNEDATTGEVMVEMLSDLKSEEREVISKLFDGVKSLDFATWGLVPTRHLWRAPNSKLELSSTSFSHFTMAVNKDSVELRNGKSKIVVHFSENKAEIVKKIVEELKTRENIAVWRAERKRAEAGEKTWRQWSDRETRELTSKGSVSGYDIEMKPAHQSGLLASVHSWKFRKSE | null | null | animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; basement membrane assembly involved in embryonic body morphogenesis [GO:2001197]; basement membrane organization [GO:0071711]; cell migration [GO:0016477]; defecation [GO:0030421]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; female gonad development [GO:0008585]; gamete generation [GO:0007276]; gonad development [GO:0008406]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; inductive cell migration [GO:0040039]; male gonad development [GO:0008584]; motor neuron axon guidance [GO:0008045]; nematode pharynx development [GO:0160094]; post-embryonic body morphogenesis [GO:0040032]; sexual reproduction [GO:0019953] | neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF15636; | 2.10.25.10;2.120.10.30; | Tenascin family, Teneurin subfamily | PTM: Probably proteolytically processed to generate a N-terminal intracellular domain. {ECO:0000269|PubMed:15936327}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15936327}. Cell membrane {ECO:0000269|PubMed:15936327}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes in the nucleus with a punctuate pattern. | null | null | null | null | null | FUNCTION: Plays a role in the gonadal basement membrane maintenance and/or adhesion early in development. Contributes to the guidance of pharyngeal neurons. {ECO:0000269|PubMed:15936327, ECO:0000269|PubMed:18632986, ECO:0000269|PubMed:20497576}. | Caenorhabditis elegans |
G5EGS3 | KLP12_CAEEL | MADTCVQVALRIRPQGNREKLEGSRVCTSVLPNDPQVTIGGDRSFTYDHVFDMPTLQYVVYESCVEKLVDGLFDGYNATVLAYGQTGSGKTHTMGTAFDAAVTQKEEDLGVIPRAIQHTFRKIAECKAQAIEQGLLEPAFEVSVQFVELYNDDVLDLLSDDRSMSSSIRIHEDSRGEIVLHGVEQRSVFDMHGTMDILKNGALNRTVAATNMNEQSSRSHAIFTLHLKQQRVAANPLDESGEQKTGELEMEMLCAKFHFVDLAGSERMKRTGATGDRAKEGISINVGLLALGNVIAALGGANGKVSHVPYRDSKLTRLLQDSLGGNSRTLMIACCSPSDSDFVETLNTMKYANRAKEIKNKVVANQDKSSKMIGELRSRIAALEAELLEFKQGRRTVDVDGHEVVNDQYHENVYLTSEVNHLRFRVKALNETLDILRTENIDLKAKQEFNSIASLPTAGSGGAEGEVDAIQSTFRKYLEELERTKSLLYESQSTCDQLRKDNARWKALGASRGSGGGNAEFNSQKLIEMAKQEVEKQRKLMESVNIGGENVSSEYSSMAQDEDGTSNEAEELLDEEDLDEDEDETAEEKQEQEESEALQIDLSEVMIELDIKEKLIDQLERAERQNQQIRETYEKKLRELMERIKDTETERDRVLNEGGKRGGNNEQMKAIKQEYELKITDLRKELKKIEALDKEHLKVIAKSQRELQEKTRLKSEVVDLKKAKVELIKKMNEDKKKQKTQQLANARAFATKEKQTRLQANKIRTLEMKDKQREQFLKKTTQEVNALRKEKAVAAATARQANRGTPRGGAAVTNSPARRVRGVVGGVQAIKELAFSAKASKVKWDVIVRKIEESARRRQIVQKMEAELERYLNERHAVMVEIVENEKQFTQSQDVIYRDGLLEAIDSAKQKLQYVQDQITYQQKLICDVDEDITASNAENEPILDVGLKKQTIKQLFDGCDTLSEARYLLQHLFDLCIDKAALAAKVESEFKECAARIEQLEQQSSLKEQLLTSIIEDKNLVDEIEGFVPSDLRKSRTSSQSSLLRSGSPSVVEDAHTLQNYKVRRHTATQEELLFANSEENSMVSDANANPTVDVGADVGDSDERKEKKKRIAFVSTSPASTSFANSTSQSPSFSRNTRFRSTVGGVSNNNNIRKSVQPLINGKGVSSTARKGISRLPSVTEDPEIGIFAKSFPGRSRSNLMSSSSSTTTTTLSSSNLLNPRGTTSSSSSKSVFARISPSWLSDTCAELIMRNNNRKQSRIVPVKDGMRGNVITRTHTLEGHARGVLSVDVNEKLMVTGSKDRTAKLWDIEACREIRTLGIHPNNVHLVKFVPFSNYVFTFSMFEARAWDYRTPECICVKVLNSSGQVNEGDSIDVSQVMPRQNTIPFLETLITAADVDPTGQLLFTSFSAYVRVWNLREWKPLGRLNAASHSPKSEVSCLRTTMTPEGSILAYTGSRDHYVKEYEVGLGTGVIESKCEFTPPHYDNVTAVLPLNGHLYTASKDVNIMKFSLKDGKREHLELRAHQQYIQSLTGFGPKGKELLVSACKDGTIRFWDVGSSSRMKLVEEYSKAHQEGINDMCSTKSMLFTASGDSTVGFWKSNAV | 3.6.4.- | null | microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231] | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF00400; | 3.40.850.10;2.130.10.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:36065637}. Note=Localizes to microtubules and to the growing microtubule plus-end. {ECO:0000269|PubMed:36065637}. | null | null | null | null | null | FUNCTION: Microtubule-binding motor protein which has ATPase activity (PubMed:36065637). In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis (PubMed:36065637). Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end (PubMed:36065637). {ECO:0000269|PubMed:36065637}. | Caenorhabditis elegans |
G5EGS5 | GBF1_CAEEL | MATNGVYIVMGEANCVVALLNKARRQYQLSQVPTLEDTDPLLRNFTDLKEVLNEVADLADMNPQTYLSPFLDVIKAQNTNGPITEAALAAVAKFLNYGLIDASSIKAANAVESIAYAVVHTKFIGGKSTGSDECVLFKILQVLRSLLLSPPGILLSNEAVCDMMQSCFRIVFEQNLSLLLRKAAESTLADMTQLIFTRLPTFVEDTRHPYIRQLVNPTEKRQKRKKKRQLSVHIETKAKEPENVPTEMTKLIGEAAETAETDGAANLGYDVVLTTDPPVDTVTHPDPPIEEIIKLAEPISAGDEADSESEGGGGEEHHERPPVRAHAGLQREIVSDEEEIDTEQTVGGEEKMPYGLPCCRELLRFLITMTNPVDRHNTESMVILGLNLLIVALEAIADFLPNYDILMPLIKNELCRNLLQLLDTNRLPVLAATNRCCFLLFESMRMHMKFQLESYLKKLQSIVLTEEKQHENGGGGTEQKEMALESLVQLWRIPGLVTEMYLNFDCDLYCGNIFEDLTKLLVENSFPTVGGHTASLLSLDALLVVIETIEQNCEDRENGRGEVAKEQEHKDLKKLGLPVLSGYDLAKKMAISTGGKASPMPVSSSIVLRSNRHAPSTELPSMSQIIEQKKRKRLIAEGTELFNQSPKKGIAFLREKGILGHDEQSLVQWLRTNPQLDKKAIADYICNRKHAEVLNAFVKSFPFENTRLDVALRMFLETFRLPGESAEIALVMQHFSEEWFRANNEPFFHVDAAFTLSYAIIMLNVDQHNPQAKRSQPPMTVDCFRRNLSGTNDSRDFDPEMLADMYQAIKTEEIVMPAEQKGTVKEDYMWKVLLRRGETAEGSFYHAPTGWNDHDLFAVCWGPAVAALSYVFDKSEHEQILQKALTGYRKCAKIAAYYGMKEVFDNLCIHLCKFTTLTSMRDGGAGGGADEDVDLSAAALLSHSSSPEAVALAFGENHKAQLATRTLFYLVHENGNILREGWRNLFEALLQLFRARLLPAELTEVEDYVDEKGWVNIQRVHQKELPHTRNDSGLLSWFGLGGGASEADRRKPTQEQLSSMKLASQVISECRPSQIVADSKYLTSTSLAELLSSIAANSAQIVEQAEPQQKTASLSGEDEDALVFYLELIVAITLENKDRLPLVWPHVRRHLEWLLSPRFGRCPVLVERAVVGLLRVANRNLFRDNTVSDDVLHSLSMLLRLSPKALFIFSRQIAFGLYELIRANAANVHKKEHWAVLFALLEAAGAAVLPDDYVMMTTTEKQQQSLRVGGDQQQQRMAYSDVEGASGRGGGAHEERAYTSEGEERRRGGYDSNSDLESRVDSAGSLLGAQKQPADWIHLDHKDAAKATEEALTALGANVVSSKKNFRQFGSLVLRNGLGRHEPAAFLKVCECLAFLLRDAVHVTPDNFESSLQCLRTMVEASLDGGVYAAGPLSGDAQNRLRSNVTDEKAVKKHHHHHHGHKKKELCTDVTEDADESRNEEQQLIGNYQQMSLHLLDLCSQLHSQTPAIFAKWAQGASPAASDLATVAFIWTDIWRPLLQAIGRLSCDCRRGVRAAALTHLQRAFLPANMATLGAAEWQSCFGEVLFPLLTKLLEPFSQMDPIGMEDTRVRTLQIVAKTLLNHLSALSALDSFPDLWMLLLDYMEQYLRVDSCGNLNEAVPESLKNMLLVMDSTGIFAATPRLYDVTVERLNKFMPELIKDTIPNPPRPGQQQSEASEPKKEHASGLEPPPPSSNSTAATSTSDPSIATAQSSISTASSVVGPLVTCPEDAGISAPIPIQHPLTEVIVHSGPTSPIGSPPQTEPPASSPPQHQHSEHQQYEQYRQQQAAAAQQYQQYNQNYPQQQQQQQQQYAYSPEHAAYYQQQYAHQQQQYAEHYANQYQHYQQQQQQQQQHPVNPTSPSVHGQYSVANPLPLPAHPAYHPIVAPSVNSAFTHVYTPPQNNAPALAPSAPTTTSADSPYFTPIPYNPSQQEKP | null | null | endoplasmic reticulum organization [GO:0007029]; endosomal transport [GO:0016197]; mitochondrion organization [GO:0007005]; regulation of ARF protein signal transduction [GO:0032012]; secretion [GO:0046903] | endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi cis cisterna [GO:0000137] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF01369;PF12783; | 1.10.220.20;1.10.1000.11; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:23840591}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23840591}. | null | null | null | null | null | FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP (By similarity). Also, plays a role in receptor-mediated endocytosis in oocytes and endosomal trafficking (PubMed:23840591). Involved in vesicle retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER) (PubMed:23840591). Plays a role in maintaining mitochondrial morphology, network organization and function (PubMed:25190516). May be required for the basolateral cell membrane localization of the serine threonine protein kinase sgk-1 in intestinal cells (PubMed:26115433). {ECO:0000250|UniProtKB:Q92538, ECO:0000269|PubMed:23840591, ECO:0000269|PubMed:25190516, ECO:0000269|PubMed:26115433}. | Caenorhabditis elegans |
G5EGS7 | SEL7_CAEEL | MAQPNQPTPQFQMAQIPLAAFFDNNESKTMLNSMNLRLNDMDLKLSLILELLATRLPDQRLPSIFTSPPQTVISEAPPQSFTPSATNSTSDKTSSSLKTELKTEDSDGDLDMEGEEDTEELFDNESQPSQRNQSPKETEVEDEKVLADGPFPEGAVKRAAEKAARSFQSTQPKVFAWQILRESVTDDELRNVQISLRTFHGETADHLLGRQLPKIRLVVEATMKYFKWDLLSTESQLSKAKLILSHLKNNAKVRNWTLREGRPNRVAPATPPVNVDLVWKRYLALLGPAGFTGILPNLPQNLCNGGTQSPSIPQIDPSLFKVDA | null | null | lateral inhibition [GO:0046331]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of cell fate specification [GO:0042659]; regulation of development, heterochronic [GO:0040034]; regulation of mesodermal cell fate specification [GO:0042661] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15020414}. | null | null | null | null | null | FUNCTION: Putative transcription factor (PubMed:19500563). Positive regulator of the lin-12/Notch signaling pathway (PubMed:15020414). Binds to specific DNA sequences in regulatory elements (PubMed:19500563). Involved in cell fate decisions that require cell-cell interactions, such as the anchor cell (AC) / ventral uterine (VU) precursor cell fate decision (PubMed:15020414). Heterochronic protein which controls the choice of stage specific cell fates, including the larval L3 stage-specific fate of seam cells (PubMed:19500563). Involved in regulating the temporal expression pattern of hunchback-like protein hbl-1, thereby playing a role in the progression between larval stages L2 and L3 (PubMed:19500563). {ECO:0000269|PubMed:15020414, ECO:0000269|PubMed:19500563}. | Caenorhabditis elegans |
G5EGT9 | RYK_CAEEL | MILRYLIFFAQLWALCLANVNMFISKEEMNRTFGVKAELNYIEMGNVSSYSTKFHYRVMANIDYLSFTWNAVGIVHYEVYVESDDSSVLPIVRIPLKGTVPESLQDFTVEYRCAGHRSGQFAVSLYFTFKYGNKEPLKVKLRQEKICASRDGRRGLNGGYEGHEVDDTDSIDKAFFVIICIAAAFLLIVAATLICYFKRSKKEDMIPTRLPTSFRNSLKSTKSAQPFLLSTPRDGPPTLSAISSAPCSSSSASGNSIIPSKPRNIDVRRALLQLYQDRDAFQSLPLDMEGTFGEVRYAIWRQVDDVLNGDVDDEEDTFCNQEAVYTKTLKNNASPIQLDRFLSDALLFYNITPHQNLSQVACVASFGRFDRPETVTDFPLVCYRHQGFGNLKKFLTICRHGDKTKGAQTLRTHQLVSLATQVSSAVAHIHKYRIVHNDIAARNCLIAEVNGRLQVQLCDSALSRDLFPADYHCLGDNENRPLKWMSPEAIANELYSSAADVWSLGVLLWELMSLGGSPHAEIDPEEVYTMILKGKRLQQPNNCPDQLYEVMLCCWRVLSEDRPSSEQVVHGLRDFNIQLSQYI | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; establishment of anatomical structure orientation [GO:0048560]; morphogenesis of an epithelium [GO:0002009]; polarity specification of anterior/posterior axis [GO:0009949]; polarity specification of proximal/distal axis [GO:0010085]; positive regulation of anterior/posterior axon guidance [GO:1905488]; positive regulation of motor neuron migration [GO:1905485]; positive regulation of sensory neuron axon guidance [GO:1905491]; regulation of asymmetric cell division [GO:0009786]; sensory neuron migration [GO:1904937]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vulval development [GO:0040025]; Wnt signaling pathway [GO:0016055] | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF02019; | 1.10.510.10;2.60.40.2170; | Protein kinase superfamily, Tyr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15369677}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the basolateral cell membrane of vulval precursor cells. {ECO:0000269|PubMed:32053105}. | null | null | null | null | null | FUNCTION: Has no detectable kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (By similarity). Receptor which may act as a receptor for Wnt ligand mom-2. Plays a role in controlling P7.p vulva precursor cell lineage orientation during vulva development (PubMed:15369677, PubMed:15649465). Regulates pop-1 asymmetric distribution in P7.p and its daughter cells (PubMed:15649465). Plays a role in the migration of ALM neurons during embryogenesis (PubMed:18622031). {ECO:0000250|UniProtKB:P34925, ECO:0000269|PubMed:15369677, ECO:0000269|PubMed:15649465, ECO:0000269|PubMed:18622031}. | Caenorhabditis elegans |
G5EGU2 | EAK6_CAEEL | MTNIREDENIFMFLCEKWILINKNHIWNRINQRINIIADFDRYQRARTISEGQRTENIHRNIYGAVPYDYNLVNLTSTQRNPLGYINASVAEFPEIGRHYIITGAAQDTQIPFFWQMVFEQKSPAIVMLLEDVELGIEKSDKYFPNNTREELKFGIYDITCKEFVKRNILEYRLLEVSVGNETHQVHHYKFHGWTEFNLPKYEDFMAFYNTMKEVGVPLLAVMKNNCMSSFFKKYHHTPPTNAPIIQCSTGGARCGVFIIIDILINLIDNRIKNSYSIEWWMLKVRSKRNHSALTNQQHSFIYDIIIKYIRTRHNQLRHLEKYLEAHANTVRMIDSTNTEDVDKFIKPRDWIVDFDERDRLIGKLQFRKRLKIEKDQVSEQKLVHLKSQLHLFQDTYKYESYVLQ | 3.1.3.48 | null | dauer larval development [GO:0040024]; dephosphorylation [GO:0016311] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | phosphoprotein phosphatase activity [GO:0004721] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16839187}. Cell membrane {ECO:0000269|PubMed:16839187}; Peripheral membrane protein {ECO:0000269|PubMed:16839187}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Putative phosphatase which, together with eak-4 and sdf-9, negatively regulates dauer larva formation downstream of insulin-like receptor daf-2 and in parallel of age-1, pdk-1 and akt-1. {ECO:0000269|PubMed:16839187}. | Caenorhabditis elegans |
G5EGU9 | SZY20_CAEEL | MSKENVVADSWDDADADPVKELMDKVEKVKLLQRKEEKKEAFFEKVKAEESSGVVSKLQTEEGLGPSAEEPKRVFLRRPKDGFAASENVIEASPPTSADTEEQPVTNVRSRSHHKLNQKEKQPAPTYEERQAAYQAARNRILGTEYKPDNQEIKEIKFIDRSKSPETLKMTQQNMVEHYGEELSRELMEQPAEIVPPERQYTPDFTQPPPSVSESGGVYNGPPGFQQKQPNFQPTLQQQSLHQQQYLDNQYMMQMNVQIPIQYHNQTQHQFVPHEASAISTTSQNSNGDGQNDQAIYYYQAPTQQPMNYIPYNLPNMAYPPPNFQPQGQLHHQMNAGQLHQIQQQQQQCQQIQHQPPQQHQQVINGQVMNQQNQRNQVNSYPQQNGAGRGQNRQPMMYQMPCNSGPTAKPPPLMNQMQNRCMTNNGQNYQNRNMQQQGQQRSYSSQPQNGQFYQNGNSNQNNPNNGRKQQHQPQQQQNKSGKFGQNRNDMQKNNYQPNLQQPPMSQNPIPFGCPPRNVNAIREQHANNGSPNTGAGILGPHPMMSASQWPALQQNRPQ | null | null | cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic chromosome segregation [GO:0045132]; negative regulation of protein localization to centrosome [GO:1904780]; positive regulation of fertilization [GO:1905516]; positive regulation of mitotic cell cycle, embryonic [GO:0045977]; positive regulation of mitotic cytokinetic process [GO:1903438]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic cell cycle, embryonic [GO:0009794]; regulation of mitotic cytokinetic process [GO:1903436]; regulation of spindle assembly [GO:0090169] | centriole [GO:0005814]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634] | RNA binding [GO:0003723] | PF12752; | null | null | PTM: Phosphorylated. May be dephosphorylated by let-92. {ECO:0000269|PubMed:21497766}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27689799}. Note=Co-localizes with atx-2 in the cytoplasm. {ECO:0000269|PubMed:27689799}.; SUBCELLULAR LOCATION: [Isoform f]: Cytoplasm {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19081077}. Nucleus, nucleolus {ECO:0000269|PubMed:19081077}. Chromosome {ECO:0000269|PubMed:19081077}. Note=Co-localizes with sas-4 at centrioles. Localizes to nucleoli during interphase and to the surface of chromosomes during meiosis and mitosis. Localizes in puncta adjacent to the male pronucleus at the centrosome during meiosis. Localization at the centrosome peaks at prometaphase and metaphase, but then decreases and expression is at its most minimal during interphase. {ECO:0000269|PubMed:19081077}. | null | null | null | null | null | FUNCTION: RNA binding protein that is required for normal cell division and cytokinesis during embryonic development (PubMed:19081077, PubMed:27689799). Functions with RNA-binding protein atx-2 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation (PubMed:19081077, PubMed:27689799). Furthermore, negatively regulates the levels of the protein kinase zyg-1 at the centrosome (PubMed:19081077, PubMed:27689799). Also involved in ensuring centrosome attachment to the nuclear envelope (PubMed:19081077). {ECO:0000269|PubMed:19081077, ECO:0000269|PubMed:27689799}. | Caenorhabditis elegans |
G5EJN7 | CYPD6_PHACH | MTSTIPTPPSIPFLGHVASIEREVPLRSFRLLSEQYGEIYELNILGRKLLVVSSAKLMSDVSDDKNFYKNMSGPLLQVRNAVGDGLFTAYGEEPNWGIAHRLLMPAFGTASIRDMFPDMLDLASQLVLKWERFGPKHRIDPAEDFTRLTLDTIALCAMSYRLNSFYRDSSHPFVQSMVDFLVECNLRANRPGLLTSVMVQTNAKYEEDIKTMTELADEIIAERRRNPTDKKDLLNIMLYSKDPKTGQSLSDVNIRNNLLTFLIAGHEPTSGLLTFALYYLIKNPEAMRKAHEEVDEVLGDQQIQLTDIGKLKYIDAILRETMRLSPTAPMRTVRPFEDITIGDGKYFVPKDYTVVINTIVAQRDPTVWGEDSNEFHPERMLDGKFEALPPNAWQPFGFGMRACIGRPFAWQEAIIALAVLLQKFDFVLDDPSYELELKQSLTIKPAHFYVHALPREGKPQLLATPSAAPFSSHARETTNASLPASPGTEAKQPMYVLYGSNTGTSESFAQRIANGAAARGFRATLGTLDSVADHLPTDGPIVIVCASFEGEPADNAAHFVERLTSLQDKPLQNLRFAVFGCGHHDWFRTYQRIPKLIDQTLEDRGAQRLVPRGEGDAGSSEFFEAFEAWETKLWEVLPEEYNTVVKQDITSGLKVETVGEGATRAVDLRQHDAALGTVIENRVLTAPGAPQKRHIEFELPEGVTSRAGDYLAILPSNPPQDVHRVLARFGMLPEQQIVISSSGPSSLPTGRQISAFDLLSGYVELSQPATARDVRTLLNVESSDATKESLKALLESYSDAVLGRRLSILDLLEQYPDIKLLFAAYLALLPSMRTRQYSISSSPLWNAQRVTLTVSVLEAPALSGRKEPFLGVASTYLANLRPGDKVQMAVRASNAAFHLPQDPRTPLVLFAAGSGLAPMRGFLQERALQKKAGREVGRAVLFFGCRSPDEDYLYSDSDLKEWEELGVVELRPAFSRALEKSEGCKYVQDRVWHDRRALDGLYEAGAKWFVCGSGKVARGVKEVLTAMIKESRGYSDEEAAAAFERATVGRFATDIFE | 1.14.14.1; 1.6.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9Y8G7}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:Q9Y8G7}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q9Y8G7}; Note=Binds 1 FMN. {ECO:0000250|UniProtKB:Q9Y8G7}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q9Y8G7}; | null | cytosol [GO:0005829] | aromatase activity [GO:0070330]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958] | PF00667;PF00258;PF00175;PF00067; | 3.40.50.360;1.10.630.10;3.40.50.80;2.40.30.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:30171007}; CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:30171007}; CATALYTIC ACTIVITY: Reaction=dodecan-1-ol + O2 + reduced [NADPH--hemoprotein reductase] = 1,5-dodecanediol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28878, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:195414; Evidence={ECO:0000269|PubMed:30171007}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76760; Evidence={ECO:0000269|PubMed:30171007}; CATALYTIC ACTIVITY: Reaction=dodecan-1-ol + O2 + reduced [NADPH--hemoprotein reductase] = 1,6-dodecanediol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76779, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28878, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:195445; Evidence={ECO:0000269|PubMed:30171007}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76780; Evidence={ECO:0000269|PubMed:30171007}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3800 uM for nonanol {ECO:0000269|PubMed:30171007}; KM=1100 uM for decanol {ECO:0000269|PubMed:30171007}; KM=420 uM for undecanol {ECO:0000269|PubMed:30171007}; KM=350 uM for dodecanol {ECO:0000269|PubMed:30171007}; KM=120 uM for tridecanol {ECO:0000269|PubMed:30171007}; KM=20 uM for tetradecanol {ECO:0000269|PubMed:30171007}; KM=10 uM for pentadecanol {ECO:0000269|PubMed:30171007}; KM=18 uM for hexadecanol {ECO:0000269|PubMed:30171007}; KM=15 uM for heptadecanol {ECO:0000269|PubMed:30171007}; KM=19 uM for octadecanol {ECO:0000269|PubMed:30171007}; KM=4500 uM for nonanoic acid {ECO:0000269|PubMed:30171007}; KM=1400 uM for decanoic acid {ECO:0000269|PubMed:30171007}; KM=610 uM for undecanoic acid {ECO:0000269|PubMed:30171007}; KM=450 uM for dodecanoic acid {ECO:0000269|PubMed:30171007}; KM=230 uM for tridecanoic acid {ECO:0000269|PubMed:30171007}; KM=65 uM for tetradecanoic acid {ECO:0000269|PubMed:30171007}; KM=30 uM for pentadecanoic acid {ECO:0000269|PubMed:30171007}; KM=38 uM for hexadecanoic acid {ECO:0000269|PubMed:30171007}; KM=36 uM for heptadecanoic acid {ECO:0000269|PubMed:30171007}; KM=28 uM for octadecanoic acid {ECO:0000269|PubMed:30171007}; | null | null | null | FUNCTION: Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of fatty alcohols (C9-15) as well as fatty acids (C9-15) at the omega-1 to omega-7 or omega-1 to omega-6 positions, respectively (PubMed:30171007). Is also able to convert naphthalene to 1-naphthol and 1-naphthol further to 1,3-dihydroxynaphthalene (PubMed:30171007). {ECO:0000269|PubMed:30171007}. | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
