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
196
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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
F1RCY6 | RENT1_DANRE | MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTQGQTQSQLDNQVNGPDGVLPNGEDAVGKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPTATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRLKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMSTAMYDAREAMIPGSVYDRSSTGRPSNMYFQTHDQVGMIGTGPNPMGSLNIPIPFNLVMPPMPPPGYLGQVNGPAAGRGAPKGKTGGRGGRQRNRGTGNHGSGQPNMPNSQASQDLVSQPFSQGPLTQGYITMSQPSQMSQPGLSQPELSQDSYLGDEFKSQMDVALSQDSTYQGERAYQHGGVTGLSQY | 3.6.4.- | null | chordate embryonic development [GO:0043009]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000624]; regulation of gene expression [GO:0010468]; T cell differentiation in thymus [GO:0033077] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270] | PF13086;PF13087;PF04851;PF18141;PF09416; | 2.40.30.230;6.10.140.1240;3.40.50.300; | DNA2/NAM7 helicase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EPU0}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPU0}. | null | null | null | null | null | FUNCTION: RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. The formation of an upf1-upf2-upf3 surveillance complex is believed to activate NMD. {ECO:0000250|UniProtKB:Q92900}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RD40 | MYCB2_DANRE | MMCAAAAAGAGGSGILSSSSHSMGLGVRVIPGAGNDFAPIGSGMGSCPVVGARSDCRSRYQLLLSGRALAERYRRIYTTAINDKEQGLNLGRGKKALSKKKLKRRQKVKSKVKTRTKTDTLDGAFPVPDIKLHSNPSAFNVYCNVRHCVLDWQQKEAALALASRNSVQSGDSDSEEEEEYREPFVKLPKIIGIGLCGVFELIKETRFSHPSLCLRSLQALLDMLQGQQPESFQTEPPDVLESLFHLLLETTVRSTGMNDPTGQTLTALSCACLFSLVVAWGDTGKTLQAVSAILTNNGSHACQTIQVPTILNALQRSVQAVLVGKIQIQEWFGNGIKRAALMNKWVLKEVNIDDDEHCLLQTDGSFLYLLCKDGLYKVGSGYSGTVRGHVYNSTSRIRNRKEKRSWLGFAQGCLLYRDMNSHNMAAIKINPETLEQEGTITVPGLQADGQNIIFTDGEYINQIAACKDDGFVVRIYATSSDPALQQELQLKLARKCLHACGISLFDLEKDLHIISTGFDEEAALIGAGREFALMKTASGKIYYTGKYQSLGIKQGGPSSGKWVELPVTKSPKIVQFSVGHDGSHALLVAEDGSVFFTGSASKGEDGESTKSRRQPKPYKPKKMIKLETKMAVYTACNNGSSSIVTKDGELYMFGKDAIYSDSTCQVSDLKGHFVTQVAMGKAHTCVLTKSGEVWTFGVNNKGQCGRDTGAMSQAGKAFGVENMATAMDEDLEDELDEKEEKSMMCQPGMHKWKLDQCMVCTVCGDCTGYGASCVSSGRPDRVPGGICGCGSGESGCSSCGCCKACARELDGQEARQRGIFDAVKEMIPLDLLLGVNIEEHIQIRQEEKRQRINRRHRLEEGRGPLVFPGPLFMNQREQVLARLRPLQAVKLMREKLKDGSSERGDKDASKITTYPPGAVRFDCELRAVQVSCGFHHSVVLMENGDVYTFGYGQHGQLGHGDVNSRGSPTLVQALPGPSTQVTAGSNHTAVLLMDGQVFTFGSFSKGQLGRPILDMPYWNAKPSPMPNIGAKYGRKATWIGASGDQTFLRIDEALINSHVLATSEIFANKHIIGLVPTSISEPPPFKCLLINKLDGSCRTFNDSEQEDLQGFGLCLDPVYDVIWRFLPVTREMCCYNAVIADARVPTASDIQALCSILSPELALPSGSHASTTRSHGALHILGCLDTLAAMQELKMGVASAEEETQAVMKVYSKEDYSVVNRFESHGGGWGYSAHSVEAIRFCADADILLGGLGLFGGRGEYTAKIKLFELGPDGGDHETDGDLLAETDVLAYDCAAREKYAMMFDEPVLLQLGWWYVAWARVSGPSSDCGSHGQATITTDDGVVFQFKSSKKSNNGTDVNAGQIPQLLYRLPSNDGNASKGKQQTSEPVHILKRTFARTVSVDCFESLLSILHWSWTTLVLGVEELRGLKGFQFTATLLDLERLRFVGTCCLRLLRVYICDIFPISASTKAIVEESSKLAECVGKTRSLLKKILSEGMDNCLTKLDNDPQGYLSQPLTLLEAVLQECHNTFTACFHSFYPTPALQWACLCDLLNCLDQDIQEANFRTSSSRLLAAVMSALCNTSVKLTSILPIAYDGEVLLRSLVKQVSTENDSALAHRFPLLVAHMEKLSHTEENLMGMTTFREVLEKMLVIVVLPVRKSLRKEVELFSPHLVSNTCGLLASIVSELTASALGSEVDGLNSLHSVKATPNRFTKTSQGRSWNTGNGSPDAICFTVDKPGVVLVGFCVYGGGGIHEYELEVLADDAQTEHPGDSAHSHRWTSLELVKGTYCTDDSPSDIAEIRLDKAVPLKENVKYAVRLRNYGSRTANGDGGITTVQCSDGVAFTFSTCSLSSNGTNQTRGQIPQILYYRSEYDGDLQSQLLSKANEEDKNCSRALSVVSVVVRAAKDLLHRAFAVDVEDIPELLSSSSLFSMLLPLILAYIGPVAASVPKAAVEVFGLVQELLPAVSALNQKYAPPTFNPNQSTDSTTGNQPEQGLSACTTSNHYAVLESDHPYKQAGVTQYKVSFPDCVRWMTVEFDPQCGTAQPEDVLRLLIPSRSLHFSGLSSKALAHETINSWTELKKFSGSSGWPTAVLVLPGNEALFSLETASDYVKDEKASFYGFKCVAVGYEFNPGLDEGIIQLEKELAYLGSVCAAALMKKDLALPIGNELEEDLEILEEASLQVCKSHSGLLGKGLALSHSPTILEALEGNLPLHLQTNEHSFLEDFITCVQSSSGGRLARWLQPDSYADPQKTSLILNKDDIRCGWPTTVVVQTKDQYGDVVHVPNMKVEVKAVPVSQKKSIQQENMKKLQRLPGTSSNSATGTDLTFGGHPAPKLEATYEPMIIKEARYIAITMMKAYENYSFEELRFASPTPKRPSENMLIRANTDGTYSANWTPGAVGLYTIHVTIDGIEIDAGLEVEVKDPPKGMIPPGTQMVKPKAEPQPSKVRKFVAKDSAGLRVRSHPSLQSEQIGIVQVNGTITFIDEIHNDDGVWLRLNDETVKKYVPNMNGYTEAWCLSFNQHLGRSLLVPVDVINSEGTWVQLDKNSVVEFCESDEGEAWSLARDRGGNQYLRHVEEQAVLEHGAQTPPPSPFSVQAFNRGMASSGAQGFDYGISNNKGDRDNMASWSVSPGSKHRQESRSSKTDSHSNRSVDQVKSKNNESLSASEALILKSDTGKLRSDSHSRSHSPNHNTLQALKADGRTSGLRAESPNPGSRSSSPKQKTFTSGRSSPSSTSSPRSSSPHDKNLPAKVSPSKVHLDPPRERSKSDSYTLDPDTLRKKKVPLMEPLRGRSTSPKPKLPPKESKGGSSNAENRAPSPHVVQENLHSEVVEVCRSSALLSNDEGNDENSELHNAEEGSSKVHFSIGKAPVKEELESRSSPKVSRKTSSRHVRPKKDKSGPLFKGENVRPTEPAKQAMSPSVAECARAVFAAFLWHEGIVHDAMACSSFLKFNPELTKEHAPIRNSLSCQQGFDEKESKLKNRHSLEISSALNMFNISPHGPDISKMGSINKNKVLSMLKEPPLPEKCEDGKESVSYEMTSHSSMRSKSILPLTLQHLVAFWEDISMATIKAATQNMIFPSPGSSAILKKKENEKDSKKTKKEKKKKEKAEVRPRGNLFGEMAQLAMGGPEKDTICELCGESHPYPVTYHMRQAHPGCGRYAGGQGYNSIGHFCGGWAGNCGDGGIGGSTWYLVCDRCREKYLREKQTAAREKVKQSRKKPLQVKTPRALPTMEAHQVIRANALFLLSLSSAAEPSLLCHHPPKPFHSHLPSLKEGVSEELPNKMGCLYLQTLARQHTENFGVYQDDNLFQDEMRYLRSTSVPAPYISVTPDACPNVFEEPGSNMKSMPPSLETSPITDSDTAKRTVFQRSYSVVASEYDKQHSASPARVKAVPRRRVHSGDAEVGSSLLRHPSPELSRLISAHGSLSKGERNFQWPVLAFVIQHHDLEGLEVAMKHALRKSACRVFAMEAFNWLLCNVTQTTSLHDILWHFVASLTPSPFETEEEEDEENKGNKENLEQEKDLGVCEHPLSDIIIAGEAAHPLPHTFHCLLQTISDLMMSLPSGSSLQQMALRCWSLKFKQSDHQFLHQSNVFHHINNILSKSDDGDSEESFNISVQSGYEAISQELCVVTCLKDLTSVVDIKTSSRPAMIGSLTDGSTETFWESGDEDKNKTKSITISCVKGINASYVSVHVDNSRDIGNKVTSMIFLCGKAVEDLCRIKQIDLDSRHMGWVTSELPGGDHHVIKIELKGPENTLRVRQVKVLGWKEGESIKIAGQISASVAQQKNCEAETLRVFRLITSQVFGKLICGDAEPTPEQEEKNLLSSPEGEDKAPSDADLKEHMVGIIFSRSKLTNLQKQVCAHIVQAIRMEATRVREEWEHAISSKENANSQPSDDDASSDAYCFELLSMVLALSGSNVGRQYLAQQLTLLQDLFSLLHTASPRVQRQVTSLLRRVLPEVTPMRLASVIGVKALPPADISDIIHSTEKGDWTKLGILDMFLGCIAKALTVQLKAKGTTIVGTAGMAAGKGVTTVTLPMIFNSSYIRRGESHWWMKGSTPPQIAEIIIKLVKDMAAGHLSDAWSRVTKNAIAETIIALTKMEEEHRSPVRCIATTRLWLALASLCVLDQDHVDRLSSGRWMGKDGQQKQMPMCDNHDDGETAAIILCNACGNLCTDCDRFLHLHRRTRTHQRQVFKEEEEAIKVDLHEGCGRTKLFWLMALADSKTMKAMVEFREHTGKPASSSSDACRFCGTRHGTELSAVGSVCSDQDCQEYAKLACSKTHPCGHPCGGVKNEDLCLPCLHGCDKTATCLKQDADDMCMICFTEALSAAPAIQLDCSHVFHLQCTRRVLENRWLGPRITFGFMSCPICKNKINHLVLKDLLDPIKELYEDVRRKALMRLEYEGLHKSEAITMSGARFFNNPAGFAMNRYAYYVCFKCKKAYFGGEARCDAEAGQGDDYDPRELICGACSDVSRAQMCSKHGTDFLEYKCRYCCSVAVFFCFGTTHFCNACHDDFQRMTSVPKEELPHCPAGPKGKQLEGSECPLHVVHPPTGEEFALGCGVCRNAHTF | 2.3.2.33 | null | axon choice point recognition [GO:0016198]; axon extension involved in regeneration [GO:0048677]; axon guidance [GO:0007411]; central nervous system projection neuron axonogenesis [GO:0021952]; circadian regulation of gene expression [GO:0032922]; developmental pigmentation [GO:0048066]; habenula development [GO:0021986]; neuromuscular process [GO:0050905]; protein ubiquitination [GO:0016567]; regulation of axon guidance [GO:1902667]; regulation of pteridine metabolic process [GO:0042068]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; retinal ganglion cell axon guidance [GO:0031290] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF08005;PF00415;PF13540; | 2.60.120.260;2.60.40.10;2.60.120.820;2.130.10.30;3.30.40.10; | RING-Cys relay (RCR) family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75592}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TPH6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7TPH6}. Note=Localizes to axon shafts and associates with microtubule cytoskeleton. {ECO:0000250|UniProtKB:Q7TPH6}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.; EC=2.3.2.33; Evidence={ECO:0000250|UniProtKB:O75592}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:O75592}. | null | null | FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (By similarity). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (By similarity). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (By similarity). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required in the visual system for correct fasciculation, targeting and mapping of retinal axons (PubMed:15590740). Acts as a regulator of pteridine synthesis (PubMed:15617681). May play a role in the regulation of the circadian clock gene expression (By similarity). {ECO:0000250|UniProtKB:O75592, ECO:0000250|UniProtKB:Q7TPH6, ECO:0000269|PubMed:15590740, ECO:0000269|PubMed:15617681}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RD85 | LOX3A_DANRE | MLRSELRDMVVAMVLWGILLPFCLSQTTSPSQDGKIKFRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICKDERLPGFAESNIIEMQVDEKRMEKIRLRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCVPGLQFTQGRVRKAKLNPVPQMRLKGGARAGEGRVEVLKGSEWGTVCDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVICNIPYMGFEKLMRLTGGRTRLEGRVELLLPAGGGVRDWGLICGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVICSDMASDLVLNAPLVEQTVYIEDRPLHLLYCAAEENCLAKSAAQASWPYGHRRLLRFSSEIHNIGKADFRPRLGRHSWVWHECHRHYHSMDIFTYYDLLSLNGTKVADGHKASFCLEDTECHEGVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVSPGNYILQVIINPNFEVAESDFTNNAMRCNCKYDGHRVWLHKCHLGDSFSEEAEKEFEHYPGQLNNKIS | 1.4.3.-; 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P16636}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:P33072}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072}; | collagen fibril organization [GO:0030199]; fibronectin fibril organization [GO:1905590]; inflammatory response [GO:0006954]; lung development [GO:0030324]; negative regulation of T-helper 17 cell lineage commitment [GO:2000329]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; roof of mouth development [GO:0060021]; somite development [GO:0061053]; spinal cord development [GO:0021510] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | copper ion binding [GO:0005507]; fibronectin binding [GO:0001968]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}. | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q9Z175}. Cytoplasm {ECO:0000250|UniProtKB:P58215}. Nucleus {ECO:0000250|UniProtKB:P58215}. Note=It is unclear how loxl3a is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (loxl2) also has intracellular and extracellular localization despite the presence of a signal sequence. {ECO:0000250|UniProtKB:P58215}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:P58215}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + acetamide + H2O2; Xref=Rhea:RHEA:51648, Rhea:RHEA-COMP:10731, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:27856, ChEBI:CHEBI:61930, ChEBI:CHEBI:131803; Evidence={ECO:0000250|UniProtKB:P58215}; | null | null | null | null | FUNCTION: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Can mediate oxidation of lysine residues that are acetylated. Also able to catalyze deacetylation of lysine residues (By similarity). {ECO:0000250|UniProtKB:P58215, ECO:0000250|UniProtKB:Q9Z175}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RDG9 | FYNB_DANRE | MGCVQCKDKEAAKLTDDRDTSLSQSGVGYRYGVDPTPQHYPAFSGTGTAVAAIPNYNNFHGAAVSQGMTVFGGISTSTHQGTLRTRGGTGVTLFVALYDYEARTEDDLSFRKGEKFQIINSTEGDWWDARSLTTGGTGYIPSNYVAPVDSIQAEDWYFGKLGRKDAERQLLSTGNPRGTFLIRESETTKGAFSLSIRDWDDVKGDHVKHYKIRKLDSGGYYITTRAQFETLQQLVQHYTERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEYMGKGSLLDFLKDGEGRALKLPNLVDMAAQVAGGMAYIERMNYIHRDLRSANILVGDSLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGKFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMQCPQDCPSSLHELMVQCWKKDAEERPTFEYLQAFLEDYFTATEPQYQPGDNL | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | cell differentiation [GO:0030154]; convergent extension involved in gastrulation [GO:0060027]; fin regeneration [GO:0031101]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | 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=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in CNTN1-mediated signaling (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RE08 | PTGIS_DANRE | MMWTALLLVGLSILVIVLYGRRTRRRNEPPLDKGMIPWLGHALEFGKDAAKFLTRMKEKHGDIFTVRAAGLYITVLLDSNCYDAVLSDVASLDQTSYAQVLMKRIFNMILPSHNPESEKKRAEMHFQGASLTQLSNSMQNNLRLLMTPSEMGLKTSEWKKDGLFNLCYSLLFKTGYLTVFGAENNDSAALTQIYEEFRRFDKLLPKLARTTINKEEKQIASAAREKLWKWLTPSGLDRKPREQSWLGSYVKQLQDEGIDAEMQRRAMLLQLWVTQGNAGPAAFWVMGYLLTHPEALRAVREEIQGGKHLRLEERQKNTPVFDSVLWETLRLTAAALITRDVTQDKKIRLSNGQEYHLRRGDRLCVFPFISPQMDPQIHQQPEMFQFDRFLNADRTEKKDFFKNGARVKYPSVPWGTEDNLCPGRHFAVHAIKELVFTILTRFDVELCDKNATVPLVDPSRYGFGILQPAGDLEIRYRIRF | 4.2.1.152; 5.3.99.4 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000255|PIRNR:PIRNR000047, ECO:0000255|PIRSR:PIRSR000047-1, ECO:0000269|PubMed:18032380}; | prostaglandin biosynthetic process [GO:0001516] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; prostaglandin-I synthase activity [GO:0008116] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626, ECO:0000255|PIRNR:PIRNR000047}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin I2; Xref=Rhea:RHEA:23580, ChEBI:CHEBI:57403, ChEBI:CHEBI:57405; EC=5.3.99.4; Evidence={ECO:0000269|PubMed:18032380}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23581; Evidence={ECO:0000305|PubMed:18032380}; CATALYTIC ACTIVITY: Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate + H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720, ChEBI:CHEBI:131859; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q16647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557; Evidence={ECO:0000250|UniProtKB:Q16647}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:Q16647}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:Q16647}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for prostaglandin H2 (at 23 degrees Celsius) {ECO:0000269|PubMed:18032380}; Vmax=1100 mol/min/mol enzyme (at 23 degrees Celsius) {ECO:0000269|PubMed:18032380}; | null | null | null | FUNCTION: Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2). {ECO:0000269|PubMed:18032380}.; FUNCTION: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation (PubMed:18032380). Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) (By similarity). {ECO:0000250|UniProtKB:Q16647, ECO:0000269|PubMed:18032380}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RE57 | DHC3A_DANRE | MRSPVPRFRDVERQASGLQPPQCLPSCHERQSSMWFIKDACGIVCAIITWFLVFFAEFVVLFVMLIPSKNLTYSLVNGTLFNSLAFLALASHFRAMCTDPGAVPKGNATKEYIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYICLISLHSLVMVVFHFLNCFEDDWTKCSTFSPPATVILLILLCFEGLLFLIFTSVMFGTQVHSICTDETGIEKLKREDPTWEKTQCWEGMKSAFGGPLSVTWFSPFTDLSCQKDDSSPVPMFPQGEIIEEDVIEIPLEPH | 2.3.1.-; 2.3.1.225 | null | peptidyl-L-cysteine S-palmitoylation [GO:0018230]; protein palmitoylation [GO:0018345]; protein targeting to membrane [GO:0006612] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | protein homodimerization activity [GO:0042803]; protein-cysteine S-myristoyltransferase activity [GO:0019705]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; protein-cysteine S-stearoyltransferase activity [GO:0140439]; S-acyltransferase activity [GO:0016417] | PF01529; | null | DHHC palmitoyltransferase family | PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8R173}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8R173}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000305|PubMed:28167757}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684; Evidence={ECO:0000305|PubMed:28167757}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; Evidence={ECO:0000305|PubMed:28167757}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; Evidence={ECO:0000305|PubMed:28167757}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; Evidence={ECO:0000305|PubMed:28167757}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; Evidence={ECO:0000305|PubMed:28167757}; | null | null | null | null | FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and regulates their association with membranes (Probable). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). {ECO:0000305|PubMed:28167757}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RET2 | SMYD5_DANRE | MAAPVDDMFSRCVDSAKASNCVDVRFINNVKGKGLFAKKPFKKGDTIFIERPLVSSQFLWNALYKYRACEYCLRALETAEENARRLSGLPALILPHPELCKVRPDRHQACPQCQVMYCSSECRQAAMDQYHKILCLGPSNDDPDHPVNKLQDAWRSVHFPPETSSVMILAKMVATIKQTQDKERWQRLFTNFCSRTANEEEEIVHKLLGEKFQGQLGLLRNLFTTALYEDRLSQWFTPEGFRSLFSLVGTNGQGIGTSSLSQWVHACDALELPRQQREQLDAFIDQLYKDIDKETGDFLNCEGSGLFLLQSSCNHSCVPNAEASFPENNFLLHLTALGDIGPGEEICISYLDCCQRDRSRHSRHKILRENYLFICSCQKCLSQMDDADMTSEDEEEVEGEGETEGEDMEDEMTDV | 2.1.1.372 | null | definitive hemopoiesis [GO:0060216]; methylation [GO:0032259]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of myeloid cell differentiation [GO:0045638]; primitive hemopoiesis [GO:0060215]; regulation of stem cell differentiation [GO:2000736]; regulation of stem cell division [GO:2000035] | null | histone H4K20 methyltransferase activity [GO:0042799]; metal ion binding [GO:0046872] | PF00856;PF01753; | 1.10.220.160;6.10.140.2220;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372; Evidence={ECO:0000250|UniProtKB:Q3TYX3}; | null | null | null | null | FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression (By similarity). Plays a crucial role in hematopoiesis during embryogenesis by negatively regulating expression of genes related to both primitive and definitive hematopoiesis (PubMed:27377701). {ECO:0000250|UniProtKB:Q3TYX3, ECO:0000269|PubMed:27377701}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1REV3 | KRIT1_DANRE | MGNQELEEVFVAVIRPKNTTSLNSKEYRAKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPISNNQGIIGKRVVHMRKFLLDGDSGGKEASLFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTNVSNPAYAVEKQTDGTLHMGYTALEIKSKLMSLEKADLCIQNPLYGSDLQYTNRVDKVIINPYFGLGAPDYSKIQIPKRDKWQHSMTSVTEDKERQWVDDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQHPEIDRHIEDQQKRSPLQVCEENKQNNWEETVNLLQQASNKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHLRMWSEIVTDLTALDPQRESPQLFLRRDVRLPLEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLNEENLKSIVPISKVKSKAHHWTNRILHEYKSLSTSEGVSKEMHHLQRLFLQNCWDIPTYGAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQAGLIVKLLMKLSGQIAPNDRAVSDKYAYG | null | null | angiogenesis [GO:0001525]; anterior/posterior axis specification [GO:0009948]; atrioventricular valve morphogenesis [GO:0003181]; blood vessel development [GO:0001568]; blood vessel lumenization [GO:0072554]; blood vessel morphogenesis [GO:0048514]; cell redox homeostasis [GO:0045454]; endothelial cell morphogenesis [GO:0001886]; heart contraction [GO:0060047]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell differentiation [GO:0045602]; regulation of establishment of cell polarity [GO:2000114]; vacuole organization [GO:0007033]; vasculogenesis [GO:0001570] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | null | PF13637;PF00373;PF16705; | 1.20.80.10;1.25.40.20;3.30.70.2240;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity). Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Plays a role in integrin signaling. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS. Probable microtubule-associated protein that may bind to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes (By similarity). Required for correct endothelial cell polarity and cell junction stabilization in cardiovascular development. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O00522, ECO:0000269|PubMed:21633110, ECO:0000269|PubMed:23007647}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F1RKQ4 | TKFC_PIG | MTSKKLVNSVAGCADDALAGLVACNPSLQLLQGHRVALRSDLDSLKGRVALLSGGGSGHEPAHAGFIGKGMLTGVIAGAVFTSPAVGSILAAIRAVAQAGTVGTLLIVKNYTGDRLNFGLAREQARAEGIPVEMVVVGDDSAFTVLKKAGRRGLCGTVLIHKVAGALAEAGVGLEEITNRVSVVAKAMGTLGVSLSSCSVPGSRPTFELSADEVELGLGIHGEAGVLRIKMATADEIVAHMLNHMTDSSNVSHVPVQSGSSVVLMVNNLGGLSYLELGIIADAAVRFLEGRGVKIARALVGTFMSALEMPGVSLTLLLVDEPLLKLIDAETTAAAWPNVAKVSVTGRKRSRAAPAEPPEAPDATAAGGATSKQMVRVLERVCTTLLGLEDQLNALDRAAGDGDCGTTHSRAARAIQGWLKESPPPASPAQLLSKLSLLLLEKMGGSSGALYGLFLTAAAQPLKAKTDLAAWSAAMDAGLEAMQKYGKAAPGDRTMLDSLWAAGQELQAWKSPGANLLPVLTKALLENAEAAAEATKNMEAGAGRASYISSARLDQPDPGAVAAAAILRAILEVLQSQGA | 2.7.1.28; 2.7.1.29; 4.6.1.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Manganese or cobalt are requested for FAD-AMP lyase activity. {ECO:0000250}; | glycerol catabolic process [GO:0019563]; negative regulation of MDA-5 signaling pathway [GO:0039534]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; FAD-AMP lyase (cyclizing) activity [GO:0034012]; glycerone kinase activity [GO:0004371]; metal ion binding [GO:0046872]; triokinase activity [GO:0050354] | PF02733;PF02734; | 1.25.40.340; | Dihydroxyacetone kinase (DAK) family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216; EC=2.7.1.29; Evidence={ECO:0000269|PubMed:7831203}; CATALYTIC ACTIVITY: Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216; EC=2.7.1.28; Evidence={ECO:0000269|PubMed:7831203}; CATALYTIC ACTIVITY: Reaction=FAD = AMP + H(+) + riboflavin cyclic-4',5'-phosphate; Xref=Rhea:RHEA:13729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:76202, ChEBI:CHEBI:456215; EC=4.6.1.15; Evidence={ECO:0000269|PubMed:7831203}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for D-glyceraldehyde {ECO:0000269|PubMed:7831203}; KM=5 uM for dihydroxyacetone {ECO:0000269|PubMed:7831203}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:7831203}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:7831203}; | FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate (PubMed:7831203). Represses IFIH1-mediated cellular antiviral response (By similarity). {ECO:0000250|UniProtKB:Q3LXA3, ECO:0000250|UniProtKB:Q4KLZ6, ECO:0000269|PubMed:7831203}. | Sus scrofa (Pig) |
F1RQM2 | AGM1_PIG | MDLDAITKHSASHAKPDGLILQYGTAGFRTKADRLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEDDNGVKLVDPLGEMLAPSWEEHATHLANAEEQDLARALVAISEEAAVNLHQDAFVVIGRDTRPSSEKLSESVIDGVTVLGGQFHDYGLLTTPQLHYMVCCRNTGGQYGEATIDGYYHKLSTAFVELSKQASCSGDDHRTLKVDCANGIGALKLKEMKHYLPQGLSVQLFNDGTKGKLNHFCGADFVKSHQKPPEGIEMKANERCCSFDGDADRIIYYYCDVDGHFHLIDGDKIATLISSFLKELLLEIGESLTVGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDLGVYFEANGHGTVLFSKAAEAKIRQLAKELEDKKGKAAKMLENVIDLFNQATGDAISDMLVIEAILALKGLTIQQWDALYTDLPNRQLKVKVADRQVISTTDAERQVVKPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQENADSLAYEVSLAVFQQAGGVGERPQPGF | 5.4.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:4996162}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:4996162}; | carbohydrate metabolic process [GO:0005975]; hemopoiesis [GO:0030097]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | null | magnesium ion binding [GO:0000287]; phosphoacetylglucosamine mutase activity [GO:0004610] | PF21405;PF21404;PF02878;PF00408; | 3.40.120.10;3.30.310.50; | Phosphohexose mutase family | null | null | CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513, ChEBI:CHEBI:57776; EC=5.4.2.3; Evidence={ECO:0000269|PubMed:468829, ECO:0000269|PubMed:4996162}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.29 mM for D-glucosamine 1-phosphate {ECO:0000269|PubMed:4996162}; KM=0.39 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:4996162}; KM=0.018 mM for fructose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; KM=0.016 mM for galactose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; KM=0.005 mM for mannose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; KM=0.002 mM for glucose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; Vmax=39.4 umol/min/mg enzyme for D-glucosamine 1-phosphate {ECO:0000269|PubMed:4996162}; Vmax=28.9 umol/min/mg enzyme for D-glucose 1-phosphate {ECO:0000269|PubMed:4996162}; Vmax=10.1 umol/min/mg enzyme for fructose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; Vmax=14.3 umol/min/mg enzyme for galactose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; Vmax=26.7 umol/min/mg enzyme for mannose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; Vmax=34.4 umol/min/mg enzyme for glucose 1,6-diphosphate {ECO:0000269|PubMed:4996162}; | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2. {ECO:0000305|PubMed:468829}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:4996162}; | null | FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation. {ECO:0000269|PubMed:468829, ECO:0000269|PubMed:4996162}. | Sus scrofa (Pig) |