G7CBF5 | IRTA_MYCT3 | MARGFQGVMLRGLGARDHQATVVDKEYIAPHFVRVRLVSPTLFDEVIVEPTSWLRFWFPDPDGSDTEFQRAYTITESDPETGRFAVDMVLHEPAGPASTWARTVEPGATIAVMSMGSRGFSVPEDPEDRPVGYLLIGDSASTPAINGIIEVVPHDIPIELYLEQHHDDDVLIPLAEHPRLRVHRVSRDDASSLAAALELRDWSNWYCWAGPEAGALKQVRTRLRDEFGFPKREVYAQAYWTEGRAMGSSRGETSTPAKPAAKTAPAKAAAKPAAASGAGTPEHAAAPAAATTGAPQAAPAPGAAQPRTPVRGRWRAEAGSRLLAPLKKPLIVSGVLQALITLIELAPFVLLVELARLLLGGAEAERLWTLGLTAVSLIGLGAVLAAAMTLWLHRVDARFAHELRGRLLTKLSRLPLGWFTRRGSASTKQLVQDDTLALHYLITHAIPDAVAAVVAPVAVLVYLFVADWRVALVLFIPVLVYLVLMSVMTIQSGSKIAQAPRWAERMGGEAGAFLEGQPVIRIFGGAAASRFRRRLDDYIDFLVSWQRPFVGKKTLMDLVTRPATFLWIILVAGVPLVVTGRMDPVNLLPFLLLGTTFGARLLGIGYGLSGIQTGMLAARRIQTVLDEPELVVRDRTGQAGTDHASGDQARPGTVELDRVSFEYRPGVPVIRDVTLTLRPGTVTALVGPSGSGKSTLAALVARFHDVTQGAIRVDGRDIRTLTADELYRRVGFVLQDAQLVHGSVAENIALAEPDAGLERIRTAARDAQIHDRITRMPDGYDSVLGAGSALSGGERQRVTIARAILADTPVLVLDEATAFADPESEYLVQQAINRLTRDRTVLVIAHRLHTITHADQIVVLDDGRIVEVGTHDELLAAGGRYRGLWDSGRYSSPDAGRPVSADAVEVGR | 7.2.2.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:32296173}; | null | plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled lipid transmembrane transporter activity [GO:0034040]; oxidoreductase activity [GO:0016491] | PF00664;PF00005;PF08021;PF04954; | 1.20.1560.10;3.40.50.80;3.40.50.300;2.40.30.10; | ABC transporter superfamily, Siderophore-Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:32296173}; Multi-pass membrane protein {ECO:0000269|PubMed:32296173}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=185 uM for mycobactin {ECO:0000269|PubMed:32296173}; | null | null | null | FUNCTION: Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT) (PubMed:32296173). Has a preference for Fe-MBT over Fe-cMBT (PubMed:32296173). Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the bacterial cell (PubMed:32296173). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296173). {ECO:0000269|PubMed:32296173}. | Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile) |
G7CES0 | LPQY_MYCT3 | MDGRQVVRARRWCATAAVALMTASTVAACGSDSGEIVISYYTPANEAATFTAVAQRCNAELGGRFRIEQRSLPREADAQRLQLARRLTGNDRSLDVMALDVVWTAEFAEAGWALPLSEDPAGLAEADATTNTLPGPLETAKWNGELYAAPITTNTQLLWYRADLMDEPPATWDEMLSEAARLHAQGGPSWIAVQGKQYEGLVVWFNTLLESAGGQVLSDDGQRVTLTDTPEHRAATVKALEIIKAVATAPGADPSITQTDENTARLALEQGRAALEVNWPYVLPSLLENAIKGGVGFLPLNENPALRGSINDVGTFAPTDEQFDLALNASKEVFGFARYPGVRPDEPARVTLGGLNLAVASTTRHKAEAFEAVRCLRNEENQRLTSIEGGLPAVRTSLYDDPQFQAKYPQYEIIRDQLINAAVRPATPVYQAMSTRMSATLAPISQIDPERTADELAEQVQQAIDGKGLIP | null | null | null | ATP-binding cassette (ABC) transporter complex [GO:0043190]; periplasmic space [GO:0042597] | trehalose transmembrane transporter activity [GO:0015574] | PF01547; | 3.40.190.10; | Bacterial solute-binding protein 1 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P9WGU9}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.thermoresistibile. Trehalose uptake is essential for virulence (By similarity). Binds deuterated trehalose with similar high affinity to trehalose, trehalose analogs including galactotrehalose, 4-azido-4-deoxy-trehalose, 6-azido-6-deoxy-trehalose, 3-azido-3-deoxy-trehalose and mannotrehalose in the order of decreasing affinity, respectively, and 2-azido-2-deoxy-trehalose and kojibiose (alpha1,2-glycosidic bond) with very low affinity. Does not recognize single glucose, 6-amino-6-deoxy-trehalose, trehalose-6-phosphate, nigerose (alpha1,3-glycosidic bond), maltose (alpha1,4-glycosidic bond), isomaltose (alpha1,6-glycosidic bond) or glycerophosphocholine. Decreased recognition of alpha,beta-trehalose and almost no recognition of beta,beta-trehalose. Substrate specificity indicates a strict requirement for an alpha1,1-linked disaccharide (PubMed:33476646). {ECO:0000250|UniProtKB:P9WGU9, ECO:0000269|PubMed:33476646}. | Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile) |
G7IYC1 | CAD2_MEDTR | MSSSNLGNVVCVTGASGYIASWLVRLLLHRGYTVKATVRDPNDPKKVDHLVKLDGAKERLQLFKANLLEEGAFDSVVQGCHGVFHTASPFYHDVKDPQAELIDPALKGTLNVLNSCAKSPSLKRVVLTSSIAAVAYNGKPRTPDVVVDETWFTDADFCAKSNLWYVVSKTLAEEAAWKFVKENNIDMVTINPAMVIGPLLQPVLNTSAAAILNLINGAQTFPNASFGWVNVKDVANAHILAYENASASGRHCLVERVAHYSEVVRILRELYPSLQLPEKCADDKPYVPIYQVSKEKAKSLGLEYTPLEVSIKETVESLKEKKFANL | 1.2.1.44 | null | phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamyl-alcohol dehydrogenase activity [GO:0045551]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; sinapyl alcohol dehydrogenase activity [GO:0052747] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:25217505}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64649; Evidence={ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:25217505}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64653; Evidence={ECO:0000269|PubMed:25217505}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for coumaraldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; KM=6.6 uM for coniferaldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; KM=730 uM for sinapaldehyde (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; Vmax=119 nmol/sec/mg enzyme with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; Vmax=27.3 nmol/sec/mg enzyme with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; Vmax=0.64 nmol/sec/mg enzyme with sinapaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:25217505}; Note=kcat is 0.46 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.10 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.24 sec(-1) with sinapaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). {ECO:0000269|PubMed:25217505}; | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:25217505}. | null | null | FUNCTION: Involved in lignin biosynthesis (By similarity). Regulates the monolignol composition by catalyzing the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (By similarity). Can use coumaraldehyde and coniferaldehyde as substrates, but barely sinapaldehyde (PubMed:25217505). {ECO:0000250|UniProtKB:A0A059TC02, ECO:0000269|PubMed:25217505}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JEE5 | CCR2_MEDTR | MPAYDNTSSVSGGDQTVCVTGAGGFIASWLVKLLLERGYTVRGTVRNPEDPKNGHLKELEGARERLTLHKVDLLDLQSIQSVVHGCHGVFHTASPVTDNPDEMLEPAVNGTKNVIIASAEAKVRRVVFTSSIGTVYMDPNTSRDVVVDESYWSDLEHCKNTKNWYCYGKTVAEQSAWDIAKENQVDLVVVNPVVVLGPLLQPTINASTIHILKYLNGAAKTYVNATQSYVHVKDVALAHLLVYETNSASGRYICCETALHRGEVVEILAKYFPEYPLPTKCSDEKNPRVKPYKFSNQKLKDLGLEFTPVKQCLYDTVRSLQEKGHLPIPPMQEDSA | 1.2.1.-; 1.2.1.44 | null | lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF01370; | 3.40.50.720; | NAD(P)-dependent epimerase/dehydratase family, Dihydroflavonol-4-reductase subfamily | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; CATALYTIC ACTIVITY: Reaction=(E)-caffeyl aldehyde + CoA + NADP(+) = (E)-caffeoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:74867, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87136; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:74869; Evidence={ECO:0000269|PubMed:20876124}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=32.7 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=23.4 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=12.4 uM for coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.48 umol/min/mg enzyme with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.32 umol/min/mg enzyme with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.35 umol/min/mg enzyme with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.44 umol/min/mg enzyme with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Note=kcat is 18.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 12.0 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 17.4 min(-1) with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). {ECO:0000269|PubMed:20876124}; | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}. | null | null | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of caffeoyl-CoA and coumaroyl-CoA to caffaldehyde and coumaraldehyde, respectively (PubMed:20876124). Also active, with a lower efficiency, toward feruloyl-CoA and sinapoyl-CoA (PubMed:20876124). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). {ECO:0000250|UniProtKB:A0A059TC02, ECO:0000269|PubMed:20876124}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JFU5 | ARGI_MEDTR | MSTIARRGFHYMQRLNSANVSPALLEKAQNRVIDAALTFIRERAKFKGELMRSLGGVAATSSLLGVPLGHHSSFHEGSAFAPPRIREAIWCDSTNSTTEEGKNLRDPRVITNVGDVPIEEIRDCGVDDKRLANVISESVKLVMDEDPLRPLVLGGDHSISFPVVRAVSEKLGGAVDILHFDAHPDLYHDFEGNYYSHASPFARIMEGGYARRLVQVGIRSITNDVREQVKKYGVETHEMRTLSRDRPILENLKLGEGVKGVYVSIDVDSLDPSIAPGVSHHEPGGLLFRDILNILQNLQGDIVGGDVVEYNPQRDTYDGITALVAAKLVRELAAKMSK | 3.5.3.1; 3.5.3.11 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:32754173}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:32754173}; | arginine catabolic process to ornithine [GO:0019547]; protein hexamerization [GO:0034214]; putrescine biosynthetic process from arginine, using agmatinase [GO:0033389]; urea cycle [GO:0000050] | mitochondrion [GO:0005739] | agmatinase activity [GO:0008783]; arginase activity [GO:0004053]; metal ion binding [GO:0046872] | PF00491; | 3.40.800.10; | Arginase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000305|PubMed:32754173}; CATALYTIC ACTIVITY: Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145, ChEBI:CHEBI:326268; EC=3.5.3.11; Evidence={ECO:0000250|UniProtKB:P46637}; | null | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000305}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L-ornithine (Probable). The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline (Probable). Possesses agmatinase activity. Catalyzes the formation of putrescine from agmatine (By similarity). {ECO:0000250|UniProtKB:P46637, ECO:0000305, ECO:0000305|PubMed:32754173}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7JIK2 | SUNN_MEDTR | MKNITCYLLLLCMLFTTCYSLNNDLDALLKLKKSMKGEKAKDDALKDWKFSTSASAHCSFSGVKCDEDQRVIALNVTQVPLFGHLSKEIGELNMLESLTITMDNLTGELPTELSKLTSLRILNISHNLFSGNFPGNITFGMKKLEALDAYDNNFEGPLPEEIVSLMKLKYLSFAGNFFSGTIPESYSEFQKLEILRLNYNSLTGKIPKSLSKLKMLKELQLGYENAYSGGIPPELGSIKSLRYLEISNANLTGEIPPSLGNLENLDSLFLQMNNLTGTIPPELSSMRSLMSLDLSINGLSGEIPETFSKLKNLTLINFFQNKLRGSIPAFIGDLPNLETLQVWENNFSFVLPQNLGSNGKFIYFDVTKNHLTGLIPPELCKSKKLKTFIVTDNFFRGPIPNGIGPCKSLEKIRVANNYLDGPVPPGIFQLPSVQIIELGNNRFNGQLPTEISGNSLGNLALSNNLFTGRIPASMKNLRSLQTLLLDANQFLGEIPAEVFALPVLTRINISGNNLTGGIPKTVTQCSSLTAVDFSRNMLTGEVPKGMKNLKVLSIFNVSHNSISGKIPDEIRFMTSLTTLDLSYNNFTGIVPTGGQFLVFNDRSFAGNPSLCFPHQTTCSSLLYRSRKSHAKEKAVVIAIVFATAVLMVIVTLHMMRKRKRHMAKAWKLTAFQKLEFRAEEVVECLKEENIIGKGGAGIVYRGSMANGTDVAIKRLVGQGSGRNDYGFKAEIETLGRIRHRNIMRLLGYVSNKDTNLLLYEYMPNGSLGEWLHGAKGCHLSWEMRYKIAVEAAKGLCYLHHDCSPLIIHRDVKSNNILLDADFEAHVADFGLAKFLYDPGASQSMSSIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELIIGRKPVGEFGDGVDIVGWINKTELELYQPSDKALVSAVVDPRLNGYPLTSVIYMFNIAMMCVKEMGPARPTMREVVHMLTNPPHSTSHNLINL | 2.7.11.1 | null | cell differentiation [GO:0030154]; phosphorylation [GO:0016310] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305}; 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:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: LRR receptor kinase involved in the regulation of root growth and root nodule organogenesis (PubMed:16240175, PubMed:16941903, PubMed:22399647). Involved in long distance nodulation signaling events (Probable) (PubMed:22399647). Involved in the autoregulation of nodulation (AON), a long distance systemic signaling from root to shoot and back again, which allows legumes to limit the number of root nodules formed based on available nitrogen and previous rhizobial colonization (Probable) (PubMed:27135324). Acts from shoot to root to control AON (PubMed:27135324, PubMed:28592666). Interacts with CLE12 and CLE13 signaling to control nodule numbers (PubMed:22168914). Required for the modulation of shoot-to-root auxin transport in response to altered nitrogen tissue concentrations and in the absence of rhizobia (PubMed:22399647). Shoot-to-root auxin transport influences lateral root density and length (PubMed:22399647). Involved in the regulation of root colonization by arbuscular mycorrhizal (AM) fungi (PubMed:16941903, PubMed:31477892). Interacts with CLE33 and CL53 signaling to repress strigolactone biosynthetic genes and strigolactone content in the roots, and consequently reduces the promotion of further colonization by AM fungi (PubMed:31477892). {ECO:0000269|PubMed:16240175, ECO:0000269|PubMed:16941903, ECO:0000269|PubMed:22168914, ECO:0000269|PubMed:22399647, ECO:0000269|PubMed:27135324, ECO:0000269|PubMed:28592666, ECO:0000269|PubMed:31477892, ECO:0000305|PubMed:22168914, ECO:0000305|PubMed:22301956}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7KDA1 | PHT18_MEDTR | MATSHGVLRSLDNAKTQSYHYLAIVIAGMGFFTDAYDLFCITAVTKLIGRLYYSDPTNHSPGILPTNVNNAITGVALCGTLAGQLFFGWLGDKLGRKKVYGITLTTMVGFALLSGLSFGSTPKTVVTSLCFFRFWLGFGIGGDYPLSAVIMSEYANQKTRGSFIAAVFAMQGVGILVAGGVAMFVSKLFLLYFPAPDFETDAVLSTQPEGDFVWRIVLMFGAVPAALTYYWRMKMPETARYTALVEGDHKKAVEDMAKVLDRNILSEESNTRIAIRPLESHSYGLFSSEFLNRHGLHLLGTTSTWFLLDIAFYSLQLTQKDIYPTSGLVYKASKMNAIEEVFQLSRAMFAVALIATVPGYWCTVFLIEKIGRFRIQLIGFLVMSVCMWFLGHNYRSFRGEESACKNGSKYSFCNGNPVMFAILFGLTLFFANFGPNSTTFIVPAELFPARLRSTCHGISAAAGKSGAIVGAFGVQSYIGNSHDKSKGTKQAIMALAVVNLLGFFFTFLVPETQGRSLEEISGEEKDFQGNNADEEISGERNGTRNASVDKSPETSMV | null | null | arbuscular mycorrhizal association [GO:0036377]; cellular response to nitrogen levels [GO:0043562]; phosphate ion transport [GO:0006817]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | hydrolase activity [GO:0016787]; 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:0000269|PubMed:25841038}; 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:0000269|PubMed:25841038}. | 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) that may be involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi (e.g. Glomus versiforme and G.intraradices) during AM symbiosis; not required for mycorrhizal arbuscule development. {ECO:0000269|PubMed:25841038}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7KGT0 | LGB8_MEDTR | MGFTEKQESLVNSSWESFKQNLSGYSVLFYTIILEKAPAAKGMFSFLKDTTGVQDSPQLQAHAAKVFEMVRDSAVQLRATGEVILGDATLGAIHIQKGVVDPHFVVVKEALLKTIKEAAGGNWSEELSTAWEVAYDGLAASIKKSMS | null | null | null | cytoplasm [GO:0005737] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | PTM: Nitrated in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-). Nitration level decrease during nodule senescence. {ECO:0000250|UniProtKB:P02234}.; PTM: Phosphorylation at Ser-45 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29868087}. Nucleus {ECO:0000250|UniProtKB:P02240}. | null | null | null | null | null | FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (By similarity). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:29868087, PubMed:32442331). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:29868087, PubMed:32442331). {ECO:0000250|UniProtKB:Q43296, ECO:0000269|PubMed:29868087, ECO:0000303|PubMed:17540516, ECO:0000303|PubMed:32442331}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7L166 | RAM1_MEDTR | MINSLCGSSNSLKEKCLQPNSSNQTNTHSKKNATNSCGDLEQINVLTPQSLNLPSLKFDLDGDVEVQSPDSSMWEAFFNDHLDNDFMISSPIRNINPNSPQASTYNNCNYNYAQGMQIQSLSGCSPPRFASQIGSLNSNNQQKGKGLSPLHRVFNSPNNQYMQHVENLSLPAIEEFLEDFQGDVDHFSSTKVSSECFDMETPISTILDSLTMQNSSSYGASVNEESTLLHGGNSSSQISQESDIYHQMGSMASASLSQALQQERYQEKHQKMQAQQQSLTVPIQIGIEQEQDSGLQLVHLLLACAEAVAKGEYMLARRYLHQLNRVVTPLGDSMQRVASCFTESLSARLAATLTTKSSSTKKLAPSSLSSSSSSSCLSTFPSNPMEVLKIYQIVYQACPYIKFAHFTANQAIFEAFEAEERVHVIDLDILQGYQWPAFMQALAARPGGAPFLRITGVGPCIESVRETGRCLTELAHSLRIPFEFHPVGEQLEDLKPHMFNRRVGEALAVNTVNRLHRVPGNHLGNLLSMIRDQAPNIVTLVEQEASHNGPYFLGRFLEALHYYSAIFDSLDATFPVESAPRAKVEQYIFAPEIRNIVACEGEERIERHERLEKWRKIMEGKGFKGVPLSPNAVTQSRILLGLYSCDGYRLTEDKGCLLLGWQDRAIIAASAWRC | null | null | arbuscular mycorrhizal association [GO:0036377]; detection of phosphate ion [GO:0010247]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to nutrient [GO:0007584]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF03514; | null | GRAS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23122845}. Cytoplasm {ECO:0000250|UniProtKB:A0A145P7T2}. | null | null | null | null | null | FUNCTION: Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. AMT2;4, AMT2;5, EXO70I, STR, RAM2, LEC5, PT4, VPY, BCP1, SCP1 and RAD1) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis and Glomus versiforme) (PubMed:23122845, PubMed:25971550, PubMed:26511916). Promotes directly the expression of RAM2, EXO70I, STR and RAD1 (PubMed:26511916). Not necessary to enable hyphopodium formation or hyphal entry into the root but essential to support arbuscule branching (PubMed:26511916). Involved in the phosphate-mediated suppression of AM fungi colonization in mycorrhiza (PubMed:26511916). Also involved in restricting mycorrhizal colonization of the root meristem (By similarity). Required for Myc factor signaling from mycorrhizal fungi, but has no function in Nod factor signaling from rhizobial bacteria (PubMed:23122845). Regulates the expression of RAM2, a glycerol-3-phosphate acyl transferase that promotes cutin biosynthesis to enhance mycorrhizal hyphopodia formation (PubMed:23122845). {ECO:0000250|UniProtKB:A0A0M4FMK2, ECO:0000269|PubMed:23122845, ECO:0000269|PubMed:25971550, ECO:0000269|PubMed:26511916}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G7LCV1 | KI106_MEDTR | MSMRLSIRTLIILAHVCLFITTTTIAQFVLDTVGEPVEGDEEYFIRPVITNKGGRSTMVSRNESCPLHVGLELTGLGRGLVVKFTPFAPHHDFDDVRVNRDLRITFQASSSCVQSTEWRLGEKDTKSGRRLIITGTDSATNGSYGNFFRIVETPLEGMYNIQWCPTEVCPSCKFECGTVDMLNENGKILLALDGGPLPLVFQKE | null | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610] | apoplast [GO:0048046]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00197; | 2.80.10.50; | Protease inhibitor I3 (leguminous Kunitz-type inhibitor) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}. | null | null | null | null | null | FUNCTION: Protease inhibitor that, together with SCP1, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis), probably by degrading SCP1 in the apoplast of the periarbuscular region. {ECO:0000269|PubMed:23662629}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
G8BAW7 | FAS2_CANPC | MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAVVDSAALDALIAENKKLARQQLETLARYLQVDLTKGEKAFIKEKEATTVLQQELDLWEAEHGEFYAKGIKPVFSPLKSRTYDSYWNWARQDLLSMWFDILFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHVELCPTYRGETYKLGKRLGEQLIENCKQILGQSPVYKDVSRITGPKTTVSAKGDIVYEEANKESVRKFEQYVFEMAQGGSMTKMKQSSIQEDLARVYKAISKQASRDSKLELQKVYDQLLKVVEGSTEIETEQTTQDALAIPTGSNTPTEEDELSTASDDDEIASLPDKTSIAQPVSSTIPNKTIPFLHIQSKSESGNWEYDRKLSSIYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRYSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVEYIYNDQKKGGLGWDLDVIIPFAAIPENGNGIDNIDSKSEFAHRIMLTNLLRLLGAVKARKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGTKLTICGAIIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVNLCQEEPVMADLNGGLQFIDNLKEFTSKLRNDLTETADIRRAVSIESAIEQKVVNGDNVDSNYNKVTVRPRANMKFDFPTLKSYDEIKQIAPDLEGMLDLENVVVVTGFAEVGPWGNARTRWEMESKGEFSLEGAIEMAWIMGMIKYHNGNLKGKPYSGWIDAKTQTPVDDKDIKAKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVIQHDLEPFECSKETAEQYKHEHGDKCEISEIEESGEYSVRILKGATLFIPKALRFDRLVAGQIPTGWDARTYGIPEDTINQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSASGPIKTPVGACATAVESVDIGIETILSGKAKVVMVGGYDDFQEEGSYEFANMNATSSAIDEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMSADLALKMGVPIHAVLAMSATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNVKYRKRQLSKRLDQIKSWESSELNYLQEEAHLAKEEFGEEFSEAEFLRERTEEIYRESKRQVADAKKQWGNAFYKSDPRIAPLRGALATFNLTIDDIGVASFHGTSTVANDKNESATIDSMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGIVPGNRNADNVDKVLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLYAVLDRSTYEDYAKRVTARNKKTYRYMHNAITRNTMFVAKDKAPYSDELTMDVYLDPLARVSKTKNEFVFTKKSVQSDKSYVSNIANSTAKALSSLNKSSKGVGVDVELLSELNIDNETFLERNFTPEEIKYCQNSANPQASFTGTWSAKEATFKALGVSSQGGGASLKEIEIVRDGNGAPQVVLNDNAKAAAKAAGVKNVNVSISHDDFQATAVALSEF | 1.1.1.100; 2.3.1.41; 2.3.1.86 | null | fatty acid biosynthetic process [GO:0006633]; mitotic nuclear membrane biogenesis [GO:0101026]; palmitic acid biosynthetic process [GO:1900535]; single-species biofilm formation on inanimate substrate [GO:0044011] | fatty acid synthase complex [GO:0005835] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; fatty-acyl-CoA synthase activity [GO:0004321]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:0000287] | PF01648;PF00106;PF18325;PF18314;PF00109;PF02801; | 3.30.70.2490;3.40.47.10;3.90.25.70;6.10.140.1410;6.10.250.1930;3.90.470.20;3.40.50.720; | Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; | null | null | null | null | FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. {ECO:0000269|PubMed:20027295}. | Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis) |
G8GER6 | PETH1_THEFU | MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF | 3.1.1.101; 3.1.1.74 | null | null | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | acetylesterase activity [GO:0008126]; cutinase activity [GO:0050525] | PF12146; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604968}. Periplasm {ECO:0000269|PubMed:23604968}. | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638}; CATALYTIC ACTIVITY: Reaction=H2O + pentanoate ester = an aliphatic alcohol + H(+) + pentanoate; Xref=Rhea:RHEA:48436, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011, ChEBI:CHEBI:50871; Evidence={ECO:0000269|PubMed:23604968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48437; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:23604968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47361; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:23604968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:23604968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:23604968}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:23604968}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=131 uM for pNP-butanoate (at 50 degrees Celsius and pH 8) {ECO:0000269|PubMed:23604968}; Note=kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50 degrees Celsius and pH 8). {ECO:0000269|PubMed:23604968}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:23604968}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:23604968). Optimum temperature is 65 degrees Celsius (PubMed:32269349). {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:32269349}; | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Probable). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:23604968, PubMed:25545638). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638, PubMed:32269349). {ECO:0000269|PubMed:23604968, ECO:0000269|PubMed:25545638, ECO:0000269|PubMed:32269349, ECO:0000305|PubMed:23604968}. | Thermobifida fusca (Thermomonospora fusca) |
G8H5M7 | TPS9_SOLHA | MAASSANKSRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFHNEIETSIQNIFDAPKQNNNLHIVSLHFRLVRQQGHYMSSDVFKQFTNQDGKFKERLTNDVQGLLSLYEASYLRVRDEEILEEALAFTTTHLKSIVSNMSNNNNSLKVEVSEALTQPIRMTLPRMEARRYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVLKMTSIIDDTFDAYATFDELEPFNDAIQRWDANAIDSIQPYMRPAYQAFLDIYSEMEQVLSKEGKLDRVYYAKNEMKKLVRAYFKETQWLNDCDHIPKYEEHMENSLVSGGYMMIPTTCLVGMEEFISIETFEWLMNDPLIVRASSLIARAMNDIVGHEVEQERGHVASLIECYMKDYGASKQEAYAKFKKDVTNAWKDINKEFFRPTEVPMFVLERVLNLTRAADTLYKEKDAYTNAKGKLKNMINSILIESVKI | 4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B + diphosphate; Xref=Rhea:RHEA:25444, ChEBI:CHEBI:5337, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.71; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25445; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + germacrene A; Xref=Rhea:RHEA:68776, ChEBI:CHEBI:33019, ChEBI:CHEBI:36517, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68777; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:68780, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68781; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E)-germacrene B, but also smaller amounts of germacrene A and C, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-humulene, germacrene A and germacrene B (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5M8 | TPS12_SOLHA | MAASSADKSRPLANFSPTVWGYHFLSYTPEISSQEKHEVDELKEIFRKMLVETCDNSTQKLVLIDTIQRLGVAYHFDNEIETSIQNIFDASKQNDNDDNLHIVSLRFRLVRQQGHYMSSDVFKQFTNQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESIVSNLSNNNKVEVSEALTQPIRMTLPRMGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNDAIQRWDINAIDSVPPYLRHAYQALLDIYSEMEQELAKEFKSDRVYYAKYEMKKLVRAYFKEAQWLNDDNHIPKYEEHMENAMVSAGYMMGATTCLVGVDEFISQETFEWIINEPLIVRASSLIARAMDDIAGHEVEQQREHGASLIECYMKDYGVSKQEAYVKFQKEVTNGWMDINKEFFCLDVQVPKFVLERVLNFTRVINTLYKEKDEYTNSKGKFKNMIITLLVESVEI | 4.2.3.-; 4.2.3.104; 4.2.3.106; 4.2.3.113; 4.2.3.15; 4.2.3.57 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019, ChEBI:CHEBI:49238, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + gamma-curcumene; Xref=Rhea:RHEA:68784, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:63696; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68785; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-curcumene and (Z)-gamma-bisabolene (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene and terpinolene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5M9 | TS14A_SOLHA | MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTETSSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVSGLLNLYEATHLRVHGEEILEDALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKYLDYENKYPYARDKLVECYFWATGVYFGPQYKRARKTLTKLIVIITITDDLYDAYATYDELVPYTDAVERCEISAMHSISPYMRPLYQVFLDYFDEMEKELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITVSSQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG | 4.2.3.-; 4.2.3.15; 4.2.3.47; 4.2.3.59 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (Z)-alpha-bisabolene + diphosphate; Xref=Rhea:RHEA:68532, ChEBI:CHEBI:33019, ChEBI:CHEBI:49241, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68533; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-acoradiene + diphosphate; Xref=Rhea:RHEA:68520, ChEBI:CHEBI:33019, ChEBI:CHEBI:172925, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68521; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:68508, ChEBI:CHEBI:33019, ChEBI:CHEBI:39242, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68509; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, beta-farnesene, (E)-gamma-bisabolene, beta-acoradiene, selinene and (Z)-alpha-bisabolene (PubMed:21818683). Low or no activity with (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene and limonene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5N0 | TPS17_SOLHA | MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSNSLEKLELINTIQCLGLAYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTITKLKQILPKLSNSQLAQQITNALKFPIKDGIVRVETRKYISFYQQNQNHNQVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFFISIIDDTYDIYGKLDELTLFTQAIERWNIDASEQLPLYMKIIYRDLLDVYDEIEKELANENKSFLVNYSINEMKKVVRGYFQEAKWYYGKKVPKMEQYMKNAISTSAYILLTTTSWLAMGNVATKDVFDWVATEPKLVVASCHIIRLLNDLVSHEEEQKRGNAASAVECYMNEYSVTQEEAHVKIRDIIENYWKDLNEEYFKVDMIIIPRVLLMCIINLTRVAEFIYKDEDAYTFSKNNLKDVISDILVDPII | 4.2.3.-; 4.2.3.106; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.47; 4.2.3.54; 4.2.3.73; 4.2.3.81 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate; Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700, ChEBI:CHEBI:175763; EC=4.2.3.73; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29512; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-gurjunene; Xref=Rhea:RHEA:68400, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763, ChEBI:CHEBI:178033; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68401; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019, ChEBI:CHEBI:49238, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene + diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019, ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene + diphosphate; Xref=Rhea:RHEA:30471, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:61679; EC=4.2.3.54; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30472; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-alpha-bergamotene and (Z)-gamma-bisabolene as well as beta-bisabolene, (Z)-alpha-bergamotene and (E)-gamma-bisabolene to a lower extent (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene, terpinolene, gamma-terpinene and (Z)-beta-ocimene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8H5N1 | TS14B_SOLHA | MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTEISSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEEILEEALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWAIGVYFGPQYKRARRTLTKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMHSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITISNQMNLITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQITNAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG | 4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.47; 4.2.3.59; 4.2.3.79 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; terpenoid biosynthetic process [GO:0016114] | null | hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019, ChEBI:CHEBI:49239, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate; Xref=Rhea:RHEA:68472, ChEBI:CHEBI:33019, ChEBI:CHEBI:49242, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68473; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:68504, ChEBI:CHEBI:33019, ChEBI:CHEBI:39242, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68505; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (+)-thujopsene + diphosphate; Xref=Rhea:RHEA:30375, ChEBI:CHEBI:33019, ChEBI:CHEBI:61737, ChEBI:CHEBI:175763; EC=4.2.3.79; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30376; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:68544, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68545; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:68508, ChEBI:CHEBI:33019, ChEBI:CHEBI:39242, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68509; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-acoradiene + diphosphate; Xref=Rhea:RHEA:68516, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:172925; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68517; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = alpha-acoradiene + diphosphate; Xref=Rhea:RHEA:68512, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:172926; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68513; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (-)-alpha-cedrene + diphosphate; Xref=Rhea:RHEA:68536, ChEBI:CHEBI:10216, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68537; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate; Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = beta-acoradiene + diphosphate; Xref=Rhea:RHEA:68520, ChEBI:CHEBI:33019, ChEBI:CHEBI:172925, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68521; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate = (-)-alpha-cedrene + diphosphate; Xref=Rhea:RHEA:68540, ChEBI:CHEBI:10216, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68541; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21818683}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21818683}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21818683}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into (+)-thujopsene, beta-bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-farnesene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-gamma-bisabolene, (E)-alpha-bisabolene, (E)-beta-farnesene, (Z)-beta-farnesene, beta-bisabolene, beta-acoradiene and alpha-acoradiene (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene (PubMed:21818683). {ECO:0000269|PubMed:21818683}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
G8JYC6 | PDF1_CAEEL | MNRFIISMIALLAVFCAVSTASPLLYRAPQYQMYDDVQFVKRSNAELINGLIGMDLGKLSAVGKRSNAELINGLLSMNLNKLSGAGRR | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; locomotion [GO:0040011]; locomotion involved in locomotory behavior [GO:0031987]; locomotor rhythm [GO:0045475]; locomotory exploration behavior [GO:0035641]; male mating behavior [GO:0060179]; parturition [GO:0007567]; positive regulation of gene expression [GO:0010628]; positive regulation of protein secretion [GO:0050714]; sleep [GO:0030431] | extracellular region [GO:0005576] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable ligand of isoforms a and b of the calcitonin receptor-like protein, pdfr-1, a G-protein coupled receptor (PubMed:18390545). May not signal through isoform c of pdfr-1 (PubMed:18390545). Involved in locomotion; more specifically mate searching behavior of males, independent of nutritional status (PubMed:18390545, PubMed:22579613, PubMed:23143519, PubMed:30024377). Involved in regulating the male-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory neurons (PubMed:30024377). Plays a role in circadian rhythms of locomotor activity (PubMed:26113231). Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity, and working in concert with neuropeptide flp-2 (PubMed:23764289, PubMed:27585848). In the presence of food, plays a role in initiating and extending exploratory roaming behavior, in opposition to 5-hydroxytryptamine (serotonin) signaling. {ECO:0000269|PubMed:18390545, ECO:0000269|PubMed:22579613, ECO:0000269|PubMed:23143519, ECO:0000269|PubMed:23764289, ECO:0000269|PubMed:23972393, ECO:0000269|PubMed:26113231, ECO:0000269|PubMed:27585848, ECO:0000269|PubMed:30024377}. | Caenorhabditis elegans |
G8JZS4 | SUSB_BACTN | MKKRKILSLIAFLCISFIANAQQKLTSPDNNLVMTFQVDSKGAPTYELTYKNKVVIKPSTLGLELKKEDNTRTDFDWVDRRDLTKLDSKTNLYDGFEVKDTQTATFDETWQPVWGEEKEIRNHYNELAVTLYQPMNDRSIVIRFRLFNDGLGFRYEFPQQKSLNYFVIKEEHSQFGMNGDHIAFWIPGDYDTQEYDYTISRLSEIRGLMKEAITPNSSQTPFSQTGVQTALMMKTDDGLYINLHEAALVDYSCMHLNLDDKNMVFESWLTPDAKGDKGYMQTPCNTPWRTIIVSDDARNILASRITLNLNEPCKIADAASWVKPVKYIGVWWDMITGKGSWAYTDELTSVKLGETDYSKTKPNGKHSANTANVKRYIDFAAAHGFDAVLVEGWNEGWEDWFGNSKDYVFDFVTPYPDFDVKEIHRYAARKGIKMMMHHETSASVRNYERHMDKAYQFMADNGYNSVKSGYVGNIIPRGEHHYGQWMNNHYLYAVKKAADYKIMVNAHEATRPTGICRTYPNLIGNESARGTEYESFGGNKVYHTTILPFTRLVGGPMDYTPGIFETHCNKMNPANNSQVRSTIARQLALYVTMYSPLQMAADIPENYERFMDAFQFIKDVALDWDETNYLEAEPGEYITIARKAKDTDDWYVGCTAGENGHTSKLVFDFLTPGKQYIATVYADAKDADWKENPQAYTIKKGILTNKSKLNLHAANGGGYAISIKEVKDKSEAKGLKRL | 3.2.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18981178}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:18981178}; | starch catabolic process [GO:0005983] | periplasmic space [GO:0042597]; plasma membrane [GO:0005886] | alpha-1,4-glucosidase activity [GO:0004558]; calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; glucan 1,4-alpha-glucosidase activity [GO:0004339] | PF14509;PF14508;PF10566; | 2.70.98.10;3.20.20.70; | Glycosyl hydrolase 97 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8955399}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000269|PubMed:18981178}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.05 mM for maltose {ECO:0000269|PubMed:18981178}; KM=0.29 mM for maltotriose {ECO:0000269|PubMed:18981178}; KM=0.64 mM for maltotetraose {ECO:0000269|PubMed:18981178}; KM=1.29 mM for maltopentaose {ECO:0000269|PubMed:18981178}; KM=2.71 mM for maltohexaose {ECO:0000269|PubMed:18981178}; KM=4.58 mM for maltoheptaose {ECO:0000269|PubMed:18981178}; KM=6.89 mM for amylose DP17 {ECO:0000269|PubMed:18981178}; KM=0.67 mM for soluble starch {ECO:0000269|PubMed:18981178}; KM=2.39 mM for kojibiose {ECO:0000269|PubMed:18981178}; KM=3.14 mM for nigerose {ECO:0000269|PubMed:18981178}; KM=6.34 mM for isomaltose {ECO:0000269|PubMed:18981178}; KM=0.31 mM for panose {ECO:0000269|PubMed:18981178}; KM=0.16 mM for p-nitrophenyl alpha-glucoside {ECO:0000269|PubMed:18981178}; Note=kcat is 182 sec(-1) for maltose. kcat is 270 sec(-1) for maltotriose. kcat is 321 sec(-1) for maltotetraose. kcat is 434 sec(-1) for maltopentaose. kcat is 346 sec(-1) for maltohexaose. kcat is 381 sec(-1) for maltoheptaose. kcat is 321 sec(-1) for amylose DP17. kcat is 115 sec(-1) for soluble starch. kcat is 141 sec(-1) for kojibiose. kcat is 207 sec(-1) for nigerose. kcat is 105 sec(-1) for isomaltose. kcat is 160 sec(-1) for panose. kcat is 161 sec(-1) for p-nitrophenyl alpha-glucoside. {ECO:0000269|PubMed:18981178}; | PATHWAY: Glycan degradation; starch degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:18981178}; | null | FUNCTION: Glucoamylase that hydrolyzes alpha-1,4-glucosidic linkages, alpha-1,6-, alpha-1,3- and alpha-1,2-glucosidic linkages during starch degradation. {ECO:0000269|PubMed:18981178, ECO:0000269|PubMed:8955399}. | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8JZS6 | SUSF_BACTN | MKKHLIYTGMFLAAIGFSACNEDFKDWADPQSNPQEESAGQLTATFTAGKDASIVMDAATADSVEIAKLSSTTAEEGSKIAVNSLTLNENHTIPFSMTEDHVFKVALAQLDSVTQEAYKSRASVVRELKISINASAVTPSGEGIQLVGNEVSITLQPATTPAVDPDGYYIVGDFTGWDGNSAQQMKKDALDENLYILEAEIESTSNFKIFPASAINGNDIDWTKALGSSVDGDDSGDNFVSWTNAGAINTALDGKIKISFDAFNYRFTVKDNSAPTELYMTGSAYNWGTPAGDPNAWKALVPVNGTKGTFWGIFYFAANDQVKFAPQANWGNDFGFVDAISQESKDLAGLSDEGGNLKVGIAGWYLVYVSVIGDDKVIEFEKPNVYLMGDTSYNGWDAQLVEQDLFTVPGTADGEFVSPAFLKDGAVRICVNPKAVSAGDWWKTEFIIFDGQIAYRGNGGDQAAVQGKTGQKVYLNFGNGTGRIE | null | null | starch catabolic process [GO:0005983]; starch metabolic process [GO:0005982] | cell outer membrane [GO:0009279]; outer membrane [GO:0019867] | starch binding [GO:2001070] | PF17142;PF16411; | 2.60.40.3610;2.60.40.3620;2.60.40.3640; | SusF family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:22910908}. | null | null | PATHWAY: Glycan degradation; starch degradation. | null | null | FUNCTION: Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has lower affinity for starch compared to SusE. {ECO:0000269|PubMed:10986238, ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:22910908}. | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8JZT0 | SUSE_BACTN | MKKISNILLAVTFALPLFTACETDNDSNPILNEPDTFTLNTPAYAANNVYDLKNAQTVELTCSQPDYGFPAATTYTVQASFEQDFIEATDESKANYTVLESTSPTAKINVDASELNNALLDLWTAVNGEQAELPTEPVAVYIRLKANITSSGKGVCFSNVIELPNVLISKSTSSLTPPKTMFIVGSMLDTDWKVWKPMAGVYGMDGQFYSMIYFDANSEFKFGTKENEYIGINDNRVTVTDKAGAGVSGSDNFVVENAGWYLFYVKAAVKGDDYQFTITFYPAEVYLFGNTTGGSWAFNDEWKFTVPATKDGNFVSPAMTASGEVRMCFKTDLDWWRTEFTLHDGEIFYRDFNLIDSWTEKGDGYSIQGSAGNVIHLNFTAGTGEKK | null | null | starch catabolic process [GO:0005983] | cell outer membrane [GO:0009279]; outer membrane [GO:0019867] | starch binding [GO:2001070] | PF14292;PF16411; | 2.60.40.3610;2.60.40.3620; | SusE family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:22910908}. | null | null | PATHWAY: Glycan degradation; starch degradation. | null | null | FUNCTION: Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF. {ECO:0000269|PubMed:10986238, ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:22910908}. | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
G8XQX1 | OXLA_DABRR | MNVFFMFSLLFLATLGSCADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVIVGAGMSGLSAAYVLAGAGHKVTVLEASERPGGRVRTHRNVKEGWYANLGPMRVPEKHRIIREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVHFKARVIKIQQNAEKVTVTYQTTQKNLLLETADYVIVCTTSRAARRITFKPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIQGGKSTTDLPSRFIYYPNHNFTTGVGVIIAYGIGDDANFFQALNLNECADIVFNDLSSIHQLPKKDLQTFCYPSIIQKWSLDKYAMGAITTFTPYQFQHFSEALTAPVGRIFFAGEYTANAHGWIDSTIKSGLTAARDVNRASEL | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063]; envenomation resulting in induction of edema in another organism [GO:0044398]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | flavin adenine dinucleotide binding [GO:0050660]; L-amino-acid oxidase activity [GO:0001716]; 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 | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21802487}. | 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:21802487}; 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:21802487}; 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:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:21802487}; 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:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:21802487}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.318 mM for L-Trp (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.49 mM for L-Leu (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=1.4 mM for L-Ile (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=12.2 mM for L-Arg (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=13.92 mM for L-Val (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=64 mM for L-Lys (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=116.48 mM for L-Ala (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; | 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:21802487). Is highly active on L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L-Val, L-Lys, and L-Ala (PubMed:21802487). Inhibits ADP- and collagen-induced platelet aggregation (PubMed:21802487). This inhibition is inhibited by catalase, indicating the importance of generated H(2)O(2) for the inhibitory effect (PubMed:21802487). This effect on platelets among snake L-amino-acid oxidases is however controversial, since some of them induce aggregation, whereas the other inhibit agonist-induced aggregation (By similarity). In vivo, this enzyme induces a rapid, substantial and reversible increase in the paw volume of mice (edema) (PubMed:21802487). In addition, myofibrosis, and inflammatory cell infiltration on the paw tissue are also observed (PubMed:21802487). {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:21802487}. | Daboia russelii (Russel's viper) (Vipera russelii) |
G8XYX6 | MOT8_DANRE | MHSESDDNTAGGTPGSEDPQAEESSSPAEEFEEQERKLAPEDSTVQLIHTGCTDKRPATPPGAHPGQGFVPPEGGFGWVVVFAATWCNGSIFGIQNSFGILHMMLVKHHEKQPDQASQFKVAWVGALAMGMIFFCSPVVSMFTDHFGCRKTAVCGAFVAFIGLLTSSFATTLGLWYFTYGILFGCGSSFAFQPSLVILGHYFRQRLGLANGVVTAGSSLFSMGLPVLLKKVVEPLGLPRTFQILSIFMLVQALLALAFKPLLPSGMCPMPGMALDGGPSTPESASRWQKGLAKIRRYFNVRVFSILTYRIWAFGVATAVLGYFVPYVHLLNFVKEQFGDTQREWLLLVCIGASSGVGRLLFGKIGDLIPGVKKIYMQVASFILLGVMSMMIPQCAVFEGLVVVFVLMGLCDGCFITIMAPIAFELVGPMQASQAIGYLLGLMAIPMTAGPPIAGLLHDHFGNYHVAFYLAGVPPIVGGIVMFFVPLVHQRMQKRRKETDDPSMDKMLKNCSNGDMLPGYTDMETHI | null | null | brain development [GO:0007420]; central nervous system development [GO:0007417]; chordate embryonic development [GO:0043009]; locomotion [GO:0040011]; neuron differentiation [GO:0030182]; oligodendrocyte differentiation [GO:0048709]; optomotor response [GO:0071632]; regulation of thyroid hormone generation [GO:2000609]; Schwann cell differentiation [GO:0014037]; spinal cord development [GO:0021510]; spinal cord oligodendrocyte cell differentiation [GO:0021529]; thyroid gland development [GO:0030878]; transmission of nerve impulse [GO:0019226] | apical plasma membrane [GO:0016324] | monocarboxylic acid transmembrane transporter activity [GO:0008028]; thyroid hormone binding [GO:0070324]; thyroid hormone transmembrane transporter activity [GO:0015349] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36021}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015; Evidence={ECO:0000269|PubMed:21952246, ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; Evidence={ECO:0000305|PubMed:21952246, ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71813; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71821; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=3,3',5'-triiodo-L-thyronine(out) = 3,3',5'-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71815, ChEBI:CHEBI:57261; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71816; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71817; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=3,3'-diiodo-L-thyronine(out) = 3,3'-diiodo-L-thyronine(in); Xref=Rhea:RHEA:71823, ChEBI:CHEBI:176514; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71824; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71825; Evidence={ECO:0000305|PubMed:31436139}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for T3 (at 26 degrees Celsius) {ECO:0000269|PubMed:21952246}; | null | null | null | FUNCTION: Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient (PubMed:21952246, PubMed:31436139). The substrate preference is 3,3-diiodothyronine (3,3'-T2) and T3 and to a lesser extentd T4 and rT3. Acts as a crucial regulator during embryonic development (PubMed:23161551). {ECO:0000269|PubMed:21952246, ECO:0000269|PubMed:23161551, ECO:0000269|PubMed:31436139}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
G9BY57 | PETH_UNKP | MDGVLWRVRTAALMAALLALAAWALVWASPSVEAQSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDYPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELDNASHFAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALSDFRTNNRHCQ | 3.1.1.101; 3.1.1.74 | null | null | extracellular region [GO:0005576] | acetylesterase activity [GO:0008126]; cutinase activity [GO:0050525] | PF12695; | 3.40.50.1820; | AB hydrolase superfamily | PTM: The disulfide bond between Cys-275 and Cys-292 contributes not only to the thermodynamic stability but also to the kinetic stability of the enzyme. {ECO:0000269|PubMed:24593046}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22194294}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:22194294}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:32269349}; CATALYTIC ACTIVITY: Reaction=4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol + H(+) + terephthalate; Xref=Rhea:RHEA:49532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30043, ChEBI:CHEBI:30742, ChEBI:CHEBI:131704; Evidence={ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:32269349}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:22194294}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:24593046}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:22194294}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:22194294}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for pNP-butanoate (at 30 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:24593046}; KM=0.21 mM for pNP-butanoate (at 50 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:24593046}; KM=0.24 mM for pNP-butanoate (at 70 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:24593046}; Note=kcat is 232 sec(-1) with pNP-butanoate as substrate (at 30 degrees Celsius and pH 8.0). kcat is 343 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8.0). kcat is 318 sec(-1) with pNP-butanoate as substrate (at 70 degrees Celsius and pH 8.0). {ECO:0000269|PubMed:24593046}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with pNP-butyrate as substrate. Shows 70% of the maximal activity at pH 7.0 and pH 9.5. {ECO:0000269|PubMed:22194294}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with pNP-butanoate as substrate (PubMed:22194294, PubMed:24593046). Optimum temperature using PET as substrate is superior to 70 degrees Celsius (PubMed:22194294). Shows 70% of the maximal activity at 30 and 70 degrees Celsius with pNP-butyrate as substrate. Has half-lives of 5 hours at 50 degrees Celsius, 80 minutes at 60 degrees Celsius, 40 minutes at 70 degrees Celsius and 7 minutes at 80 degrees Celsius (PubMed:22194294). Is thermostable, with a determined melting temperature (Tm) of 84.7 degrees Celsius (PubMed:32269349). {ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:24593046, ECO:0000269|PubMed:32269349}; | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:22194294). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters), with a preference for short-chain substrates (C4 substrate at most) (PubMed:22194294, PubMed:24593046). Cannot hydrolyze olive oil (PubMed:22194294). Is also able to degrade poly(ethylene terephthalate), the most abundant polyester plastic in the world (PubMed:22194294, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:22194294). {ECO:0000269|PubMed:22194294, ECO:0000269|PubMed:24593046, ECO:0000269|PubMed:32269349}. | Unknown prokaryotic organism |