F1RRV3 | THYG_PIG | MALALWVFALLGSACLVSANIFEYQVDAQPLRPCELQRERAFLKRADYVPQCAEDGSFQTVQCKKDGGSCWCVDADGREVPGSRQPGRPVACLSFCQLQKQQILLSSYINSTATSYLPQCQDSGAYAPVQCDVRREQCWCVDAEGMEVYGTRRLGRPARCPGSCEIRNRRLLHGVGDKSPPQCSADGTFLPVQCKFVNTTDMMFFDLVHSYNRFPDAFVTFSSFRSRFPEVSGYCHCADSQGRELAGTGLELLLDEIYDTVFAGLDLASSFTETTLYRILQRRFLAVQLVTSGRFRCPTKCEVERFAATSFGHPYVPSCGRDGEYQAGQCQQEGLCWCVDAQGQEIPGTRRPSEPLSCAEGQSCPSERRRALSRLHLGPSGYSGQRGSFLAAERGPVSQTVPSFAASCPLPLKELFVESGILQPVVQGQKKEVTAATESLLKEGLRGIFPSRELARLALQFTANPKRLQQNLFGGRFLANVGQFNLSGALGTRGTFNFSHFFQQLGLPGFQKRQALADPAKSLSVGLDSNPATEAPEALKMGVAMNKTVVGSFGFEVNLQENRNALTFLSSLLELPEFLLFLQHAISVPEDIARDLGDVMEMALSSQGCEQTPGSLFVPSCTAEGSYEDVQCFAGECWCVDARGRELAGSRARGGRPRCPTACEKQRERMQSLLGRQPAGSSVFVPSCTREGHFLPVQCFSSDCYCVDADGQPIPGTRTAPGEPKQCPTPCQLQAEQAFLGTVRGLISNPSEPPVLSSIYIPQCSASGQWRRVQCDGPPEQAFEWYERWGAQSRSGQELTPAELLMKIMSYREAASGSFRLFIQNLYEAGQQGIFPGLARYSSLQDVPLAVLEGNLTQATGNILLEPYLFWQILNGQLPRYPGPYSDFSAPLAHLDLRSCWCVDEAGRKLEGTQTEPSKVPACPGSCEEVKLRVLQFIKEAEEIVMVSNSSQFPLGESFLAAKGIRLTDEELALPPLSPSRETFLEKFLSGSDYAIRLAAQSTFSFYQRRRVALSDAPRTSGPLQPYPYVPQCDALGSWEPVQCHAATGHCWCVDGEGAYLPASLAARSPQVLQCPTPCETSRVRGLLSAWKQAGSQVRPSPKDLFIPACTETGEFARLQASEASTWCVDPASGEAMPPGTNSSAPCPGLCEVLQRGVPSRRASPGTTPACRAEDGGFAPVQCDPAQGSCWCVLGSGEEVPGTRVAGSQPACERPQLWQTIQTRGQFQLQLPPGKVCSADYAGLLPTFQVVILDELTARGFCRIQVTTARTPVSIPVCDDSTVRVGCLSLDRLGVNVTWTLRLEDAPPASLPDLRDIEEALAGKDLVGRFADLIQSGTFQLHLDSRTFPADPSIHFLQGNSLGTSPRTRFGCVEGSRQVPATSNTSQDPLGCVRCPEGSYFQEEQCIPCPAGFYQEQTGSLACAPCPAGTTTTSVGAFSQTHCVTACQRDEAGLQCDQDGQYRASQRDRASGKAFCVDSEGRRLPWSETQAPLVDAQCLMMRKFEKLPESKVIFTADVAVLGSIVPDSESSLMQCLADCARDEACSFLTVSLEGSEGSCDFYAWTSDNIACTSSGQEEDALGTSKATSLGSLTCQVKVRPGDGVAPAVYLKKGQEFATIGQKRFEQTGFQNALSGLYSPVVFSASGASLTEAHLFCLLACDRDSCCDGFILTQVQGGPIICGLLSSPDVLLCHVRDWRDPSEAQADATCPGVTYDQDSRQGTLRLGGQEFKSLTPREGARDTFTSFQQVYLWKDSDMGSRSESMGCRRDMQPRPESPEETDLTAELFSPVDLNQVIVSENRSLPSQQHRLFKHLFSLQQAHLWCLSRCVQEPSFCQLAEITDSSPLYLTCTLYPEAQVCDDVMEASPRGCRRILPRRPNALFQRRVVLQDRVKNFYTRLPFQKLTGLSIRHKVPMADKAISSGFFECERLCDVDPCCTGFGFLNVSQLKGGEVTCLTLNSLGLQTCSEENGGSWRLLACGSPDTEVRTYPFGWYQKPAVQNDAPSFCPSAALPPVPEKVALDSWQPLPPSSVVVDPSIRNFDVAHISTAAVGDFSAARERCLLECSRHQACLVTTLQTRPGAVRCMFYADTQSCTHSLQAQNCQLLLREEATHIYRKPDIPLPGLGSSAPTVTIATHGQLLGTSQAIQLGASWKQVDQFLGVPYAAPPLAESRFRAPEPLNWTGTWDATKPRASCWQPGIRPATAPGVSEDCLYLSVFVPQSLTPNSSVLVFFHNGAEGPLAMAVDGSFLAAVGNLIVVTASYRTGVFGFLSSGSSEVSGNWGLLDQVAALTWVQTHIGVFGGDPRRVALAADRGGADVAGIHLLTSRATNSRLFRRAVLMGGSVLSPAAVIRPDRAQQQAAALAKEVGCPPRPSQKWYPASAGACQPPNDAQMQLLAVSGPFHYWGPVVDGQLLREAPARALQRPPRAKLDLLIGSSQDDGLIDRAKAVKRFEESQGRTSSKTAFYQALQNSLGGEAGDPGVQAAATWYYSLEHDTDDYASFSRALEAATRDYFIICPVIDMASHWARTARGNVFMYHAPESYSHGSLELLADVRYAFGLPFYPAYEGQFTQEEKSLSLKIMQYFSNFVRSGNPNYPHEFSRKAPEFAAPWPDFVPGDGAESYKELSVLLPNRQGLKKADCSFWSKYILSLKASADEAEDGPLAESEEEDRPGLTEDLLGLPELASKSYSK | null | null | hormone biosynthetic process [GO:0042446]; thyroid hormone generation [GO:0006590] | extracellular space [GO:0005615] | hormone activity [GO:0005179]; identical protein binding [GO:0042802] | PF00135;PF07699;PF00086; | 3.40.50.1820;4.10.800.10;2.10.50.10; | Type-B carboxylesterase/lipase family | PTM: Iodinated on tyrosine residues by TPO (PubMed:12325367). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2500 is coupled to donor Tyr-2467, acceptor Tyr-2690 in monomer 1 is coupled to donor Tyr-2690 in monomer 2 and acceptor Tyr-1241 in monomer 1 is coupled to donor Tyr-108 in monomer 2 (By similarity). {ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:12325367}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250|UniProtKB:P01266}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones (By similarity). In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL (By similarity). Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4 (PubMed:11082042). Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones (By similarity). {ECO:0000250|UniProtKB:O08710, ECO:0000269|PubMed:11082042}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12387814}. Note=Secreted into the follicular lumina of the thyroid (PubMed:12387814). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (By similarity). {ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:12387814}. | null | null | null | null | null | FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:7021557). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (PubMed:7021557). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (By similarity). One dimer produces 7 thyroid hormone molecules (By similarity). {ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:7021557}. | Sus scrofa (Pig) |
F1RRW5 | ACE_PIG | MGAASGCRWPWPPLLPLLLMLLLPPPPLPVALALDSALQPGNFTADEAGAEDFAQSFNSSSEQVLFQSTAASWAHDTNITEENARRQEEAALISQEFSEVWGQKAKALYDPIWQNFTSRTLRRIIGVVRTLGSANLSPAKRQQYNSLLSNMTRIYSTAKVCFPNKTATCWSLDPELTNILATSRSYTLLLYAWEGWHNAAGIPLKPLYQDFTALSNEAYKQDGFSDTGAYWRSLYDSPTFTEDLERLYHQLEPLYLNLHAYVRRALHRQYGDRFINLRGPIPAHLLGNMWAQSWNNIYDMVVPFPGKPSLDVTSAMVQKGWNVTHMFRVAEEFFTSLGLLPMPPEFWAESMLEKPSDGREVVCHASAWDFYNRKDFRIKQCTQVTMDQLSTVHHEMGHVQYYLQYKDQHVSLRRGANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTSDWESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPLYNYDWWYLRTKYQGVCPPVVRNETHFDAGAKYHVPNVTPYIRYFVSFILQFQFHQALCKEAGHQGPLHQCDIYQSTRAGAKLRAVLQAGSSRPWQEVLKDMVGSGALDAQPLLDYFQPVTQWLEEQNQRSGDILGWPEYQWRPPMPDNYPEGIDLVSDEAEASKFVEEYDRRSQVVLNEYAEANWDYNTNITAEGSKRVLEKSTQMANHTVKYGIWARKFDVANIQNFTLKRMIKKIQDLERAALPFKELEEYNQILLDMETAYSVASVCHANSTCLQLEPDLTNLMATSRSYEELLWAWKGWRDKVGRAILPYFPKYVELTNKAARLNGYEDGGDAWRAAYEMPFLEQELEQLFQELQPLYLNLHAYVRRALHHHYGPEHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSASKMDASEAMINQGWTPQRMFKEADNFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFFNGKDFRIKQCTTVNMEDLVVAHHEMGHIQYFMQYKDLPVTFREGANPGFHEAIGDVLALSVSTPKHLRSINLLKSEDDGYEEDINFLMKMALDKVAFVPFSYLVDQWRWRVFDRSITKENYNQEWWSLRLKYQGLCPPVARSQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHKGPLHKCDIYQSKEAGRRLADAMKLGLSKPWPEAMQLITGQPNVSASAMMTYFKPLLDWLVTENGRHGEKLGWPQYNWTPNSARLEGSFAGTGRVNFLGLNLEEQQARVGQWVLLFLGVTLLVATMGLTQRLFSIRHQILRRTHRGPQFGSEVELRHS | 3.4.15.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P12821}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Binds 3 chloride ions per subunit. {ECO:0000250|UniProtKB:P12821}; | amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; angiotensin-activated signaling pathway [GO:0038166]; arachidonic acid secretion [GO:0050482]; bradykinin catabolic process [GO:0010815]; cell proliferation in bone marrow [GO:0071838]; heart contraction [GO:0060047]; hormone catabolic process [GO:0042447]; hormone metabolic process [GO:0042445]; kidney development [GO:0001822]; male gonad development [GO:0008584]; negative regulation of gap junction assembly [GO:1903597]; negative regulation of gene expression [GO:0010629]; neutrophil mediated immunity [GO:0002446]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; positive regulation of systemic arterial blood pressure [GO:0003084]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of angiotensin metabolic process [GO:0060177]; regulation of blood pressure [GO:0008217]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of hematopoietic stem cell proliferation [GO:1902033]; regulation of synaptic plasticity [GO:0048167]; regulation of systemic arterial blood pressure by renin-angiotensin [GO:0003081]; spermatogenesis [GO:0007283]; substance P catabolic process [GO:0010814] | endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | bradykinin receptor binding [GO:0031711]; calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; chloride ion binding [GO:0031404]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; mitogen-activated protein kinase binding [GO:0051019]; mitogen-activated protein kinase kinase binding [GO:0031434]; peptidase activity [GO:0008233]; peptidyl-dipeptidase activity [GO:0008241]; tripeptidyl-peptidase activity [GO:0008240]; zinc ion binding [GO:0008270] | PF01401; | 1.10.1370.30; | Peptidase M2 family | PTM: [Angiotensin-converting enzyme, soluble form]: Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region. Cleavage can take place at different sites of the juxtamembrane stalk region. {ECO:0000250|UniProtKB:P12821}.; PTM: Phosphorylated by CK2 on Ser-1302; which allows membrane retention (By similarity). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (By similarity). {ECO:0000250|UniProtKB:P12821, ECO:0000250|UniProtKB:P12822}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12821}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.; SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble form]: Secreted {ECO:0000250|UniProtKB:P12821}. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine; Xref=Rhea:RHEA:63560, ChEBI:CHEBI:15377, ChEBI:CHEBI:58506, ChEBI:CHEBI:147350, ChEBI:CHEBI:147392; EC=3.4.15.1; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63561; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg; Xref=Rhea:RHEA:71451, ChEBI:CHEBI:15377, ChEBI:CHEBI:132988, ChEBI:CHEBI:133147, ChEBI:CHEBI:147352; Evidence={ECO:0000305|PubMed:4962200}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452; Evidence={ECO:0000305|PubMed:4962200}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9); Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190693, ChEBI:CHEBI:190700; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8); Xref=Rhea:RHEA:71463, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190694, ChEBI:CHEBI:190699; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71464; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-6); Xref=Rhea:RHEA:71471, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190696, ChEBI:CHEBI:190697; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71472; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11); Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362, ChEBI:CHEBI:190704, ChEBI:CHEBI:190706; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-aspartate; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377, ChEBI:CHEBI:190701, ChEBI:CHEBI:190702, ChEBI:CHEBI:190703; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71456; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-tyrosylglycylglycine; Xref=Rhea:RHEA:71483, ChEBI:CHEBI:15377, ChEBI:CHEBI:189868, ChEBI:CHEBI:190708, ChEBI:CHEBI:190709; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71484; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-tyrosylglycylglycine; Xref=Rhea:RHEA:71487, ChEBI:CHEBI:15377, ChEBI:CHEBI:190689, ChEBI:CHEBI:190708, ChEBI:CHEBI:190710; Evidence={ECO:0000250|UniProtKB:P12821}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71488; Evidence={ECO:0000250|UniProtKB:P12821}; CATALYTIC ACTIVITY: Reaction=H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine + Met-enkephalin; Xref=Rhea:RHEA:70675, ChEBI:CHEBI:15377, ChEBI:CHEBI:189868, ChEBI:CHEBI:189869, ChEBI:CHEBI:189870; Evidence={ECO:0000250|UniProtKB:P09470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70676; Evidence={ECO:0000250|UniProtKB:P09470}; | null | null | null | null | FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (By similarity). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (By similarity). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (By similarity). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:4962200). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (By similarity). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (By similarity). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (By similarity). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (By similarity). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (By similarity). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (By similarity). {ECO:0000250|UniProtKB:P09470, ECO:0000250|UniProtKB:P12821, ECO:0000269|PubMed:4962200}.; FUNCTION: [Angiotensin-converting enzyme, soluble form]: Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region. {ECO:0000250|UniProtKB:P12821}. | Sus scrofa (Pig) |
F1RT67 | IMPA3_PIG | MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGMGGEPGGGAAGPGAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGADDKMTSGDVLSNRKMFYLLKTAFPNVQINTEEHVDATDQEVILWDRKIPEDILKEIATPQEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDGGSNVKARTSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASVRVDHQALVRKLPDLEKTGHK | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; skeletal system development [GO:0001501] | endomembrane system [GO:0012505]; trans-Golgi network membrane [GO:0032588] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3',5'-nucleotide bisphosphate phosphatase activity [GO:0097657]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250|UniProtKB:Q9NX62}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}. Note=The catalytic core is predicted to reside within the Golgi lumen. {ECO:0000250|UniProtKB:Q9NX62}. | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q80V26}; | null | PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}. | null | null | FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4. {ECO:0000250|UniProtKB:Q80V26}. | Sus scrofa (Pig) |
F1RWC3 | CUBN_PIG | MVNNMSLLFLWSLVIFLTFAESYGEAGGPELQRHKRNTELQQPRMAAERGNLVFFTGLAQNIEFRTGSQGKIKLNDEDVGECLRQIQKNKFDIMNLKRGIIGLPQNVSSQIHQLESKLVDLERRFQSLQLTVDGKVCSSNPCQNGATCLNLHDSFFCICPSQWKGPLCSDDVNECEIYSGTPLGCQNGATCINTPGSYSCLCSPETHGPQCASKYDDCEGGSEMRCVHGICEDLTRVQAGEPRFRCICHAGWTSPSNSTACTLDRDECSSWPAPCSALVPCFNTLGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSYYCPSCPPGYQGDGRMCTLIDLCSVNNGGCHPHAACSLILGSLPLCTCLPGYTGNGYGLHGCVPLSNVCLTRPCLHGQCMETASGYVCNCDSGWAGMNCTENINECLSNPCLNGGTCVDGINAFSCECTRFWTGSLCHLPQQVCGGTMSDVSGSFSYMSPDVGYVHDVDCFWVLRTEEGKVLRITFTFFQLESVDNCPHEFLQIHDGDSPAAFPLGRFCGSSPPHELLSSDNALYFHFFSEHLRNERGFTIRWETRQPECGGVLTGTYGSLKSPGYPGKYPPGRDCVWKVIASPDLLITFTFGTLSLEHHDDCRKDYLEIRDGPLHQDPVLGKFCTSLSVPPLQTTGPFARIHFHSDNQINDQGFHITYLTTPSDLHCGGNFTDPEGLLSPDLSGPFTHSRQCIYVITQPLGEQIQVNFTHVELEGQSGCSQSYIEVRDDQTLLGKVCGNETPSHIKSITNSIWIRLKIDASVVRASFGAAYQVACGGELTGEGVIRSPFYPNVYPGERICRWTIHQPQSQVVLLNFTAFEMGSSAHCDTDYIEIGSSPVLGSPENKKYCGTDIPSFITSVYNSLHVVFVKSSSTENHGFMAKFSTEALACGEILTESSGIIQSPGHPNIYPHGVNCTWHILVQPGHLIHLEIRQFHLEFHYNCTRDYLEIYDTVSDTSLGRYCGKSIPPSLTSNTNSLKLIFVADADLAYEGFVINYEATDASAGNTTALLYRRIWIFTSPNFPSNYPNNMECIYRITVETSQQIALHFTDFSLEEPIGGACAADYVEITNGGYASSPPLGKYCGSNPPPRIISHSNKLWLKFKSDFFGSGPGFSAYWDGSLTGCGGNLTTPTGTFTSPNYPMPYYHSSECFWWLKSSHGSPFELEFNDFHLEYHPNCTLDYLDVYDGLSTSSHLLTRLCGNEKPPLIRSTGDSMSLKLRTDEGQQGGGFLVKYQQTCDNVVIVNRTYGILESIHYPKPYSVNQRCNWTIQATAGNTVNYTFLAFELESHANCSTDYLELYDGPQRMGRFCGAVIPPSGSTTGSRLQVLFHTDGVGQGERGFQMQWLVHGCGGELSGDTGTFSSPGYPVGYPANKECIWYIHSSPGSSIQLTIHDFDVEYHATCNFDVLEIYGGPDFHSPRIAQLCVQRSAENPMQVSSTGNELALRFKTDSSVNGRGFNVSWRAVPGGCGGIFQAPSGEIHSPNYPSPYRSNTECTWLIQVEKNHRVLLNFTDFDLEPQDSCIMAFDGLSSATARLVGVCGRQQLSNPIISTGSSLFVRFQSGPSRQSRGFRAQFRQACGGHILTDSFDTISSPRFPASYPNNQNCSWIIQAQPPFNHITLSFSHFGLESSSTCTRDFVEILDGSHSDAPLRGRYCGSSMPHPITSFGNALMLRFVSDSSVNFDGFHATYVASTSACGGIFHMAEGIFNSPGYPEVYPSNVECVWNIASSPGNQLQLSFITFQLEDSRDCSRDFVEIREGNATGRLVGRYCGNVLPLNYSSIIGHDLWIKFVSDGSGSGVGFQAAFNNIFGNDHIVGTHGKVASPLWPRNYPHNSNYQWIVNVNESQVIHGRILEMDVEGTFNCYYDKLRIYDGADIHSRLIGTYCGAQTESFSSTGSSLTFQFSSDSSISGRGFLLEWFAMDASDGPLPTIATGACGGFLRTGDAPVFLYSPGWPGSYSNGADCMWLIQAPDSTVELNILSLDIESHRTCDYDKLVIRDGDNNMAQELAVLCGREIPGPIRSTGEYMTIRFTSDFSVTRAGFNASFHKSCGGYLHADRGIITSPGYPEAYTSNLNCSWHVQVQQGLSIAVHFEQPFQVSNRDAFCNQGDYLVLKNGPDIYSPPLGPHGGNGRFCGSRPSSTLFTSDNELFVQFISDNSNEGQGFKITYEAKSLACGGNIYIHDADSSGYVASPNHPDNYPQHADCIWVIAAPSGRPIRLEFEDQFSIEITPNCTSSYLELRDGADSNAPVLAKFCGTSLPPSQLSSGEVMYLRFRSDNSPTHAGFKAKYSIAQCGGTVTGQSGVIESSGYPALPYANNLFCEWRLQGLSGHYLTIHFEDFNLQNSSGCERDFVEIWENHTSGNLLGRYCGNTVPDSIDTSGNVALVRFVTDGFLTASGFRLRFDSSMEGCGGDLQGPTGTFTAPNYLNPNPHGWMCEWRITVQEGRRVTLTLNDLRLEAHPFCNSEHVAVFNGIRSNSPQLEKRCSSVNGSNEIRSSGNTMKVVYFTDGSRPYGGFTASYTSSEDAVCGGSLTNSPEGNFTSPGYDGTRNYSRNLNCEWTLSNSNQGNSSIYIDFEDFYLESHQDCQFDVLEFRVDNADGLLIWRLCGSSKPTMPLVIPYPQVWIHFVTNERVEHIGFRARYSFTDCGGIQIGDHGVISSPNYPASYDSLTHCSWLLEAPQGHTITLTFSDFDIEAHASCAWDSVTVRNGGSPGSPIIGHYCGSSNPRTIQSGSNQLVVIFNTDSSVQNGGFYATWNTETSGCGGILHSDTGTIRSPHWPQNFPENSRCSWTVITHPSKHLEISFDNNFLIPSGDSQCLNSFVKVWAGTQEADKDLLATSCGNVSPGRIITPRNAFTAVFQSQETPAQGFSASFLSRCGRNFTNPSGYIVSPNYPKQYDNNMNCTYIIEASPLSVILLKVVSFHLEARSTVSGSCDSDGVHIIRGHSLSSTPLVTLCGDEALSPVTISGPVLLNFYSNAHTTDFGFKFSYRITPCGGTFNLSFGIIKSPSYSYSNYPNDMHCLYTVTVRDDRVIQLKFNDFDLVPSTFCSQDYLEIYDGSNISDPLLGKFCGSTLPPNVKSSNNTMFLVFKTDSVHTARGWKISFRETLGPQQGCGGYLTGSTHTFGSPDSDSNGRYDKNLNCIWFITAPVNKLIKLTFSTFALEAATSLQRCIYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFVSDSSLEREGFNATYTLLDMPCGGTYNATWTSQSIWSPSSSDPDVPLTTCTWVIEAPLHQQVEITVWTFQLHSQDCDQNYLEFRDPPERNGNPGIRFCGRNASAVPTFYSSLSTAIIIFKSEVFNTDSRVGFTYRIAGCSREYQKAFGRLRSPGWPAGYASDADCAVVLRAPQNHTISLFFHAFGLEDSGGCTRDFLEVRNGSESTSPLLGKYCGTLLPNPIFSQSRDLYLRFKSDSATSGRGYEIIWTSSPSGCGGTLYGDSGLVTSPGYPGTYPNHTHCEWVIIAPGGRPVTVSFSFISIDDPGECVQNYLMLYDGPDANSPSSGPYCGADTDVAPFAASSHRVFIRFHAEAAARPSALRLTWAS | null | null | cholesterol metabolic process [GO:0008203]; protein transport [GO:0015031] | apical plasma membrane [GO:0016324]; clathrin-coated pit [GO:0005905]; endosome [GO:0005768]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765] | calcium ion binding [GO:0005509]; cobalamin binding [GO:0031419]; serine-type endopeptidase activity [GO:0004252] | PF00431;PF00008;PF12947;PF07645;PF12661; | 2.10.25.10;2.60.120.290; | null | PTM: The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide. {ECO:0000250|UniProtKB:O60494}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60494}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9JLB4}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60494}. Cell membrane {ECO:0000250|UniProtKB:O60494}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60494}. Membrane, coated pit {ECO:0000250|UniProtKB:O60494}. Endosome {ECO:0000250|UniProtKB:O60494}. Lysosome membrane {ECO:0000250|UniProtKB:O70244}; Peripheral membrane protein {ECO:0000305}. Note=Lacks a transmembrane domain and depends on interaction with AMN for location at the plasma membrane (By similarity). Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells (By similarity). {ECO:0000250|UniProtKB:O60494, ECO:0000250|UniProtKB:O70244}. | null | null | null | null | null | FUNCTION: Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. {ECO:0000250|UniProtKB:O60494}. | Sus scrofa (Pig) |
F1S5L4 | GPAT1_PIG | MDESALTLGTIDVSYLPNSSEYSIGRCKHASEEWGECGFRPPVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDRFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATEMNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGQKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNTIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSDAVDEGTDMSINESRNAADESFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCITITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGSGGPASPSLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILTVAEQDDQEDISPSLAEQHWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFIHNFSGPVPEPEYLQKLHKYLINRTERRVAVYAESATYCLVKNAVKMFKDIGVFKETKQKKVSVLELSSTFLPQCNRQKLLEYILSFVVL | 2.3.1.15 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; diacylglycerol biosynthetic process [GO:0006651]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid biosynthetic process [GO:0008654]; triglyceride biosynthetic process [GO:0019432] | mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886] | glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P97564}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97564}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57597, ChEBI:CHEBI:74547; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597, ChEBI:CHEBI:74544; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597, ChEBI:CHEBI:74565; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; CATALYTIC ACTIVITY: Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64716, ChEBI:CHEBI:64840; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204; Evidence={ECO:0000250|UniProtKB:Q9HCL2}; | null | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000250|UniProtKB:Q9HCL2}. | null | null | FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids. {ECO:0000250|UniProtKB:Q9HCL2}. | Sus scrofa (Pig) |
F1SPM8 | AAK1_PIG | MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTESEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSFFSFKLLKKECPVPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRAMVQPPPQVAGSSNQPGLLASVPQPKTQAPPSQPLPQSQAKQPQAPPAPQQPPSAPAQGLPAQAQATPQHQQQLFLKQQPQPPQPQPQAQAPPVKSLKFYPFYPMCKGRQTVSSQFQAVHPAAQQPAIAQFPAVSQGSSQQQLIQNFYQQQQQQQQQQQLATTLHQQQLLTQQAALQQKTTVAAIQPPQAQPATASQPPPAQEPAQIQAPVRQQPKVQTTPPPAIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQPTQGDAFAASSFAAGTAEKRKGGQAVDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVASNRTDSLTGEDALIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL | 2.7.11.1 | null | endocytosis [GO:0006897]; positive regulation of Notch signaling pathway [GO:0045747]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of clathrin-dependent endocytosis [GO:2000369]; regulation of protein localization [GO:0032880] | cell leading edge [GO:0031252]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; terminal bouton [GO:0043195] | AP-2 adaptor complex binding [GO:0035612]; ATP binding [GO:0005524]; Notch binding [GO:0005112]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q2M2I8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:F1MH24}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P0C1X8}. Presynapse {ECO:0000250|UniProtKB:P0C1X8}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells. {ECO:0000250|UniProtKB:P0C1X8}. | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q2M2I8}; | null | null | null | null | FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis (PubMed:11877457). Preferentially, may phosphorylate substrates on threonine residues (By similarity). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (By similarity). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (By similarity). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity). {ECO:0000250|UniProtKB:Q2M2I8, ECO:0000269|PubMed:11877457}. | Sus scrofa (Pig) |