G9FRD6 | HSDHB_CLOSR | MNFREKYGQWGIVLGATEGIGKASAFELAKRGMDVILVGRRKEALEELAKAIHEETGKEIRVLPQDLSEYDAAERLIEATKDLDMGVIEYVACLHAMGQYNKVDYAKYEQMYRVNIRTFSKLLHHYIGEFKERDRGAFITIGSLSGWTSLPFCAEYAAEKAYMMTVTEGVAYECANTNVDVMLLSAGSTITPTWLKNKPSDPKAVAAAMYPEDVIKDGFEQLGKKFTYLAGELNREKMKENNAMDRNDLIAKLGKMFDHMA | 1.1.1.201 | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | null | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; ketoreductase activity [GO:0045703]; nucleotide binding [GO:0000166] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:20233, ChEBI:CHEBI:15378, ChEBI:CHEBI:35349, ChEBI:CHEBI:47789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.201; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20235; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=NADP(+) + ursocholate = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADPH; Xref=Rhea:RHEA:53856, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137880; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53858; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=7-oxolithocholate + H(+) + NADPH = NADP(+) + ursodeoxycholate; Xref=Rhea:RHEA:47540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47541; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=3alpha,7beta-dihydroxy-12-oxo-5beta-cholan-24-oate + NADP(+) = 7,12-dioxo-lithocholate + H(+) + NADPH; Xref=Rhea:RHEA:53864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137789, ChEBI:CHEBI:137886; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53866; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=7beta-hydroxy-3,12-dioxo-5beta-cholan-24-oate + NADP(+) = dehydrocholate + H(+) + NADPH; Xref=Rhea:RHEA:53860, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137881, ChEBI:CHEBI:137882; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53862; Evidence={ECO:0000305|PubMed:22198717}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.59 mM for ursocholate {ECO:0000269|PubMed:22198717}; KM=2.3 mM for 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate {ECO:0000269|PubMed:22198717}; KM=3.06 mM for ursodeoxycholate {ECO:0000269|PubMed:22198717}; KM=2.65 mM for 7-oxolithocholate {ECO:0000269|PubMed:22198717}; KM=1.5 mM for 7,12-dioxo-lithocholate {ECO:0000269|PubMed:22198717}; KM=1.58 mM for dehydrocholate {ECO:0000269|PubMed:22198717}; Note=kcat is 407000 sec(-1) for the oxidation of ursocholate. kcat is 203000 sec(-1) for the reduction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate. kcat is 430000 sec(-1) for the oxidation of ursodeoxycholate. kcat is 639000 sec(-1) for the reduction of 7-oxolithocholate. kcat is 413000 sec(-1) for the reduction of 7,12-dioxo-lithocholate. kcat is 146000 sec(-1) for the reduction of dehydrocholate. {ECO:0000269|PubMed:22198717}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Shows a maximum of activity at pH 8.5 in the oxidation of ursocholate, and between pH 7.0 and 8.0 when tested in the reduction reaction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, with a gradual drop on the alkaline side and a sharp drop on the acidic side. {ECO:0000269|PubMed:22198717}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. No activity is detected above 60 degrees Celsius. {ECO:0000269|PubMed:22198717}; | FUNCTION: 7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxosteroids, such as 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, 7-oxolithocholate, 7,12-dioxo-lithocholate and dehydrocholate, to the corresponding 7beta-hydroxysteroids. Is also able to catalyze the reverse oxidation reactions. Together with 7alpha-HSDH encoded in the adjacent gene, is likely involved in the epimerization of the hydroxy group at C-7 of primary bile acids through 7-keto bile acid intermediates. {ECO:0000269|PubMed:22198717}. | Clostridium sardiniense (Clostridium absonum) |
G9FRD7 | HDHA_CLOSR | MKRLEGKVAIVTSSTRGIGRASAEALAKEGALVYLAARSEELANEVIADIKKQGGVAKFVYFNAREEETYTSMVEKVAEAEGRIDILVNNYGGTNVNLDKNLTAGDTDEFFRILKDNVQSVYLPAKAAIPHMEKVGGGSIVNISTIGSVVPDISRIAYCVSKSAINSLTQNIALQYARKNIRCNAVLPGLIGTRAALENMTDEFRDSFLGHVPLNRVGRPEDIANAVLYYASDDSGYVTGMIHEVAGGFALGTPQYSEYCPR | 1.1.1.- | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | null | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=cholate + NADP(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADPH; Xref=Rhea:RHEA:48508, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48509; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholate + NADP(+) = 7-oxolithocholate + H(+) + NADPH; Xref=Rhea:RHEA:53820, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78605; Evidence={ECO:0000269|PubMed:22198717, ECO:0000269|PubMed:24810359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53821; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADP(+) = 7,12-dioxo-lithocholate + H(+) + NADPH; Xref=Rhea:RHEA:53840, ChEBI:CHEBI:11901, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137789; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53841; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=7alpha-hydroxy-3,12-dioxo-5beta-cholanate + NADP(+) = dehydrocholate + H(+) + NADPH; Xref=Rhea:RHEA:65024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137881, ChEBI:CHEBI:156270; Evidence={ECO:0000269|PubMed:22198717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65025; Evidence={ECO:0000305|PubMed:22198717}; CATALYTIC ACTIVITY: Reaction=glycochenodeoxycholate + NADP(+) = 7-oxoglycolithocholate + H(+) + NADPH; Xref=Rhea:RHEA:65056, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137818; Evidence={ECO:0000269|PubMed:24810359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65057; Evidence={ECO:0000305|PubMed:24810359}; CATALYTIC ACTIVITY: Reaction=NADP(+) + taurochenodeoxycholate = 7-oxotaurolithocholate + H(+) + NADPH; Xref=Rhea:RHEA:65060, ChEBI:CHEBI:9407, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137724; Evidence={ECO:0000269|PubMed:24810359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65061; Evidence={ECO:0000305|PubMed:24810359}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.06 mM for cholate {ECO:0000269|PubMed:22198717}; KM=0.96 mM for 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate {ECO:0000269|PubMed:22198717}; KM=0.09 mM for chenodeoxycholate {ECO:0000269|PubMed:22198717}; KM=0.13 mM for 7-oxolithocholate {ECO:0000269|PubMed:22198717}; KM=5.7 mM for 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate {ECO:0000269|PubMed:22198717}; KM=1.14 mM for 7,12-dioxo-lithocholate {ECO:0000269|PubMed:22198717}; KM=3.5 mM for dehydrocholate {ECO:0000269|PubMed:22198717}; KM=0.013 mM for chenodeoxycholate {ECO:0000269|PubMed:24810359}; KM=0.012 mM for glycochenodeoxycholate {ECO:0000269|PubMed:24810359}; KM=0.016 mM for taurochenodeoxycholate {ECO:0000269|PubMed:24810359}; Note=kcat is 343000 sec(-1) for the oxidation of cholate. kcat is 13600 sec(-1) for the reduction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate. kcat is 9390 sec(-1) for the oxidation of chenodeoxycholate. kcat is 977 sec(-1) for the reduction of 7-oxolithocholate. kcat is 222000 sec(-1) for the oxidation of 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate. kcat is 30600 sec(-1) for the reduction of 7,12-dioxo-lithocholate. kcat is 22600 sec(-1) for the reduction of dehydrocholate (PubMed:22198717). kcat is 21.2 sec(-1) for the oxidation of chenodeoxycholate. kcat is 19.6 sec(-1) for the oxidation of glycochenodeoxycholate. kcat is 11.5 sec(-1) for the oxidation of taurochenodeoxycholate (PubMed:24810359). {ECO:0000269|PubMed:22198717, ECO:0000269|PubMed:24810359}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Shows a maximum of activity between pH 7.5 and 8.0 both in the oxidation reaction of cholate and in the reduction reaction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate. {ECO:0000269|PubMed:22198717}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. No activity is detected above 60 degrees Celsius. {ECO:0000269|PubMed:22198717}; | FUNCTION: 7alpha-hydroxysteroid dehydrogenase that catalyzes the NADP(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as cholate, chenodeoxycholate, glycochenodeoxycholate and taurochenodeoxycholate, to the corresponding 7-oxosteroids (PubMed:22198717, PubMed:24810359). Is also able to catalyze the reverse reduction reactions (PubMed:22198717). Together with 7beta-HSDH encoded in the adjacent gene, is likely involved in the epimerization of the hydroxy group at C-7 of primary bile acids through 7-keto bile acid intermediates (PubMed:22198717). {ECO:0000269|PubMed:22198717, ECO:0000269|PubMed:24810359}. | Clostridium sardiniense (Clostridium absonum) |
G9I930 | PA2HB_MICTN | MDKMNPAHLLVLAAVCVSLLGASSIPPQALNLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCKPLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ | null | null | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; ion channel regulator activity [GO:0099106]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, K49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22094702}. | null | null | null | null | null | FUNCTION: Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1 (PubMed:22094702, PubMed:24507937). Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM) (PubMed:22094702). The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM) (PubMed:22094702). On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality (PubMed:22094702). Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively (PubMed:22094702). The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 toxin overlap, explaining why these toxins are mutually exclusive (PubMed:22094702, PubMed:24507937). In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers (PubMed:22094702). {ECO:0000269|PubMed:22094702, ECO:0000269|PubMed:24507937}.; FUNCTION: Monomer: does not have phospholipase A2 activity but may maintain some lipid-binding character from its PLA2 lineage, which could aid in effecting neuronal depolarization. {ECO:0000305|PubMed:22094702}. | Micrurus tener tener (Texas coral snake) |
G9M9M3 | F6H22_IPOBA | MPSTTLSTVLSDINDFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPIEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDAVEYLKSCEMVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPRPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390; EC=1.14.11.61; Evidence={ECO:0000269|PubMed:22169019}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.46 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=6.12 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.35 sec(-1) with feruloyl-CoA as substrate. kcat is 0.33 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity toward caffeoyl-CoA (PubMed:22169019). {ECO:0000269|PubMed:22169019}. | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9M9M4 | F6H21_IPOBA | MPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICDAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAEEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDEEAAQYWPPSCRDDALEYLKSCEMVSRKLLEALMQGLNVNEIDDAKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVLANETNDRISVPVFVNPKPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390; EC=1.14.11.61; Evidence={ECO:0000269|PubMed:22169019}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.06 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=15.25 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.55 sec(-1) with feruloyl-CoA as substrate. kcat is 0.64 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA (PubMed:22169019). {ECO:0000269|PubMed:22169019}. | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9M9M5 | F6H28_IPOBA | MMPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICNAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAQEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDQEAAQYWPPSCRDDALEYLKSCELVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPKPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE | 1.14.11.61; 1.14.11.62 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9C899}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | coumarin biosynthetic process [GO:0009805]; phenylpropanoid biosynthetic process [GO:0009699]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; 4-coumaroyl 2'-hydroxylase activity [GO:0102312]; metal ion binding [GO:0046872] | PF03171;PF14226; | null | Iron/ascorbate-dependent oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57868, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85008, ChEBI:CHEBI:142398; EC=1.14.11.62; Evidence={ECO:0000269|PubMed:22169019}; CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390; EC=1.14.11.61; Evidence={ECO:0000269|PubMed:22169019}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.34 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019}; KM=7.92 uM for p-Coumaroyl-CoA {ECO:0000269|PubMed:22169019}; Note=kcat is 0.28 sec(-1) with feruloyl-CoA as substrate. kcat is 0.28 sec(-1) with p-Coumaroyl-CoA as substrate. {ECO:0000269|PubMed:22169019}; | PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:22169019}; | null | FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis (PubMed:22169019). Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA (PubMed:22169019). {ECO:0000269|PubMed:22169019}. | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
G9MAN7 | TPS4_SELML | MAKVLFSSFQQTGISGSLKSGQLSGVFINGTNLKSNAHAKRFRKNSTSSITIRCCASNSPTLENTKLAGAPEKRQKKKQLPYQGILHVPGDRVEELDTRETSLLVAEVKGWLMKLASGKGEISPSAYDTAWVARIASESDSSLPEFPEALEWIINSQLPDGSWGDDRHLQLYDRVLSTLSCLVTLKTWDIGHNSIAQGTKFLRENMIKLKQDDGDLLSGFEVTFPMMLHEAKQLGLDIPYETEFTRLLEISTKKKLAKIPLDKLHSAPTTLLYSLEGLQDLEIDWQKILKLQSKDGSFLSSPSSTACVYLKTKDRKSLQYLQNAMEDQNYAVPCHYPIDLFESLWVVDTIERLGIDVFFRDEIKAVLDYVYSFWTNEGIGWGSTCLVNDIDDTAMAFRILRMHGYNVSPDAFNQFWLPGDKFCCFVGELSHGVSEMLNLHRASQVDFPNEAILTKTFKYSHDYLLNVDSAHMDKWATKKNLMGEVAFELANPFHDCLPRIYNNAYIKHYGMDDLWIAKTIYRLPLVNNKVFLELANRYAQQCQLYQPAELTKLVNWWHSSRFEDIPSTRLTANIDMLPYIYYVICATFHEQEFAQLRVFFSKACCLNTLFDDLMDCATSIEELDRLQNVIERWDISLSHELPLEYRIPFQEFYNTVLVMTEAASKIHKNLSPEFICKYLSGIYTKLIKSEIADARWKIEGYIPSFEEYMENAEVSISTWVHVLMSILFCGEPLTEEILNTIYDSRPLKLDRIICRLCNDIQTYKIEMKLGQPTQGVSCYMKEHPGATEEDALVYLQSLLEKTKRELNESYFITHENDLPKNIKRFNFEMVRMMLITYNETRQVDLFRNPDNELKDMIKFCLETYRTL | 4.2.3.131; 5.5.1.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | 5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate biosynthetic process [GO:1901949]; 5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate catabolic process [GO:1901948]; diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946] | chloroplast [GO:0009507] | copalyl diphosphate synthase activity [GO:0050559]; magnesium ion binding [GO:0000287]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:22027823}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635, ChEBI:CHEBI:58756; EC=5.5.1.12; Evidence={ECO:0000269|PubMed:22027823}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | null | null | FUNCTION: Bifunctional diterpene cyclase that catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate (GGDP) producing successively (+)-copalyl diphosphate and miltiradiene. {ECO:0000269|PubMed:22027823}. | Selaginella moellendorffii (Spikemoss) |
G9MAP1 | CLAHY_LACPN | MGALFMVKSKAIMIGAGLSNMAAAVYLIQDGHWDGKDITFYGVDMHGANDGGATTDFTNEYWNKNHPMANTTGYVARGGRMLNYRTYVDLMDLLDRIPSVTEPGMTAAEDTRDFDAKHRTYDIARLMQGGKGIINAGKLGFNNKDRTLLTKLIMMPDSEETKLDNVSIAEYFKDDPHMFQTNFWYMWETTFAFRTQSSAQELRRYMHQMIYEFTQIEHLVGVNRTRYNQFESMILPLIKYLQGQGVTFIDNKIVKDWQFKDTPMQDEITVTGLVIEDAQTGETEEVEVDEDTAVIFTNGSITDSATMGDYNTPAPENMDYGVSASLWKKATERFYNLGTPDKFFNDRNASEWVSFTLTTKNHLFLNEIVRITTQEPGNALNSFLSTTPITPLNQKDVNMSIVVHHQPHFTTQQPNETVLWGYFLYPRRQGEFVNKPYIKMTGKEMAQELIGQLSKVDPGPGNIKDKEKENLDSIVNNIPVYMPYASALFNNRAKSDRPEVLPKHSTNLAFTGEFAEQPYQMIFTEQSAVRSGEIAAYHFAGVPMDNLVKTPRYDKDPKTLLKATKKMFD | 4.2.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25476761}; Note=FADH2 seems to be the active cofactor and is produced through the reduction of FAD by NADH. {ECO:0000269|PubMed:25476761}; | fatty acid metabolic process [GO:0006631]; response to toxic substance [GO:0009636] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | FAD binding [GO:0071949]; oleate hydratase activity [GO:0050151] | PF06100; | 3.50.50.60; | Oleate hydratase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22093837}. Cytoplasm {ECO:0000269|PubMed:22093837}. Note=Is not strongly linked to the membrane because this enzyme is also present in the soluble cell-free extracts. {ECO:0000269|PubMed:22093837}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + H2O = (10S)-hydroxy-(12Z)-octadecenoate; Xref=Rhea:RHEA:75723, ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:194434; Evidence={ECO:0000269|PubMed:24127592, ECO:0000269|PubMed:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75724; Evidence={ECO:0000269|PubMed:24127592, ECO:0000305|PubMed:25476761}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75725; Evidence={ECO:0000269|PubMed:24127592, ECO:0000305|PubMed:25476761}; CATALYTIC ACTIVITY: Reaction=(10E,12Z)-octadecadienoate + H2O = (10S)-hydroxy-(12Z)-octadecenoate; Xref=Rhea:RHEA:75727, ChEBI:CHEBI:15377, ChEBI:CHEBI:77200, ChEBI:CHEBI:194434; Evidence={ECO:0000269|PubMed:24127592}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75729; Evidence={ECO:0000269|PubMed:24127592}; 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:24127592, ECO:0000305|PubMed:25476761}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75753; Evidence={ECO:0000269|PubMed:24127592, ECO:0000305|PubMed:25476761}; CATALYTIC ACTIVITY: Reaction=(10E)-octadecenoate + H2O = 10-hydroxyoctadecanoate; Xref=Rhea:RHEA:75755, ChEBI:CHEBI:15377, ChEBI:CHEBI:143089, ChEBI:CHEBI:194438; Evidence={ECO:0000269|PubMed:24127592}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75757; Evidence={ECO:0000269|PubMed:24127592}; CATALYTIC ACTIVITY: Reaction=(9E,11E)-octadecadienoate + H2O = 10-hydroxy-(11E)-octadecenoate; Xref=Rhea:RHEA:75763, ChEBI:CHEBI:15377, ChEBI:CHEBI:194439, ChEBI:CHEBI:194440; Evidence={ECO:0000269|PubMed:24127592}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75765; Evidence={ECO:0000269|PubMed:24127592}; CATALYTIC ACTIVITY: Reaction=(9Z,11E)-octadecadienoate + H2O = 10-hydroxy-(11E)-octadecenoate; Xref=Rhea:RHEA:75759, ChEBI:CHEBI:15377, ChEBI:CHEBI:17539, ChEBI:CHEBI:194439; Evidence={ECO:0000269|PubMed:24127592}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75761; Evidence={ECO:0000269|PubMed:24127592}; 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:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75768; Evidence={ECO:0000305|PubMed:25476761}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + H2O = (10S)-hydroxy-(12Z,15Z)-octadecadienoate; Xref=Rhea:RHEA:75771, ChEBI:CHEBI:15377, ChEBI:CHEBI:32387, ChEBI:CHEBI:194447; Evidence={ECO:0000269|PubMed:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75772; Evidence={ECO:0000305|PubMed:25476761}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75773; Evidence={ECO:0000305|PubMed:25476761}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + H2O = (10S)-hydroxy-(6Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:75775, ChEBI:CHEBI:15377, ChEBI:CHEBI:32391, ChEBI:CHEBI:194448; Evidence={ECO:0000269|PubMed:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75776; Evidence={ECO:0000305|PubMed:25476761}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75777; Evidence={ECO:0000305|PubMed:25476761}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoate + H2O = (10S)-hydroxy-(6Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:75779, ChEBI:CHEBI:15377, ChEBI:CHEBI:77222, ChEBI:CHEBI:194449; Evidence={ECO:0000269|PubMed:25476761}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75780; Evidence={ECO:0000305|PubMed:25476761}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92 uM for linoleate {ECO:0000269|PubMed:25476761}; KM=98 uM for 10-hydroxy-cis-12-octadecenoate {ECO:0000269|PubMed:25476761}; Note=kcat is 0.026 sec(-1) for the hydration of linoleate. kcat is 0.0012 sec(-1) for the dehydration of 10-hydroxy-cis-12-octadecenoate. {ECO:0000269|PubMed:25476761}; | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:22093837, ECO:0000269|PubMed:24127592}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for the hydration of linoleic acid and for the dehydration of 10-hydroxy-cis-12-octadecenoic acid (HYA).; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius for the hydration of linoleic acid and 37 degrees Celsius for the dehydration of 10-hydroxy-cis-12-octadecenoic acid (HYA). {ECO:0000269|PubMed:25476761}; | FUNCTION: Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism (PubMed:22093837, PubMed:24127592, PubMed:25476761). Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha-linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy-cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12-octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position (PubMed:25476761). As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome (PubMed:24127592). Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12-hydroxy, 3-hydroxy, and 9-hydroxy fatty acids (PubMed:25476761). {ECO:0000269|PubMed:22093837, ECO:0000269|PubMed:24127592, ECO:0000269|PubMed:25476761}. | Lactiplantibacillus plantarum (Lactobacillus plantarum) |
H0VCJ6 | NAAA_CAVPO | MRSPGIVLLLLLLLLLPPGAAPCPADLCPAPPRVNVSLDAAPAARWLPVLRLFDPGLLRAAVARIVGDRVPKWRDVIGKLVAEMESFLPQPYTKEIRGISDFLNLSLADGFIVNLAYEASAFCTSVVAQDSRGHIYHGRNLDYPFGDLLRKMTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPYKFTVSGDERDKGWWWENMIAALFQGHSPVSWLIRTTLSESEDFEASVYKLAKTPLIADVYYIVGGTAPGEGVVVTRNRGGPADIWPLDPLNGAWFRVETNYDHWKPVPKSDDRRTPAIKALNATGQANLSLEALFQVLSVVPVCNKITVYTTVMSAATPDKYMTRIRNLS | 3.5.1.23; 3.5.1.60 | null | fatty acid metabolic process [GO:0006631]; lipid catabolic process [GO:0016042]; N-acylethanolamine metabolic process [GO:0070291]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; sphingosine metabolic process [GO:0006670] | lysosome [GO:0005764]; membrane [GO:0016020] | ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-(long-chain-acyl)ethanolamine deacylase activity [GO:0047412]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF15508; | null | Acid ceramidase family | PTM: N-glycosylated (PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}.; PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}. | CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine + hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain fatty acid + ethanolamine; Xref=Rhea:RHEA:17505, ChEBI:CHEBI:15377, ChEBI:CHEBI:15897, ChEBI:CHEBI:57560, ChEBI:CHEBI:57603; EC=3.5.1.60; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17506; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine; Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57603, ChEBI:CHEBI:85263; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoylethanolamine = ethanolamine + tetradecanoate; Xref=Rhea:RHEA:45452, ChEBI:CHEBI:15377, ChEBI:CHEBI:30807, ChEBI:CHEBI:57603, ChEBI:CHEBI:85262; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45453; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57756, ChEBI:CHEBI:72956; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292; Evidence={ECO:0000250|UniProtKB:Q02083}; | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q02083}. | null | null | FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. {ECO:0000250|UniProtKB:Q5KTC7}. | Cavia porcellus (Guinea pig) |
H0VVW3 | APOA1_CAVPO | MKAVLLVVAALFLAGSQARHFWQQDDPKTSWDVVKEFANKYVDAVKESGKGYVEQLDASSLGQQLNLRLSDNWDTLSTILTKLQADFGLATQEFWDTLEKETEWLKQIVSEDLQDVKHKVQPYLENFQKKVQEEVEHYREKVRPLGIELRDGARQKLQELQEKLTPLGEDLRDRTREHVDVLRTQLAPFSEEMRQRLAKRLEELKDSATLADYHAKASEHLKMLGEKAKPALEDLRQGLLPVLENLKASILSSIDQASKQLAAQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180] | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}. | Cavia porcellus (Guinea pig) |
H0WFA5 | BUCKY_DANRE | MEGINNNSQPMGVGQPHHPVNHTRPFFYVQPPSQPYFMYQWPMNPYGHYGFPGPALHFGRPYMAPYQFMQYPGYVIPHAPMQPIDYRRINPHYPSVASYDLRVRHHFQNAGMHRETACSEVQTDPSDSVNKLIDKIESLKACELGSDKGPNNVVSSTPDVVQGEKLTRLNEDSNLEVATKECKEDPVTRPTTYSDSAYDAESSQGRLDECVFSDVLPLDSSSVHEEEEEEEKDVNEEDEPQTVADEICSQNEMSASTTSNVFCSGVQSIADPTECHDLEKLGDEQKQDIPSADAAAVIEPLISLSEDFDLPYQILRLPCNKTTTGLSLEREIDPLVYFDSPSTLLPPQNYLSSIGSAYSYSYYPQVTQERQSVLSPSIDELSSRDEMFSTDVEDLEVVPGHVYVGGGRLAEASDMPVRSRKELPSVDKTCSVCQKTCACCGSTLQDEVGMCKMAEHSHPERDEMSDQDCDYDLEAEVRSNCESPRVSKRKCCSRHALPSCGHHCAKHRHRKLLCEGQESCDLREQARVHPKGECCEEYGALAKADKRIQKGALCRPCIEQQWREGVVSDQENWASCGAKPRSWRQVTGPQDQGRTPLRRSTCKSIHQQRPRSEYNDYDETEFTYCQRGRGSMKKRGSRY | null | null | morphogenesis of follicular epithelium [GO:0016333]; oocyte animal/vegetal axis specification [GO:0060832]; oocyte anterior/posterior axis specification [GO:0007314]; pole plasm assembly [GO:0007315]; spermatogenesis [GO:0007283] | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737] | null | null | null | null | PTM: Symmetric dimethylarginine modification promotes interaction with tdrd6. {ECO:0000269|PubMed:30086300}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:30086300}. Cleavage furrow {ECO:0000269|PubMed:26253407}. Note=Localizes to nuage (a peri-nuclear protein-RNA aggregate that associates closely with mitochondria), the Balbiani body during oogenesis, and in the germ plasm upon fertilization (PubMed:19249209, PubMed:30086300). Accumulates at embryonic cleavage furrows (PubMed:26253407). {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:26253407, ECO:0000269|PubMed:30086300}. | null | null | null | null | null | FUNCTION: Prion-like protein required for the formation of Balbiani body (electron-dense aggregates in the oocyte) and germ plasm assembly, and for the establishment of oocyte polarity during early oogenesis (PubMed:18582455, PubMed:19249209). Mobility and aggregation properties are improved by tudor domain-containing protein tdrd6 through interaction with dimethylated arginines Tri-RG domains (PubMed:30086300). Establishes oocyte polarity through interactions with RNA-binding proteins rbpms2 and dazl, initiating a positive feedback loop amplification mechanism in the Balbiani body (PubMed:24496621). Interaction of BUC protein and mRNA with rbpms2 and dazl is required to mediate Balbiani body formation (PubMed:24496621). Involved in recruitment of germ plasm to embryonic cleavage furrows and dorsoventral patterning through interaction with Kinesin-1/KIF5BA (PubMed:26253407). {ECO:0000269|PubMed:18582455, ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:24496621, ECO:0000269|PubMed:26253407, ECO:0000269|PubMed:30086300}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
H0YL14 | TM250_HUMAN | MPVMPIPRRVRSFHGPHTTCLHAACGPVRASHLARTKYNNFDVYIKTRWLYGFIRFLLYFSCSLFTAALWGALAALFCLQYLGVRVLLRFQRKLSVLLLLLGRRRVDFRLVNELLVYGIHVTMLLVGGLGWCFMVFVDM | null | null | cilium assembly [GO:0060271]; cytoskeleton-dependent cytokinesis [GO:0061640]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of viral process [GO:0048524] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; septin complex [GO:0031105]; septin ring [GO:0005940] | GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090] | PF17685; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:21667337}. Cytoplasm {ECO:0000269|PubMed:21667337}. Note=Upon HHV-1 infection, accumulates arround the nuclear membrane and translocates into the nucleus. | null | null | null | null | null | FUNCTION: May play a role in cell proliferation by promoting progression into S phase. {ECO:0000269|PubMed:21667337}.; FUNCTION: (Microbial infection) Promotes human herpes simplex virus 1/HHV-1 proliferation. {ECO:0000269|PubMed:21667337}. | Homo sapiens (Human) |
H0ZAB5 | GALT3_TAEGU | MALKKAPKLFKTFFHWKLWKFSIIVFVFLVFLFLLQREVGVQDFKDEAGIEPVVGKKSHVLGLVLNAMNNIKGAKPKMQIKAPIRQTKVPGERHCLPGHYTPVELKPFLDRPLQDPNAPGASGKAFKTINLNSEEQKEKQAGEEKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSIIIVFHNEAWSTLLRTVHSVMYTSPAILLKEIILVDDASVDEYLHDKLDEYVKQFQIVKVVRQKERKGLITARLLGASVATGETLTFLDAHCECFYGWLEPLLARIAENPVAVVSPDIASIDLNTFEFSKPSPYGHSHNRGNFDWSLSFGWESLPKHENKRRKDETYPIRTPTFAGGLFSISKDYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHTFPKGTQVITRNQVRLAEVWMDEYKEIFYRRNTEAAKIVKQKTFGDISKRIDLRQRLQCKNFTWYLSNVYPEAYVPDLNPLFSGYLKNIGNRMCLDVGENNHGGKPLIMYSCHGLGGNQKELCLHASKGPVQLRECTYKGQKTFAVGEEQWLHQKDQTLYNEALHMCLTGNGEHPSLASCNPSDPFQKWIFGQND | 2.4.1.41 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:31932717}; | protein O-linked glycosylation via threonine [GO:0018243] | Golgi cisterna membrane [GO:0032580] | carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653] | PF00535;PF00652; | 2.80.10.50; | Glycosyltransferase 2 family, GalNAc-T subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. {ECO:0000250|UniProtKB:Q14435}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; Evidence={ECO:0000250|UniProtKB:Q14435}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:31932717}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=170 uM for FGF23 NAPIPRRHTRSAEDDS peptide {ECO:0000269|PubMed:31932717}; | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:31932717). Glycosylates FGF23 (PubMed:31932717). {ECO:0000269|PubMed:31932717}. | Taeniopygia guttata (Zebra finch) (Poephila guttata) |
H1AE14 | LP9D_PHACH | MKAFFAVLAVVSAPFVLGHYTFPDFIEPSGTVTGDWVYVRETQNHYSNGPVTDVTSPEFRCYELDLQNTAGQTQTATVSAGDTVGFKANSAIYHPGYLDVMMSPASPAANSPEAGTGQTWFKIYEEKPQFENGQLVFDTTQQEVTFTIPKSLPSGQYLLRIEQIALHVASSYGGAQFYIGCAQLNVENGGNGTPGPLVSIPGVYTGYEPGILINIYNLPKNFTGYPAPGPAVWQG | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:23525113}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:23525113}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22132148}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:22132148, ECO:0000269|PubMed:30238672}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding only C1 oxidation products (PubMed:22132148, PubMed:30238672). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:22132148). {ECO:0000269|PubMed:22132148, ECO:0000269|PubMed:30238672}. | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
H1UBK1 | MAP2_CAEEL | MPPANGKKGKKGGAAKAVRRIQYRPKSFKHSRFVKHAHFWSAAPEEDFDAILAEMQLADAKTAAKEATKKDAKGGKGKANGSAAATAAPEEAKQAWQAEIAAMKPIDEQFPDGKFPHGIDESPYYLKGKDGRVATDRESNEEKKALDISYEEVWQDYRRSAEAHRQVRKYVKSWIKPGMTMIEICERLETTSRRLIKEQGLEAGLAFPTGCSLNHCAAHYTPNAGDTTVLQYGDVCKIDYGIHVRGRLIDSAFTVHFDPKFDPLVEAVREATNAGIKESGIDVRLCDVGEIVEEVMTSHEVELDGKSYVVKPIRNLNGHSIAQYRIHAGKTVPIVKGGEQTKMEENEIYAIETFGSTGKGYVHDDMETSHYMKNFELADEKIPLRLQKSKGLLNLIDKNFATLAFCRRWIDRLGETKYLMALKDLCDKGIVDPYPPLCDVKGCYTAQWEHTILMRPTVKEVVSRGDDY | 3.4.11.18 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000255|RuleBase:RU003653}; | germ cell proliferation [GO:0036093]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | aminopeptidase activity [GO:0004177]; exopeptidase activity [GO:0008238]; initiator methionyl aminopeptidase activity [GO:0004239]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235] | PF00557; | 3.90.230.10;1.10.10.10; | Peptidase M24A family, Methionine aminopeptidase eukaryotic type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_03175}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000269|PubMed:15474045}; | null | null | null | null | FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins (PubMed:15474045). The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (PubMed:15474045). Required for germ cell proliferation and/or differentiation (PubMed:15474045). {ECO:0000269|PubMed:15474045}. | Caenorhabditis elegans |
H1VQB1 | DPCHD_COLHI | MSPAEIIRPAAKVQLMDSKAHGNNHEEIIRAPLNYLLDLPGKEVRSKLMSAFNQWLRIPEEKLEVIKRIVMLLHNASLLLDDIQDSSTLRRGLPVSHSIFGIAQTINAANYAFFLAQQEIPKLEDPRAFEVFTEELLNLHRGQGMDIYWRDASICPTEEEYFTMVSNKTGGLFRLAVRLMQLASESDRDYVPLVNVMGLIFQVRDDYLNLQSTAYTKNKGFGEDLTEGKFSFPIIHSIRSNPSNIQLSSILKQRTTDVDVKLFAVAYIESTGSFEHCRKTLAELMAQAKAIIEGMEGDSSESLSVMNQILTMLGLDGNEVPR | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:32286350}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B (PubMed:32286350). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350). {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}. | Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose fungus) |
H1ZV37 | GEOB_CASD6 | MTIDHQHIFVGGQWIAPKSTQRSNILNASTEELVGSVPKCNNEDMDRAVAAAREAMRSLAWAGLDGKGRAQHLRRFADAVERRGQQLARSVSLQNGMPINVADQLESAFVVSLLRYYASLAENLVEEEARPSPTGSTTLVRRDPVGVVGAIIPWNFPVALSIFKIAPALAAGCAVVVKPSSGTVLDSYVLAEAAAEAGLPPGVINWVPGDRGIGSHLVSHPGVDKVAFTGSTSAGRIIAEACARLLRPVTLELGGKSAAIVLEDADLDALIRSLPMSSVLNNGQACFSCTRILAPAGRYDEVVDAIAGAVSAYSVGDALDRATVVGPMASAAHRDSVQRYIELGTGEARLVVGGGRTSQDRGWFVQPTVFADVDNRSRIAREEIFGPVLSIIRYEGEDEAVEIANDSEYGLGGTVWSTDHDHAVTIARRMETGTVGINGYMPDLNAPFGGVKSSGMGRELGPESIGAYQRYKSVYLLG | 1.2.1.86 | null | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098] | null | geranial dehydrogenase activity [GO:0034832]; NAD binding [GO:0051287] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geranial + H2O + NAD(+) = geranate + 2 H(+) + NADH; Xref=Rhea:RHEA:34351, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67260; EC=1.2.1.86; Evidence={ECO:0000269|PubMed:22286981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34352; Evidence={ECO:0000269|PubMed:22286981}; CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + perillyl aldehyde = 2 H(+) + NADH + perillate; Xref=Rhea:RHEA:31299, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62641; Evidence={ECO:0000305|PubMed:24952578}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31300; Evidence={ECO:0000305|PubMed:24952578}; | null | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578}. | null | null | FUNCTION: Involved in the degradation of the monoterpenes beta-myrcene and limonene (PubMed:22286981, PubMed:24952578). During anaerobic degradation of beta-myrcene, catalyzes the NAD(+)-dependent oxidation of geranial to geranic acid (PubMed:22286981). Seems to be specific for the trans-isomer geranial, since it does not act on the cis-isomer neral (PubMed:22286981). During degradation of limonene, catalyzes the NAD(+)-dependent conversion of perillyl aldehyde to perrilic acid (Probable). {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578, ECO:0000305|PubMed:24952578}. | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