F1SVH1 | RGYRB_METKA | MVLKRAADMVPKGFRDLVEPILDDCADLEELADRVVETEMEPDEVRRRDVGNTDSNEPVAIFGSSCVLCGGDCSSVRLTSRIGICERCLPVDTETLREVLKEARKRHGYVGEALLMFILVERYSPDRVEEFFRRYVWPELFTEIVDRVFDRATGFRLYSAQRVWTRRLVKGCSFSILAPTGTGKTSWGSLVAAVFGHAGRRVYYLVPTTTLVRQVENRIKGFARDAELDVDVVAYHAAMPTQAKREALERISSGDFDVLITTAQFLVHRVEDLEKLNFDLILVDDVDAIIRGTGRNVDRVLRVAGLEQEEIDSAYRLATLRRRYYSLRDWLRSLEDRGDKRAERVREELREVEREIEELEELLKRVKKERDLARIVFMSATGAAAPSRRLAVVRELFDFEVGAGGEGLRNIQDIAVISEPSPEAVERIVRKAGVKGGLIFVPQRLPGEKKAREIVEELAEHLRSSGIEARAIHAGTPAEEREEAIDGFSEGDVDVLVAVASPYGVIVRGLDLPQAARYAVFYGVPRQRIRLTPREEDLKDPTYVASALSNLARLLDDRRARSRLEGVAGRLWRIIRRGTWIRERLEEAVEPLSLNTLMKLAKRDPEDIAEQLDVDRWLARHVQTLAEGVRELTRLLGDPDRVKALAEEATTVAVYEEGEEAYLEVPDLRTYIQASGRVSRLFAGGVTFGLSFVLCPEDERELRTLNGLIRRMSYTYGSEFEWRSYPKSLDMKEIGLELKEISDEELEELVRKVDEDRERVRKVLAGELKPEETGRLARSALMIVESPNKARMIASLFSQRPSRRRLNGGVAYEAAADGLHLTVVATQGHVADLVEEPGVHGVLRIDERWVPMYDVLGRCSECGEQVVGSEECPNCGGEVELKTPLLESIRELASEADVILIGTDPDTEGEKIGWDVFNYLGWTTAQVYRTEFHEVTRRGISEALKEESWKNVDAGRVSAQILRRVADRWIGFSLSQDLWDVFKHLEIKLGELPSGSRIEVRLDIPSGVEVVDFRRTFDEDSSVRSRSVRLRREGDEYVVRTRISRGGDVTYTATLLDPNRKLGDRNGVRPELVRVRASVNGEPVDPNVKLEPMTWLSAGRVQTPVLGWIIDRAREYRETEFYACRAEVPADDVTIRALIEELKVPRALTEKLDEATIRVLSKIAEEGPDAEFSEEEVGRFTETELFERKDGRYRLSEEGRKVLESEGVIGLMLHLAGVSGR | 5.6.2.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O51934}; Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:O51934}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9153263}; | DNA topological change [GO:0006265] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; reverse gyrase activity [GO:0160097] | PF00270;PF00271;PF01751; | 2.60.510.20;3.30.56.120;3.40.50.140;3.40.50.300;2.20.20.30;1.10.460.10; | Type IA topoisomerase family; DEAD box helicase family, DDVD subfamily | PTM: The N-terminus is partially blocked (PubMed:8552584). {ECO:0000269|PubMed:8552584}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q97ZZ8}. | 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; Evidence={ECO:0000269|PubMed:8157633, ECO:0000269|PubMed:9153263}; | null | null | null | null | FUNCTION: Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling (PubMed:8157633). Increases the linking number in steps of +1 (PubMed:8157633). Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner (PubMed:8157633). Hydrolyzes ATP only in the presence of DNA (PubMed:8157633). The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues (PubMed:8157633). There are about 1000 heterodimers per cell (PubMed:8157633). May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication (By similarity). {ECO:0000250|UniProtKB:O51934, ECO:0000250|UniProtKB:Q08582, ECO:0000269|PubMed:8157633}.; FUNCTION: This subunit expressed in E.coli only has DNA-dependent ATPase activity at 80 degrees Celsius (PubMed:9153263). Reverse gyrase activity is reconstituted after incubation at 80 degrees Celsius for 5 minutes, positive supercoiling requires ATP and Mg(2+) (PubMed:9153263). In the presence of ATP it binds and nicks substrate but does not make closed product (PubMed:9153263). {ECO:0000269|PubMed:9153263}. | Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) |
F1SVH7 | FPOB_METMA | MGEVKETKTNNSKENPEEEVPGVITTTTSAIHNFLKKTKAQDIINWGRKNSLWFMTQPMGCCGVEMIATGCAHYDTDRFGIIPRNSPRHADVMIISGYVTKKYLPALKRLWDQMPAPKWVIAMGDCAISGGPFYESYSTVQNIDEIFPIDVYIPGCPPRPEALIQGFVELQEKIKARKDRGTEY | 1.5.98.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; | aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; methanogenesis [GO:0015948]; methanol metabolic process [GO:0015945]; mitochondrial respiratory chain complex I assembly [GO:0032981] | plasma membrane [GO:0005886] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; Methanosarcina-phenazine hydrogenase activity [GO:0051911]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038]; reduced coenzyme F420 dehydrogenase activity [GO:0043738] | PF01058; | 3.40.50.12280; | Complex I 20 kDa subunit family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=methanophenazine + reduced coenzyme F420-(gamma-L-Glu)(n) = dihydromethanophenazine + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:54752, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.3; Evidence={ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for F(420)H(2) (at 37 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; Vmax=17 umol/min/mg enzyme (at 37 degrees Celsius and pH 7) {ECO:0000269|Ref.1}; Note=Measured for the whole complex.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 39 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone. {ECO:0000269|PubMed:10751389, ECO:0000269|Ref.1}. | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) |
F1T160 | BBLA_TOBAC | MFPLIILISFSLASLSETATGAVTNLSACLINHNVHNFSIYPTSRNYFNLLHFSLQNLRFAAPFMPKPTFIILPSSKEELVSTIFCCRKASYEIRVRCGGHSYEGTSYVSFDASPFVIVDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIVYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQILEKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNTTPIEIFPQFNALYLGPKTEVLSISNETFPELGVKNDECKEMTWVESALFFSELADVNGNSTGDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKISDQAIAFPHRKGNLFAIQYLAQWNEEDDYMSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMVDDYLLRNASSSSPSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE | 1.1.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:21343426}; | alkaloid biosynthetic process [GO:0009821]; nicotine biosynthetic process [GO:0042179]; response to jasmonic acid [GO:0009753] | plant-type vacuole [GO:0000325] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21343426}. | null | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21343426}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:21343426). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (PubMed:21343426). {ECO:0000269|PubMed:21343426}. | Nicotiana tabacum (Common tobacco) |
F1T161 | BBLC1_TOBAC | MFPLIILISFSFTFLSASATSGAGEGVANLSTCLINHNVHNFSMYPTSRNYFNLLDFSLQNLRFAASNMPKPTVIILPNSKEELVSTILCCRQTSYEIRVRCGGHSYEGTSSVSFDGSPFVIIDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKASDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGVAADSVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLVKVPKIVTTFKISKPGSKQYVAPLLYKWQIVAPNLADDFTLGVQMIPIDLPADMKYGNPTPIEICPQFNGLYLGPKTEAVSILNEAFPELNVKNDDAKEMTWIESALFFSDLDNIFGNSSDDISHLKERYLGVKICFKGKSDYVKTPFSMDGIMTALVEHEKNPNAFLVFDPYGGAMDKISAQAIAFPHRKGNLFAIQYYAQWNEEDDAKSNEHIEWIRGFYNKMAPFVSSSPRGAYVNYLDMDLGMNMDDDYLLRNASSRYSSSVDAVERARAWGEKYFLNNYDRLVKAKTKIDPLNVFRHEQSIPPTLGSTQEHNYSSE | 1.1.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O64743}; | alkaloid biosynthetic process [GO:0009821]; nicotine biosynthetic process [GO:0042179]; response to jasmonic acid [GO:0009753] | plant-type vacuole [GO:0000325] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21343426}. | null | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21343426}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:21343426). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (PubMed:21343426). {ECO:0000269|PubMed:21343426}. | Nicotiana tabacum (Common tobacco) |
F2JXJ3 | LODA_MARM1 | MALSVHPSIGVARLGNANTDNFVLNPMEIGGLPYEHDVDLKPTTTVVNFKDEAGCIRRQGQVFKVFGASNEELTLDSPNVKNIEWTVHLANKKAAWYEFRELNGNLLYGRDNSYSARGVPWRNASKTASSERQSLIIDLGPRSVSGVMATVEISINNIPETYLHPSYPSGELLQGSKHFESLGTLRTDSQGRLIVLGGYGFAGGNTDLSGYGGGDDWYDDISDGSVTCVVTYSDDSSETSTAWMVVGSPDFAPEIVNISTLSDTCFDVGVRNFDLVPDMYDSATGHYKSDYVANFDRDILPIIQRISQYQWVSNVQSMSGFFSFQFDYRDGSAANKANRMKYYNYFRQLDNKVIGDYDQPQQVLMSSEVEGDILPLMPMNSGSNSVSSSNFYDLTDNVVEKFLALDATQLFLLGQWAEGEFTAGPADDYPVSDMDTASIGNCVGLPMCPGIEMTWSLQNPVIYKDAYQIKHYQDKAYFDVNGLTPERDECEEETGCEPGDLTKRMACPWQADFFNCTIQTVNFSEPSVNKASQTETVTSRTHYEWGNLPAGVSVPDQSSVSATKNVDEKVPLPPAYYSYWWPPQSPWDVLTGELDTEGQLHSHLPAGQQINYARGINSYSQMVEHWSALAFIRDRNQNNDGFPFFTETERNHELFDFKEVLVGQVTGNSEDNETSLPVFFINANKESLEGKGTKKGKLMASYFEERAFSKVRSSNIRPRSGTRMRG | 1.4.3.20 | COFACTOR: Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252; Evidence={ECO:0000269|PubMed:17030025, ECO:0000269|PubMed:20025674}; Note=Contains 1 cysteine tryptophylquinone per subunit. {ECO:0000269|PubMed:17030025, ECO:0000269|PubMed:20025674}; | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; negative regulation of single-species biofilm formation [GO:1900191] | extracellular region [GO:0005576] | L-lysine 6-oxidase activity [GO:0033736]; quinone binding [GO:0048038] | PF18417;PF17990; | null | null | PTM: The cysteine tryptophylquinone (CTQ) is generated by oxidation of the indole ring of a tryptophan residue to form tryptophylquinone, followed by covalent cross-linking with a cysteine residue. {ECO:0000269|PubMed:23908359}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652194, ECO:0000269|PubMed:20025674}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:22548, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551, ChEBI:CHEBI:58321; EC=1.4.3.20; Evidence={ECO:0000269|PubMed:16547036, ECO:0000269|PubMed:17030025}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 uM for L-lysine; Note=Also uses N(2)-acetyl-L-lysine as substrate.; | null | null | null | FUNCTION: Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. Also has autotoxic activity. Involved in biofilm differentiation; responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization. {ECO:0000269|PubMed:15652194, ECO:0000269|PubMed:18502869, ECO:0000269|PubMed:20025674}. | Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1) |
F2SG60 | MDR3_TRIRC | MAPTEEANVTKPTGELRPDEKLNYEEDVKCSGSSSTTVGKTAYDTDDISQSQAAELQDLARQLSRASRQGGLDVENEPQQVINPFLDSESDPELNPDSKSFNVAKWLKTILQITSRDPERFPKRTAGVSFRNMNVHGYGTAADYQSDVGNLPLKAWSGIMSMLGLRKKVRIDILRDFEGLVKSGEMLVVLGRPGSGCSTLLRTLSGETHGLYLDEGNDIQYQGISWEQMHKNFRGEVIYQAETETHFPQMTVGDTLYFAARARAPANRLPGVSREQYAIHMRSMVMSMLSLSHTINTQVGNEYIRGVSGGERKRISIAETTLSGSPLQCWDNSTRGLDSANALEFVKSLRLSTKYSGTTAIVAIYQAGQAIYDIFDKAVVLYEGHQIYFGNAVRAKEYFIEMGFDCPSRQTTADFLTSVTSPSERRVRPGYESRVPQTPAEFAQRWKESEDRRILMQEIDEYNKTYPLHGEQLQKFQASRLAEKSRSTSKSSPYTLSYPMEIKLCMWRGFQRLKGDMSMTLTSIIGNIAMSLIIASVFYNQQETTDSFFSRGSLLFFAILMNAFASSLEILTLWHQRPIVEKHDKYALYHPSSEAISSILVDMPAKLAVAIVFNLIIYFMTNLRRTPGHFFIFFLFSFTTTLTMSNVFRSIAAVSRTLSQALVPTSIFMLALVIYTGFTIPVRDMRPWFKWISYINPIQYAFESLMINEFHDREFKCAVYIPSGPGYSNVSGTSKICAAKGAMAGKPTVSGDVFLRETYSYYASHMWRNYGIIVAFFLFFLFVYITATELVSAKPSKGEILVFPKGKVPAFLKQSKKKQDPEAASTQEKQPVETSGHDQTAAIVKQTSVFHWESVCYDIKIKKESRRILDNVDGWVKPGTLTALMGVSGAGKTTLLDVLANRVTMGVVTGEMLVDGRLRDDSFQRKTGYVQQQDLHLEISTVREALTFSALLRQPNTTPYEEKVAYVEEVIKMLGMEEYANAVVGVLGEGLNVEQRKRLTIGVEIAAKPDLLLFFDEPTSGLDSQTAWSICTLMRKLADHGQAVLCTIHQPSAMLMQEFDRLLFLASGGRTVYFGELGKHMSTLIEYFESKGAPKCPPDANPAEWMLEVIGAAPGSKTDIDWPAVWRDSAERVEVRRHLAELKSELSQKPQTPRLTGYGEFAMPLWKQYLIVQHRMFQQYWRSPDYIYSKACLAIVPTLFIGFTFYKEQVSLQGIQNQMFAIFMFMILFPNLVQQMMPYFVIQRSLYEVRERPSKTYSWIAFMISSVVVEIPWNALLTVPAFFCWYYPIGFYKNAIPTDAVTERSGTMFLLILIFLMFSSTFSSMVIAGIEQAETGGNIAQLCFSLTLVFCGVLVSPTAMPGFWIFMYRLSPFTYFVSAVLSTGVGRTDIVCAANEILRLTPAAGQTCMEYLGPYTKFAGGRILTPDATDMCEFCAVADTDTFLKGVNIIFDERWRNIGILFGYIAFNMVGAIGLYWLLRVPKRKSGVKQGQQPQKQANETKA | null | null | xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | plasma membrane [GO:0005886] | ABC-type azole transporter activity [GO:0140394]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF19055;PF00005;PF14510;PF06422; | 3.40.50.300; | ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31501141}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out) + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate + voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46081, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=(2R,4S)-ketoconazole(in) + ATP + H2O = (2R,4S)-ketoconazole(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48336, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61921; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=(2S,4R)-ketoconazole(in) + ATP + H2O = (2S,4R)-ketoconazole(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:47518, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61925; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=(R)-miconazole(in) + ATP + H2O = (R)-miconazole(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82894, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61929; Evidence={ECO:0000269|PubMed:31501141}; CATALYTIC ACTIVITY: Reaction=(S)-miconazole(in) + ATP + H2O = (S)-miconazole(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61932, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82897, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31501141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61933; Evidence={ECO:0000269|PubMed:31501141}; | null | null | null | null | FUNCTION: Pleiotropic ABC efflux transporter involved in the modulation susceptibility to azoles, including fluconazole, itraconazole, ketoconazole, miconazole and voriconazole. {ECO:0000269|PubMed:31501141, ECO:0000269|PubMed:33896045}. | Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot fungus) |
F2WP51 | LPAKS_PSESP | MKLNALSTATHGSRSSPVKLWKFSTSFLLAASIIVSGQSWAAETAKPATDATKAANDALLKELPFDDKTSFDLAHKGFIAPLPAEPIKGEKGNMIWDPSKYGFIKEGEAAPDTTNPSLWRQSQLINISGLFEVTDGIYQVRNYDLSNMTIVEGKDGITIFDPLISQETAKAALDLYYKHRPKKPVVAVIYTHSHVDHYGGVRGVVDEADVKAGKVKIYAPLGFLEHAVAENVMAGTAMSRRASYMYGNLLPPDAKGQLGAGLGTTTSAGTVTLIPPTDIIKETGETHVIDGLTYEFMYAPGSEAPAEMLYYIKEKKALNAAEDSTHTLHNTYSLRGAKIRDPLAWSKYLNEALKLWGDDVQVMYAMHHWPVWGNKEVREQLSLQRDMYRYINDETLRLANKGYTMTEIAEQVKLPKKIATKFSNRGYYGSLNHNVKATYVLYLGWFIGNPATLWELPPADKAKRYVEMMGGADAVLKKAKEYYDKGDFRWVAEVVNHVVFAEPNNQAAKNMQADALEQLGYQAESGPWRNFYLTGAQELRNGVQQLPTPDTASPDTVKAMDLDLFFDFLAMRLKGPDVADKHITLNLDFTDLKQKYTLEMVNGVLNHTEGMQAKNADATVTLTRETLNNVMLKQTTLKDAESSGDIKIEGDKGKLEELMSYMDNFDFWFNIVTP | 3.1.6.21 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21318560, ECO:0000269|PubMed:28442601}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9I5I9}; | dodecyl sulfate metabolic process [GO:0018909] | outer membrane-bounded periplasmic space [GO:0030288] | linear primary-alkylsulfatase activity [GO:0018741]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF14864;PF14863;PF00753; | 1.25.40.880;3.60.15.30;3.30.1050.10; | Metallo-beta-lactamase superfamily, Type III sulfatase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q9I5I9}. | CATALYTIC ACTIVITY: Reaction=a primary linear alkyl sulfate ester + H2O = a primary alcohol + H(+) + sulfate; Xref=Rhea:RHEA:67908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:16189, ChEBI:CHEBI:157685; EC=3.1.6.21; Evidence={ECO:0000269|PubMed:21318560, ECO:0000269|PubMed:28442601}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=264.3 uM for SDS {ECO:0000269|PubMed:21318560}; KM=74.2 uM for SDS {ECO:0000269|PubMed:28442601}; Vmax=33.8 umol/min/mg enzyme {ECO:0000269|PubMed:21318560}; Note=kcat is 4.88 sec(-1) with SDS as substrate. {ECO:0000269|PubMed:28442601}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:21318560}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Retains more than 90% activity after incubation at 65 degrees Celsius for 1 hour. {ECO:0000269|PubMed:21318560}; | FUNCTION: Alkylsulfatase that cleaves primary alkyl sulfates such as sodium octyl sulfate and the widely used detergent sodium dodecyl sulfate (SDS). {ECO:0000269|PubMed:21318560, ECO:0000269|PubMed:28442601}. | Pseudomonas sp |
F2XF95 | PINS1_PICGL | MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYREQAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLSLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYEYKYRDGYSVANIETKSLVKRTVIDPVTL | 4.2.3.119; 4.2.3.120 | 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]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; pinene synthase activity [GO:0050550] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate; Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.120; Evidence={ECO:0000269|PubMed:21385377}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate; Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.119; Evidence={ECO:0000269|PubMed:21385377}; | null | PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21385377}. | null | null | FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene (PubMed:21385377). {ECO:0000269|PubMed:21385377}. | Picea glauca (White spruce) (Pinus glauca) |
F2XF96 | PINS2_PICGL | MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELINPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGLRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIGSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEEALQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFGRHRHVEYYTLASCIAFEPQHSGFRLGFAKTCHIITILDDMYDTFGTVDELELFTAAMKRWNPSAADCLPEYMKGMYMIVYDTVNEICQEAEKAQGRNTLDYARQAWDEYLDSYMQEAKWIVTGYLPTFAEYYENGKVSSGHRTAALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGVTEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVKRTVIDPVTL | 4.2.3.119; 4.2.3.120 | 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]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; pinene synthase activity [GO:0050550] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate; Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.120; Evidence={ECO:0000269|PubMed:21385377}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate; Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.119; Evidence={ECO:0000269|PubMed:21385377}; | null | PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21385377}. | null | null | FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene (PubMed:21385377). {ECO:0000269|PubMed:21385377}. | Picea glauca (White spruce) (Pinus glauca) |
F2XF99 | FARNS_PICXS | MASVDQSQLCSKSVSMSLSVDDGVQRRTGDYHSNLWDDDFIQSLSTPYGAPCYRERAERLIGEVKEMFNSVRLSPLNDLLQGLSMVDSVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGRESVVTDLNSSALGFRALRLHGYPVSSDVFKDQNGQFACSANTQTEGEMRGVLNLFRASLVAFPGEKVMEDAERFSAIYLKEALKTVPICSGSLSGEIEYVLEYGWLTNFPRLEARNYIDIFGKDTSPCLQTEKLLELAKLEFNIFHSLQQRELKQVSRWWKDSGFSQLTFTRHRHVEFYTLASCIAIEPKHSAFRLGFAKLCYLGIVLDDIYDTFGTMDELELFTAAIKRWDPSATECLPEYMKGVYMVFYECVNQMAREAEKTQGRDTLSYARNTWEAVFDAFLEEAKWISSGYIPTFEEYLENGKVSFGYRAATLQPILTLDVPLPLHILQEIDFPSRFNDLAASILRLRGDVCGYKAERSRGEEASSISCYMKDNPGATEEDALNQIDTMIKEKIKELNWEFLKPDSNVPISSKKHAFDILRAFYHLYKYRDGFSIANNETKSLVMRTLLETVPF | 4.2.3.106; 4.2.3.46 | 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}; | gibberellin biosynthetic process [GO:0009686]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099]; sesquiterpenoid biosynthetic process [GO:0016106] | chloroplast [GO:0009507] | (E)-beta-ocimene synthase activity [GO:0034768]; alpha-farnesene synthase activity [GO:0052578]; lyase activity [GO:0016829]; magnesium ion binding [GO:0000287] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46; Evidence={ECO:0000269|PubMed:21385377}; 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:21385377}; | null | PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21385377}.; PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:21385377}. | null | null | FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of sesquiterpene and monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to (3E,6E)-alpha-farnesene and of (2E)-geranyl diphosphate (GPP) to (E)-beta-ocimene (PubMed:21385377). {ECO:0000269|PubMed:21385377}. | Picea engelmannii x Picea glauca (Hybrid white spruce) |
F2XFA8 | PINS1_PICSI | MALVSIAPLASKSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELISPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGFRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEESLQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITILDDMYDTFGTVDELELFTAAMKRWDPSAADCLPEYMKGVYLILYDTVNEMSREAEKAQGRDTLDYARRAWDDYLDSYMQEAKWIATGYLPTFAEYYENGKVSSGHRTSALQPILTMDIPFPPHILKEVDFPSKLNDLACAILRLRGDTRCYKADRARGEEASSISCYMKDNPGATEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVKRTVIDPVTL | 4.2.3.119; 4.2.3.120 | 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]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpenoid biosynthetic process [GO:0016099] | chloroplast [GO:0009507] | lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; pinene synthase activity [GO:0050550] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate; Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.120; Evidence={ECO:0000269|PubMed:21385377}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate; Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.119; Evidence={ECO:0000269|PubMed:21385377}; | null | PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21385377}. | null | null | FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (1S,5S)-beta-pinene (PubMed:21385377). {ECO:0000269|PubMed:21385377}. | Picea sitchensis (Sitka spruce) (Pinus sitchensis) |
F2XFB2 | LEVOS_PICSI | MALLSSSLSSHIPTGAHHLTLNAYANTQCIPHFFSTLNAGTSAGKRSSLYLRWGKGSNKIIACVGEDSVSAPTLLKREFPPGFWKDHVIDSLTSSHKVAASDEKRIETLISEIKNMFRSMGYGETNPSAYDTAWVARIPAVDGSEQPEFPETLEWILQNQLKDGSWGEGFYFLAYDRILATLACIITLTLWRTGEIQVQKGIEFFKTQAVKIEDEADSHRPSGFEIVFPAMLKEAKVLGLDLPYELPFIKKIIEKREAKLERLPTNILYALPTTLLYSLEGLQEIVDWQKIIKLQSKDGSFLTSPASTAAVFMRTGNKKCLEFLNFVLKKFGNHVPCHYPLDLFERLWAVDTVERLGIDRHFKEEIKDALDYVYSHWDERGIGWARENLVPDIDDTAMGLRILRLHGYNVSSDVLKTFRDENGEFFCFLGQTQRGVTDMLNVNRCSHVAFPGETIMEEAKTCTERYLRNALEDVGAFDKWALKKNIRGEVEYALKYPWHRSMPRLEARSYIEHYGPNDVWLGKTMYMMPYISNEKYLELAKLDFNHVQSLHQKELRDLRRWWTSSGFTELKFTRERVTEIYFSPASFMFEPEFATCRAVYTKTSNFTVILDDLYDAHGTLDDLKLFSDSVKKWDLSLVDRMPEDMKICFMGFYNTFNEIAEEGRKRQGRDVLGYIRNVWEIQLEAYTKEAEWSAARYVPSFDEYIENASVSIALGTVVLISALFTGEILTDDVLSKIGRGSRFLQLMGLTGRLVNDTKTYEAERGQGEVASAVQCYMKDHPEISEEEALKHVYTVMENALDELNREFVNNREVPDSCRRLVFETARIMQLFYMDGDGLTLSHETEIKEHVKNCLFHPVA | 4.2.3.18; 4.2.3.32 | 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}; | diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]; green leaf volatile biosynthetic process [GO:0010597]; response to wounding [GO:0009611] | chloroplast [GO:0009507] | abietadiene synthase activity [GO:0050554]; levopimaradiene synthase activity [GO:0052678]; lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate; Xref=Rhea:RHEA:25548, ChEBI:CHEBI:29616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635; EC=4.2.3.32; Evidence={ECO:0000269|PubMed:21385377}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate; Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635; EC=4.2.3.18; Evidence={ECO:0000269|PubMed:21385377}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:16415217}.; PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21385377}. | null | null | FUNCTION: Terpene synthase (di-TPS) involved in the biosynthesis of diterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:21385377). Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to isopimaradiene (PubMed:21385377). {ECO:0000269|PubMed:21385377}. | Picea sitchensis (Sitka spruce) (Pinus sitchensis) |
F2XG53 | CAS3_STRTR | MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV | 3.1.-.-; 3.6.4.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Mn(2+) or Mg(2+) or Ca(2+). ATPase and nuclease activities are dependent on divalent cations, for ATPase Mn(2+) is marginally preferred over Mg(2+) or Ca(2+).; | defense response to virus [GO:0051607] | cytosol [GO:0005829] | ATP binding [GO:0005524]; DNA nuclease activity [GO:0004536]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA helicase activity [GO:0003724] | PF18395;PF18019;PF00270; | 1.10.3210.30;3.40.50.300; | CRISPR-associated nuclease Cas3-HD family; CRISPR-associated helicase Cas3 family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction. {ECO:0000269|PubMed:21343909}. | Streptococcus thermophilus |
F2Y4A3 | SPHK2_ARATH | MENDQFMCPTDIITGIVFIDGELAMLTLTADGELRWTEYGLRQYLSMKKDVLGFIVEGKQIRVKAVVEKEAGGICCGQFGGDFVRKDFVFEPLIDQNGWCYKLRQYLDSLGRPKRLLVFVNPFGGKKSAREIFVKEVKPLFEDADVQLEIQETKYQLHAKEFVKSMDVSKYDGIVCVSGDGILVEVVNGLLERADWRNALKLPIGMVPAGTGNGMIKSLLDTVGLRCCANSATISIIRGHKRSVDVATIAQGNTKFFSVLMLAWGLIADIDIESEKFRWMGSARIDFYALQRIICLRRYNGRILFLPAPGFEGYGQPASCSLYQEPHVSDKEVGYQGPETKFEDLEWREMKGPFVTIWLHNVPWGSENTLTAPAAKFSDGYLDLIVLKNCPKLVLLSLMRQTSSGTHVESPYIVYIKVKAFVLEPGALVDEPDKEGIIDSDGEVLARGKRTYKCDQKALMSYDKLQVTVDQGLATLFSPEY | 2.7.1.91 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cellular response to abscisic acid stimulus [GO:0071215]; phosphorylation [GO:0016310]; response to abscisic acid [GO:0009737]; sphingolipid metabolic process [GO:0006665]; sphingosine biosynthetic process [GO:0046512] | plant-type vacuole membrane [GO:0009705] | ATP binding [GO:0005524]; D-erythro-sphingosine kinase activity [GO:0017050]; phosphatidic acid binding [GO:0070300]; sphinganine kinase activity [GO:0008481] | PF00781;PF19279; | 2.60.200.40; | null | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:21330371}; Peripheral membrane protein {ECO:0000305|PubMed:21330371}. Note=Associated with the tonoplast. | CATALYTIC ACTIVITY: Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+); Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216; EC=2.7.1.91; Evidence={ECO:0000269|PubMed:21330371}; | null | null | null | null | FUNCTION: Involved in the production of sphingolipid metabolites. Phosphorylates sphingosine and various l sphingoid long-chain base (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-erythro-dihydrosphingosine, but has a very few activity toward D,L-threo- dihydrosphingosine. Is required for abscisic acid (ABA) signaling that mediates stomatal closure, inhibition of seed germination and root elongation. May function upstream of PLDALPHA1 and phosphatidic acid (PA) in an amplification response to ABA that mediates stomatal closure. {ECO:0000269|PubMed:21330371, ECO:0000269|PubMed:22275366}. | Arabidopsis thaliana (Mouse-ear cress) |
F2YMG0 | PRS56_MOUSE | MPLAMLLLLLLLLSPDSQTAHGHPLYTRLSPGALQVLSAQGTQALQAAQRSAQWAIKRVLMEIQHRLHECQGPGRPRPQAPLLQDPPEPVQCGERHQGVANTTRAHGRIVGGSTAPSGAWPWLVRLQLGGLPLCGGVLVAASWVLTAAHCFAGASNELLWTVMLAEGPQGEQAEEVQVNRILPHPKFDPQTFHNDLALVQLWTPVSPEGPARPICLPQGSREPPAGTPCAIAGWGALFEDGPESEAVREARVPLLSADTCQKVLGPGLRPSTMLCAGYLAGGIDSCQGDSGGPLTCSEPGPRPREVLFGVTSWGDGCGEPGKPGVYTRVTVFKDWLQEQMSAGPSTREPSCRELLNWNAREEEPFTDAPGLCAFYARQCLGSESSCARLALQQCLQRRRRCELRSLAHTLLGLLRGAQELLGPRPGLRRGVSAPARSAPSLQELPGHNPREQRLYSGSRIAGTWLQKPKPERRPETKGCPGLEPLQQKLAAIQRAHAWILQIPAEHLAMNFHEVLADLGSKTLTGLFRAWVRAGLGDQRVVFSGLVGLEPSTLAHSLPRLLVQALKAFRSASLTEGEPQAPWIGADQGQRLGKERQGQLQPPVP | 3.4.21.- | null | blood coagulation [GO:0007596]; camera-type eye development [GO:0043010]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21532570}; Peripheral membrane protein {ECO:0000269|PubMed:21532570}. | null | null | null | null | null | FUNCTION: Serine protease required during eye development. {ECO:0000269|PubMed:21532570}. | Mus musculus (Mouse) |
F2YTN4 | MOMT1_SOLHA | MALSMDNIVISNEEEICMMKAMHLPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSLLTCNITKNDDGNVHTTYNLTPLSQSLISDKDGTSIAPFLLLATDPVGVHACFHLKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNKAMQNLTCIEMKRIVECYNGFQGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMWDSIPQGELIILKAVLHSLDDEDCVKILKNCWRALPNDGKVVVIEQIQPKYPETNLLSKRSFSFDISMMIMFHGGKERTKQQFEDLAKQAGFTYIKVVARAYYSWLIELYKY | 2.1.1.-; 2.1.1.267 | null | aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259] | null | myricetin 3'-O-methyltransferase activity [GO:0033799]; protein dimerization activity [GO:0046983]; quercetin 3'-O-methyltransferase activity [GO:0102822]; rhamnetin 3'-O-methyltransferase activity [GO:0102447] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = H(+) + laricitrin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:25629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:60006; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25630; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=laricitrin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + syringetin; Xref=Rhea:RHEA:25633, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:60006; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25634; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=a 3'-hydroxyflavone + S-adenosyl-L-methionine = a 3'-methoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55332, ChEBI:CHEBI:15378, ChEBI:CHEBI:27741, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138730; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=a 5'-hydroxy-3'-methoxyflavone + S-adenosyl-L-methionine = a 3',5'-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138731, ChEBI:CHEBI:138732; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = H(+) + isorhamnetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60944, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60945; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = H(+) + rhamnacene + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73271, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706, ChEBI:CHEBI:192768; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73272; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine = 3,3'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74715, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789, ChEBI:CHEBI:194063; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74716; Evidence={ECO:0000269|PubMed:21343428}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for myricetin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:21343428}; KM=0.21 uM for laricitrin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:21343428}; KM=16.64 uM for S-adenosyl-L-methionine (in the presence of myricetin) {ECO:0000269|PubMed:21343428}; Note=kcat is 1.59 sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 0.45 sec(-1) with laricitrin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 0.47 sec(-1) with S-adenosyl-L-methionine as substrate (in the presence of myricetin) (PubMed:21343428). {ECO:0000269|PubMed:21343428}; | PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:21343428}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 with myricetin as substrate (in the presence of S-adenosylmethionine). {ECO:0000269|PubMed:21343428}; | null | FUNCTION: Flavonoid 3'/5'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:21343428). Catalyzes S-adenosylmethionine-dependent regioselective 3'/5'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including myricetin and quercetin, but inactive toward kaempferol (PubMed:21343428). Mediates the formation of 3'-methyl derivatives from quercetin, myricetin, 3-methyl quercetin and 7-methyl quercetin (rhamnetin), producing 3'-methyl quercetin (isorhamnetin), 3'-methyl myricetin (laricitrin), 3,3'-dimethyl quercetin (3-O-methylisorhamnetin) and 7,3'-dimethyl quercetin (7-O-methylisorhamnetin), respectively (PubMed:21343428). Triggers the 5'-O-methylation of 3'-methyl myricetin (laricitrin), thus leading to production of 3',5'-dimethyl myricetin (syringetin) (PubMed:21343428). {ECO:0000269|PubMed:21343428}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
F2YTN5 | MOMT2_SOLHA | MASNNNCAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP | 2.1.1.-; 2.1.1.155; 2.1.1.82 | null | aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259] | null | 3',4',5'-trimethylmyricetin 7-O-methyltransferase activity [GO:0102439]; 3-methylquercitin 7-O-methyltransferase activity [GO:0030757]; kaempferide 7-O-methyltransferase activity [GO:0102450]; kaempferol 4'-O-methyltransferase activity [GO:0033803]; myricetin 7-O-methyltransferase activity [GO:0102435]; protein dimerization activity [GO:0046983]; quercetin 7-O-methyltransferase activity [GO:0102432]; rhamnetin 4'-O-methyltransferase activity [GO:0102448]; syringetin 7-O-methyltransferase activity [GO:0102441] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = H(+) + rhamnetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73116; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = H(+) + kaempferide + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15105, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789; EC=2.1.1.155; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15106; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 7-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74719, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194065; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74720; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 7,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74775, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194067; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74776; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3',4'-O-dimethylquercetin + 2 H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74723, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194064; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74724; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16181, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710; EC=2.1.1.82; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16182; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 7,4'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74731, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192706, ChEBI:CHEBI:194068; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74732; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 7,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194069; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74736; Evidence={ECO:0000269|PubMed:21343428}; CATALYTIC ACTIVITY: Reaction=3',4',5'-O-trimethylmyricetin + S-adenosyl-L-methionine = 7,3',4',5'-O-tetramethylmyricetin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74739, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194070, ChEBI:CHEBI:194071; Evidence={ECO:0000269|PubMed:21343428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74740; Evidence={ECO:0000269|PubMed:21343428}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.68 uM for myricetin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:21343428}; KM=2.27 uM for kaempferide (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:21343428}; KM=2.3 uM for rhamnetin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:21343428}; KM=18.71 uM for S-adenosyl-L-methionine (in the presence of kaempferide) {ECO:0000269|PubMed:21343428}; Note=kcat is 7.40x10(-3) sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 5.76x10(-3) sec(-1) with kaempferide as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 6.40x10(-3) sec(-1) with rhamnetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 1.64x10(-2) sec(-1) with S-adenosyl-L-methionine as substrate (in the presence of kaempferide) (PubMed:21343428). {ECO:0000269|PubMed:21343428}; | PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:21343428}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with myricetin as substrate (in the presence of S-adenosylmethionine). {ECO:0000269|PubMed:21343428}; | null | FUNCTION: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects (PubMed:21343428). Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including myricetin, quercetin and kaempferol (PubMed:21343428). Mediates the formation of 4'-methyl derivatives from kaempferol, 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin) and 3'-methyl myricetin, producing 4'-methyl kaempferol (kaempferide), 3',4'-dimethyl quercetin (4'-O-methyl isorhamnetin), 7,4'-dimethyl quercetin (4'-O-methyl rhamnetin, rhamnacene) and 3',4'-dimethyl myricetin, respectively (PubMed:21343428). Triggers the 7-O-methylation of quercetin, myricetin, 4'-methyl kaempferol (kaempferide), 3-methyl quercetin, 3',5'-dimethyl myricetin (syringetin) and 3',4',5'-trimethyl myricetin, thus leading to production of 7-methyl quercetin (rhamnetin), 7-methyl myricetin, 7,4'-dimethyl kaempferol (7-O-methyl kaempferide), 3,7-dimethyl quercetin, 7,3',5'-trimethyl myricetin (7-O-methyl syringetin) and 7,3',4',5'-tetramethyl myricetin, respectively (PubMed:21343428). {ECO:0000269|PubMed:21343428}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
F2Z4R5 | T163B_DANRE | MTDSSSASDPTAGPVDPGPAPSAPDPALEDPASTPANGHHPNQADSFNMEQQMKIGEPEDNAGLLESSMRLKPHEAQSYRKKALWVSWVSIVVTMILAIAAFTVSIMRHSASAFGFAFDATLDVLSSIIVLWRYSNAAAVHSAHREYIACVILGVVFILSAITILVKAIHDLATKLEPEVDDFLYSVSVISGVVCTVLCVCKFMLGKVLTSRALITDGFNSLVGGVMGFSILISAEVFKHEPSVWFLDGTIGILIGLIILAYGVKLLKDMVPRIRQTRHYERFE | null | null | myelination [GO:0042552]; oligodendrocyte development [GO:0014003] | early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672] | monoatomic cation transmembrane transporter activity [GO:0008324]; zinc ion binding [GO:0008270] | PF01545; | 1.20.1510.10; | TMEM163 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8C996}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:A9CMA6}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi-pass membrane protein {ECO:0000255}. Note=Glutamatergic synaptic vesicles. {ECO:0000250|UniProtKB:A9CMA6}. | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8TC26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29352; Evidence={ECO:0000250|UniProtKB:Q8TC26}; | null | null | null | null | FUNCTION: Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By similarity). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (PubMed:35455965). {ECO:0000250|UniProtKB:A9CMA6, ECO:0000250|UniProtKB:Q8TC26, ECO:0000269|PubMed:35455965}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F3Y5P4 | GRDN_CAEEL | MKEKHENWSHPLAFWLCDCAAIIPNPATQNFAKNDFLDGLLMLNLMKFINPHFSENEKNGQSLYEELLNQISQFYEKNLDQVIVCKMPEISILESSGEIDEITFEELKKLLLLLLGCAIQSDHKKVFVDRITGFDQTIQAELAACIQKLTESDEIVQNLEDFERRKMKETDEVGGGGGSIEDVDSDDMESSTTSSSNGEIAIKQQDQSFLMSRSTSPTSELRHQTLQIANLQHEMRQMRTQAENRDEECQKLELDNEEKAQKIKILENERLKLVDFKKKWKSVNDDLQEANCKIEKLQNLVGIEKKYREARDGKELYKSKYDIVVKKNLEMEETITTLEKNLKTLQMEMKEKFGVEDNLQRMRNTIDDLEAEISKKNLEIEDFLDEKHRMDREIKELKEIVHQMEVPSTTTTPRIMDSLADQLENAKQDEFEMMKAEIRKLRAQTEGATPETTIIQCNQDLDTLRSQLSTEQHQTAQLHLEIQKMQVEKEQIDGNMERIGIELEEMSAQVENLNLERDEAVKQLLEARRKFGEFQMGQSRDLEEKWSKEVEKSNKISKKCEILEEKLQESDFLLAKSRDEAKKLQFELDEALEETSHVTRSLSSEKNTLKAKLLELQDQVEAQTLELLNQKNCGKRLEDRDQMISNLHNLKNELENDLKTCQTQLELESKKLQRLREDLVLEKSRRADLIGRIHSLCTTLSLNGANFEKINNDDELIDNIDDIMMNALVAVKRERDDLRIQGNQQIQELHDLKRDIEKLRRSESESLNESDDRVRELTRENMHTKEQVFMLQEKLRELNLELSTKNDEIDMVKASIEELNRNSTASCTSNAEIARLQVSIRNSQIQEDLVKQENTKLRDELQEMQKMSKKRSQNLDELENMHKTLLVDHSRLQQLHNLLTRDYDEAKKESMELRQKVQNIPRQQAVFMNANIRELEAKLSEEISRREQLEKEHKMCRIHCENLRRDITELVQTRDELSLELRRAHDTCHNKNNQIDELKKQLNQKISEVNKLSSKIEALSQLNRTYNEENRNLSRQLEILLTQNKELLQRALHDKDQYHLEMKDFQDQLSALRRHKEKLEDKIMDQYRTMENKKSTPERKQPLVKRAAKALINRRRATSNGGSTTEDSSVYSADERSSPPLAGTNEDVDHLPPTCSSSDDHDVISPDFSAKNPLLRSRNDFMGGSVRSPRRYGNDHDGHIYTSPFLPPRVPIRNSPMTSSLRSRPPPPPYNRSPAHKIEQNSSFFEPIAHSTPNSSILEERRVVGEGEKRELVRDKEERIDKTLSYYENVNLPQNPPDLPENSDLKPNESTIWHEYGCV | null | null | amphid sensory organ dendrite retrograde extension [GO:0003391]; ciliary basal body organization [GO:0032053]; ciliary transition zone assembly [GO:1905349]; cytoplasmic microtubule organization [GO:0031122]; cytoskeleton-dependent intracellular transport [GO:0030705]; positive regulation of cilium assembly [GO:0045724]; positive regulation of dendrite extension [GO:1903861]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of protein localization to cilium [GO:1903566]; protein localization to ciliary transition zone [GO:1904491] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737] | dynein light intermediate chain binding [GO:0051959]; microtubule binding [GO:0008017] | PF19047; | 1.10.418.10; | CCDC88 family | null | SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:33460640}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:33460640}. Note=Enriched at the proximal ends of centrioles (PubMed:27623382). Localizes to the cilium basal body in AQR and PQR sensory neurons (PubMed:33460640). Localizes to the cilium basal body in the outgrowing AQR dendrite (PubMed:33460640). Localizes to puncta near dendrite contacts in the nose (PubMed:31988188). {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:31988188, ECO:0000269|PubMed:33460640}. | null | null | null | null | null | FUNCTION: Scaffolding protein that plays a role in ciliogenesis, cilium positioning and dendrite anchoring in sensory amphid neurons including AWB, AWA, AWC, ADL and ASI, the phasmid neurons PHA and PHB and the gas sensing neurons AQR, PQR, URX and BAG (PubMed:27623382, PubMed:31988188). Its role in cilium positioning may be through regulation of the localization of cell adhesion proteins such as the apical junction protein ajm-1, and the ciliary scaffolding protein Rootletin/che-10 (PubMed:27623382). Plays a more prominent role in regulating dendrite morphogenesis in AQR than in PQR neurons (PubMed:33460640). Regulates localization of hmr-1 to the distal AQR dendrite (PubMed:33460640). During embryonic elongation, required for the anchoring of URX and BAG dendrites to the presumptive nose (PubMed:31988188). {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:31988188, ECO:0000269|PubMed:33460640}. | Caenorhabditis elegans |
F3YDF1 | YMEL1_DROME | MFSTTTHSVPYLYLGNFSRKPHYYSVNRTKLHGSAGAARLSKSTSTSSRSHDLVLDLRNLLSRSSASIQGMVERAARLNGILDRRLVDDVLAKVTSMLPSMRDVRVTLEESATQIGRVQLQNYQFEVSLTGAAGSVPTGANVKVIPTITPGLLRPLFSQQQLNQIRGFKTDRSIEAEQKRNPTMTSRLKNALANSPQRLDGDTPLQAEKLRRLLAKSEEHGFNKAESLKIAFAEGYLAAANSEDSPKSGKTMKYLKTLQTIVVIVVFLGIFLSFFTTSNGSVFRSIQLGNQVEVDPEEINVTFEDVKGCDEAKQELKEVVEFLKSPEKFSNLGGKLPKGVLLVGPPGTGKTLLARAVAGEAKVPFFHAAGPEFDEVLVGQGARRVRDLFKAAKARAPCVIFIDEIDSVGAKRTNSVLHPYANQTINQLLSEMDGFHQNAGVIVLGATNRRDDLDQALLRPGRFDVEVMVSTPDFTGRKEILSLYLTKILHDEIDLDMLARGTSGFTGADLENMINQAALRAAIDGAETVSMKHLETARDKVLMGPERKARLPDEEANTITAYHEGGHAIVAFYTKESHPLHKVTIMPRGPSLGHTAYIPEKERYHVTKAQLLAMMDTMMGGRAAEELVFGTDKITSGASSDLKQATSIATHMVRDWGMSDKVGLRTIEASKGLGTGDTLGPNTIEAVDAEIKRILSDSYERAKAILRKHTREHKALAEALLKYETLDADDIKAILNESQT | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96TA2}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q96TA2}; | mitochondrion organization [GO:0007005]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00004;PF17862;PF01434; | 1.10.8.60;3.40.50.300;1.20.58.760; | AAA ATPase family; Peptidase M41 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:26160069}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:26160069). Plays an important role in regulating mitochondrial morphology and function by cleaving Opa1, giving rise to a form of Opa1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (PubMed:31125351). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins (PubMed:26160069, PubMed:31125351). Required to control the accumulation of nonassembled respiratory chain subunits such as ND-30 (PubMed:26160069). {ECO:0000269|PubMed:26160069, ECO:0000269|PubMed:31125351}. | Drosophila melanogaster (Fruit fly) |
F4HPR5 | DRP5A_ARATH | MANSNTYLTTPTKTPSSRRNQQSQSKMQSHSKDPINAESRSRFEAYNRLQAAAVAFGEKLPIPEIVAIGGQSDGKSSLLEALLGFRFNVREVEMGTRRPLILQMVHDLSALEPRCRFQDEDSEEYGSPIVSATAVADVIRSRTEALLKKTKTAVSPKPIVMRAEYAHCPNLTIIDTPGFVLKAKKGEPETTPDEILSMVKSLASPPHRILLFLQQSSVEWCSSLWLDAVREIDSSFRRTIVVVSKFDNRLKEFSDRGEVDRYLSASGYLGENTRPYFVALPKDRSTISNDEFRRQISQVDTEVIRHLREGVKGGFDEEKFRSCIGFGSLRDFLESELQKRYKEAAPATLALLEERCSEVTDDMLRMDMKIQATSDVAHLRKAAMLYTASISNHVGALIDGAANPAPEQWGKTTEEERGESGIGSWPGVSVDIKPPNAVLKLYGGAAFERVIHEFRCAAYSIECPPVSREKVANILLAHAGRGGGRGVTEASAEIARTAARSWLAPLLDTACDRLAFVLGSLFEIALERNLNQNSEYEKKTENMDGYVGFHAAVRNCYSRFVKNLAKQCKQLVRHHLDSVTSPYSMACYENNYHQGGAFGAYNKFNQASPNSFCFELSDTSRDEPMKDQENIPPEKNNGQETTPGKGGESHITVPETPSPDQPCEIVYGLVKKEIGNGPDGVGARKRMARMVGNRNIEPFRVQNGGLMFANADNGMKSSSAYSEICSSAAQHFARIREVLVERSVTSTLNSGFLTPCRDRLVVALGLDLFAVNDDKFMDMFVAPGAIVVLQNERQQLQKRQKILQSCLTEFKTVARSL | null | null | cytokinesis by cell plate formation [GO:0000911] | cell plate [GO:0009504]; membrane [GO:0016020]; microtubule [GO:0005874]; phragmoplast [GO:0009524] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017] | PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18809930}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18809930}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:18809930}. Note=Localizes in the forming cell plate during cytokinesis. | null | null | null | null | null | FUNCTION: Probable microtubule-associated force-producing protein that is targeted to the forming cell plate during cytokinesis. May play a role in cell division. {ECO:0000269|PubMed:18809930}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HPZ9 | LIG6_ARATH | MASDSAGATISGNFSNSDNSETLNLNTTKLYSSAISSISPQFPSPKPTSSCPSIPNSKRIPNTNFIVDLFRLPHQSSSVAFFLSHFHSDHYSGLSSSWSKGIIYCSHKTARLVAEILQVPSQFVFALPMNQMVKIDGSEVVLIEANHCPGAVQFLFKVKLESSGFEKYVHTGDFRFCDEMRFDPFLNGFVGCDGVFLDTTYCNPKFVFPSQEESVGYVVSVIDKISEEKVLFLVATYVVGKEKILVEIARRCKRKIVVDARKMSMLSVLGCGEEGMFTEDENESDVHVVGWNVLGETWPYFRPNFVKMNEIMVEKGYDKVVGFVPTGWTYEVKRNKFAVRFKDSMEIHLVPYSEHSNYDELREFIKFLKPKRVIPTVGVDIEKFDCKEVNKMQKHFSGLVDEMANKKDFLLGFYRQSYQKNEKSDVDVVSHSAEVYEEEEKNACEDGGENVPSSRGPILHDTTPSSDSRLLIKLRDSLPAWVTEEQMLDLIKKHAGNPVDIVSNFYEYEAELYKQASLPTPSLNNQAVLFDDDVTDLQPNPVKGICPDVQAIQKGFDLPRKMNLTKGTISPGKRGKSSGSKSNKKAKKDPKSKPVGPGQPTLFKFFNKVLDGGSNSVSVGSETEECNTDKKMVHIDASEAYKEVTDQFIDIVNGSESLRDYAASIIDEAKGDISRALNIYYSKPREIPGDHAGERGLSSKTIQYPKCSEACSSQEDKKASENSGHAVNICVQTSAEESVDKNYVSLPPEKYQPKEHACWREGQPAPYIHLVRTFASVESEKGKIKAMSMLCNMFRSLFALSPEDVLPAVYLCTNKIAADHENIELNIGGSLISSALEEACGISRSTVRDMYNSLGDLGDVAQLCRQTQKLLVPPPPLLVRDVFSTLRKISVQTGTGSTRLKKNLIVKLMRSCREKEIKFLVRTLARNLRIGAMLRTVLPALGRAIVMNSFWNDHNKELSESCFREKLEGVSAAVVEAYNILPSLDVVVPSLMDKDIEFSTSTLSMVPGIPIKPMLAKIAKGVQEFFNLSQEKAFTCEYKYDGQRAQIHKLLDGTVCIFSRNGDETTSRFPDLVDVIKQFSCPAAETFMLDAEVVATDRINGNKLMSFQELSTRERGSKDALITTESIKVEVCVFVFDIMFVNGEQLLALPLRERRRRLKEVFPETRPGYLEYAKEITVGAEEASLNNHDTLSRINAFLEEAFQSSCEGIMVKSLDVNAGYCPTKRSDSWLKVKRDYVDGLGDTLDLVPIGAWYGNGRKAGWYSPFLMACFNPETEEFQSVCRVMSGFSDAFYIEMKEFYSEDKILAKKPPYYRTGETPDMWFSAEVVWEIRGADFTVSPVHSASLGLVHPSRGISVRFPRFISKVTDRNPEECSTATDIAEMFHAQTRKMNITSQH | 6.5.