H1ZV38 | GEOA_CASD6 | MNDTQDFISAQAAVLRQVGGPLAVEPVRISMPKGDEVLIRIAGVGVCHTDLVCRDGFPVPLPIVLGHEGSGTVEAVGEQVRTLKPGDRVVLSFNSCGHCGNCHDGHPSNCLQMLPLNFGGAQRVDGGQVLDGAGHPVQSMFFGQSSFGTHAVAREINAVKVGDDLPLELLGPLGCGIQTGAGAAINSLGIGPGQSLAIFGGGGVGLSALLGARAVGADRVVVIEPNAARRALALELGASHALDPHAEGDLVAAIKAATGGGATHSLDTTGLPPVIGSAIACTLPGGTVGMVGLPAPDAPVPATLLDLLSKSVTLRPITEGDADPQRFIPRMLDFHRAGKFPFDRLITRYRFDQINEALHATEKGEAIKPVLVF | 1.1.1.144; 1.1.1.347 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P11766}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766}; | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098] | null | alcohol dehydrogenase (NAD+) activity [GO:0004022]; NAD binding [GO:0051287]; perillyl-alcohol dehydrogenase activity [GO:0018457]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH; Xref=Rhea:RHEA:34347, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980, ChEBI:CHEBI:17447, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.347; Evidence={ECO:0000269|PubMed:22286981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34348; Evidence={ECO:0000269|PubMed:22286981}; CATALYTIC ACTIVITY: Reaction=NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde; Xref=Rhea:RHEA:10664, ChEBI:CHEBI:15378, ChEBI:CHEBI:15420, ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.144; Evidence={ECO:0000269|PubMed:22286981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10665; Evidence={ECO:0000269|PubMed:22286981}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for geraniol {ECO:0000269|PubMed:22286981}; KM=7 uM for (S)-perillyl alcohol {ECO:0000269|PubMed:22286981}; KM=45 uM for nerol {ECO:0000269|PubMed:22286981}; KM=86 uM for citronellol {ECO:0000269|PubMed:22286981}; KM=21 uM for cumic alcohol {ECO:0000269|PubMed:22286981}; KM=170 uM for benzyl alcohol {ECO:0000269|PubMed:22286981}; Vmax=10 umol/min/mg enzyme with geraniol as substrate {ECO:0000269|PubMed:22286981}; Vmax=18 umol/min/mg enzyme with (S)-perillyl alcohol as substrate {ECO:0000269|PubMed:22286981}; Vmax=18 umol/min/mg enzyme with nerol as substrate {ECO:0000269|PubMed:22286981}; Vmax=11 umol/min/mg enzyme with citronellol as substrate {ECO:0000269|PubMed:22286981}; Vmax=14 umol/min/mg enzyme with cumic alcohol as substrate {ECO:0000269|PubMed:22286981}; Vmax=47 umol/min/mg enzyme with benzyl alcohol as substrate {ECO:0000269|PubMed:22286981}; Note=The values given here are for the native GeDH, the values for the recombinant protein can be found in another article (PubMed:22286981).; | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:22286981}; | null | FUNCTION: Involved in the degradation of the monoterpenes beta-myrcene and limonene (PubMed:22286981, PubMed:24952578). During anaerobic degradation of beta-myrcene, catalyzes the NAD(+)-dependent oxidation of geraniol to geranial (PubMed:22286981). Can also catalyze the oxidation of (S)-perillyl alcohol to perillyl aldehyde, and to a lesser extent, the oxidation of nerol, citronellol, cumic alcohol, and benzyl alcohol (PubMed:22286981). Cannot use NADP(+) instead of NAD(+) as cosubstrate (PubMed:22286981). {ECO:0000269|PubMed:22286981, ECO:0000269|PubMed:24952578}. | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
H2AM12 | GP_SBVBH | MLLNIVLISNLACLAFALPLKEGTRGSRCFLNGELVKTVNTSKVVSECCVKDDISIIKSNAEHYKSGDRLAAVIKYYRLYQVKDWHSCNPIYDDHGSFMILDIDNTGTLIPKMHTCRVECEIALNKDTGEVILNSYRINHYRISGTMHVSGWFKNKIEIPLENTCESIEVTCGLKTLNFHACFHTHKSCTRYFKGSILPELMIESFCTNLELILLVTFILVGSVMMMILTKTYIVYVFIPIFYPFVKLYAYMYNKYFKLCKNCLLAVHPFTNCPSTCICGMIYTTTESLKLHRMCNNCSGYKALPKTRKLCKSKISNIVLCVITSLIFFSFITPISSQCIDIEKLPDEYITCKRELANIKSLTIDDTYSFIYSCTCIIVLILLKKAAKYILYCNCSFCGMVHERRGLKIMDNFTNKCLSCVCAENKGLTIHRASEKCLFKFESSYNRTGLIIFMLLLVPTIVMTQETSINCKNIQSTQLTIEHLSKCMAFYQNKTSSPVVINEIISDASVDEQELIKSLNLNCNVIDRFISESSVIETQVYYEYIKSQLCPLQVHDIFTINSASNIQWKALARSFTLGVCNTNPHKHICRCLESMQMCTSTKTDHAREMSIYYDGHPDRFEHDMKIILNIMRYIVPGLGRVLLDQIKQTKDYQALRHIQGKLSPKSQSNLQLKGFLEFVDFILGANVTIEKTPQTLTTLSLIKGAHRNLDQKDPGPTPILVCKSPQKVVCYSPRGVTHPGDYISCKSKMYKWPSLGVYKHNRDQQQACSSDTHCLEMFEPAERTITTKICKVSDMTYSESPYSTGIPSCNVKRFGSCNVRGHQWQIAECSNGLFYYVSAKAHSKTNDITLYCLSANCLDLRYAFRSSSCSDIVWDTSYRNKLTPKSINHPDIENYIAALQSDIANDLTMHYFKPLKNLPAIIPQYKTMTLNGDKVSNGIRNSYIESHIPAINGLSAGINIAMPNGESLFSIIIYVRRVINKASYRFLYETGPTIGINAKHEEVCTGKCPSPIPHQDGWVTFSKERSSNWGCEEWGCLAINDGCLYGSCQDIIRPEYKIYKKSSIEQKDVEVCITMAHESFCSTVDVLQPLISDRIQLDIQTIQMDSMPNIIAVKNGKVYVGDINDLGSTAKKCGSVQLYSEGIIGSGTPKFDYVCHAFNRKDVILRRCFDNSYQSCLLLEQDNTLTIASTSHMEVHKKVSSVGTINYKIMLGDFDYNAYSTQATVTIDEIRCGGCYGCPEGMACALKLSTNTIGSCSIKSNCDTYIKIIAVDPMQSEYSIKLNCPLATETVSVSVCSASAYTKPSISKNQPKIVLNSLDETSYIEQHDKKCSTWLCRVYKEGISVIFQPLFGNLSFYWRLTIYIIISLIMLILFLYILIPLCKRLKGLLEYNERIYQMENKFK | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; modulation by virus of host process [GO:0019048]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF03557;PF03563; | null | Nairovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic cleavages by host furin-like protease and MBTPS1/S1P endopeptidase yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.; PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}. | SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8JSZ3}.; SUBCELLULAR LOCATION: [Glycoprotein C]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion (By similarity). Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (By similarity). Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). {ECO:0000250|UniProtKB:Q8JSZ3}.; FUNCTION: [Glycoprotein C]: Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion (By similarity). The spikes at the surface of the virion are formed by an N-terminal extension of glycoprotein C (PubMed:30787296). Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors (By similarity). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (By similarity). Exposure to potassium is necessary for the conformational change leading to fusion (By similarity). {ECO:0000250|UniProtKB:A6XIP3, ECO:0000250|UniProtKB:Q8JSZ3, ECO:0000269|PubMed:30787296}. | Bovine Schmallenberg virus (isolate Bovine/BH80/Germany/2011) (SBV) |
H2B3G5 | LI601_CANLF | MKLLLLCLGLILVHAHEEENDVVKGNFDISKISGDWYSILLASDIKEKIEENGSMRVFVKDIEVLSNSSLIFTMHTKVNGKCTKISLICNKTEKDGEYDVVHDGYNLFRIIETAYEDYIIFHLNNVNQEQEFQLMELYGRKPDVSPKVKEKFVRYCQGMEIPKENILDLTQVDRCLQARQSEAAQVSSAE | null | null | null | extracellular region [GO:0005576]; extracellular space [GO:0005615] | odorant binding [GO:0005549]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23464525, ECO:0000305|PubMed:22515174}. | null | null | null | null | null | null | Canis lupus familiaris (Dog) (Canis familiaris) |
H2DF87 | RHVI1_ROSHC | MDTSTSAYAPLPGEDPLFSGHPPASLRRSWKGFAVIFASVLFLLSLVGLIIHQGPQQPPDVMPDKQDEHHHPQSTTPASETTASWEPRGKALGVSAKSNPPVSDELSYNWTNAMFSWQRTAFHFQPERNWMNDPNGPLFYKGWYHLFYQYNPDSAIWGNITWGHAVSTDLIHWLYLPIAMVADQWYDANGVWSGSATLLPDGQIVMLYTGDTVDAVQVVCLAHPANLSDPLLLDWVKYSGNPVLTPPPGILTTDFRDPTTAWTGPDGKWRITIGSKVNTTGISFVYHTEDFKTYNMSKGVLHAVPGTGMWECIDFYPVAINGSKGVETSVNNPSVKHVLKASLDNTKVDHYALGTYFEENETWVPDNPGLDVGIGLRYDYGRYYASKTFYDQNKERRILRGWINETDTESDDLAKGWASVQTIPRTVLFDNKTGTNLIQWPVEEIEELRLNNTDFSDVLVEAGTVVELDIGTATQLDILVEFELEPLESSETVNSSVGCGGGAVDRGTFGPFGILVIADETLTELTPIYFNLANSTEGDVITYFCADERRSSKAPDVFKQVYGSEVPVLDGEKHFARVLRALRKEVGR | 3.2.1.26 | null | carbohydrate metabolic process [GO:0005975] | membrane [GO:0016020]; vacuolar lumen [GO:0005775] | beta-fructofuranosidase activity [GO:0004564] | PF00251;PF11837; | null | Glycosyl hydrolase 32 family | PTM: Glycosylated. {ECO:0000269|PubMed:27083698}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27083698}; Single-pass type II membrane protein {ECO:0000255}. Vacuole lumen {ECO:0000250|UniProtKB:Q39041}. Note=May be released into the lumen of the vacuole from the tonoplast through a proteolytic processing. {ECO:0000250|UniProtKB:Q39041}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000269|PubMed:22505690}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:27083698}; | null | FUNCTION: Acidic vacuolar invertase involved in light-induced bud burst (PubMed:22505690, PubMed:27083698). {ECO:0000269|PubMed:22505690, ECO:0000269|PubMed:27083698}. | Rosa hybrid cultivar |
H2E7Q8 | POPB_GALM3 | MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE | 3.4.21.26 | null | proteolysis [GO:0006508] | cytosol [GO:0005829] | oligopeptidase activity [GO:0070012]; serine-type endopeptidase activity [GO:0004252] | PF00326;PF02897; | 3.40.50.1820;2.130.10.120; | Peptidase S9A family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for the full alpha-amanitin 35mer proprotein {ECO:0000269|PubMed:29051530}; KM=51 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=19 uM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=8 uM for the 25mer IFGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=28 uM for the 25mer IWGIGSNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=10 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIS {ECO:0000269|PubMed:29051530}; KM=25 uM for the 19mer IWGIGCNPDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=380 uM for the 14mer IWGIGCNPWTAEHV {ECO:0000269|PubMed:29051530}; KM=24.4 uM for the 13mer IWGIGCNPWTAEH {ECO:0000269|PubMed:29051530}; | null | null | null | FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). {ECO:0000269|PubMed:22202811, ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}. | Galerina marginata (strain CBS 339.88) |
H2ELN1 | TER_NICLA | RRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYSRRIETKVNALVTAIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA | 4.2.3.-; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | alpha-pinene biosynthetic process [GO:0046248]; circadian rhythm [GO:0007623]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; limonene biosynthetic process [GO:0046250]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; pinene synthase activity [GO:0050550]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate; Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663; Evidence={ECO:0000269|PubMed:21527560}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21527560}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent (PubMed:21527560). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene, alpha-pinene and 1,8-cineole (PubMed:21527560). {ECO:0000269|PubMed:21527560}. | Nicotiana langsdorffii (Langsdorff's tobacco) |
H2EQR6 | DSG21_DANRE | MARRISPVVAFLLCFGLSHFFEAEARLQHSVALHRQKREWIVPPQILEENVDYTKKDFIAKIRSDKEVAHMKYLRYSLRGVGADQEPFNLFVVNPETGYVRITGILDRESISQYNLSGIALFTDGSIAENDIGLRIKVKDQNDNAPVFGVMNPGAVDELSAVGTEVMRLNCFDADEPGNPNSQIKYEIVDQQPAGQSMFTVENNRRVVVANPNLDRETVDQYVLLVKASDLNGAPGGNAATGTVTIKINDVNDNVPTLGGPYEASIEENTEKVEVMRLKVSDLHLKGTDNWEGDCYIASGNEAGYFSIHMDPKTNEAVLMLDKAVDYEDVKDLNLGIGVANKAPFHPSVSGGSQGATISFGGSGGGAGSGAAGGAGAMGGASGSGGGTGASSWSSSGVPLYNVNIKVKNQPEGPKFFPGTKAIPISEGKAFDSTEIIARYPAIDTDTGKEATNVKYIKSSDPDNWLTIDEKTGAIRMNKAPDRESKYLVNGTYYAKVLSITQDLPSKTATGTIAIQVEDFNDHCPTLISNVQTLCTDKDAVLVTAKDEDAPPNGAPFDFNIVSEGTAGKWTVEYMNDTTAIFRTHEKLWPGPHELMVEVTDQQGLKCPEPQKLQVDVCTCKNQGGCDRTATGDAKKGSRLGPAGIGLLLLALLALLLIPLLLLLCTCGMTGAFTDMPFETKVHLISSNTEGQGEDRDVPLMCPPSNVDGMGFMTKDYMAVGAMHSAGLGLGVGAGVGAAGFLESTSTMGGRGYNEMELDYMNSIGRNNAYSSRDMAGDFDGMALSDGYLCEYYSQKSRVVDGFGKDDPMVYDYEGKGSPVGSVGCCSLLEDQNDLEFLNDLGPKFTTLADICGGKKTEIPAPAPAPLPPPPKPVVDRSEVVSSTTNILNTGNIATNRVNTVNVASNMATASSTRVENVLVTDNRPTMITSVHPAPTLLVQPQPMYYMVEQQPSTVLVAERPAMTQGMYVLNSGPVAEGMVVQGGNIAANTLTRGERMVLVFRGGPAQALNNGMLHTSNLSGSQLLLVDGGATSGQVLQGTIQRGVAGSQGLMFVDGQGGQVIQGSINNGISTHGGSQNVFYVENKGGSSVVQGGLQMGKASTAGSLIGDVGIGGSSVKITQNPSSHKVVVQERKVVTTQSVK | null | null | convergent extension involved in gastrulation [GO:0060027]; desmosome assembly [GO:0002159]; epiboly involved in gastrulation with mouth forming second [GO:0055113]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156] | desmosome [GO:0030057]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509] | PF01049;PF00028; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:Q14126}. Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion (By similarity). Required for embryogenesis, specifically for progression of epiboly and normal convergence-extension movements during gastrulation (PubMed:22235774). {ECO:0000255|RuleBase:RU004358, ECO:0000269|PubMed:22235774}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
H2FH31 | LEC_CREGR | MTTFLIKHKASGKFLHPYGGSSNPANNTKLVLHSDIHERMYFQFDVVDERWGYIKHVASGKIVHPYGGQANPPNETNMVLHQDRHDRALFAMDFFNDNIMHKGGKYIHPKGGSPNPPNNTETVIHGDKHAAMEFIFVSPKNKDKRVLVYA | null | null | null | null | carbohydrate binding [GO:0030246] | null | 2.80.10.50; | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8-10 for the hemagglutinating activity of the human erythrocytes. {ECO:0000269|PubMed:9568372}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Hemagglutinating activity of the human erythrocytes is fully maintained after heating at 50 degrees Celsius for 3 hours. The activity is partially lost after heating at 55 degrees Celsius and completely lost after heating at 65 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:9568372}; | FUNCTION: Galactose-binding lectin (PubMed:23886951, PubMed:27010847, PubMed:28636877, PubMed:9568372). Binds both alpha and beta anomer of galactose (Gal), but has a stronger interaction with the glycans having alpha Gal at the non-reducing end and binds beta Gal weakly only in highly branched glycans. Has high affinity to Galalpha1-4Galbeta1-4GlcNAc (PubMed:28636877). Binds N-acetyl-2-deoxy-2-amino-galactose (2-deoxy-GalNAc) (PubMed:23886951, PubMed:9568372). Binds N-acetylgalactosamine (GalNAc) (PubMed:26439416). Binds porcine stomach mucin (PSM) with high affinity (PubMed:26439416, PubMed:30486373). Binds galactosamine (PubMed:27010847). Binds laminin, bovine submaxillary mucin (BSM), fibronectin, type I collagen and gelatin with a decreasing affinity, respectively (Ref.3). Has hemagglutinating activity towards human type A erythrocytes (PubMed:26439416, PubMed:9568372, Ref.3). Hemagglutinates also human type 0, B and AB erythrocytes as well as rabbit and mouse erythrocytes (PubMed:9568372). Agglutinates both Gram-positive and Gram-negative bacteria including B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254, respectively. No agglutination activity towards Gram-positive S.amurskyense CMM 3673. Has bacteriostatic activity on S.amurskyense CMM 3673, B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254. However, has no agglutination nor bacteriostatic activity on Gram-negative C.scophthalmum CIP 104199 or A.troitsensis KMM 3674 (PubMed:23886951). Inhibits growth of fungi from the genera Aspergillus, Penicillium, Trichoderma and st. Mycelia. Inhibits germination of spores and hyphal growth of them (PubMed:25482060). Has dose-dependent cytotoxic effect on the human globotriaosylceramide (Gb3)-expressing Burkitt's lymphoma (Raji) cell line. Binds to Gb3 in these cells leading to activation of caspase-9/3 and PARP (PubMed:28636877). Has dose-dependent cytotoxic effect on the Gb3-expressing human MCF-7 breast cancer cell line (PubMed:27010847). No cytotoxic effect on myelogenous leukemia K562 cell line, which does not express Gb3 (PubMed:28636877). Activates immune responses in mice and increases cytokine production of TNF-alpha, IL-6 and MCP-1 in the serum and the peritoneal lavage of mice. Induces TNF-alpha and IL-6 secretion in mouse RAW264.7 macrophages, mouse bone marrow-derived macrophages, human THP-1 macrophages, human peripheral blood mononuclear cells (PBMCs) and human blood monocyte-derived macrophages. TNF-alpha production in macrophages could not be inhibited by GalNAc, GalN or Gal, indicating that induced cytokine production is separate from its sugar binding activity. Increases intracellular reactive oxygen species levels, expression and phosphorylation of protein kinases PKC alpha/delta, expression of COX-2 and NF-kappaB, and activates the MAPK pathway by increasing the phosphorylation of ERK1/2, JNK1/2 and p38 in mouse RAW264.7 macrophages. Induces endotoxin tolerance in lipopolysaccharide(LPS)-activated macrophages by down-regulating IRAK2 expression, reducing JNK1/2 phosphorylation and NF-kappaB activation. Can slightly increase the bactericidal activity of RAW264.7 macrophages (PubMed:28740170). Has DNA-binding activity (PubMed:27010847). Recognizes pathogen-associated molecular patterns (PAMPs) and binds to LPS from E.coli, but has only little binding to beta-1,3-glucan from E.gracilis and peptidoglycan from S.aureus. Activates secretion of TNF-alpha and IFN-gamma by the human peripheral blood cells (HPBCs) (PubMed:31905927). May be involved in innate immunity acting as an antibacterial and antifungal agent involved in the recognition and clearance of pathogens (PubMed:23886951, PubMed:25482060, PubMed:31905927). {ECO:0000269|PubMed:23886951, ECO:0000269|PubMed:25482060, ECO:0000269|PubMed:26439416, ECO:0000269|PubMed:27010847, ECO:0000269|PubMed:28636877, ECO:0000269|PubMed:28740170, ECO:0000269|PubMed:30486373, ECO:0000269|PubMed:31905927, ECO:0000269|PubMed:9568372, ECO:0000269|Ref.3}. | Crenomytilus grayanus (Gray mussel) (Mytilus grayanus) |
H2KY84 | CMTA1_CAEEL | MNNSVTRLLFKRLLTLQLCHHFDIIPHRDQSFDCVQMQQPQNETANNFIPSIQLLWSTDPPQIRPDGTYPQAVELFPCFKDKWNTKEEILNIILAANADPKSNCVTVQSSPRPCSSSQFIYPRLDNAWYKNDGYIWKKRTNGKQNREDHLNLKISGHPHISAKYIHSAIVPTFHRRSYSVPDSDCHVLVHYLNVKTNNKIDDQAEEIARSMIENKVFISLSQLHDQLSPIFLQTLNVNQLVAEINEHLKKKGVNLPTSPLPQEPSSSTSRELERRNSCSSAFRKGLSSVALRRQPSANSEIDANHIGTMLKRFGCNGSSSDRISIIQPTMQNFQSIRSHQNHVAMESRSPSGDGDSRPITFEEDASYQQLSIKSSTNVSTPASAFAEKMKIRSGSQESPMGPPSSSSVTSTSLIPIIEMTPSSSSLKGGQKMLVVGGYYRKGHEYKISFGRGRMMPAVLIHAGVLSCVIPPSAKPEVVQIRVFCNGQAISTASEFTYEPQSAHLIKENDDTLVQIFEKIRIMACAFNAYSSIENIQSSSCMESLLANIVQQIDNEVSSQNLNYKTELLNGSAHFPSKTVLHLVASLDYDRLFEALIDLSRKVPACREFDIFARDNDGSTPLHTACKNSASRIARLIISIDSSAIDVVDDRGRTPVEVAPEHSIDMLSDKNNEEERVNATELWVMTNGKAFTTDKILDGKISRAPIAEKPDDLLREATSSYSIMSEMYEGPMLQAGTSRECDEDCESCCDPDSTQQLHVEIAMDTDVHVPDSPKMARLFHAVTSPGIVVPPNARARMADLARQIIEALPDRIKRNSEVSMCPDEEDPGQNHHGGVEPMFYQQASCSMSTDSPNMMDDYFDMMATETRNDIFTEPRSTETTETSASKSAQLFATHCNFFDDRSFASSSTRANTFESDTLDFDKDLGEFFTIHVDRFVDPIQQRLANLKYNDDEQRDVYEAAMVIQRAYRVYRARSTTRRQEDIERRAALKIQGCYRRYKQFCYFKKLHNAAIVVQKHFRMRKRDDKEEGAVEAVIASVPEHPTLDGQSICIQVPKTNSTMLRERAATTIQVAYRYRHRKRQAAARKIQNFMRQNRNNVNIDDGHTQHLIAENACAKRRRYVACPQTSGDQRNKRDSDGERKRDAHHDAPEFIPIGATPSSTTIPHRPTQRHHPWDQLKPPYGCGTLA | null | null | positive chemotaxis [GO:0050918]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to oxygen levels [GO:0070482] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; transcription coregulator activity [GO:0003712] | PF03859; | 1.20.5.190;1.25.40.20;2.60.40.10; | CAMTA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:34499028}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:34499028). Positively modulates neuronal levels of the ubiquitous Ca2+ sensor calmodulin/cmd-1, probably by direct binding to the cmd-1 promoter, thereby regulating Ca2+ signaling, physiology, and behavior (PubMed:34499028). {ECO:0000269|PubMed:34499028}. | Caenorhabditis elegans |