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P56709}; | base-excision repair, DNA ligation [GO:0006288]; DNA biosynthetic process [GO:0071897]; DNA integration [GO:0015074]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; lagging strand elongation [GO:0006273]; positive regulation of cellular response to X-ray [GO:2000685]; response to bleomycin [GO:1904975]; response to cold [GO:0009409]; response to molecule of bacterial origin [GO:0002237]; response to oxidative stress [GO:0006979]; response to UV-C [GO:0010225]; seed development [GO:0048316]; seed germination [GO:0009845] | DNA ligase III-XRCC1 complex [GO:0070421] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872] | PF04679;PF01068;PF04675;PF07522; | 3.30.1490.70;3.40.50.12650;1.10.3260.10;3.30.470.30;2.40.50.140;3.60.15.10; | ATP-dependent DNA ligase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000250|UniProtKB:P56709, ECO:0000255|PROSITE-ProRule:PRU10135}; | null | null | null | null | FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair (Probable). Required to maintain seed viability (e.g. longevity and storability) and during seed germination, probably by repairing DNA damage accumulated during seed development, storage and/or imbibition. Facilitates seed germination in cold conditions (2 degrees Celsius) and under oxidative stress (e.g. menadione, a genotoxic agent). Involved in repair of X-ray-induced damage (PubMed:20584150). {ECO:0000269|PubMed:20584150, ECO:0000305}.; FUNCTION: Limits stable root transformation by A.tumefaciens T-DNA. {ECO:0000269|PubMed:25641249}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HQ84 | COG3_ARATH | MATKAASSSSLPKSGAISKGYNFASTWEQSAPLTEQQQAAIVSLSHAVAERPFPANLVHEHVHRPENGLSVSVEDTHLGDSGAIEAVLVNTNQFYKWFTDLESAMKSETEEKYRHYVSTLTERIQTCDNILHQVDETLDLFNELQLQHQGVTTKTKTLHDACDRLLMEKQKLMEFAEALRSKLNYFDELENVSSNFYSPNMNVSNSNFLPLLKRLDECISYIEDNPQYAESSVYLLKFRQLQSRALGMIRTYILAVLKTAASQVQAAFRGTGGNKTSVSEGVEASVIYVRFKAAANELKPVLEEIESRSARKEYVQILAECHRLYCEQRLSLVKGIVHQRVSDFAKKEALPSLTRSGCAYLMQVCHMEHQLFTHFFPASSEEVSSLAPLVDPLSTYLYDILRPKLIHEANIDLLCELVHILKVEVLGDQSARQSEPLAGLRPTLQRILADVNERLTFRARTYIRDEIANYTPSDEDLDYPAKLEGSPNTTSETDLRDDENADVFKTWYPPLEKTLSCLSKLYRCLEQAVFTGLAQEAVEVCSLSIQKASKLIIKRSTTMDGQLFLIKHLLILREQIAPFDIEFSVTHKELDFSHLLEHLRRILRGQASLFDWSRSTSLARTLSPRVLESQIDAKKELEKCLKTTCEEFIMSVTKLVVDPMLSFVTKVTAIKVALSSGTQNHKVDSVMAKPLKEQAFATPDKVVELVQKVYAAIQQELLPILAKMKLYLQNPSTRTILFKPIKTNIVEAHTQVESLLKAEYSAEEQANINMISIQDLQTQLDNFL | null | null | autophagy [GO:0006914]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; pollen tube growth [GO:0009860] | cis-Golgi network [GO:0005801]; Golgi membrane [GO:0000139]; Golgi transport complex [GO:0017119] | protein homodimerization activity [GO:0042803] | PF20671;PF04136; | null | COG3 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:27448097}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40094}; Cytoplasmic side {ECO:0000250|UniProtKB:P40094}. | null | null | null | null | null | FUNCTION: Acts as a component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking (PubMed:27448097). Involved in pollen tube growth by modulating Golgi morphology and vesicle trafficking homeostasis leading to the deposition of cell wall components and proteins at the pollen tube tip (PubMed:27448097). Required for sporophytic development (PubMed:27448097). {ECO:0000269|PubMed:27448097}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HQA1 | PAF1_ARATH | MASYRPPYPPLPQPPSQNSLAPPPPPPSLPPPVPPPPPSHQPYSYPPPPPPPPHAYYQQGPHYPQFNQLQAPPPPPPPSAPPPLVPDPPRHQGPNDHEKGASKQVGRRERAKPDPSKHHHRSHLPHSKKIETEEERRLRKKRELEKQRQDEKHRQQMKNSHKSQMPKGHTEEKKPTPLLTTDRVENRLKKPTTFICKLKFRNELPDPSAQLKLMTIKRDKDQFTKYTITSLEKLWKPKIFVEPDLGIPLDLLDLSVYNPPKVKAPLAPEDEELLRDDDAVTPIKKDGIRRKERPTDKGMSWLVKTQYISSINNESARQSLTEKQAKELREMKGGINILHNLNNRERQIKDIEASFEACKSRPVHATNKNLQPVEVLPLLPYFDRYDEQFVVANFDGAPIADSEFFGKLDPSIRDAHESRAILKSYVVAGSDTANPEKFLAYMVPSLDELSKDIHDENEEISYTWVREYLWDVQPNANDPGTYLVSFDNGTASYLPLPMRLNLRKKRAREGRSSDEIEHFPVPSRVTVRRRSTVSVIEHKDSGVYSSRVGASSSKMRRLEDEGGLGRSWKHEPEQDANQYSDGNEDDYSE | null | null | flower development [GO:0009908]; negative regulation of flower development [GO:0009910]; transcription elongation by RNA polymerase II [GO:0006368] | Cdc73/Paf1 complex [GO:0016593]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; RNA polymerase II complex binding [GO:0000993] | PF03985; | null | PAF1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20363855}. | null | null | null | null | null | FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time. Required for the expression of the flowering repressors and MAD-box genes FLC, AGL27/FLM and AGL31/MAF2. Required for histone H3 trimethylation on 'Lys-4' H3K4me3 at the FLC and AGL27/FLM loci (PubMed:15520273). Involved in the control of seed dormancy and germination (PubMed:21799800). {ECO:0000269|PubMed:15520273, ECO:0000269|PubMed:20363855, ECO:0000269|PubMed:21799800}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HQE2 | RTEL1_ARATH | MGFTVVSRSGSPTRRENQKRRVCFRLLLRLLRRGFVVLSAESDPKMPNYSIRGINVEFPFEAYQSQIIYMDRVIESLQNKCHALLESPTGTGKTLCLLCATLAWRKSLGSFSTRKDRKNSAIPWSDSDEPLSQSGGGGGGAFPTIVYASRTHSQLRQVIKELKRSSYRPKMVVLGSREQLCVNEEVNSLRGKALTNACQYLCKKRGKRQCNHFNRLPDYLKHNPHIGDEPVDIEDLVNIGKDSGPCPYYITRELHKDVDIIFAPYNYLISNGYRKFLKVNWTNSVLIFDEAHNLESLCADSASFDLPSVLLSACISEAQECVQLAAARRDSLNDVSINPENFAILKGLLLKLQELISKVPIPKRDEGFTKPGPYIYEMLKSLNITHETAPKLIGTVEEAAVFLEEEKQRTATNAGSKLEIIADMLKLIFRENGSNHADVYRVHVQELEQNSTDVMKGKVSRTLSWWCFSPGITMLDIAQKGVGSIILTSGTLSPMDSLAQELKLDFPIRLENPHVISSNQLWAGVVSTGPSGYVLNSSYRNRDVPEYKQELGNAIVNFSRVVPEGLLIFFPSYYLMDSCITFWKNGCYRNSMTVWERICKLKKPVIEPKDSSLFPAAMRDFSEKLQDRATSGVVFFAVCRGKVSEGLDFADGAGRAVVITGLPYARVTDPRVKLKREFLDEQSQLADVKLPRSTLLSGSMWYSQEAARAVNQAIGRVIRHRHDYGAIIFCDDRFEQPSQQSKISLWIRPNVKCYSRYGEVISDLARFFRTERSNFPARLVTEQENNIVSTLLPVESIEDNPTPAFGNSNLKNVGVAQNELSRLEAFPPANRASPLERDGNNVKRNGLTILKHTGKIPRIVKGDVMQGCSSRKAKLVELSDDEETPVERRCEVVDLESDNCETQTCVTEVLASSTCLNTMGLKKKRKVPESQGSASSSVLTAKGNGGGDKKEASASAFLSQVKEKLNTEEYKKFIGYMQALKKKEIKLANVMQSIVQLFCGSERDHLLMGFKDFVPVKYRPAYEECIKTRKRQSIIFGNSN | 3.6.4.12 | null | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; interstrand cross-link repair [GO:0036297]; maintenance of rDNA [GO:0043007]; mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication [GO:0070716]; negative regulation of DNA recombination [GO:0045910]; negative regulation of t-circle formation [GO:1904430]; pollen development [GO:0009555]; recombinational repair [GO:0000725]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair via homologous recombination [GO:0010569]; root development [GO:0048364]; telomere maintenance [GO:0000723]; telomeric loop disassembly [GO:0090657] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA polymerase binding [GO:0070182]; metal ion binding [GO:0046872] | PF06733;PF13307; | 1.20.1160.20;3.40.50.300; | Helicase family, RAD3/XPD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: ATP-dependent DNA helicase implicated in DNA replication, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates (PubMed:25516598, PubMed:25595823). Also plays a role in preserving the stability of 45S rDNA repeats (PubMed:27760121). {ECO:0000269|PubMed:25516598, ECO:0000269|PubMed:25595823, ECO:0000269|PubMed:27760121}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HQM3 | NCER1_ARATH | MELSLVRLWNTCFPSFFYISTVLFLLTGGGVYSHSEYLIGLGSYDITGPAADVNMMGYANMEQVASGIHFRLRARTFIVSEPQGKRVVFVNLDACMASQIVKLKVIERLKARYGDLYTEQNVGISGIHTHAGPGGYLQYVVYIVTSLGFVRQSFDALVDGIENSIIQAHENLRPGSIFLNNGELLDAGVNRSPSAYLNNPSKERSKHKYNVDKEMTLLKFVDDQWGPVGSFNWFATHGTSMSRTNSLISGDNKGAASRFMEDWYEQNTAERSYSEEFISDEIPRRVSSLIENHQDSHHELLELASYFESQPGKPVTRISSSARRVRSALRKADKPGFVSAFCQTNCGDVSPNVLGAFCLDTGLPCDFNHSTCGGKNEMCYGRGPGYPDEFESTRIIGERQFKMALELFNKASEQLQGKVDYRHVYVDFSQLNVTLPKKDGKSEVVKTCPAAMGFAFAAGTTDGPGAFDFTQGDDKGNPFWRLVRNVLKTPDKKQIDCHYPKPILLDTGEMTKPYDWAPSILSLQVLRIGQLFILSVPGEFTTMAGRRLRYAVKTQLKNSGNKDLSGEIHVVIAGLANGYSQYVTTFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLSKSLVLDMPVQPGPQPPDLLDKQLSFLTPVMMDTTPSGDSFGDVISDVPKNLSLKRGNGQVTVVFRSACPRNDLLTEGTFTLVERLEQKDKTWTPVYDDDDLCLRFKWSRHKKLSSRSQATVEWRIPESASPGVYRITHFGAAKKLFGSVHHFTGSSSAFVVT | 3.5.1.23 | null | cellular response to oxidative stress [GO:0034599]; ceramide catabolic process [GO:0046514]; intracellular sphingolipid homeostasis [GO:0090156]; long-chain fatty acid biosynthetic process [GO:0042759]; sphingosine biosynthetic process [GO:0046512] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325] | ceramidase activity [GO:0102121]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF04734;PF17048; | 2.60.40.2300; | Neutral ceramidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VA70}. Endoplasmic reticulum {ECO:0000269|PubMed:26150824}. Golgi apparatus {ECO:0000250|UniProtKB:Q0JL46}. | 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:O06769}; | null | null | null | null | FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates sphingolipid homeostasis. Promotes oxidative stress resistance. {ECO:0000269|PubMed:26150824}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HRI2 | HEI10_ARATH | MRCNACWRDLEGRAISTTCGHLLCTEDASKILSNDGACPICDQVLSKSLMKPVDINPNEEWINMAMAGISPQILMKSAYRSVMFYIAQRDLEMQYKMNRVVAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRSEYESVKRTAIQPANNFYPRHQEPDFFSNPAVNMMENRETIRKDRSFFSPATPGPKDEIWPARQNSSNSGPFDISTDSPAIPSDLGNRRAGRGHPVYGGGGTANPQSTLRNLILSPIKRSQLSRSRPQLFTL | 2.3.2.27 | null | chiasma assembly [GO:0051026]; homologous recombination [GO:0035825]; meiotic cell cycle [GO:0051321]; protein ubiquitination [GO:0016567]; reciprocal meiotic recombination [GO:0007131] | chiasma [GO:0005712]; chromosome [GO:0005694] | metal ion binding [GO:0046872]; transferase activity [GO:0016740] | PF14634; | 1.20.5.1000;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22844245}. Chromosome {ECO:0000269|PubMed:22844245}. Note=Dynamic localization on the meiotic chromosomes. Present as numerous foci on the chromosome axes and the synaptonemal complex central element until pachytene. From pachytene to diakinesis, restricted to a limited number of sites that correspond to class I crossovers. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis. {ECO:0000269|PubMed:22844245}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HRJ4 | M3K3A_ARATH | MPTWWGRKSCKNKDDNHRGIISTDRDIKSSAVVVDPPLTPTRGGTPRCSREFAGASSAFSGFDSDSTEKKGHPLPRPLLSPVSIHHQDHVSGSTSGSTSVSSVSSSGSADDQSQLVASRGRGDVKFNVAAAPRSPERVSPKAATITTRPTSPRHQRLSGVVSLESSTGRNDDGRSSSECHPLPRPPTSPTSPSAVHGSRIGGGYETSPSGFSTWKKGKFLGSGTFGQVYLGFNSEKGKMCAIKEVKVISDDQTSKECLKQLNQEINLLNQLCHPNIVQYYGSELSEETLSVYLEYVSGGSIHKLLKDYGSFTEPVIQNYTRQILAGLAYLHGRNTVHRDIKGANILVDPNGEIKLADFGMAKHVTAFSTMLSFKGSPYWMAPEVVMSQNGYTHAVDIWSLGCTILEMATSKPPWSQFEGVAAIFKIGNSKDTPEIPDHLSNDAKNFIRLCLQRNPTVRPTASQLLEHPFLRNTTRVASTSLPKDFPPRSYDGNFSLQPTREPYPGRLSHDNYAKQPLSRTIKSPSRENVRAITSLPVSPCSSPLRQLGPAYKSCFLSPPHPSYAFPGQDSGYNLAEFAASPFRMKKDAMMEPSSFRTQTPNSPLRSRLV | 2.7.11.25 | null | pattern recognition receptor signaling pathway [GO:0002221]; phosphorylation [GO:0016310]; regulation of defense response to bacterium [GO:1900424]; regulation of defense response to fungus [GO:1900150] | null | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | null | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q9C5H5}; 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q9C5H5}; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
F4HRT5 | CRWN1_ARATH | MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEWSSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANALVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQEGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKARELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALDRKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTEEERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERLKKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLFEEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSRFLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKMLKLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVAADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRKRGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEEGIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKVSIGKKLWTFLTT | null | null | nucleus organization [GO:0006997]; regulation of nucleus size [GO:0097298] | chromatin [GO:0000785]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | null | null | null | CRWN family | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}; Peripheral membrane protein {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:24667841}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (PubMed:24667841). Mostly localized at the nuclear periphery and, to a lesser extent, in the nucleoplasm (PubMed:17873096). Localized on the condensing chromatin during prometaphase to anaphase, but transferred from the decondensing chromatin to the reassembling nuclear envelope during early telophase. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. | null | null | null | null | null | FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:17873096, PubMed:23396599, PubMed:24308514, PubMed:24824484). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514, ECO:0000269|PubMed:24824484}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HRV8 | ASY1_ARATH | MVMAQKLKEAEITEQDSLLLTRNLLRIAIFNISYIRGLFPEKYFNDKSVPALDMKIKKLMPMDAESRRLIDWMEKGVYDALQRKYLKTLMFSICETVDGPMIEEYSFSFSYSDSDSQDVMMNINRTGNKKNGGIFNSTADITPNQMRSSACKMVRTLVQLMRTLDKMPDERTIVMKLLYYDDVTPPDYEPPFFRGCTEDEAQYVWTKNPLRMEIGNVNSKHLVLTLKVKSVLDPCEDENDDMQDDGKSIGPDSVHDDQPSDSDSEISQTQENQFIVAPVEKQDDDDGEVDEDDNTQDPAENEQQLARVKDWINSRHLDTLELTDILANFPDISIVLSEEIMDQLVTEGVLSKTGKDMYIKKRDKTPESEFTFVKEEADGQISPGKSVAPEDYLYMKALYHSLPMKYVTITKLHNMLDGEANQTAVRKLMDRMTQEGYVEASSNRRLGKRVIHSSLTEKKLNEVRKVLATDDMDVDVTETINKTNGPDAKVTADVSTCGGIHSIGSDFTRTKGRSGGMQQNGSVLSEQTISKAGNTPISNKAQPAASRESFAVHGGAVKEAETVNCSQASQDRRGRKTSMVREPILQYSKRQKSQAN | null | null | chiasma assembly [GO:0051026]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic recombination checkpoint signaling [GO:0051598]; synaptonemal complex assembly [GO:0007130] | chromatin [GO:0000785]; chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794]; nucleoplasm [GO:0005654] | null | PF02301; | 3.30.900.10; | null | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12186950}. Nucleus {ECO:0000269|PubMed:12186950}. Note=During interphase-early leptotene, distributed as numerous punctuate foci throughout the chromatin. At zygotene and pachytene, shows a continuous localization along chromosomal axes. {ECO:0000269|PubMed:12186950}. | null | null | null | null | null | FUNCTION: Required for normal meiosis in male and female gametophytes. Plays a crucial role in coordinating the activity of DMC1, a key member of the homologous recombination machinery (PubMed:18504359). Acts at the interface between the developing chromosome axes and the recombination machinery to ensure DMC1-mediated interhomolog recombination (PubMed:17785529). {ECO:0000269|PubMed:17785529, ECO:0000269|PubMed:18504359}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HS99 | REC1_ARATH | MAPKNNRGKTKGDKKKKEEKVLPVIVDVIVNLPDETEAILKGISTDRIIDVRRLLSVNFDTCHVTNYSLSHEIRGSRLKDTVDVSALKPCVLTLTEEDYNEGTAVAHVRRLLDIVACTTCFGPSPEKSDSVKSAQVKGGGKNSKQSDTSPPPSPASKDTVVDEAGETSHSFPKLGSFYEFFSLAHLTPPLQYIRLATKRETEDIAKEDHLLSIDVKLCNGKLVHIEGCRKGFYSIGKQRIICHNLVDLLRQISRAFDNAYSDLLKAFSERNKFGNLPYGFRANTWLIPPTAAQSPAAFPPLPVEDERWGGDGGGQGRDGSYDLVPWSNEFAFIASMPCKTAEERQVRDRKVFLLHNLFVDVATFRAIKAVQKVMAEPVLAEEDSEVLYSETVRDLTVTVTRDTSNASSKVDTKIDGIQATGLDKKKLMERNLLKGLTADENTAAHDVATLGTISLKYCGYIAVVKLEKESEELSPPSQIVDLLEQPEGGANALNINSLRFLLHKSSPEQNKKTPQQHDDELTSSREFVSKMLEESIAKLEGEEIDRDSIMRWELGACWIQHLQDQKNTEKDKKQTGEKSKNELKVEGLGKPLKSLNSSKKKTDVSSPKTPQTALSSQVDAVSSEADTAASLQSDAEKNAQENVLILKNLLSDAAFTRLKESDTGLHHKSLQELVDLAQNYYTEVAIPKLVADFGSLELSPVDGRTLTDFMHTRGLRMRSLGYVVKLSDKLSHVQSLCVHEMIVRALKHILQAVISAVATDTDKIAIKVAAALNMMLGIPENVAATPHNPWNVHPLIFRWLEKFLKKRYDYDLNAFSYKDLRKFAILRGLCHKVGIELIPRDFDMDSPAPFRKTDVVSLVPVHKTFYFKSMQQAACSSADGRQLLESSKTALDKGKLEDAVTYGTKALAKLVAVCGPYHRMTAGAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLAVFYYRLQHTELALKYVKRALYLLHLTCGPSHPNTAATYINVAMMEEGLGNVHVALRYLHKALKCNQRLLGPDHIQTAASYHAIAIALSLMEAYHLSVQHEQTTLRILRAKLGPDDLRTQDAAAWLEYFESKAFEQQEAARNGTPKPDASIASKGHLSVSDLLDYINPSHNAKGKESVAAKRKNYILKLKEKSKQSNVSEHLVEIPREKQKEMSEEDTEETGSEEGKSSEENHETILAPVEEPPSPPVIEDATMDNSNPITSSDVSTEPQHPDGSEDGWQPVQRPRSAGSYGRRMKQRRASIGKVYTYQKKNVEADIDNPLFQNATQQNDKYYILKKRTASYSSYADHHSPGLTTQGTKFGRKIVKTLAYRVKSTQPSSGNAKTAGETSEEDGLKTDASSVEPPTLSSTVQSEAYHTKNSVVSLGKSPSYKEVALAPPGSIAKYQVWVPQAEVSDKQEDDEMEKKTEQGTSMELTRDEQMITGLEEEVKKEISADPESNITQGEEEIKVELQPSEGVLGGSHINENDESGGGIQVEEQVEVELINDGVTDMIHSTREQQVIDQLAADSEDLKAKLSISTTDSGDASRGLLPNKKLSASAAPFNPSSPPSIIRPTPIGMNIGPSWPVNMTLHHGPPPPYPSPPTTPNLMQPMSFVYPPPYSQSVPTSTYPVTSGPFHPNQFPWQLNVSDFVPRTVWPGCHPVEFPPPHMITEPIAATVLEPTVILPTDIDTSGVEETKEGTQDVAVADEVMDSVNHVNNAVARSETENGNRKSEEGEKTFSILLRGRRNRKQTLRMPISLLNRPYDSQPFKLGYSRVIRDSEAPKSVA | null | null | chloroplast localization [GO:0019750]; organelle organization [GO:0006996]; regulation of glucose metabolic process [GO:0010906] | cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634] | mRNA binding [GO:0003729] | PF15044;PF12807;PF13424; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26862170}. Cytoplasm, cytosol {ECO:0000269|PubMed:26862170}. Note=Excluded from the nucleus upon treatment with amitrole, which inhibits cell expansion and chloroplast function. {ECO:0000269|PubMed:26862170}. | null | null | null | null | null | FUNCTION: May act as the scaffold of a protein complex, which sequesters key factors that are required for the G2 to M transition in meristematic tissues (By similarity). Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment (PubMed:26862170). {ECO:0000250|UniProtKB:F4JKH6, ECO:0000269|PubMed:26862170}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HT77 | RBA1_ARATH | MTSVSPRYRNVPVPKVFLSFRGEEIRHGFISHLADALERYGIMFIIDKDEQRGNDLTSLLLRIKESKVALVIFSSRFAESRFCMDEIVKMKECVDERKLLVIPIFYKVRARDVSGRTGDFGKKFWALAQKSRGCQIKEWMEALECISNKMGLSLGDGRSEADFIKEIVKEVERVLATFTSEDTEDHHCQTVKLLKGLVVGCLAHQELPLVLVFTQVYYYVKFSIFFIEEIFSSCFRKGFVLKPCKEDLQINSISIPGIDLENFKNMMQQAMYELNQMLLQSLGNIDPHRDVAFENQPQDQPDSPIALPEERRVALEATKFCGHAAYWWNQTKTTRARIGKVLIHFWEKLKKKFKDTYDRTVRI | 3.2.2.-; 3.2.2.6 | null | cAMP biosynthetic process [GO:0006171]; cGMP biosynthetic process [GO:0006182]; defense response [GO:0006952]; defense response by callose deposition [GO:0052542]; DNA catabolic process [GO:0006308]; induction of programmed cell death [GO:0012502]; NAD catabolic process [GO:0019677]; NADP catabolic process [GO:0006742]; positive regulation of plant-type hypersensitive response [GO:0034052]; positive regulation of programmed cell death [GO:0043068]; RNA catabolic process [GO:0006401]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | hydrolase activity [GO:0016787]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | PF01582; | 3.40.50.10140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28137883}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28137883}. Note=Forms aggregate-like cyto-nucleoplasmic puncta. {ECO:0000269|PubMed:28137883}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000269|PubMed:31439793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:31439793}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:31439793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000269|PubMed:31439793}; | null | null | null | null | FUNCTION: Disease resistance (R) protein that specifically recognizes the HopBA1 type III effector protein from P.syringae, and triggers cell death (PubMed:28137883). Acts as a NAD(+) hydrolase (NADase): in response to pathogen-recognition, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439793). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which the cyclizing bond is unknown (PubMed:31439793). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:31439793). {ECO:0000269|PubMed:28137883, ECO:0000269|PubMed:31439793}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HTH8 | KTN82_ARATH | MAKRGYKLQEFLAHSANVNCLSIGKKTSRLFITGGDDYKVNLWAIGKPTSLMSLCGHTSAVDSVAFDSAEVLVLAGASSGVIKLWDVEEAKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDANLKIWDIRKKGCIQTYKGHSRGISTIRFTPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKFHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGSTRPEATGVRSIKFHPDGRTLFCGLDDSLKVYSWEPVVCHDGVDMGWSTLGDLCISEGKLLGCSYYQNSVGIWVSDISQIEPYGIGSADKKECVEKILSALDDQSFDRIKSTPRRSSSPDYETKEIKNIYIDSTGGNSAVAHKSGSLSTPATSTGQAGDNKSLVVHSVVPRDSDIGKDSSDSGKESITFSKTKPGMLLRPAYVRKTPTKFDETKKQSVAVGYLKKSGLDGEKKLDTETAFDSEMSGRNPYDADDSIIKSITNKFEQALLPESPTDEAKCMLLKPPRVQRSPSTKYNEARWATSTDSGALDSKKNGLESSRDMDLPTGLRDDRGSNPCEEDIENKSISSRSERVLSPEKAGDELKSLESPGGSKESKSVKVVRGVKVVSGRTRSLVERFERGEKITHSEDKAASATVVHSSNSVEEEPLTASVQTVSMMPTQVMPVKLDQATNSTTVDVPVLSTRRTKSTPVRVMPVVLGRDTSMATDTPPVTSTRPDRTSATNLTSDVSGVTSKRQTRTSPAPVMPMILNQTTKMKSDEPSITSTWPDRTSATDLTSDVSGVISSRQTRTSPAPVMPMKLNQKTKIKSDEPPITSTRPDRPSATNLTSDESPVTSTRQAKTSPAPVTPVILNQRQTTNMKSDEPPVISTRPLRTSSARVMPVILNQASTTYDERPLSSSRSARTSPARIMPMKLNQADNMPSYEPPVALTRSARNSPARVIPVKLNQATNVTADASHIRSRQRFSPTQTLATPAVFDQVTDMTLDETTKTQQSSDILTQKEEPQISGREDDGDIWEILMRTHSEVLNTLQSRLTKLQIVRHFWERSDIKGAIAALRKLSDHSVQADVINILTDKTEILTLDLFSQLAPVLTGLLGSKTERPVNVSLEMLLKLVAVFGTVIQSTVSARRVVGVDLHAEERLQICQSCSAELQKVQKILPLLTRRGGLIARKAQELNLVLQTP | null | null | microtubule depolymerization [GO:0007019]; microtubule severing [GO:0051013]; regulation of unidimensional cell growth [GO:0051510]; response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651] | Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; katanin complex [GO:0008352]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630] | microtubule binding [GO:0008017] | PF13925;PF00400; | 2.130.10.10; | WD repeat KATNB1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites. {ECO:0000269|PubMed:28978669}. | null | null | null | null | null | FUNCTION: May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites (PubMed:28978669). Together with other KTN80s, regulates cell elongation by modulating MT organization (PubMed:28978669). Negative regulator of abscisic acid (ABA) responses (PubMed:21421380). May function as a substrate receptor for cullin-RING ubiquitin ligase 4 complexes (CRL4), a family of E3 ligases involved in protein degradation (PubMed:21421380). {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:21421380, ECO:0000269|PubMed:28978669}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HTM3 | GCS1_ARATH | MTGASRRSARGRIKSSSLSPGSDEGSAYPPSIRRGKGKELVSIGAFKTNLKILVGLIILGIIVIYFVINRLVRHGLLFDESQKPRVITPFPAPKVMDLSMFQGEHKESLYWGTYRPHVYFGVRARTPLSLVAGLMWLGVKDEMYVMRHFCENSDDLSTFGWREHNGRDYGRQELVENDMVIETSFVKSKGDGLGYGGDWAVRIDVKNKGLNDDVKRSAHLFFYLADEGGNVLNLGQDGLDFQGSSLLVSGSREDVGDWQIHLKSQNQLETHYSGFKTPHIYNLSDLVQQNLALQARKFGRLQLSDTSEDSSNIYIFQISGRLPFTIDIPFISGIKGESSNVEKRLTSLTGLPLSDLLKKKHQEFDAKFNECFKLSEKHDSETLGVGRTAIANMLGGIGYFYGQSKIYVPKSTQPGSRDNFLLYWPAELYTAVPSRPFFPRGFLWDEGFHQLLIWRWDIRITLDIVGHWLDLLNIDGWIPREQILGAEALSKVPEEFVVQYPSNGNPPTLFLVIRDLIDAIRMEKFVASEKDEVLSFLERASVRLDAWFQWFNTSQKGKEIGSYFWHGRDNTTTQELNPKTLSSGLDDYPRASHPSEDERHVDLRCWMYLAADCMHSITELLGKEDKLSKENYNSTVKLLSNFNLLNQMHYDSDYGAYFDFGNHTEKVKLIWKEVIQENGQLSRQLVRKTFGKPKLKLVPHLGYVSFFPFMSRIIPPDSPILEKQLDLISNRSILWSDYGLVSLAKTSSMYMKRNTEHDAPYWRGPIWMNMNYMILSSLYHYSIVDGPYREKSKAIYTELRSNLIRNVVRNYYETGYIWEQYDQVKGTGKGTRLFTGWSALTLLIMSEDYPIF | 3.2.1.106 | null | epidermal cell differentiation [GO:0009913]; oligosaccharide metabolic process [GO:0009311]; protein N-linked glycosylation [GO:0006487]; root epidermal cell differentiation [GO:0010053] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739] | alpha-1,4-glucosidase activity [GO:0004558]; Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [GO:0004573] | PF03200;PF16923; | 1.50.10.10;2.70.98.110; | Glycosyl hydrolase 63 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17138701, ECO:0000269|PubMed:19995436}; Single-pass type II membrane protein {ECO:0000269|PubMed:17138701, ECO:0000269|PubMed:19995436}. | CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082, ChEBI:CHEBI:132537; EC=3.2.1.106; | null | PATHWAY: Glycan metabolism; N-glycan degradation. | null | null | FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor. Required for the accumulation of seed storage proteins, the formation of protein bodies, cell differentiation, cellulose biosynthesis and organization (in cell walls), cell shape determination and organization (e.g. epidermal cells), and embryo development. Involved in root development. {ECO:0000269|PubMed:11230125, ECO:0000269|PubMed:11901167, ECO:0000269|PubMed:18503769}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HU51 | ACH2_ARATH | MNTESVVEFLGNVPLLQKLPSSSLKKIAQVVVPKRYGKGDYVVREDQTWDGCYFILQGEAQVSGPDEEDNRSEFLLKQYDYFGVGLSGNVHSADIVAMSQLTCLVLPRDHCHLLETNSIWQSDTSLDKCSLVERILQLDPLELNIFRGITLPDAPIFGKVFGGQFVGQALAAASKTVDFLKVVHSLHSYFLLVGDIDIPIIYQVHRIRDGNNFATRRVDAVQKGNIIFILLASFQKEQQGFEHQESTMPSVPDPDTLLSLEELRESRITDPHLPRSYRNKVATRNFVPWPIEIRFCEPSNSTNQTKSPPRLNYWFRAKGRLSDDQALHRCVVAFASDLIFCGVGLNPHRRKGVKSAALSLDHAMWFHRPLRADEWLLYVIVSPTAHETRGFVTGQMFNRKGELVVSLTQEALLREARPPKPSGTSKL | 3.1.2.2; 3.1.2.20 | null | acyl-CoA metabolic process [GO:0006637]; fatty acid catabolic process [GO:0009062]; protein homotetramerization [GO:0051289] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; medium-chain fatty acyl-CoA hydrolase activity [GO:0052815] | PF13622;PF02551;PF00027; | 2.40.160.210;2.60.120.10; | C/M/P thioester hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:O14734}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000250|UniProtKB:O14734}. | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20; Evidence={ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000269|PubMed:14660652}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000269|PubMed:14660652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000269|PubMed:14660652}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.8 uM for 18:1-CoA {ECO:0000269|PubMed:14660652}; KM=17.8 uM for 12:0-CoA {ECO:0000269|PubMed:14660652}; Vmax=13 umol/min/mg enzyme with 18:1-CoA as substrates {ECO:0000269|PubMed:14660652}; Vmax=14.5 umol/min/mg enzyme with 12:0-CoA as substrates {ECO:0000269|PubMed:14660652}; Vmax=21 umol/min/mg enzyme with 16:1-CoA as substrates {ECO:0000269|PubMed:14660652}; | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0.; | null | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:11171266, PubMed:14660652). Active with both medium chain and long chain acyl-CoAs (e.g. 12:0-CoA, 14:0-CoA, 16:0-CoA, 18:0-CoA, 16:1-CoA, 18:1-CoA, 18:2-CoA and 20:4-CoA) as substrates, palmitoleoyl-CoA (16:1-CoA) being the favorite substrate (PubMed:11171266, PubMed:14660652). {ECO:0000269|PubMed:11171266, ECO:0000269|PubMed:14660652}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HU55 | BSK4_ARATH | MGGQSSKIGTCCSHKTTALEAPDVENKENGEVNGVHSFREYSLEQLKIATSCFALENVVSEHGETAPNVVYQGKLENHMKIAIKRFSGTAWPDPRQFLEEARLVGQLRSKRMANLLGYCCEGGERLLVAEFMPNETLAKHLFHWDTEPMKWAMRLRVALYISEALEYCSNNGHTLYHDLNAYRVLFDEECNPRLSTFGLMKNSRDGKSYSTNLAFTPPEYLRTGRITAESVIYSFGTLLLDLLTGKHIPPSHALDLIRDRNLQTLTDSCLEGQFSDSDGTELVRLTSCCLQYEARERPNIKSLVTALISLQKDTEVLSHVLMGLPQSGTFASPPSPFAEACSGKDLTSMVEILEKIGYKDDEDLSFMWTEQMQEAINSKKKGDIAFRRKDFSEAIEFYTQFLDLGMISATVLVRRSQSYLMSNMAKEALDDAMKAQGISPVWYVALYLQSAALSVLGMEKESQIALTEGSILEARKISASTQN | 2.7.11.1 | null | brassinosteroid mediated signaling pathway [GO:0009742]; phosphorylation [GO:0016310] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF07714; | 1.25.40.