H2KY86 | HELQ_CAEEL | MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKSTDPDGICQLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERMDAVLKQCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPMVGRERLGKAQYLQMAGRAGRAGFDTKGDCITIIKAGEEERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHYFITIEPLEQDVASEPSAQASSIPRVPGKISPSDLGNAVFNAGFDPDEATRLHADLVSSLNQGVIFASHFHLLFIITPYEQVCNINWDLFLLMYNALPSSERKLLAECGLEEKFILEAIITRVDLTAGTPRMRLYIALMLQKIWNHEPMYTVAERFGVEKGWLQATLQSSISQAASIAKFSEKITTMWPLRKLLPELVQRLSEAAQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARANPLKLVQELGTIRMAQANSIIASARMVLRDQVDEKMEELDVWGVATDSFNYF | 3.6.4.12 | null | DNA double-strand break processing involved in repair via single-strand annealing [GO:0010792]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; resolution of meiotic recombination intermediates [GO:0000712] | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]; single-stranded DNA helicase activity [GO:0017116] | PF00270;PF00271;PF20470;PF21099; | 1.10.3380.20;3.40.50.300; | Helicase family, SKI2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDG4}. Chromosome {ECO:0000250|UniProtKB:Q8TDG4}. Note=Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q8TDG4}. | 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:0000250|UniProtKB:Q8TDG4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q8TDG4}; | null | null | null | null | FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair (PubMed:18472307, PubMed:34880204). Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA) (PubMed:34880204). {ECO:0000269|PubMed:18472307, ECO:0000269|PubMed:34880204}. | Caenorhabditis elegans |
H2KYH3 | RING2_CAEEL | MDDSPGPSTSKSARDKAENAEENTSDSSSDSEVSSASEKSEESRPSSEKKKVITRVIPVRPPTRDKGHRVNLLESGNESETKSLYQRAKEGIPSYKGKPEIKLPTTSEQYYDLEEVLMNPARMEGRELTLNAYDAVRNKYNVLPGKSVCEADLQKVIGSFSCDVCQELIQGSIMTKKCGHRFCDQCILVAFMRSGNTCPTCRQNLGSKRELQQDPRFDQLIYQVVESRSIVGRMMAENREHEKDVYFGRKGYIEGGSDWNKRYGIDPNSKLKAPRPLKSAGRKKIRWFHESDEDGSVRKVMESKKGAPKEDDTNYLENDKEGTSVAAEKEVLEEGEMDFPIEIKSSDEEQTDLDDEEESMLDSDFEISDNEDVSKPSCSTSKKTTNRSRDSSESDNDSRDNELQKKKRKMKRKNVPKTDGSDVSNESFDEDASGEVVATKLIKESKKKPCGRPKKKFAPELIEGDIPTPSEDSLTSSDEERDDNAADPYAFVFQKEFNRDPRRDGHPEKDKLYNFDFMIDMNHQVDRKFEKDGEIHVISDDSNSEHESDEAEDRESSIDSEHEKEISKFLSHRQPLPNPTSVDDDCQVITVVKKDVKQSAITSKPGETSPDSSSKIEEKPDKVSEEVSDDEMTPEHITADKGTDTFLNNIMEHDDEMYGGYLFRPGDTGISRPKVQRAPGTNRLSMNVCPEAVYVVYPQPVLKEGKKKLVIPPEDYEISSDETVTLSDSEETSPSAEMEQSETSEAGPSTIIKTSGTERETQGSSSPSEPSTSRDRKMHKRKLDTRRRKLADDSDLSDFDVFSIDGNELVATGKPIIKHKVFYDSANRMPSKSNLDFTGRRNAREIPMEEISRLAEEQVAHEEYKIHRRRQVVLEAVEAASKKLNVYVDTTEEEEIEEEETPEEEVVKVASPTAPIATENPTTSTAPFEEGVAMKETPIEEIFFDPDEPCSSAQAAQRELIIERVGKEQQIIEDSLEQNRKPSSKTVKESESREAQEPRIEKDEMESEQQKKDADNPTVEVDKESEASSSESDKSDFEDETLDAQSKTVKISLKHEKTVSDEEIEDFDTKFGEFVATADAKMIKRTIGEYVSTEFLKLVAQQPAVTDEVLALGFCVRNTDQEFSTIKETGKRTNKNPDDVRLESMVKNFRESFAAKHRPVPRKLPTNIERMYIERAHMVKYKHVVDMEPLHMKILIALQKQQIAATCANLSQPVTVTPEEHAEQVQLLHNLQNPSILRPLLNNPQFALTLHKAQQQAIQQQRAQQKAQTQKELAARQAEQARVEELARKRIAQEDAEKALRQKGEQMSNVSGIPVSSDQNAQSSNAQQTGLIENQTTTTNSDSLTRPNTLADNSHLGESQQIPVIESIQSSTSEALKESENYKDMPILTPASTVSSKSSAPATRRPSRPCSSYDRPSSPSVVIRERLGSDGALINRPPNRCNIDKSRSRSPISRAPVETVRINDHGQNETILAGNITHTVETTILEEGTSIGQDSTIRYDGECSTTQYIDKTIDLDNSKNGTNVDEEQSNVLKLRENDLNREMLRYANRYHPSTMLAMGNLSINERHNKVQQVLASQELQDLIARHTSGAVSQTQVEVVGGEGVCAGTSDAIGETDEDDDVEEEPEFTVDQLELAKKILKQRQGLESSEDSDSDEDMVYDNVDGSVIRRAPHKKRETRKKKNIFVPNIPPKIRRKYVDKKIEMERAKYRARIKSQKMASIRIAVPQKPTQQFATPQQPVRGPGKHSAAAAARATPKPKKAKMSNVQMSIVQPPLPLHQLQGHMSAPTKITAVPNVAAGFHQNQQQLYSDMAQAPQSTPIRTTPQPGTGSAPQAQTPQSHLAQLGQFVNGANQQQAPQQQGMYTAAQLQAMQAAVAQTAQAAQAAYAAEAAYQAQVAQQARAAPPQQLVQRQVPVGHPGQVNVPMPAQMLNQGNPQMAVNPAQAQMMDERRKMEEVNAVYHLMQSRGQFPPTNQELFQVQFAQAQADLRSAAAQAAQAAQAQAQMTNMRAQAEAVARQQAMMKQEQARAQAAAKEAARLKAETEAAKAKVQAEAEARRKAEQEMRVRQAQAAQTQAAQAQAQSQAHAQNQAQTQAIVEIQRMIQSGQPLSMQQMQQLQQMSQVQMQHAQQVQQMQQMQMQQLQMQQFAARMQQGTPKPAVSQQAVQQGMPAGIQGMPTGMGMQQLQGLGMPGMQLPQQAGQSQQTSQAQQQQLFMQLQLQQQQLMQHQLQQQLQMQQHQQHQQQQQQIQMQQQQQLAQQGLVPNVSSAWLQQQAQLAQQQQQVVQQNLLMRVPSAQTPVAPRAPTVAPQSVVQQAPAPATPIAISVATTQVTRPETVEPFRSISSGTGTGTERINNNVELELWPTNGYSEKKRKEGSQASPIFGASAGDSTFYHVACLIRSRSACNADDVGSLWVLRLEDQTLLQFQLQQTLAEAQRFVGKQHLVIFYDDVMSGEVQQSKEYVINREFKPSNRQIPN | 2.3.2.27 | null | negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of vulval development [GO:0040027]; nematode male tail tip morphogenesis [GO:0045138]; protein ubiquitination [GO:0016567]; regulation of cell migration [GO:0030334]; reproduction [GO:0000003] | PcG protein complex [GO:0031519]; ubiquitin ligase complex [GO:0000151] | chromatin binding [GO:0003682]; histone ubiquitin ligase activity [GO:0140852]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF13923; | 3.30.40.10; | null | null | null | 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; Evidence={ECO:0000250|UniProtKB:Q99496}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q99496}. | null | null | FUNCTION: E3 ubiquitin-protein ligase playing a central role in histone code and gene regulation (By similarity). Involved in ubiquitination of histone H2A (PubMed:19211678). Plays a role in the formation of the male-specific genital sensilla (simple sense organs) known as rays (PubMed:19211678). Required for normal migration of the hermaphrodite specific neurons (HSN) and for extension of some neuronal processes (PubMed:19211678). Represses vulval fates in hypodermal cells that do not normally contribute to vulval development (PubMed:19211678). {ECO:0000250|UniProtKB:Q99496, ECO:0000269|PubMed:19211678}. | Caenorhabditis elegans |
H2KYH4 | HAM2_CAEEL | MPYRAELKRPDLKGSFPCSICQKVFCHSSSLSRHRMQAHFKSYTCTTCNNEIPSNDTLRSHMYRVHNITRMFMCRCCNWAFPDKTSLHIHMQSMLKNGTPGEAAVLAKSSDVVDSTSESGSPRQSPPFSPDLLMQKRMLQVAANNNNIGSIFPTLLKSPDSKSMFPLDLSNMGPSQFLSAWLANNPINTAALNLAAQQTPSKDSIQSSNISDYDDLEVQTTEEDIKFEVESSDVSPRSVIVKTEPTFKRELEHDADIDVEGDDGEPPLKMTIDDKNIHISHDQPSPTVSDSHISGGSSSHSGESLKCFDCQVARGKLVAVEDKCRAYEKTIRELQVQVDFLRKIQPNPMPPVMLPPPMMPMPSPGPNNLFQNPAMRMLLNNLIHMNRPSVVP | null | null | cell fate determination [GO:0001709]; cell migration [GO:0016477]; regulation of DNA-templated transcription [GO:0006355]; regulation of neuron differentiation [GO:0045664]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10049362}. | null | null | null | null | null | FUNCTION: Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation (PubMed:10049362). {ECO:0000269|PubMed:10049362}. | Caenorhabditis elegans |
H2KYJ8 | NHR66_CAEEL | MPPINEPTATTTSASSVWQGMTQLKSQVDLINIARGILSTPATTSTSCLDIQNSTPIIGSLASGKSQTPILTATMTPQIGLTGLGSLTSLPPELLLQFARLDGFNLLPAVGSPAIPSSSSCSEPSTSQASTVVSAPTLPPPSPLTSLPQKPAPLMPSGHVTTVDQQNRQQHQQQQRQQQQAQQQNSMARKYSMDTIQHHTMQHPHQLQYIPNHFMTASTDVFAAMDMSQKQSSPPGIFKIVAAKNEPSSSSNSQPGTPAMGDRRAVPACAICGTDSTGIHFGVDACAACSAFFRRTVVLNKDYSCNKGGKCTVVKDGSAGQKCRACRFRKCISSGMDKNSVQHRRDAIGKYSAGVKRELSPDAEFEPSAKVSTVSEPSTSSGPSGGFNQNVSSPAGIPRVPSTLRTTQASTCMNSACGQKSVLHELICRQNFLTEQRQLFYAGCLGDWFRKPSSIENQTLSELTDFSSCMFHLWKIEPRLAADFMNRNRYLDPLPIVEKLKIYRNFVIMRQSVEEPYLTWRHGGLEKRWFVMPNNTYIDFNNIAKYFENGALKDLKLDYETTTNLFLPSFTHAMDTIGEKMKKNNITETELTILLGLVLLDPGIYGIHESTRKFLKRIRDQLIHDVYMYYEDEMSHLYDPEIRMADIFMLVAAIKIHSIKTSENMHMLRVFDLIPADACFNQMLDVESVNVSPDGQKDSEAEQGPSPVSVPEAARGSYQDDDMPPVLEKNCDL | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122] | nucleus [GO:0005634] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU004334}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:33259792). Binds to regulatory elements and regulates transcription of target genes, including the potassium channel accessory subunit mps-2 (PubMed:33259792). Negatively regulates transcription of mps-2, thereby modulating age-dependent memory decline (PubMed:33259792). In concert with nuclear hormone receptor nhr-49, involved in regulating target genes with roles in sphingolipid breakdown and lipid remodeling (PubMed:22511885). Plays a role in modulating mitochondrial morphology and function (PubMed:22511885). {ECO:0000269|PubMed:22511885, ECO:0000269|PubMed:33259792}. | Caenorhabditis elegans |
H2KYQ5 | GYG1_CAEEL | MSEAWITLATNDNYAQGALVLVHSLRTAGTTRKIHCLISNEVSAPVRKQLEEHFDDVSIVDVFNSNDSDNLRLIERPDLGVTFTKLHCWRLTQYTKCVFLDADTLVLRNADELFTRPDFSAASDIGWPDSFNSGVFVYVPNNETYRQLVDFAVTHGSYDGGDQGLLNDFFSNWRDLPSEHRLPFIYNMTAGAFYTYAAAYKRYGANTKIVHFIGSVKPWHGSAAVHTGEHFQQWQKIYHAHVNHTSRTNEHAAVFPSHHHTPEHRSHSADHPKIERKDSIVREIGNFVMHVVQSVNILPSYDTDANTSDSHRNNEPHKHDQQREEHHELPHNKFQTPHEESQDIVGSTDCFGSQMPKYNADSETDREVEQITNNTPCPAFVPFERREEYQAASPSTEERRAAWEAGQPDYLGRDAFVHIQEALNRALNE | 2.4.1.186 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P13280}; Note=Divalent metal ions. Required for self-glucosylation. Manganese is the most effective. {ECO:0000250|UniProtKB:P13280}; | glycogen biosynthetic process [GO:0005978] | cytoplasm [GO:0005737]; striated muscle dense body [GO:0055120] | glycogenin glucosyltransferase activity [GO:0008466]; glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751] | PF01501; | null | Glycosyltransferase 8 family, Glycogenin subfamily | PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-194. {ECO:0000250|UniProtKB:P13280}. | null | CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:0000269|PubMed:24982189}; CATALYTIC ACTIVITY: Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140574; EC=2.4.1.186; Evidence={ECO:0000269|PubMed:24982189}; | null | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:24982189}. | null | null | FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for gsy-1. {ECO:0000269|PubMed:24982189}. | Caenorhabditis elegans |
H2KYS3 | DAF9_CAEEL | MHLENRVLSSVLDYASKFYKRMSSLVFFSANSIQVQMNISQSSWIKCRDWMAFALSHHIIMGIYLLILRNFLPQVVPDFEWQHYFMRVFIVHIIYIIISYFIRITRYPPGPPPMAVFGNSPFVNILTPEQTFLEYREIYGPIFTLHLSQPTIILAEYKTIQEALVKNGQQTSGRSSAESFVLFTGDRLNGDGVILAMRQKWKDMRHEISRFMNKWYGAPMDELVLHHTRCLEQELAKIAETKSLIDLRDPLAGAIANVIQQITIGRNYMYQDQEFQTQLRDINAVVKEIMTAEVFFVNCYPWLRYLPEGILRKWTNYKRSGFRLQQWFRTILEEHHVNRHQGDFMSHMIDLQESKQEQFRDLSIILTCGDMWTGGMETTVTTLRWGIIYLLNNPEVQAKCQMEILDVFGNDIPDMGKMNQTPYVRATLSEIQRLANVLPWAIPHKTIEECNIGGYDIPVNTEIIPALGAVLFDPNVFESPKQFKPERFLDEEGKYRVMEEFRPFGLGPRVCLGERIARTELYLIFASLLQNFRFYLNRGDPIPVAERVIGGITAPPKPYATRVEYLGNRLIN | 1.14.14.- | null | cell-cell signaling [GO:0007267]; cholesterol metabolic process [GO:0008203]; dauer larval development [GO:0040024]; organic acid metabolic process [GO:0006082]; regulation of cell migration [GO:0030334]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to dendrite-like structure in XXXL/R cells. {ECO:0000269|PubMed:12783794}. | CATALYTIC ACTIVITY: Reaction=5alpha-cholest-7-en-3-one + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = (25S)-Delta7-dafachronate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66620, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:71542, ChEBI:CHEBI:71550; Evidence={ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66621; Evidence={ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}; CATALYTIC ACTIVITY: Reaction=cholest-4-en-3-one + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = (25S)-3-oxocholest-4-en-26-oate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:66624, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:71541; Evidence={ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66625; Evidence={ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}; | null | PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis. {ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:22505847}. | null | null | FUNCTION: Converts the 3-keto steroids 4-cholesten-3-one and lathosterone into the carboxylic metabolites 3-keto-4-cholestenate (Delta(4)-dafachronic acid, Delta(4)-DA) and 3-keto-7,(5a)-cholestenate (Delta(7)-dafachronic acid, Delta(7)-DA) respectively, by catalyzing successive oxidations at C-26 (PubMed:16529801, PubMed:22505847). Dafachronic acids bind directly to the nuclear hormone receptor (NHR) DAF-12, suppressing dauer formation and inducing reproductive growth (PubMed:11782415, PubMed:12783794, PubMed:16529801, PubMed:22505847). In a non-cell autonomous manner, negatively regulates body wall muscle arm extensions to motor neurons probably by preventing daf-12 isoform b activation (PubMed:18436204). May be involved in thermotolerance (PubMed:24957743). {ECO:0000269|PubMed:11782415, ECO:0000269|PubMed:12783794, ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:18436204, ECO:0000269|PubMed:22505847, ECO:0000269|PubMed:24957743}. | Caenorhabditis elegans |
H2KYS8 | CPNA1_CAEEL | MVFDARLGYDPDEWEECPEPEHFLVFSGFTRYMLTFAAIAFVYYFFKLLDDKNKKESGEKEEPQTSVESVLAKAGDKLHDVKEQVQQHIPESAEELMREADQYLKEQAHSVQNNVHQFAEQAANKFPSLEVDLNLGHPIDATREKFDTVLSSVNNHLHETKNMDLSPTSRDSTQFEQIPSIAPEESAFGHDFEHVPPHLKTAAEQYYAQQHQPPPVPQHKIVQPVPISPTDQQLLHEFDIYDAPAHQRMNQISEQLGQLGQKTPAQLQQLQHAQLAHQQLQQQGVFQPIQQPSPLQIQTHPQQPYFDFSQLSPASQARYNQQQFVDISQLSPGAGALIAEQQASGAFQPVTKKLGREKRLSEQDERALQDWEKEKALLEADRLKKLLDHEVGGDSTDLDSSQKAYDHFAPASHISYESHSGAAQIQPMTPTAPKRADVPAPQVTSITNVRDSQLTDYDISDFHAHDEPHYHTVLTPQQLQQNQQQHQQPSAIDRRRTTADSDDYVKVSEPIYDYPPKGHEAPVAEPKRISPTEAAQLQELYQEYDLGLDLPGVAPIQGVAKPPVQQRTPLQIQQQVVQNVQNQPNMMARQNSVPESPRTVINVPISRKTDVPIQVQQQQNQFSYNVPIQVKDDPRNLATADLFVQDAQEYVAHQQNQQDKGSFVMEEEMLSLHEPETGSNKKKLTPKNPSFEATSRQVRTNDVFERIEHDEHDDMTYAPEIQSVEIPPDQMSETSENMIDYFDKVAAESEQQIQHLQEQQNTLKKQQIETSIPDSSLLKPVGRAPQILPAFGNRISSNSSLGSAGRSGSGVSSSDVYPYRHLRKQSSLLSVLGVTSMQEMLLAITSLDSLSEAMRKAGLETTNLIFGIDYTASNKYQGEESFGGRSLHTIHPHVTNPYQQVISILGRTLAPFAGQGRLGVYGFGDAKTGDWSVFNLKGEGGDCRSLDEVLNVYNTVTPTVALSGPTNFAPLIYQAMEICQKSRDYHILVIIADGQVTNERATRRAIVQACQHPLSIIVVGVGDGPWDMMRIFDESLPKRPWDNFHFVEFHEIVKKSTNMEDGDVKLAVQSLLEIPDQYRCICELGLLDRSIPPRGSEIRREMMHNPL | null | null | positive regulation of sarcomere organization [GO:0060298]; protein ubiquitination [GO:0016567] | basal plasma membrane [GO:0009925]; M band [GO:0031430]; nucleus [GO:0005634]; striated muscle dense body [GO:0055120] | phosphatase binding [GO:0019902]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin-protein transferase activity [GO:0004842] | PF07002; | null | Copine family | null | SUBCELLULAR LOCATION: Basal cell membrane {ECO:0000269|PubMed:23283987}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23283987}. Note=Colocalizes with unc-89, unc-112, pat-3 and pat-6 at the M-line and with alpha-actinin, unc-112, pat-3 and pat-6 in dense bodies. In body wall muscle cells, colocalizes with beta-integrin pat-3 at integrin adhesion sites. {ECO:0000269|PubMed:23283987}. | null | null | null | null | null | FUNCTION: Involved in the assembly of dense bodies and M lines during body wall muscle development. Acts by recruiting downstream of integrin-associated protein pat-6/actopaxin several dense bodies and M line components including unc-89, lim-9, scpl-1 and unc-96 to integrin-mediated attachment sites. {ECO:0000269|PubMed:23283987}. | Caenorhabditis elegans |
H2KYU6 | NPL41_CAEEL | MVLEVPQTERVNDVDVFLSTQDGQIQRPKGPNCRHPVRQKCTNCLPVDPFDEEYLKEKDIKHMSFHAHVRKLLGSQGKGTTLKKPLENFRCSLKPNCDAHKPFPKGICTKCKPQVVTLNRQKFRHVDNIQIENQELVNQFLDYWRLSGHQRVGFLIGQYQPHLEVPLGIKATVAAIYEPPQHCREDGIEFLEDKNQKTIDNLLEMLGLQRVGWIFTDCWTANSAEGTVHYTRHKDSFFLSAEECITAAMLQNQHPNITEYSMDRHYGSKFVTVVASGDESMHVNFHGYQVSNQCAAMVEADILCPTLYTPELAYVRETPLSEEHYITDVQFSMKNEYGAEVMKNGRPLPVEYLLVDVPAGMPKEPHYTFHVGTSNKSKSAKFNVENRQAIGQLQGGANLIQYSSEFSKNQFLEQATNFHFLLYLVTNDQVQISDEWMKRLCDAVKAQDRGTAMEWAQECEDWHQLMALAHANGGSGNDVSDIPVIPNGDPFSGSSSGGSGGAVWNCGHCTFQNEAARQDCSMCGLPAAD | null | null | positive regulation of protein localization to nucleus [GO:1900182]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098] | metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625] | PF05021;PF05020; | 3.40.140.10; | NPL4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18728180}. Nucleus {ECO:0000269|PubMed:18728180}. Note=Localizes to the cytoplasm during mitosis. Nuclear localization upon nuclear membrane re-assembly is cdc-48-dependent. {ECO:0000269|PubMed:18728180}. | null | null | null | null | null | FUNCTION: In association with ufd-1 and ATPase cdc-48.1 and/or cdc-48.2, involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:22768338). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:22768338). During S phase and in association with ufd-1, cdc-48.1 and/or cdc-48.2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CGM helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564). {ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}. | Caenorhabditis elegans |
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