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12912986}; Lipid-anchor {ECO:0000305|PubMed:12912986}. | 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}; 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}; | null | null | null | null | FUNCTION: Probable serine/threonine kinase that acts as a positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK6, BSK7 and BSK8. {ECO:0000269|PubMed:23496207}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HU58 | TAD1_ARATH | MEEDWGKTVSEKVISAYMSLPKKGKPQGREVTVLSAFLVSSPSQDPKVIALGTGTKCVSGSLLSPRGDIVNDSHAEVVARRALIRFFYSEIQRMQLTSGKSNEAKRQRIDSETSSILESADSSCPGEVKYKLKSGCLLHLYISQLPCGYASTSSPLYALKKIPSTQVDDSLLVQASDICSSRHSDVPEIGSNSNKGNGSQVADMVQRKPGRGETTLSVSCSDKIARWNVLGVQGALLYQVLQPVYISTITVGQSLHSPDNFSLADHLRRSLYERILPLSDELLTSFRLNKPLFFVAPVPPSEFQHSETAQATLTCGYSLCWNYSGLHEVILGTTGRKQGTSAKGALYPSTQSSICKQRLLELFLKETHGHKRESSKSKKSYRELKNKATEYYLMSKIFKGKYPFNNWLRKPLNCEDFLIN | 3.5.4.34 | COFACTOR: Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130; Evidence={ECO:0000250|UniProtKB:P53065}; Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit. {ECO:0000250|UniProtKB:P53065}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | adenosine to inosine editing [GO:0006382]; tRNA modification [GO:0006400] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634] | double-stranded RNA adenosine deaminase activity [GO:0003726]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; tRNA-specific adenosine deaminase activity [GO:0008251]; tRNA-specific adenosine-37 deaminase activity [GO:0043829] | PF02137; | null | ADAT1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23355609}. | CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855, Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34; Evidence={ECO:0000269|PubMed:23355609}; | null | null | null | null | FUNCTION: Involved in RNA editing. Catalyzes the specific deamination of adenosine-37 in the cytosolic tRNA-Ala. Generates inosine at the position 3'-adjacent to the anticodon tRNA-Ala. {ECO:0000269|PubMed:23355609}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVA6 | TAF6B_ARATH | MVTKESIEVIAQSIGLSTLSPDVSAALAPDVEYRVREVMQVYHQLQLYFCPLISSLTCRRNLQEAIKCMRHARRTTLMAHDVDSALHFRNLEPTSGSKSMRFKRAPENRDLYFFDDKDVELKNVIEAPLPNAPPDASVFLHWLAIDGIQPSIPQNSPLQAISDLKRSEYKDDGLAARQVLSKDLQIYFDKVTEWALTQSGSTLFRQALASLEIDPGLHPLVPFFTSFIAEEIVKNMDNYPILLALMRLARSLLHNPHVHIEPYLHQLMPSIITCLIAKRLGRRSSDNHWDLRNFTASTVASTCKRFGHVYHNLLPRVTRSLLHTFLDPTKALPQHYGAIQGMVALGLNMVRFLVLPNLGPYLLLLLPEMGLEKQKEEAKRHGAWLVYGALMVAAGRCLYERLKTSETLLSPPTSSVWKTNGKLTSPRQSKRKASSDNLTHQPPLKKIAVGGIIQMSSTQMQMRGTTTVPQQSHTDADARHHNSPSTIAPKTSAAAGTDVDNYLFPLFEYFGESMLMFTPTHELSFFL | null | null | RNA polymerase II preinitiation complex assembly [GO:0051123] | SAGA complex [GO:0000124]; SLIK (SAGA-like) complex [GO:0046695]; transcription factor TFIID complex [GO:0005669] | protein heterodimerization activity [GO:0046982]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; transcription coactivator activity [GO:0003713] | PF02969;PF07571; | 1.10.20.10;1.25.40.770; | TAF6 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Not redundant with TAF6. {ECO:0000269|PubMed:16039640}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVG8 | CSK_ARATH | MLLSAIASQTLLSSNPNLHFSNSIPNPRPSNPSLKLLNASSSSSSSSSSSIFTRGLRYVNHTVSNEESEPGGGETMVASASAIASAIRGASTTPVEFTQMIEKDHLKTKIILPSPDFQRLCLEQLDLFRQIVDPNAVLSIYVRPAGSYVMDRLELRRVTCYPSVNAGDVVILVGNFGIPAGLRAAEASLSSQQVELVSKHRAAVFPMVKHPFVVGFLVAELPVEAEEEEEEEEEEKPHGVNQFLSPEEAYALPASANTKSPRVKLPSVKVFTEEQRSYAINISRTLAMAYVMDQKTMLLQQSSWQNNVRMSKLVEQIRGPLSTMRTLSKMLSTHTKRNQISHDIVEDLIVQGDQIKDTLEELQDAVHLTKANIVRHNEEALKKINKTHNETRRSKYEHKDPIDGSQISSTRLSLGSGLDDSEMPMPPLALAPLQMHSIRPCDISNVLLDMVETVRPLALTQQRVVELGENSASLQVAVEEPALRQALSNLIEGALLRTHVGGKVEILSTRAPAGGSLVVIDDDGPDMRYMTQMHSLTPFGAELLSENMVEDNMTWNFVAGLTVAREILESYGCVIRVISPRSSDAALGAGGTRVELWLPAFPAAVSEANEA | 2.7.10.2 | COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:31925322}; Note=The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer. {ECO:0000269|PubMed:31925322}; | detection of redox state [GO:0051776]; photosystem stoichiometry adjustment [GO:0080005]; protein autophosphorylation [GO:0046777]; regulation of gene expression [GO:0010468]; regulation of photosynthesis [GO:0010109] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570] | 3 iron, 4 sulfur cluster binding [GO:0051538]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein histidine kinase activity [GO:0004673]; protein self-association [GO:0043621]; quinone binding [GO:0048038] | PF02518; | 3.30.565.10; | Chloroplast sensor kinase protein family | PTM: Autophosphorylated, possibly on tyrosine residues, in photosystem I (PS I) light and in the presence of manganese ions Mn(2+), to a lesser degree, in the presence of calcium ions Ca(2+), but not in the presence of magnesium ions Mg(2+). Dithiothreitol (DTT) stimulates autophosphorylation (PubMed:18632566). Phosphorylated on Ser-188 in vivo after exposure to far-red light (when plastoquinone (PQ) is oxidized). Not phosphorylated under orange light (reduces PQ) (PubMed:31925322). {ECO:0000269|PubMed:18632566, ECO:0000269|PubMed:31925322}. | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18632566}. Note=Associates with thylakoid membranes. {ECO:0000305|PubMed:31925322}. | 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=2.7.10.2; Evidence={ECO:0000305|PubMed:18632566}; | null | null | null | null | FUNCTION: Sensor kinase that senses the plastoquinone (PQ) redox state involved in stoichiometry adjustment of both photosystems (e.g. long-term adaptation via transcriptional regulation of reaction center genes of photosystems I and II) and state transitions (e.g. short-term adaptation involving reversible post-translational phosphorylation of light-harvesting complex II, LHC II), thus linking photosynthesis with gene expression in chloroplasts (PubMed:18632566, PubMed:22039472). Autophosphorylates, probably on a tyrosine residue (PubMed:18632566). Probably phosphorylates SIGA/SIG1 in response to plastoquinone redox state modification (PubMed:23754813). Reduced PQ suppresses its autophosphorylation activity. Represses expression of a number of chloroplast-encoded genes (PubMed:31925322). {ECO:0000269|PubMed:18632566, ECO:0000269|PubMed:22039472, ECO:0000269|PubMed:23754813, ECO:0000269|PubMed:31925322}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVJ3 | POD1_ARATH | MAIRSSGRKLSFEILSQNSSFENDDTSIRRSSSDPITGNVASESPRDYGKRKRSKKKKKKVNQVETILENGDSHSTIITGSSGDFGETTTMFENRLNYYGGGGSGSSGGGCVVTLLDGQTVHHNGFNFGELRQRNVNGSVDGSNDERWSDTLSSDKKLYMEETSVELSPSENPPFQEVQHQFPRSEINGNVVRRLDTEASLDWKQLVADDPDFLSAETRSPMKYFMEEIYGGISLRSTTTPGNDIERERIYDTIFRLPWRCEVLIDTGFFVCVNSFLSLLTVMPIRVLLIFMDAFKNRQFRRPSASELSDLACFLVLATGTILLGRTDISLIYHMIRGQSTIKLYVVYNILEIFDRLCQSFCGDVFGALFSSAKGLSISPPEKLRFSTWRFVSDLALTMAASILHSFILLAQAITLSTCIVAHNNALLALLVSNNFAEIKSSVFKRFSKDNIHGLVYADSIERFHISAFLVSVLAQNILESEGAWFGNFIYNATTVFFCEMMIDIIKHSFLAKFNDIKPIAYSEFLQALCEQTLNIRPEDRKTNLTFVPLAPACVVIRVLTPVYAAHLPYSPLPWRMLWMVILFVITYIMLTSLKVLIGMGLRKHATWYINRCRRRNSSHLHND | null | null | embryo development ending in seed dormancy [GO:0009793]; maintenance of protein localization in endoplasmic reticulum [GO:0035437]; pollen tube guidance [GO:0010183]; positive regulation of cilium assembly [GO:0045724] | endoplasmic reticulum lumen [GO:0005788]; membrane [GO:0016020] | null | PF05346; | null | TAPT1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:21954464}. Note=Exclusive ER lumen localization and no membrane localization in PubMed:21954464. | null | null | null | null | null | FUNCTION: Probable component of the calreticulin 3 (CRT3) complex, acting probably as a co-chaperone involved in protein retention in the endoplasmic reticulum lumen. Required for micropylar pollen tube guidance. Plays an essential role in cell plate orientation or positioning in early embryo patterning. {ECO:0000269|PubMed:21954464}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVS0 | BTSL2_ARATH | MGGGNLHSLPPENASVSASYAVTVGNTKLSDAPVLFFVYCHKAFRAQLVELRRFATDAAEADSFSGDLAVELSRKFEFLKLVYKYHSAAEDEVIFLALDKRVKNIVSNYSLEHAGTDDLFTSIFHWLHVLEEEIGSRSDVLREVILCIGTIQSSICQHMLKEERQVFPLLIEKFSFREQASLVWQFICSVPVMVLEDFLPWMISHLSHEEKIEVENCIKDVAPNEDSLQQVISSWLLDDSQSSCGTPTEIMKGVQYVNVSKSLKKSPESHPSSGCFQRFWEWSKKSLSIPNVGRSPIHGLRLFQNAIEKDLRDIQEGLCQAKFQTLILDLDVLMARLNFLADVLVSYSNAFKKFFHPVLEEMTARRSSTAKQFNIDDCLENFQRLLYKSADDKTKTDNFLLQLQEELESLIIQVTKQFAIQRTEVFPIISKNCNHEMQKQLLYTSIHVLPLGLLKCVILWFSAHLSEEESQSILHFLSLEDSSPKKSFPRLLLQWLRFGYSGKTSVERFWKQLDVMFKVRCSCQKEHTEEASGSFSNQTQLQLCKVSKDVYPRKKDKSSTCFMSMDLAVGDMYETPYSSRMNQQMTFSGKLKPPLHLPDFFGEKNMDDPMIMDVKPIDLLFFFHKAMKMDLDYLVCGSTRLAADFRFLAEFQQRFHMIKFLYQIHSDAEDEIAFPALEAKGQLKNISHSFSIDHELETKHFDKVSFILNEMSELNMLVSTINTTAADHDRKMKYERLCLSLREICKSMHKLLSEHIQHEETELWGLFRNCFSIEEQEKIIGCMLGRISGEILQDMIPWLMESLTSDEQLAAMSLWRQATRKTMFVEWLTEWYNGHVLQEEAGEANNDPFGDSDPLEIVWKYLFEASADGEKGSMRSSLLKLPKTNFTGIMNQPPPNYKVEVGKKEEKDLERSESKKICRGSNQEGDKEQTDKMSQKVSQFGPSKKYEQLLTMSEEELVVVIKKISCDSSLDPQKKDYIKQNLLMSRWNISQRTYNLEPSSLSSNMETVHGQHPSYRDPHSLIFGCNHYKRNCKLLAPCCDKLFTCIRCHDEEADHSVDRKQITKMMCMKCLLIQPIGANCSNTSCKSSMGKYFCKICKLYDDERKIYHCPYCNLCRVGKGLGIDYFHCMKCNACMSRTLVEHVCREKCLEDNCPICHEYIFTSSSPVKALPCGHLMHSTCFQEYTCSHYTCPVCSKSLGDMQVYFKMLDALLAEEKMPDEYSNKTQVILCNDCGRKGNAPYHWLYHKCTTCGSYNSRLL | null | null | intracellular iron ion homeostasis [GO:0006879]; iron import into cell [GO:0033212]; iron ion import across plasma membrane [GO:0098711]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of iron ion transport [GO:0034756] | membrane [GO:0016020]; nucleus [GO:0005634] | ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01814;PF05495;PF13639;PF14599; | 2.20.28.10;1.20.120.520;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q8LPQ5}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Probable E3 ubiquitin-protein ligase that may regulate the response to iron deficiency and thus contributes to iron homeostasis. {ECO:0000250|UniProtKB:Q8LPQ5}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVW5 | VAD1_ARATH | MAMLSTASVSGSVDLPRGTMKVDSSASPEVVSDLPPSSPKGSPDRHDPSTSSPSPSRGGDNQSEVISKSEEYRQLFRLPADEILVQDFNCACQESILMQGHMYLFIHYICFYSNIFGYETKKIIPFAEISCVKRAKTAGIFPNAIEILAGGKKYFFASFLSRDEAFKLIHDGWLEYGSAVKSEGEILVTEPQVSDGVVKRARSSMDLANELDIPVRDETLHLSSSSSLPVISQNGVPPSSVQRHAEPDVDVVAANTFNWKPEDTDAPKLSSDFTKVAEAKFSIPVEEFFRLFFSDGAVSFVESFHKNCGDKEFRCTSWQPHEKLGHTRNVSFQHPIKIYFGAKFGGCQESQKFRMYRNSHLVIETSQEISDVPYADYFTVEGVWDLKRDCRDSVEGCILDVYVNVAFSKRTVWKGKIVQSTLEECREAYAHWIRMAHELLKQKKLENQEGNKLIEDGEPLAAREERVSECDEEGKVEMVGEGVVKKSLKEAWVNLTSFVKRQSGTRQVIVLAFAVILLMQVTIVVLLKKGGGGQVEYHERYDEYSVNGETLGWLEKRMHFLREEMMMVEDRLQRMRQDHAALKAQFHHLERLLRRNKQ | null | null | defense response to bacterium [GO:0042742]; ethylene-activated signaling pathway [GO:0009873]; negative regulation of programmed cell death [GO:0043069]; plant-type hypersensitive response [GO:0009626]; response to ethylene [GO:0009723]; response to salicylic acid [GO:0009751] | chloroplast [GO:0009507]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020] | null | PF02893;PF16016; | 2.30.29.30; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Plastid, chloroplast {ECO:0000255}. | null | null | null | null | null | FUNCTION: Involved in ethylene- and salicylic acid-dependent cell death control associated with cells in the vicinity of vascular bundles. {ECO:0000269|PubMed:15269331, ECO:0000269|PubMed:17720753}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HVY0 | CER1_ARATH | MATKPGVLTDWPWTPLGSFKYIVIAPWAVHSTYRFVTDDPEKRDLGYFLVFPFLLFRILHNQVWISLSRYYTSSGKRRIVDKGIDFNQVDRETNWDDQILFNGVLFYIGINLLPEAKQLPWWRTDGVLMAALIHTGPVEFLYYWLHKALHHHFLYSRYHSHHHSSIVTEPITSVIHPFAEHIAYFILFAIPLLTTLLTKTASIISFAGYIIYIDFMNNMGHCNFELIPKRLFHLFPPLKFLCYTPSYHSLHHTQFRTNYSLFMPLYDYIYGTMDESTDTLYEKTLERGDDIVDVVHLTHLTTPESIYHLRIGLASFASYPFAYRWFMRLLWPFTSLSMIFTLFYARLFVAERNSFNKLNLQSWVIPRYNLQYLLKWRKEAINNMIEKAILEADKKGVKVLSLGLMNQGEELNRNGEVYIHNHPDMKVRLVDGSRLAAAVVINSVPKATTSVVMTGNLTKVAYTIASALCQRGVQVSTLRLDEYEKIRSCVPQECRDHLVYLTSEALSSNKVWLVGEGTTREEQEKATKGTLFIPFSQFPLKQLRRDCIYHTTPALIVPKSLVNVHSCENWLPRKAMSATRVAGILHALEGWEMHECGTSLLLSDLDQVWEACLSHGFQPLLLPHH | 4.1.99.5 | null | alkane biosynthetic process [GO:0043447]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; response to water deprivation [GO:0009414]; sterol biosynthetic process [GO:0016126]; wax biosynthetic process [GO:0010025] | endoplasmic reticulum membrane [GO:0005789] | aldehyde oxygenase (deformylating) activity [GO:1990465]; C-4 methylsterol oxidase activity [GO:0000254]; iron ion binding [GO:0005506]; octadecanal decarbonylase activity [GO:0009924] | PF12076;PF04116; | null | Sterol desaturase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19892830, ECO:0000269|PubMed:22773744}; Multi-pass membrane protein {ECO:0000269|PubMed:19892830, ECO:0000269|PubMed:22773744}. | CATALYTIC ACTIVITY: Reaction=a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+); Xref=Rhea:RHEA:21440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17176, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83563; EC=4.1.99.5; Evidence={ECO:0000269|PubMed:21386033, ECO:0000269|PubMed:22773744}; | null | null | null | null | FUNCTION: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex. Involved in epicuticular wax biosynthesis and pollen fertility. {ECO:0000269|PubMed:21386033, ECO:0000269|PubMed:22773744, ECO:0000269|PubMed:8718622}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HW04 | DPOE1_ARATH | MSGDNRRRDRKDTRWSKKPKVVNTAEDELESKLGFGLFSEGETRLGWLLTFSSSSWEDRDTGKVYSCVDLYFVTQDGFSFKTKYKFRPYFYAATKDKMELELEAYLRRRYERQVADIEIVEKEDLDLKNHLSGLQKKYLKISFDTVQQLMEVKRDLLHIVERNQAKFDALEAYESILAGKREQRPQDCLDSIVDLREYDVPYHVRFAIDNDVRSGQWYNVSISSTDVILEKRTDLLQRAEVRVCAFDIETTKLPLKFPDAEYDQIMMISYMVDGQGFLIINRECVGEDVEDLEYTPKPEFEGYFKVTNVKNEVELLQRWFYHMQELKPGIYVTYNGDFFDWPFIERRASHHGIKMNEELGFRCDQNQGECRAKFACHLDCFAWVKRDSYLPQGSHGLKAVTKAKLGYDPLEVNPEDMVRFAMEKPQTMASYSVSDAVATYYLYMTYVNPFIFSLATIIPMVPDEVLRKGSGTLCEMLLMVEAYKANVVCPNKNQADPEKFYQNQLLESETYIGGHVECLESGVFRSDIPTSFKLDSSAYQQLIDNLGRDLEYAITVEGKMRMDSISNYDEVKDEIKEKLEKLRDDPIREEGPLIYHLDVAAMYPNIILTNRLQPPSIVTDEICTACDFNRPGKTCLRKLEWVWRGVTFMGKKSDYYHLKKQIESEFVDAGANIMSSKSFLDLPKVDQQSKLKERLKKYCQKAYKRVLDKPITEVREAGICMRENPFYVDTVRSFRDRRYEYKTLNKVWKGKLSEAKASGNSIKIQEAQDMVVVYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGVVTYTGAKIIQNARLLIERIGKPLELDTDGIWCCLPGSFPENFTFKTIDMKKLTISYPCVMLNVDVAKNNTNDQYQTLVDPVRKTYKSHSECSIEFEVDGPYKAMIIPASKEEGILIKKRYAVFNHDGTLAELKGFEIKRRGELKLIKVFQAELFDKFLHGSTLEECYSAVAAVADRWLDLLDNQGKDIADSELLDYISESSTMSKSLADYGEQKSCAVTTAKRLAEFLGVTMVKDKGLRCQYIVACEPKGTPVSERAVPVAIFTTNPEVMKFHLRKWCKTSSDVGIRLIIDWSYYKQRLSSAIQKVITIPAAMQKVANPVPRVLHPDWLHKKVREKDDKFRQRKLVDMFSSANKDVVLDTDLPVTKDNVEDIEDFCKENRPSVKGPKPIARSYEVNKKQSECEQQESWDTEFHDISFQNIDKSVNYQGWLELKKRKWKVTLEKKKKRRLGDLRSSNQVDTHEINQKVGQGRGGVGSYFRRPEEALTSSHWQIIQLVPSPQSGQFFAWVVVEGLMLKIPLSIPRVFYINSKVPIDEYFQGKCVNKILPHGRPCYSLTEVKIQEDQFKKESKKRAALLADPGVEGIYETKVPLEFSAICQIGCVCKIDNKAKHRNTQDGWEVGELHMKTTTECHYLKRSIPLVYLYNSTSTGRAIYVLYCHVSKLMSAVVVDPFNGNELLPSALERQFRDSCLELSLDSLSWDGIRFQVHYVDHPEAAKKIIQRAISEYREENCGPTVAVIECPDFTFMKEGIKALDDFPCVRIPFNDDDNSYQPVSWQRPAAKIAMFRCAAAFQWLDRRITQSRYAHVPLGNFGLDWLTFTIDIFLSRALRDQQQVLWVSDNGVPDLGGINNEEAFFADEVQQTSLVFPGAYRKVSVELKIHNLAVNALLKSNLVNEMEGGGFMGFEQDVNPRGINSNDNTSFDETTGCAQAFRVLKQLIHSCLTDVRKSKNIYADSILQRLSWWLCSPSSKLHDPALHLMLHKVMQKVFALLLTDLRRLGAIIIYADFSKVIIDTVKFDLSAAKAYCESLLSTVRNSDIFEWILLEPVHYWHSLLFMDQYNYAGIRADDEISLDEVTIEPKWSVARHLPEYIERDFIIIIAKFIFDPWKFAIENKKGSSESLEAQMIEYLREQIGSTFINMLVKKVDDIMSHMKEINVSDASRVSGQAPKGDYSLEFIQVISAVLALDQNVQQDVLVMRKSLLKYIKVKECAAEAEFLDPGPSFILPNVACSNCDAYRDLDICRDPALLTEKEWSCADTQCGKIYDREQMESSLLEMVRQRERMYHMQDVVCIRCNQVKAAHLTEQCECSGSFRCKESGSEFSKRMEIFMDIAKRQKFRLLEEYISWIIYGPSY | 2.7.7.7 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P15436}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436}; | base-excision repair, gap-filling [GO:0006287]; DNA replication proofreading [GO:0045004]; embryonic root morphogenesis [GO:0010086]; leading strand elongation [GO:0006272]; mitotic cell cycle [GO:0000278]; negative regulation of long-day photoperiodism, flowering [GO:0048579]; nucleotide-excision repair, DNA gap filling [GO:0006297]; regulation of cell division [GO:0051302] | apoplast [GO:0048046]; epsilon DNA polymerase complex [GO:0008622] | 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; nucleotide binding [GO:0000166]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310]; zinc ion binding [GO:0008270] | PF00136;PF03104;PF08490; | 1.10.132.60;3.30.342.10;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P15436}; | null | null | null | null | FUNCTION: DNA polymerase II, which participates in chromosomal DNA replication. Required for the timing and determination of cell fate during plant embryogenesis and root pole development, by promoting cell cycle and cell type patterning. Necessary for proper shoot (SAM) and root apical meristem (RAM) functions. Involved in maintaining epigenetic states, controlling hypersensitive response (HR), and mediating abscisic acid (ABA) signaling. Required for flowering repression through a mechanism involving epigenetic gene silencing. May participate in processes involved in chromatin-mediated cellular memory. {ECO:0000269|PubMed:16212602, ECO:0000269|PubMed:16278345, ECO:0000269|PubMed:19244142, ECO:0000269|PubMed:19947980}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HW51 | CHR20_ARATH | MEANEESLKGKIEKLEGKEVIVESKEDEMDIIIEENREAEQEVMEVKARDGRGEQNDVLMEENNNQGEQKDEEMQDASSRSESSDFNSDEDEQILSRRDDELDLEKPLSEEEIDELISDLLAVESKAAEAQEALEKESLSKVESEVREELAQALRGDELDEAVAAEMMTFKDEWEATLDELETESATLLEQLDGAGIELPKLYEMIESQAPNGCYTEAWKQRAHWVGTQVTKETVESLANAERFLHTHRPVRKRHGKLLEEGASGFLEKKLADGAVKESLAGTSELDWSSLNKVFSEKRDESVSFGSKQWASVYLASTPHQAAAMGLEFPGVNEVEEIEEIDASLADPFLADAIDNERELALTEEQKTNYIRVKEEDDITCDRVLQLRLKRKRRKKRSKQVIRCAAENMDDDSVYLDGNNTTPNFAKDQVKSPETSTQVHNSEVNIEENGNFSNSDVDKMTPSTHINVDAKRDDSQNPANNFRCTACNKVAVEVHSHPLLEVIVCMDCKRSIEDRVSKVDDSLERHCEWCGHIADLIDCRTCEKLFCASCIKRNIGEEYMSEAQSSGWDCCCCSPIPLQRLTLELEKAMRDKKSIELSSDSSSDSSSDNNSVDTDADVNVTISSKKKSKKKIRRIIDDAELGKDTRTKIAIEKARQERLRSLQFSARYKTISSMGDVKSIPEGAEVEVLGDAHSGYIVNVVREIGEEAVRVPRSISAKLKVHQVTGIRFMWENIIQSISRVKSGDKGLGCILAHTMGLGKTFQVIAFLYTAMRCVDLGLKTALIVTPVNVLHNWRSEFEKWMPSEVKPLRIFMLGDVSRERRFDLLTKWRKKGGVFLMGYTNFRNLSLGRGVKDLNAARGICNALRDGPDILVCDEAHIIKNTKADTTQALKQVKCQRRIALTGSPLQNNLMEYYCMVDFVREGFLGSSPEFRNRFQNPIENGQHMNSTAEDVKIMNQRSHILYEQLKGFVQRMDMNVVKKDLPPKTVFVISVKLSPLQRILYQRFLELYGFSDGRTDERMRKNFFAAYQVLAQILNHPGIPQLRSEDSKNGRRGSIVDIPDDCSSDENIDYNMVTGEKQRTMNDLQDKVDGYLQKDWWVDLLQKNNYKVSDFSGKMILLLDILSMSADVGDKALVFSQSIPTLDLIELYLSRVPRHGKQGKFWKKGKDWYRIDGKTESSERQKLVDRFNEPDNKRVKCTLISTRAGSLGINLYAANRVIIVDGSWNPTYDLQAIFRAWRYGQKKPVFAYRLMARGTIEEKIYKRQVTKEGLAARVVDRQQVHRTISKEEMLHLFEFDDDDEKSEAVTEISKQNEAGHSNLVEQAILWTKKATLSRVGGDKLMENLLQRHGPNWISSFHEHETLLQENEEERLTKEEKDMAWEVYRRALEWEEVQRVPFSESPVVPKPSPSTQTEPLPQPKGFNRSRFVNRNCTRIAHQLTLISQGLKVGSSTVCGECGRVIRWEDVIPASKLSAVIVN | 3.6.4.- | null | DNA repair [GO:0006281]; maintenance of rDNA [GO:0043007]; pollen development [GO:0009555] | chromosome, telomeric region [GO:0000781]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; metal ion binding [GO:0046872] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61687}. Chromosome, telomere {ECO:0000250|UniProtKB:Q61687}. | null | null | null | null | null | FUNCTION: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes (By similarity). Involved in DNA repair of gamma-irradiation-mediated damages (PubMed:16547115). {ECO:0000250|UniProtKB:Q61687, ECO:0000269|PubMed:16547115}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HWY6 | MYO11_ARATH | MRNSGTPVNIIVGSHVWIEDSDVAWIDGLVEKINGQDVEVQATNGKKITAKLSKIYPKDMEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPFGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPQEELEKYKLGHPKTFHYLNQSKCFELVGISDAHDYIATRRAMDIVGMSEKEQEAIFRVVAAILHLGNVEFTKGKEVDSSVPKDDKSKFHLNTVAELLMCDVKALEDALCKRVMVTPEEVIKRSLDPQSALISRDGLAKTIYSRLFDWLVEKINVSIGQDATSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVQYQSDLFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNSTEPHYIRCVKPNNLLKPAVFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLYPRALEGNYEEKAAAQKILDNIGLKGYQVGKTKVFLRAGQMAELDARRTMVLSAAAKKIQRRIRTHQAQRRFILLRKATISLQALCRGRLSSKIFDNLRRQAAAVKIQKNARRLHSRKSYKNLHVAALVVQTGLRAMAAHKQFRFRKQTKAATTIQAQFRCHRATLYFKKLKKGVILSQTRWRGKLARRELRQLKMASRETGALKEAKDMLEKKVEELTYRAQLEKRSRVDLEEEKNQEIKKLQSSLEEMRKKVDETNGLLVKEREAAKKAIEEAPPVVTETQVLVEDTQKIEALTEEVEGLKANLEQEKQRADDATRKFDEAQESSEDRKKKLEDTEKKAQQLQESVTRLEEKCNNLESENKVLRQQAVSIAPNKFLSGRSRSILQRGSESGHLSVDARPSLDLHSHSINRRDLSEVDDKPQKSLNEKQQENQELLIRCIVQHLGFQGKRPVTACIIYKCLLQWRSFEVERTSVFDRIIQTIGQAIETQDNNNILAYWLSNASTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMTQSFRGTPQGVNLAMINGGVDTLRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNNLKSNHVPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEHWCYNATDEYAGSSWDELKHIRQAIGFLVIHQKPKKTLDEISHELCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMERIEIGDVEPPPLIRENSGFSFLLPCSD | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; organelle localization [GO:0051640]; pollen tube growth [GO:0009860]; vesicle transport along actin filament [GO:0030050] | cytoplasm [GO:0005737]; myosin complex [GO:0016459]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146] | PF01843;PF00612;PF00063;PF02736; | 1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family, Plant myosin class XI subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18503043}. Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or organelles. | null | null | null | null | null | FUNCTION: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks, mitochondria and peroxisomes. {ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:21914656}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HX15 | LPAI_ARATH | MSSTCSSPSAVEDPELGFRIDLDWTAGDSEDQVALRLESQLMVALPAPHDTVVVELKGIGDDDEGGLENVGLEMRVEKRREPLRAVTLMKAVGSGQQYDGVGVLTRLMRSDMMPAAIPAPAIDVASSCGVHWKTVTSLSLSGCGLLVMPVEVTELPLLEKLCLEHNKLSVLPPEIGKLKNLKILRVDNNMLISVPVELRQCVGLVELSLEHNKLVRPLLDFRAMAGLRILRLFGNPLEFLPEILPLHQLRHLSLVNIRIVSDENLRSVNVQIETENTSYFGASRHKLSAFSPLIFRSSSCHHPLLASTLVKIMQDEGNRSVIGKDENAVRQLISMITSDNQHVVEQACVALSSLARDVGVAMQLMKCDIMKPTETVLKSSSPDEVISVLQVVVTLAFVSDSVSQKMLTKDMLKALKSLCAHKNPEVQRQALLAVGNLAFCLENRRILITSESLRELLMRLIVTPEPRVNKAAARALAILGENEILRRSIKGRQVPKQGLRILTMDGGGMKGLATVQILKEIEKGSGKPIHELFDLICGTSTGGMLAIALGVKLMTLEQCEEIYKNLGKLVFAESVPKDNEAASWREKLDQLYKSSSQSFRVVIHGSKHSANEFERLLKEMCADEDGDLLIESAVKNVPKVFVVSTLVSVMPAQPFIFRNYQYPVGTPEMSYAFSDHSGGSTLTSSTASDQAGYYKQSAFMGSCKHQVWQAIRASSAAPYYLDDFSVDSYRWQDGAIVANNPTIFAIREAQLLWPDTKIDCLVSIGSGSVPTRVRKGGWRYLDTGQVLIESACSVERVEEALSTLLPMLPEIQYFRFNPVDDRCGMELDETDPAIWLKLEAAIEEFIQSNPQVFKNVCERLTLPFLNDEKWCDNLKPRFMNGKLPNSRVESSPSLGWRRNVLLMEAQHSPDSGRVKYHARALESFCSNNGIKLSSLHTTATPGCQKPSPGTAFPTPFTSPLITGSLPPSPLLFTPELGPQKFNRIDMVPPLSLDGGHVGKTVMSPPSSPPRQRQLYLPLRQMHEKLQNLPQVGILHLSLQNDSNGSILSWQNDVFVVAEPGDLADKFLQSVKVSILSVMQSNRRKAASVLSNICSISDLVRSKKCFQVGNIIHRYIGRQTLVMEDDQEIASFMFRRTVPSAHLTPDDIRWMVGAWRDRIIVFSGTFGPTQAVVKAFLDSGAKAVIGPSNEPQETPLITSQGSSEYNIGDQNGKFEIGEEEDEDEEVNEETEREEMEPPTPTSDWEDSDHEKTNRDGKYCGLWEDDEEEVSEFVCQLYDQLFRENSRVDVALQKALASHRKLRYTCHLPNV | 3.1.1.- | null | arachidonic acid metabolic process [GO:0019369]; defense response to fungus [GO:0050832]; fatty acid metabolic process [GO:0006631]; jasmonic acid biosynthetic process [GO:0009695]; lipid catabolic process [GO:0016042] | chloroplast [GO:0009507]; membrane [GO:0016020] | acylglycerol lipase activity [GO:0047372]; calcium-independent phospholipase A2 activity [GO:0047499]; phospholipase activity [GO:0004620] | PF00514;PF13855;PF01734; | 3.40.1090.10;1.25.10.10;3.80.10.10; | Patatin family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305|PubMed:12226489}. | null | null | null | null | null | FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidylserine (PS) and phosphatidylinositol (PI). Hydrolyzes phospholipids at both the sn-1 and sn-2 positions. Involved in basal jasmonic acid production and promotes resistance to the necrotrophic fungal pathogen Botrytis cinerea. {ECO:0000269|PubMed:17475618}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HXL0 | PLIP2_ARATH | MDSLCLNSGLHGVIPAITAVGNGGCGGVVEVRATASAPSQKRGPFGFSFKYPLTPFWSRGGGGGIASRRRSGLCLDDAVLVDSGDSRKPIAEETAVEMDTERRNGSWVLKILDVQSTWKHEEEEDDDEVEDEDGDEDEEVELDDAVVSEDDGGCDVCSVLEDDGNEANKFQLDRESFSKLLRRVTLPESKLYAQLSYLGNLAYSISKIKPANLSKYYGLRFVTSSAEKTESALKAENGEVSGETKPIVEAEEEVEEEEKNKSRKISASAAYEIVASAASYLHSRTNNILPFNSSSKAENSDKHDVNLTNAESSSDVAYSVTSVVAAEEDVKQAVADDLKSTISSPCDWFICDDDQSHTRFVVIQGSESLASWQANLLFEPIEFEGLGAIVHRGIYEAAKGMYEQMLPEVKAHIKTHGTSAKFRFTGHSLGGSLSLLLNLMLLVRGEVPASSLLPVITYGAPFVLCGGDRLLKKLGLPKSHVQAIVMHRDIVPRAFSCNYPYHVAELLKAVNGNFRSHPCLNKQSMLYSPMGELLILQPDETFSPGHELLPSGNGLYLLTSDFESPDIEDSDEERLRAAQTVFLNTPHPLDILSDRSAYGSSGTIQRDHDMNSYLKAVRSVIRKEVNQIRRAKREHRRSLWWPILVARESGSSGIAVSNGQINGQDFSGMMQTGRKSLQRFSRLVASQHMPLIVVMLFPVKLLFLGAFNVFSFR | 3.1.1.26; 3.1.1.32 | null | defense response to insect [GO:0002213]; lipid catabolic process [GO:0016042]; positive regulation of defense response [GO:0031349] | chloroplast [GO:0009507]; chloroplast membrane [GO:0031969]; chloroplast stroma [GO:0009570] | 1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity [GO:0102549]; 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; galactolipase activity [GO:0047714]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | PF01764; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:29666162}; Peripheral membrane protein {ECO:0000305}. Plastid, chloroplast stroma {ECO:0000269|PubMed:29666162}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+); Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:56636, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:76084, ChEBI:CHEBI:84822; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56637; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:42027, ChEBI:CHEBI:76084; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56641; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74667, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:29666162}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38788; Evidence={ECO:0000269|PubMed:29666162}; | null | null | null | null | FUNCTION: Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic monogalactosyldiacylglycerol (MGDG). May function downstream of abscisic acid (ABA) and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG). {ECO:0000269|PubMed:29666162}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HXP9 | MYO9_ARATH | MVRECFTFLNIFVLHSIGSHVWFEDPEVAWIDGEVEKINGQEVVIQATTGKKVTAKLSKIYPKDVEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPLGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPQEEIEKYKLGHPKTFHYLNQSKCFELVGISDAHDYLATRRAMDIVGISEKEQEAIFRVVAAILHIGNIDFTKGKEVDSSVPKDEKSKFHLKTAAELLMCDLKALEDALCKRVMITPEEVIKRSLDPQSAVTSRDGLAKTVYSRLFDWLVDKINKSIGQDANSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVLYQSELFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNCTEPHYIRCVKPNNLLKPAIFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLSPAALEGNFDEKVACQKILDNMGLKGYQIGKTKVFLRAGQMAELDARRAEVLSSAAKKIQRRIRTHQAQKRFIVLRKATISLQAICRGRLSCKHYDNLRREAAAVKIQKNGRRHYSRKSYKKLHVASLVVQTGLRAMAARKQFRFRKQTKAATIVQAQWRCHRAISYYKKLKNGVVLSQTRWRGRLAKRELRKLKMAARETGALKEAKDMLEKKVEELTYRVQLEKRSRGDLEEAKTQEILKLKSSFEEMRKKVDETNALLLKEREAAKKAAEEAPPVIKETQILVEDTKKIELMTEELESVKVTLENEKQRADDAVRKFEEAQESLEDKKKKLEETEKKGQQLQESLTRMEEKCSNLESENKVLRQQAVSMAPNKFLSGRSRSILQRGSESGHLAVDARSNLDLHSHSINHRDPSEVEDKPQKSLNEKQQENQDLLIRSIVQHLGFQGNRPITACIIYKCLLQWRSFEVERTSVFDRIIQTIGHAIETQDNNNTLAYWLSNTSTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMSQSFRGAPPGVNLAMINGAAGGGADTFRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNTLKSNNVPSFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLSELEHWCFKATNEYAGSSWDELKHIRQAIGFLVVHQKPKKTLDEISHDLCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMEKFEIADIEPPPLIRENSGFSFLLPVSE | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; organelle localization [GO:0051640]; pollen tube growth [GO:0009860]; vesicle transport along actin filament [GO:0030050] | cytoplasm [GO:0005737]; myosin complex [GO:0016459]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146] | PF01843;PF00612;PF00063;PF02736; | 1.10.10.820;1.20.5.190;1.20.58.530;3.30.70.1590;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family, Plant myosin class XI subfamily | null | null | null | null | null | null | null | FUNCTION: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks and mitochondria. {ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:21914656}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HXU3 | KNATM_ARATH | MDVKKDENSILENMKQEINHSLKEEAQEEEEILKKRISSHPLYGLLLHSHLNCLKVCSGDFDSPEIMNTADDLALSKLSLHPDSSSEATSSELDQFMVLFFFSPCQNIFTQQKTTFHVLLFFPLQINLTFKYSKFILPRKKQ | null | null | leaf proximal/distal pattern formation [GO:0010589]; positive regulation of DNA-templated transcription [GO:0045893] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677] | PF03790; | null | null | null | SUBCELLULAR LOCATION: [Isoform KNATM-B]: Cytoplasm {ECO:0000269|PubMed:18398054}. Nucleus {ECO:0000269|PubMed:18398054}. | null | null | null | null | null | FUNCTION: [Isoform KNATM-B]: Transcriptional regulator involved in leaf proximal/distal patterning. May act by sequestering BELL transcription factors. {ECO:0000269|PubMed:18398054}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HXY7 | PSS1_ARATH | MEPNGYRKERRKEQHLGRMNGGGGDVETDLDPWTAWAYKPRTISLLLIGACFLIWASGALDPDSTTSDDLVTSVKRGVWAMIAVFLAYSLLQAPSTVLIRPHPAIWRLVHGMAVIYLVALTFLLFQRRDDARQFMKFLHPDLGIELPEKSYGADCRIYVPDHPTNRFKNLYDTVFDEFFLAHIFGWWGKAILIRNQPLLWVLSIGFELLEVTFRHMLPNFNECWWDSIVLDILICNWFGIWAGMYTVRYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAHWDKDEWHPLQGPWRFIQVLTLCIIFLTVELNTFFLKFSLWIPPRNPVILYRLILWWLIAIPTTREYNSYLQDRKPVKKVGAFCWLSLGICIVELLICIKFGSGLYPTEMPLWVVTLWGSVGLGLVAFLLSWTWKIQKILAQKRR | 2.7.8.8 | null | microsporogenesis [GO:0009556]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylserine biosynthetic process [GO:0006659] | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965] | CDP-diacylglycerol-serine O-phosphatidyltransferase activity [GO:0003882]; L-serine-phosphatidylethanolamine phosphatidyltransferase activity [GO:0106245] | PF03034; | null | CDP-alcohol phosphatidyltransferase class-I family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21554450}; Multi-pass membrane protein {ECO:0000269|PubMed:21554450}. Nucleus envelope {ECO:0000269|PubMed:21554450}. Note=Mainly localized in nuclei and ER membranes during pollen development. | CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8; Evidence={ECO:0000269|PubMed:21554450}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 1/2. | null | null | FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Is essential for phosphatidylserine (PS) biosynthesis and PE seems to be the most plausible substrate. Plays an important role in microspore maturation. {ECO:0000269|PubMed:21554450}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HXZ1 | BRO1_ARATH | MASSSLSNLMLAIHEKKTSSVDLYRPLRNYVTFTYSEREAQLIDDDLETLKQLRSDIERVSDPSPAARRDLLISYYKVLCLVETRFPISPDKDHVNAVSFVWYDAFKQKHKATQQNIHLEKAAVLFNLGASYSQIGLGHDRTTVDGRRQASHAFMAAAGAFAHLRDNESIKATIGPSTTVDVSVECVGMLERLMVAQAQECVFENTIAKGSTPGVSAKIARQVGIFYEEALSALIISPLKDHFDKGWISHVQLKAALFYGEACFRYGKELHEKEEIAEEIARLRSGASRLAEAKKSSRGAPAQLIEAMNTLESSINGNLDRAVKENDRVYLMRVPSPSSLSPLPAFSMVKPMNMTDILDASKEKMFSILVPDSSAKALSRYTEMVDDVIRTQAERLQQASELTRVRLKEMDLPDSILAVDGNSALPVDLKEDVEAVQISGGPAGLEAELQQLRDLKRVNQELLVHTEELLQKEATEDSQFRSQFGTRWTRPQSSTLTKNLQDRLNRFAANLKQAGESDVKIERSVRDNSALMSILDRRPIESAVPTLARPIMSLDATEDAIVGTLKQSLRQLENLGAQRAGLEDMLKEMKRKDDILPKLMTITGSYEDMFRKEISKYDHICEDISQNIEVQEQLLMQIQAQNEEFSTIFNLEDYKASKEKCYKQIQAAIMKYREIKENINEGLKFYVTLQDAITNVKQQCSDFVMTRSIQCRDMIEDVQRQMSGLSFQDHRSSGPYPSVHQPTASSPPPPPETQNPSHPHPHAPYYRPPEQMSRPGYSIPPYGPPPPYHTPHGQAPQPYPPQAQQQPHPSWQQGSYYDPQGQQPRPPYPGQSPYQPPHQGGGYYRQ | null | null | early endosome to late endosome transport [GO:0045022]; endosome to plasma membrane protein transport [GO:0099638]; multivesicular body organization [GO:0036257]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; vacuole organization [GO:0007033] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; late endosome [GO:0005770]; multivesicular body [GO:0005771]; plasmodesma [GO:0009506] | protein self-association [GO:0043621]; ubiquitin binding [GO:0043130] | PF13949;PF03097; | 1.20.120.560;1.20.140.50;1.25.40.280; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016}. Late endosome {ECO:0000269|PubMed:26324913}. Endosome, multivesicular body {ECO:0000269|PubMed:26342016, ECO:0000269|PubMed:26902184}. | null | null | null | null | null | FUNCTION: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen (Probable). Associates with FREE1 and ELC to perform function in the ESCRT-I complex. Binds ubiquitin in vitro (PubMed:26902184). Plays a role in the biogenesis of vacuole and multivesicular bodies (MVBs) (PubMed:26324913, PubMed:26342016). Required for the endosomal location of AMSH3 (PubMed:26324913). Mediates high-affinity phosphate transporter trafficking to maintain phosphate homeostasis. Regulates vacuolar degradation of PHT1-1 (PubMed:26342016). {ECO:0000269|PubMed:26324913, ECO:0000269|PubMed:26342016, ECO:0000269|PubMed:26902184, ECO:0000305|PubMed:26342016}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HY56 | RLT1_ARATH | MEMGSDGEDQKIRSVVGDANLNNKKKKIDNNSSSKDGRVKPKRQMKTPFQLETLEKVYSEEKYPSEATRAELSEKLDLSDRQLQMWFCHRRLKDKKDGQSNKPVKSSVAAVQSASVNELPAAAGSVPEQDSRSDSGSESGCSPYSNSRRNFASGSSSSRAELDEYETMGKPSYESRLSTMVHRAIVCIEAQLGEPLRDDGPILGMEFDPLPPGAFGTPIAMQKHLLHPYESDLYERHDPRPRRSHAAARSFHEQQSLDDPSSFTPNMYERYSENHARGMDYEVARSRISSFMHANGPVPRSYVTPGHASRNCSTSQQDMPSPIESAHHGDRFLLEKDSSVLGTEDPYLLPDGVRKSSDVHRKGKINDGRLGRGSETRENHGPKDLEKLEIQRKKNEERMRKEMERNERERRKEEERLMRERIKEEERLQREQRREVERREKFLQRENERAEKKKQKDEIRREKDAIRRKLAIEKATARRIAKESMDLIEDEQLELMELAAISKGLPSVLQLDHDTLQNLEVYRDSLSTFPPKSLQLKMPFAISPWKDSDETVGNLLMVWRFLISFSDVLDLWPFTLDEFIQAFHDYDSRLLGEIHVTLLRSIIRDVEDVARTPFSGIGNNQYTTANPEGGHPQIVEGAYAWGFDIRSWKKHLNPLTWPEILRQLALSAGFGPKLKKKHSRLTNTGDKDEAKGCEDVISTIRNGTAAESAFASMREKGLLAPRKSRHRLTPGTVKFAAFHVLSLEGSKGLTVLELADKIQKSGLRDLTTSKTPEASISVALTRDVKLFERIAPSTYCVRAPYVKDPKDGEAILADARKKIRAFENGFTGPEDVNDLERDEDFEIDIDEDPEVDDLATLASASKSAVLGEANVLSGKGVDTMFCDVKADVKSELEKEFSSPPPSTMKSIVPQHSERHKNTVVGGVDAVIDESNQGQSWIQGLTEGDYCHLSVEERLNALVALVGIANEGNSIRTGLEDRMEAANALKKQMWAEAQLDNSCMRDVLKLDLQNLASSKTESTIGLPIIQSSTRERDSFDRDPSQLLDETKPLEDLSNDLHKSSAERALINQDANISQENYASKRSRSQLKSYIGHKAEEVYPYRSLPLGQDRRHNRYWHFAVSVSKSDPCSRLLFVELHDGKWLLIDSEEAFDILVASLDMRGIRESHLRIMLQKIEGSFKENACKDIKLARNPFLTEKSVVNHSPTDSVSPSSSAISGSNSDSMETSTSIRVDLGRNDTENKNLSKRFHDFQRWMWTETYSSLPSCARKYGKKRSELLATCDACVASYLSEYTFCSSCHQRLDVVDSSEILDSGLAVSPLPFGVRLLKPLLVFLEASVPDEALESFWTEDQRKKWGFRLNTSSSPGELLQVLTSLESAIKKESLSSNFMSAKELLGAANAEADDQGSVDVLPWIPKTVSAVALRLSELDASIIYVKPEKPEVIPEDENEQISLFPRDSPFKGKGPREQEDQDEVAPNPGNRNKKRARVSLGSGSNRKVKRKKAQSGLNKFVVGRRNVAVNSNLMAVELNHQVPGKGKRTVRKRPERIDEDNSHLVNRMANIVRPKSEEVEEDEEEEEQTFRDINEDWAAGETPREMEEDWANETPNRMMTPMQVDDESDNSVGVESEDEDGGGQFVDYSQRNKWGLDWNSNLNVAIEEDEEEEVVGVGRVEGEDDAEMSESSEDDDVPANNAANNYDRESEGYSSSDS | null | null | flower development [GO:0009908]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; regulation of transcription by RNA polymerase II [GO:0006357]; vegetative to reproductive phase transition of meristem [GO:0010228] | ISWI-type complex [GO:0031010] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF02791;PF05066;PF00046;PF15612;PF15613; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}. | null | null | null | null | null | FUNCTION: Transcriptional regulator required for the maintenance of the plant vegetative phase. In association with CHR11 or CHR17 may prevent the early activation of the vegetative-to-reproductive transition by regulating key genes that contribute to flower timing, such as FT, SEP1, SEP3, AGL8/FUL, SOC1 and FLC. {ECO:0000269|PubMed:22694359}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HYF3 | DCYD1_ARATH | MRGRSLTLSRVKLELARRSMSATSVPSMADFLTKKPYSPPSWASHLRPLPSHTFSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEALTNALKEKLEKEGKKPYVIPVGGSNSLGTWGYIEAAREIEEQLNYRPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDGLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPKCWEGRKILFIHTGGLLGLYDKVDQMASLMGNWSRMDVSESVPRKDGVGKMF | 3.5.99.7; 4.4.1.15 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:15720402}; | D-cysteine catabolic process [GO:0019447]; ethylene biosynthetic process [GO:0009693]; stress response to cadmium ion [GO:1990170] | chloroplast [GO:0009507]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | cobalt ion binding [GO:0050897]; D-cysteine desulfhydrase activity [GO:0019148]; hydrolase activity [GO:0016787] | PF00291; | 3.40.50.1100; | ACC deaminase/D-cysteine desulfhydrase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15720402}. | CATALYTIC ACTIVITY: Reaction=D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) + pyruvate; Xref=Rhea:RHEA:11268, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:35236; EC=4.4.1.15; Evidence={ECO:0000269|PubMed:15720402}; CATALYTIC ACTIVITY: Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7; Evidence={ECO:0000269|PubMed:15720402}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for D-cysteine {ECO:0000269|PubMed:15720402}; Note=kcat is 6 sec(-1) for D-cysteine as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15720402}; | null | FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. Is mainly responsible for the degradation of cysteine to generate H2S, a regulator of stomatal movement and closure. Has high affinity for D-cysteine.; FUNCTION: Possesses 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase activity. Acts as a regulator of ACC levels and causes changes in ethylene levels. | Arabidopsis thaliana (Mouse-ear cress) |
F4HZB2 | BCHA1_ARATH | MKWATLLKDIKEKVGLAQSSDSDPFPVDLTAPPSSSSSSSSPSFTYPSSSSLHHFNFSPSSRDNHELELDFKRLWEEFRSSSSEKEKEAALNLTVDIFCRLVKRHANVDQLVTMLVETHIFSFVIGRAFVTDIEKLKIGSKTRSLNVEKVLRFFSDVTKEGFSPGANLLTAVEVLVSGPIDKQSLLDSGIFCCLIHVLIALLAYDELSKSKITGDLEVVSAEKDAGYIVLQTRRLEVEGSVVHIMKALASNPSAAQSLIEDDSLESLFNMVANGSITVFSQYKEGLVPLHNIQLHRHAMQILGLLLVNDNGSTARYIRKHHLIKVLLMAVKEFDPSCGDSAYTMGIVDLLLECVELSYRPEAGGVRLREDIRNAHGYHFLVQFALVLSSLPKNPIFVSSNHDSGSDDPEVFHDGENTNSTENADFSSQNFAPSLSRLLDVLVTLAQTGPAEPSVGRASRSSQTKPTGHSRSRTSSVDSIYDETWEQGSGKVKDLEAVQMLQDIFLKAENKDLQAEVLNRMFKIFSSHVENYRLCQELRTVPLLVLNMAGFPSSLQDIILKILEYAVTVVNCVPEQELLSLCCLLQQPITSQLKHTILSFFVKLISFDQQYKKVLREVGVLEVLQDDLKQHKLLIGPDQYSGVSSHSDRKPSSGSFRKNLDTKDAIISSPKLMESGSGKLPVFEVDNTITVGWDCLISLLKKAEANQSSFRAANGVAIILPFLISDAHRSGVLRILSCLITEDTKQVHHDELGAVVDLLKSGMVTGISGHQYKLHDDAKCDTMGALWRIVGVNGSAQRVFGEATGFSLLLTTLHTFQGKREHMDESDLTVYIKLFKYLFRLMTAAVCENAVNRMKLHAVITSQTFFELLAESGLLCVELERQVIQLLLELALEVVVPPFLTSESTALATIPENENTTFVVTTPSGQFNPDKERIYNAGAVRVLIRSLLLFSPKMQLEFLRLLESLARASPFNQENLTSIGCVELLLEIIYPFLAGSSPFLSYALKIVEILGAYRLSPSELRMLFRYVLQMRIMNSGHAIVGMMEKLILMEDTALEHLSLAPFVELDMSKTGHASVQVSLGERSWPPAAGYSFVCWFQFRNFLTTQGKESEASKAGGSSKTRMTSAQQHEQNIFRMFSVGAVSNESPFYAELYFQEDGILTLATSNSHSLSFSGLEIEEGRWHHLAVVHSKPNALAGLFQASVAYVYLDGKLRHTGKLGYSPSPVGKSLQVTVGTPATCARVSDLTWKTRSCYLFEEVLTSGCIGFMYILGRGYKGLFQDADLLRFVPNQACGGGSMAILDSLDTDMTSSSNGQKFDGSNRQGDSKADGSGIVWDLERLGNLAFQLPGKKLIFAFDGTCSEFIRASGNFSLLNLVDPLSAAASPIGGIPRFGRLVGNVSICRQSVIGDTIRPVGGMTVVLALVEAAESRNMLHMALSLLACALHQNPQNVKDMQTIRGYHLLALFLRPKMTLFDMQSLEIFFQIAACEALFSEPKKLESVQSNITMPPTETIFENSYEDLSLSRFRYDSSSVGSHGDMDDFSVPKDSFSHLSELETDIPVETSNCIVLSNADMVEHVLLDWTLWVTSPVSIQIALLGFLENLVSMHWYRNHNLTILRRINLVEHLLVTLQRGDVEVPVLEKLVVLLGCILEDGFLTSELENVVRFVIMTFNPPEVKSRSSLLRESMGKHVIVRNMLLEMLIDLQVTIKAEDLLELWHKIVSSKLITYFLDEAVHPTSMRWIMTLLGVCLASSPNFSLKFRTSGGYQGLLRVLQNFYDSPDIYYILFCLIFGKPVYPRLPEVRMLDFHALVPNDGSYVELKFIELLDSVVAMAKSTYDRLIMQSMLAHQSGNLSQVSASLVAELIEGAEMTGELQGEALMHKTYAARLMGGEASAPAAATSVLRFMVDLAKMCPQFSTACRRAEFVENCADLYFSCVRAAYAVKMAKQLSVKAEEKHINDADDSGSQGSLPHDQDQSTKTSISVGSFPQGQVSLGSEDMSLPANYVVNDKMENILPPPTQDTSKSLQGVEDVKKQDDHHVGPSASSERDFQDFTGNPVQVQATDSQSSASFPMIESPLLSEKSSLKVSFTPSPSPVVALASWLGSNYNESKSSTLGSPSLESYVSVNEVDASSERKSGSQGSSAANAFFTVSPKLLLETDETGYGGGPCSAGASAVLDFMAEALADLVTEQIKAVPVLESILEMVPFYVDPESVLVFQGLCLSRVMNYLERRLLRDDEEDEKKLDKAKWSVNLDAFCWMIVDRVYMGAFSQPAGVLRALEFLLSMLQLANKDGRVEEVTPSGKGLLSLGRATRQLDAYVHSILKNTNRMVLYCFLPSFLITIGEEDLLSQLGLLVESKKRPSPNPATDESGIDISTVLQLLVANRRIIFCPSNLDTDLNCCLCVNLISLLLDQRKSVQNMSLDIVKYLLVHRRSALEDLLVTKPNQGQNFDVLHGGFDKLLTGNLPEFFKWLESSDKIINKVLEQCAAIMWVQYIAGSAKFPGVRIKGMEGRRKREMGRKSRDMSKLDLKHWDQLNERRYALEVLRDAMSTELRVVRQNKYGWILHAESEWQTHLQQLVHERGIFPMRKSKGTEDPEWQLCPIEGPYRMRKKLERCKLKIDSIQNVLDGKLELGEIELPKVKNEDGPVISDTDSEPPFLLSELYDESFLKESDDFKDVASARNGWNDDRASSTNEASLHSALDFGGKSSIASVPITDTTHVKSETGSPRHSSSAKMDETNGREEKSEKELNDDGEYLIRPYLEHLEKIRFRYNCERVVDLDKHDGIFLIGEFCLYVIENFYIDEDGCICEKECEDELSVIDQALGVKKDVSGSSDFHSKSSTSWTTTVKTGAVGGRAWAYGGGAWGKEKMCMTGNLPHPWRMWKLNNVHEILKRDYQLRPVAIEIFSMDGCNDLLVFHKKEREEVFKNLVAMNLPRNSMLDTTISGSAKQESNEGGRLFKLMAKSFSKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWVLADYDSESLDFSDPKTFRKLHKPMGCQTPEGEEEFRKRYESWDDPEVPKFHYGSHYSSAGIVLFYLIRLPPFSSENQKLQGGQFDHADRLFNSIKDTWLSAAGKGNTSDVKELIPEFFYMPEFLENRFSLDLGEKQSGEKVGDVFLPPWARGSVREFILKHREALESDYVSENLHHWIDLIFGYKQRGKAAEEAVNVFYHYTYEGNVDIDAVTDPAMKASILAQINHFGQTPKQLFPKAHVKRRTDRKIPLHPLKHSMHLVPHEIRKCSSSISQIITFHDKVLVAGANCFLKPRGYTKYITWGFPDRSLRFMSYDQDKLLSTHENLHESNQIQCAGVSHDGRIVVTGAEDGLVCVWRVSKDGPRGSRRLRLEKALCAHTAKVTCLRVSQPYMMIASGSDDCTVIIWDLSSLSFVRQLPDFPVPISAIYINDLTGEIVTAAGTVLAVWSINGDCLAVANTSQLPSDSVLSVTGSTSSDWLETSWYVTGHQSGAVKVWRMIHCTDPVSAESKTSSSNRTGGLNLGDQVPEYKLILHKVLKFHKQPVTALHLTSDLKQLLSGDSAGQLLSWTVPDETLRASMKQASLKQASLKQASLKQASSV | null | null | cellular response to salt stress [GO:0071472]; mucilage extrusion from seed coat [GO:0080001]; multidimensional cell growth [GO:0009825]; P-body assembly [GO:0033962]; positive regulation of root hair elongation [GO:1902892]; regulation of intracellular mRNA localization [GO:1904580]; regulation of vacuolar transport [GO:1903335]; trichome morphogenesis [GO:0010090]; vacuole organization [GO:0007033] | cytoplasm [GO:0005737]; P-body [GO:0000932]; root hair tip [GO:0035619] | null | PF02138;PF14844;PF00400; | 2.60.120.200;1.10.1540.10;1.25.10.10;2.30.29.30;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26133670}. Cytoplasm, P-body {ECO:0000269|PubMed:26133670}. Note=Recruited to P-bodies by DCP1 in a salt stress-dependent manner. {ECO:0000269|PubMed:26133670}. | null | null | null | null | null | FUNCTION: Involved in cell morphogenesis (PubMed:19392685). May have a function in membrane fusion or membrane composition (PubMed:19392685). Required for salt stress tolerance (PubMed:26133670). Regulates the salt stress-dependent post-transcriptional stabilization, cytoplasmic agglomeration, and localization to P-bodies of a subset of salt stress-regulated mRNAs (PubMed:26133670). {ECO:0000269|PubMed:19392685, ECO:0000269|PubMed:26133670}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HZD1 | JMJ24_ARATH | MQVNFDETCDSVIRMNANEQTRSANGIGNGNGESIPGIPDDLRCKRSDGKQWRCTAMSMADKTVCEKHYIQAKKRAANSAFRANQKKAKRRSSLGETDTYSEGKMDDFELPVTSIDHYNNGLASASKSNGRLEKRHNKSLMRYSPETPMMRSFSPRVAVDLNDDLGRDVVMFEEGYRSYRTPPSVAVMDPTRNRSHQSTSPMEYSAASTDVSAESLGEICHQCQRKDRERIISCLKCNQRAFCHNCLSARYSEISLEEVEKVCPACRGLCDCKSCLRSDNTIKVRIREIPVLDKLQYLYRLLSAVLPVIKQIHLEQCMEVELEKRLREVEIDLVRARLKADEQMCCNVCRIPVVDYYRHCPNCSYDLCLRCCQDLREESSVTISGTNQNVQDRKGAPKLKLNFSYKFPEWEANGDGSIPCPPKEYGGCGSHSLNLARIFKMNWVAKLVKNAEEIVSGCKLSDLLNPDMCDSRFCKFAEREESGDNYVYSPSLETIKTDGVAKFEQQWAEGRLVTVKMVLDDSSCSRWDPETIWRDIDELSDEKLREHDPFLKAINCLDGLEVDVRLGEFTRAYKDGKNQETGLPLLWKLKDWPSPSASEEFIFYQRPEFIRSFPFLEYIHPRLGLLNVAAKLPHYSLQNDSGPKIYVSCGTYQEISAGDSLTGIHYNMRDMVYLLVHTSEETTFERVRKTKPVPEEPDQKMSENESLLSPEQKLRDGELHDLSLGEASMEKNEPELALTVNPENLTENGDNMESSCTSSCAGGAQWDVFRRQDVPKLSGYLQRTFQKPDNIQTDFVSRPLYEGLFLNEHHKRQLRDEFGVEPWTFEQHRGEAIFIPAGCPFQITNLQSNIQVALDFLCPESVGESARLAEEIRCLPNDHEAKLQILEIGKISLYAASSAIKEVQKLVLDPKFGAELGFEDSNLTKAVSHNLDEATKRPQQNSCT | 2.3.2.27 | null | heterochromatin formation [GO:0031507]; negative regulation of DNA methylation-dependent heterochromatin formation [GO:0090310]; positive regulation of gene expression [GO:0010628]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of regulatory ncRNA processing [GO:0070920]; regulation of transcription by RNA polymerase II [GO:0006357] | histone deacetylase complex [GO:0000118]; Ino80 complex [GO:0031011]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | chromatin DNA binding [GO:0031490]; histone binding [GO:0042393]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator activity [GO:0003712]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630] | PF02373;PF08879;PF10497; | 2.60.120.650; | JARID1 histone demethylase family | PTM: Self-ubiquitinates. {ECO:0000269|PubMed:26798133, ECO:0000269|PubMed:26979329}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26979329}. | 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:0000269|PubMed:26798133, ECO:0000269|PubMed:26979329}; | null | null | null | null | FUNCTION: Binds histone H3 but seems to have lost demethylase activity probably due to its inability to bind iron Fe(2+) (PubMed:26979329). Possesses E3 ubiquitin ligase activity and targets directly CMT3 for proteasomal degradation to initiate destabilization of the heterochromatic state (e.g. CHG cytosine methylation and H3K9me2) of endogenous silenced loci (PubMed:26798133, PubMed:26979329). Required for the removal of repressive H3K9me2 histone marks to facilitate the transcription of AtSN1, AtMu1c, solo LTR and SDC, thus counteracting their transcriptional silencing (PubMed:26119694, PubMed:26979329). Mainly required to promote the basal level transcription of silenced loci such as TE and repeats targeted by RNA-dependent DNA methylation (RdDM) for silencing, a specialized branch of the RNA interference (RNAi) pathway (PubMed:26119694, PubMed:26979329, PubMed:28400174). Cooperates also with RNAi pathways for gene silencing both by contributing to the production of 24-nt siRNA to initiate RdDM and by recruiting RDR2 to enable local transcripts to make dsRNA (PubMed:26119694, PubMed:28400174). Antagonizes histone H3K9 demethylase IBM1/JMJ25 function (PubMed:28400174). {ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26798133, ECO:0000269|PubMed:26979329, ECO:0000269|PubMed:28400174}. | Arabidopsis thaliana (Mouse-ear cress) |
F4HZG9 | ICP55_ARATH | MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPHLMAEGEVTPGIRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERGLCMFMPESTPKDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNVQSASQRYTNLDDFQNSASLGKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIPSSFDCPERFQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLLNNHCHDNSARTSPVSLCKVKGLHTNRNPRRLF | 3.4.11.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Note=Binds 2 manganese ions per subunit. {ECO:0000305}; | protein stabilization [GO:0050821]; proteolysis [GO:0006508] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | aminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; peptidase activity [GO:0008233] | PF05195;PF00557; | 3.90.230.10;3.40.350.10; | Peptidase M24B family | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:25732537}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:25732537}. | null | null | null | null | null | FUNCTION: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome. {ECO:0000269|PubMed:25732537, ECO:0000269|PubMed:25862457, ECO:0000269|PubMed:28936218}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I096 | MED13_ARATH | MWTNVFRIGGLHNVSWFQFLPSETELNPGFDRSSRAEQNEVATYLVLSSHLRLQKEGFLTTWTNSFVGPWDPSQGLYNPDEKIKLWLFLPGRHSSISDKAQAAVSKLRVVASGIWVAPGDSEEISVAFSQSLRNCIERALSGISYMRFGDVFSKFSPQSEEYLRRGQPTVEFIFAATEEAVFVHVIISAKNVRTLSSGDAERMLRSSLKNSSYRLPAFRKCLGLAKSEDNRLCYINTSHRPMLFPPVIVSPHGMRGSLTGFCPNDLVKQVYFSSGNLKTSTGYVGLPSHIGRGSRLINGNHCYVEVTLGCCQNRNDNTSQANSTFAVNLPHNQCPEPSVGSKDHRKGQSDLSSVCEKKFIYPAEAVLVPILQSAFAKFSLKRAGDFDCLGASENKSDGFYEKNGYNSSGSSRNSSISSTSSASSGSGWRMTSRTGDLDADADSLTCRQSGLTCNDDRLKMGSKRPRTGMAESFGQVGIENDQIGWDWDADDDDDDREVGMDIKALLSEFGDFGDFFENDALPFGEPPGTAESHVLVFPPDSADVGSSPVDMMDVSDQIVLPVGFSSFESFNPVPPIIDECLIKSQEVLHSSITSVPSNQMSISSTGEFDHLLKAEAMMTFAPEYGAVEAPMSEISSTFFKSPYLPKSHKVESSNSRTSNYVYGATPPTTDSDGAGDMILFGSKSCIGNNAGRTLYHSREHYTQVEGRKGRHDKLPTVISDNSSTKEGVSQSIHSKHSAANAVKVVQGKKTDGISAVVSTLLSSKTLLATDVGSVMFQAFMCRMRHIITSSKHSSPVSLTRLSGNFFLNQLSNEPSTLTDNISARNEIYKKDIPTRIAGDFDGGMLDSHMSAPVGVWRTVSVPKTAKPASSPNIEAGSSLPHSSFSEDSLLSYGQRQPLQDLLDGIALLVQQATSFVDLALDSDCGDGPYGWLALEELWRRELSCGPSAGHAGCGGTLASCHSLDIAGVKLVDPLSAEVFPSSVITLLQSDIKTALKSAFGQSDGPLSVTDWCKGRNQSGDGGSISEGFTAESALSEVNGVNISDDFIIDKYFGKQAVSNAIDGGKGDETAQSQDIYSSELLRPTLFVLPSPAILVGYQDDWLKISTNSLTHWEKAPFEPYALPKSINYAVVCPDIDPLTCAATDFFQQLGTGESTSLSFVKEVMLKHDRNWLGTHLPQSLGNQMEKDVGRLSSSGFVLLDCPQSMKIESNNTSLLGSLSDYFLSLSNGWNVNSYLKSLSKALKGLKLGSGLYTNQKEGSGSPCVVVYIVCPFPDPSAVLRTIVESSIALGSVIQSDRDRRSILNSQVARAFSSSTAVDEASISHIPVLSGFSVPKLVLQVVSVDSIFRITSPSFNELVILKDTAFSVYNKARRISRGMPNDAFFSSSLPSRSSSALTPMNSISGIWKDCGGSRMTGSTHPRDGEIDVSLRTSGWDTSTSWQIPRSGGLSCDPNRNGDFYLNDEIFYLFEPLFILSEPGSVERGVSPTFTSLGSESSKPIPEDGGRGSGPGMNSMEGITSGSSSQGDVSQLEGKAIPSLHCCYGWTEDWRWLVSIWTDARVLQQGCQILQACSSPDNGSFKPRDFVITRIGNFFELEYQEWQKAIYSAGGPEIKKWPIQLRRSAPSGIATNSNGSSLQQQDLSLIQERASSTSTLYSSHSKQSTFVKGSMGQSAGRKQIMGGQTISGTPRGLFQWVHSISFASISLDHSLHFVLPAELVSAGGGQSSTGMSSVNYIEGFTPVKSLGSTAFSYMMIPSPNMRFLHPSPLQLPTCLTAESPPLAHLLHSKGYAIPLSTGFVVSKAVPSMRKDSRINVKEEWPSVLSVSLIDYYGGYDNAHDKILQGIVKQGGGTKETRDFEVESHLILESIAAELHALSWMTVSPAYLDRRTALPFHCDMVLRLRRLLHFADKEVSRIPDKTGV | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of development, heterochronic [GO:0040034]; regulation of radial pattern formation [GO:0090213] | mediator complex [GO:0016592] | transcription coactivator activity [GO:0003713] | PF11597;PF18296; | null | Mediator complex subunit 13 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts closely together with MAB12. Involved in the regulation of embryo patterning and cotyledon organogenesis. May act through transient repression of specific genes such as the ones responsive to auxin. {ECO:0000269|PubMed:20023166, ECO:0000269|PubMed:21257604, ECO:0000269|PubMed:22247249}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I0K2 | SCKL2_ARATH | MASLSFTQFLSFPRCNADVPCLLQSHGFVKFRGERWNGKQSFSMAAGRRKLSESAPLEEEGNDGNGAVVGKKPSKSVKRTTKKKVVVKDEPLEEISEFLVDNDDVLDKESIVSALKPKKTRTRKKAAAASSDVEEVKTEKKVRRKRTVKKDKDVEDDLATIMDAEVSDVEEALAVESTDTESEEEEIDLSKHEGEDISHTYGWPPLVCCFGSAQHAFVPSGRPANRLLDYELHERMRDAKWAPEKYIRAPGGCAGGVAIALASLGGKVAFMGKLGADDYGQAMLYYLNVCKVQTRSVKIDGKRVTACSTMKISKRGRLKSTCIKPCAEDSLSKSEINVDVLKEAKMFYFSTHSLLDKKMMSTTIQAIKISKQLGNVIFYDLNLPLPLWHSSEETKSFIQEVWNLADVIEITKQELEFLCGIEPTEEFDTENNDISKFVHYPPETVEQLWHENLKVLFVTNGTSKIHYYTKEHNGAVSGMEDVPITPFTRDMSASGDGIVAGLIRMLTVQPDLMNNKGYLERTARYAIECGIIDQWLLAQTRGYPPKDDMEEEEDDEEEDEVESDPNGIRSITEKEYRTSKPYDEPDGPYVMKPVEEREYKKLELVGSMFEDGSL | null | null | chloroplast organization [GO:0009658]; etioplast organization [GO:0009662]; phosphorylation [GO:0016310]; plastid transcription [GO:0042793]; regulation of DNA-templated transcription [GO:0006355] | chloroplast nucleoid [GO:0042644]; plastid-encoded plastid RNA polymerase complex [GO:0000427] | kinase activity [GO:0016301] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:20511297}. | null | null | null | null | null | FUNCTION: Required for proper chloroplast development, most likely through regulating plastid-encoded polymerase (PEP) dependent chloroplast transcription. Acts as a component of the transcriptionally active plastid chromosome that is required for plastid gene expression. {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:20511297, ECO:0000269|PubMed:22770232, ECO:0000269|PubMed:24019900}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I171 | MD15A_ARATH | MDNNNWRPSLPNGEPAMDTGDWRTQLPPDSRQKIVNKIMETLKKHLPFSGPEGINELRRIAARFEEKIFSGALNQTDYLRKISMKMLTMETKSQNAAGSSAAIPAANNGTSIDSIPTNQGQLLPGSLSTNQSQAPQPLLSQTMQNNTASGMTGSTALPSSMPPVSSITNNNTTSVVNQNANMQNVAGMLQDSSGQHGLSSNMFSGPQRQMLGRPHAMSSQQQQQPYLYQQQLQQQLLKQNFQSGNVPNPNSLLPSHIQQQQQNVLQPNQLHSSQQPGVPTSATQPSTVNSAPLQGLHTNQQSSPQLSSQQTTQSMLRQHQSSMLRQHPQSQQASGIHQQQSSLPQQSISPLQQQPTQLMRQQAANSSGIQQKQMMGQHVVGDMQQQHQQRLLNQQNNVMNIQQQQSQQQPLQQPQQQQKQQPPAQQQLMSQQNSLQATHQNPLGTQSNVAGLQQPQQQMLNSQVGNSSLQNNQHSVHMLSQPTVGLQRTHQAGHGLYSSQGQQSQNQPSQQQMMPQLQSHHQQLGLQQQPNLLQQDVQQRLQASGQVTGSLLPPQNVVDQQRQLYQSQRTLPEMPSSSLDSTAQTESANGGDWQEEVYQKIKSMKETYLPDLNEIYQRVAAKLQQDSMPQQQRSDQLEKLRQFKTMLERMIQFLSVSKSNIMPALKDKVAYYEKQIIGFLNMHRPRKPVQQGQLPQSQMQPMQQPQSQTVQDQSHDNQTNPQMQSMSMQGAGPRAQQSSMTNMQSNVLSSRPGVSAPQQNIPSSIPASSLESGQGNTLNNGQQVAMGSMQQNTSQLVNNSSASAQSGLSTLQSNVNQPQLSSSLLQHQHLKQQQDQQMQLKQQFQQRQMQQQQLQARQQQQQQQLQARQQAAQLQQMNDMNDLTSRQGMNVSRGMFQQHSMQGQRANYPLQQLKPGAVSSPQLLQGASPQMSQHLSPQVDQKNTVNKMGTPLQPANSPFVVPSPSSTPLAPSPMQVDSEKPGSSSLSMGNIARQQATGMQGVVQSLAIGTPGISASPLLQEFTSPDGNILNSSTITSGKPSATELPIERLIRAVKSISPQALSSAVSDIGSVVSMVDRIAGSAPGNGSRASVGEDLVAMTKCRLQARNFMTQEGMMATKKMKRHTTAMPLSVASLGGSVGDNYKQFAGSETSDLESTATSDGKKARTETEHALLEEIKEINQRLIDTVVEISDDEDAADPSEVAISSIGCEGTTVRFSFIAVSLSPALKAHLSSTQMSPIQPLRLLVPCSYPNGSPSLLDKLPVETSKENEDLSSKAMARFNILLRSLSQPMSLKDIAKTWDACARAVICEYAQQFGGGTFSSKYGTWEKYVAAS | null | null | positive regulation of fatty acid biosynthetic process [GO:0045723]; response to salicylic acid [GO:0009751] | mediator complex [GO:0016592]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; transcription coactivator activity [GO:0003713] | PF16987; | 1.10.246.20; | Plant Mediator complex subunit 15 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. | Arabidopsis thaliana (Mouse-ear cress) |
F4I1S7 | ELP2_ARATH | MSENTKVEAKRVFIGAGCNRVVNNVSWGASGLVSFGAQNAVAVFCPKTAQILTTLPGHKASVNCTHWLPTSKFAFKAKKLDRQYLLSGDSDGIIILWELSTLNNDWRHVLQLPLSHKKGVTCITAYMVSETDAMFASASSDGVVNVWDVSFPSQPSEECKVVCLDSICVDTKAIVTLSLAELPQNPGRFALALGGLDNKIKLYSGERTGKFTSVCELKGHTDWIRSLDFSLPLHTTEEIPNSIMLVSSSQDKVIRIWKLVLVGDVGSWRREITLASYIEGPVFVSGTFTYQISVESVLIGHEDWVYSVEWQPPVIDFIDGRLVNHQPLSILSASMDKTMMIWRPEKKTGVWVNVVCVGELSHCALGFYGGHWSPNSLSILAHGYGGAFHLWRNVSSSKESENWQMQKVPSGHFAAVTDVTWARTGEYLLSVSQDQTTRVFSAWKNDEGNEAEDEHWHELARPQVHGHDINCVAMVQGKGNHRFVSGAEEKVVRVFEAPLSFLKTLNHTCAGGEGSFPEDLQADVQVLGANMSALGLSQKPIYLHSSSEPLERNGGGEGLDTFETVPEAAPAELKEPPIEDQLAFHTLWPESHKLYGHGNELFSLCSDHKGNLVASSCKAQSASMAEIWLWEVGTWKAVGRLQSHSLTVTHLEFSYDDTLLLSVSRDRHFSVFSIQRTDNGEVSHKLMAKVEAHKRIIWACSWNPFGHQFATSSRDKTVKIWSVENDARIKQILVLPPFGSSVTAVAWTGLDRNEKSGCVAVGMESGLIELSNVKIIETEEGTTATAALALRLEPFMCHVSAVNRLAWRPTEKCESNQSLRWLTSCGDDNCVRVFNFKF | null | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952]; negative regulation of anthocyanin metabolic process [GO:0031538]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of defense response [GO:0031349]; regulation of leaf development [GO:2000024]; response to abscisic acid [GO:0009737]; response to oxidative stress [GO:0006979]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; elongator holoenzyme complex [GO:0033588]; nucleus [GO:0005634] | null | PF00400; | 2.130.10.10; | WD repeat ELP2 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus {ECO:0000250|UniProtKB:Q6IA86}. | null | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}. | null | null | FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Prevents abscisic acid (ABA) signaling leading to stomatal closure and seedling growth inhibition. Involved in oxidative stress signaling. Prevents anthocyanin accumulation. Accelerator of defense gene induction required for rapid defense gene induction, and for the establishment of both basal and effector-triggered immunity (ETI), in a NPR1-independent manner, but is not required for systemic acquired resistance (SAR) establishment (PubMed:19500300, PubMed:20807211). {ECO:0000250|UniProtKB:Q6IA86, ECO:0000269|PubMed:19500300, ECO:0000269|PubMed:20807211}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I1T7 | NP214_ARATH | MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNSNGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKHSYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVDSIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLAVTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPYFVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQRLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKLQKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTGYVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGPLRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDKTIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARRGVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNASSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSERLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSNTTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFESSKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIPISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSLFPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQSTVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASSPTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSGELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGGSNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGFGGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK | null | null | embryo development ending in seed dormancy [GO:0009793]; mRNA transport [GO:0051028]; protein transport [GO:0015031]; RNA export from nucleus [GO:0006405]; zygote asymmetric cell division [GO:0010070] | mitochondrion [GO:0005739]; nuclear pore [GO:0005643] | structural constituent of nuclear pore [GO:0017056] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. | null | null | null | null | null | FUNCTION: Required for normal embryogenesis and seed viability. Involved in the first asymmetrical cell division of the zygote. Regulates the number and planes of cell divisions required for generating the normal embryo proper and suspensor, apical-basal axis, cotyledons and meristem. {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:22898497}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I240 | JMJ17_ARATH | MLLCDSCNKGWHIYCLSPPLKHIPLGNWYCLECLNTDEETFGFVPGKCLLLEDFKRIADRAKRKWFGSGTVSRTQIEKKFWEIVEGSGGEVEVMYGNDLDTSVYGSGFPRIGDQRPESVEADIWDEYCGSPWNLNNMPKLKGSMLQAIRHNINGVTVPWLYLGMLFSSFCWHFEDHCFYSVNYLHWGEAKCWYGIPGSAASAFEKVMRKTLPDLFDAQPDLLFQLVTMLSPTVLQENKVPVYTVLQEPGNFVITFPKSFHAGFNFGLNCAEAVNFATADWLPYGGSGAELYRLYRKPSVISHEELLCVVAKGNCCNNEGSIHLKKELLRIYSKEKTWREQLWKSGILRSSPMFVPECADSVGIEEDPTCIICQQFLHLSAIVCNCRPSVFACLEHWKHLCECEPTKLRLEYRYTLAELDMMVQEVEKFGGCKTQETKISQRPSSGTKRSIALNKKEGMQVSQARPADKWLLRASKVLDAAFSSVEYATLLKESEQFLWAGSEMDRVRDVTKSLNKAKIWAEAVSDCLSKVEGEVNDDSMKVHLEFIDELLRVNPVPCFNSGYLKLKDYAEEARKLSEKIDSALSSSPTITQLELLHSEVSRSPISLKKHEILSKKISSAKMLAKRAKRYLTDAKPPGIEMDALFKLNSEMLELHVQLPETEGILDLVKKSESARDKSNKVLTGSLSLENVEELLHEFDSFSINVPELNILRQYHVDTLSWISRFNDVMVDVREGKDQRKLISDLSSLLRDGASLGIQVEGLPLVEVELKKASCREKARTVYTARKSLDFIEQLLSEAVILHIEEEEIFVEISGILSTARCWEERASTILENETQMYELKDLVRMSVNIDAVLPTLQGIENTISSAETWLQKSEPFLSATSSMASSPCSMLELPVLKDLVTQAKLLNVQLQEPRILETLLLNCERWQCDNHQLLQETEDLLDNAKIDDGTHSNILPKIMDLITRVDSARRSGLALGLNFDELPKLRTASLKLGWCCKTITLSSSSPTSELLEDVGKPSLQHIQQHLKEGQTLEILPEEYYLGKRLMELKDTGLEWAKRARKVVTDSGALALEDVFELISEGENLPVHAEQELQSLRARSMLHCICLKPYNSRSMVSCSQCGEWYHTYCLKLHWRPKAYVCSACCPLAETTPQIDPARATEPERPSLNQRRTRMVATDAAVNDLKWKTRKHIKRTTKRSPQVHILPWFFT | 1.14.11.67 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8GUI6}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6}; | abscisic acid-activated signaling pathway [GO:0009738]; developmental growth [GO:0048589]; negative regulation of gene expression, epigenetic [GO:0045814]; plant organ development [GO:0099402]; regulation of DNA-templated transcription [GO:0006355]; regulation of stomatal closure [GO:0090333]; response to abscisic acid [GO:0009737]; response to water deprivation [GO:0009414] | chromatin [GO:0000785]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565] | PF02373;PF00628;PF08429;PF02928; | 2.60.120.650;3.30.40.10; | JARID1 histone demethylase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:31038749}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:31038749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213; Evidence={ECO:0000269|PubMed:31038749}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60216, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:31038749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217; Evidence={ECO:0000269|PubMed:31038749}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60220, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:31038749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60221; Evidence={ECO:0000269|PubMed:31038749}; CATALYTIC ACTIVITY: Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67; Evidence={ECO:0000269|PubMed:31038749}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60209; Evidence={ECO:0000269|PubMed:31038749}; | null | null | null | null | FUNCTION: Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression (PubMed:31038749). Active on H3K4me1, H3K4me2 and H3K4me3 (PubMed:31038749). Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation (PubMed:31038749). Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression (PubMed:31038749). Together with JMJ14 and JMJ16, required for plant growth and development (PubMed:31038749). {ECO:0000269|PubMed:31038749}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I2H7 | TPX2_ARATH | MEATAEESVSTLVTTMVDETYEFLAPRWFDFVNGETEDESRRAELWFQSALSCAPSPSVPRIKARRSFKVEAMCNFNEAEEETLKDKEPLEPVVPIVSLQSQPSQAKKAEVAPSKASTVKPSRISSKDAEVNNKTVDASDPTTEPIEDKENIAPACTPKPPMQFSLGAKSVDLKKQQTARKIASLLKNPSTLRPKNQSQAKGSHQKSVKGETNLNNIASTTNLIQENQAIKRQKLDDGKSRQILNPKPATLLHKTRNGLVNTGFNLCPSVTKHTPKENRKVYVREQIAPFVSTAELMKKFQTSTRDLFVQNRPKLTLTRPKEPEFVTSQRARPLRVKSSAELEEEMLAKIPKFKARPVNKKILAAPALPAPQRSTPHLPEFQEFHLQTMARANQHAETSSIASTEVSKQHNDQKHHLTEPKSPVLQTMLRARPTIAKTTAELEQEELEKAPKFKAKPLNKKIFESKGEMGIFCNTKKHITIPQEFHFATDERISRPESVLDIFDKLSLNSESCHEKPLPRNTAPNPFNLKTEERGAEKEKKFYMELMYKKLGDVKARVPKANPYPYTTDYPVVPPKPEPKQCTQPEPFQLESLVRHEEEMRREREERRRMETEEAQKRLFKAQPVIKEDPIPVPEKVRMPLTEIQEFNLHVEHRAVERADFDHKIKEKENQYKRYREESEAAKMVEEERALKQMRKTMVPHARPVPNFNKPFLPQKSNKGTTKAKSPNLRVIKRTERRTMMARPTISAATSASAVHCLMYPGSSFNKLKKKTVLTNIVHCLMYPDSSLLN | null | null | cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly [GO:0090307]; regulation of mitotic spindle organization [GO:0060236]; spindle assembly [GO:0051225] | chloroplast envelope [GO:0009941]; microtubule [GO:0005874]; nuclear microtubule [GO:0005880]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; phragmoplast [GO:0009524]; spindle [GO:0005819] | microtubule binding [GO:0008017]; protein kinase activator activity [GO:0030295] | PF06886;PF12214; | null | TPX2 family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Located in the nucleoplasm during interphase until late G2, in the perinuclear region during early prophase, and at the spindle during mitosis. Localized on a specific subset of phragmoplast microtubules in early telophase. | null | null | null | null | null | FUNCTION: Regulates prospindle assembly during late prophase and at the onset of mitosis, before nuclear envelope breakdown (NEB). Is exported from the nucleus shortly before NEB and organized into two polar crescents. After NEB, is progressively associated with the forming spindle. Probably mediates AUR1 activation and localization to spindle microtubules. Has a microtubule binding capability and is able to trigger microtubule assembly induced by RanGTP in a heterologous system. Not involved in phragmoplast assembly, nuclear envelope reformation, and cortical microtubule assembly at the onset of G1 (PubMed:18941054). Involved in the formation of specific nuclear and perinuclear microtubular arrays in the nuclei of acentrosomal plant cells. Fungi and plants have acentrosomal microtubule arrays because they lack centrosomes. They use other microtubule organizing center (MTOC) structures to organize their microtubules. May function through interaction with importin (PubMed:24006426). {ECO:0000269|PubMed:18941054, ECO:0000269|PubMed:24006426}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I2J8 | CATIN_ARATH | MGSHGKGKRDRSGRQKKRRDESESGSESESYTSDSDGSDDLSPPRSSRRKKGSSSRRTRRRSSSDDSSDSDGGRKSKKRSSSKDYSEEKVTEYMSKKAQKKALRAAKKLKTQSVSGYSNDSNPFGDSNLTETFVWRKKIEKDVHRGVPLEEFSVKAEKRRHRERMTEVEKVKKRREERAVEKARHEEEMALLARERARAEFHDWEKKEEEFHFDQSKVRSEIRLREGRLKPIDVLCKHLDGSDDLDIELSEPYMVFKKKKVRIGIWLNFQLSITNVYVEAEYKNDSACLLLRSRVDILLNKGLTVKDMEELRDDIKMYLDLDRATPTRVQYWEALIVVCDWELAEARKRDALDRARVRGEEPPAELLAQERGLHAGVEADVRKLLDGKTHAELVELQLDIESQLRSGSAKVVEYWEAVLKRLEIYKAKACLKEIHAEMLRRHLHRLEQLSEGEDDVEVNPGLTRVVEENEEEINDTNLSDAEEAFSPEPVAEEEEADEAAEAAGSFSPELMHGDDREEAIDPEEDKKLLQMKRMIVLEKQKKRLKEAMDSKPAPVEDNLELKAMKAMGAMEEGDAIFGSNAEVNLDSEVYWWHDKYRPRKPKYFNRVHTGYEWNKYNQTHYDHDNPPPKIVQGYKFNIFYPDLVDKIKAPIYTIEKDGTSAETCMIRFHAGPPYEDIAFRIVNKEWEYSHKKGFKCTFERGILHLYFNFKRHRYRR | null | null | embryo development ending in seed dormancy [GO:0009793]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | null | PF10312;PF09732; | null | CACTIN family | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:23454656}. | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Required for embryogenesis (PubMed:23454656). {ECO:0000250|UniProtKB:Q8WUQ7, ECO:0000269|PubMed:23454656}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I2N7 | RLK7_ARATH | MAPSLRNFNFFHRFSTFLVFSLFSVVSSDDLQVLLKLKSSFADSNLAVFDSWKLNSGIGPCSFIGVTCNSRGNVTEIDLSRRGLSGNFPFDSVCEIQSLEKLSLGFNSLSGIIPSDLKNCTSLKYLDLGNNLFSGAFPEFSSLNQLQFLYLNNSAFSGVFPWKSLRNATSLVVLSLGDNPFDATADFPVEVVSLKKLSWLYLSNCSIAGKIPPAIGDLTELRNLEISDSGLTGEIPSEISKLTNLWQLELYNNSLTGKLPTGFGNLKNLTYLDASTNLLQGDLSELRSLTNLVSLQMFENEFSGEIPLEFGEFKDLVNLSLYTNKLTGSLPQGLGSLADFDFIDASENLLTGPIPPDMCKNGKMKALLLLQNNLTGSIPESYANCLTLQRFRVSENNLNGTVPAGLWGLPKLEIIDIEMNNFEGPITADIKNGKMLGALYLGFNKLSDELPEEIGDTESLTKVELNNNRFTGKIPSSIGKLKGLSSLKMQSNGFSGEIPDSIGSCSMLSDVNMAQNSISGEIPHTLGSLPTLNALNLSDNKLSGRIPESLSSLRLSLLDLSNNRLSGRIPLSLSSYNGSFNGNPGLCSTTIKSFNRCINPSRSHGDTRVFVLCIVFGLLILLASLVFFLYLKKTEKKEGRSLKHESWSIKSFRKMSFTEDDIIDSIKEENLIGRGGCGDVYRVVLGDGKEVAVKHIRCSSTQKNFSSAMPILTEREGRSKEFETEVQTLSSIRHLNVVKLYCSITSDDSSLLVYEYLPNGSLWDMLHSCKKSNLGWETRYDIALGAAKGLEYLHHGYERPVIHRDVKSSNILLDEFLKPRIADFGLAKILQASNGGPESTHVVAGTYGYIAPAEYGYASKVTEKCDVYSFGVVLMELVTGKKPIEAEFGESKDIVNWVSNNLKSKESVMEIVDKKIGEMYREDAVKMLRIAIICTARLPGLRPTMRSVVQMIEDAEPCRLMGIVISKESDVKVKEIS | 2.7.11.1 | null | innate immune response [GO:0045087]; protein autophosphorylation [GO:0046777]; response to oxidative stress [GO:0006979]; seed germination [GO:0009845] | membrane [GO:0016020] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | 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}; 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}; | null | null | null | null | FUNCTION: Plays a role in pattern-triggered immunity (PTI) signaling induced by pathogen-associated molecular patterns (PAMPs). Acts as a receptor for PIP1 defense peptide. PIP1 is an endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response (PubMed:25188390). Involved in the control of seed germination speed, in tolerance to oxidative stress and in maintaining seed longevity (PubMed:20811905). {ECO:0000269|PubMed:20811905, ECO:0000269|PubMed:25188390}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I313 | SCY2A_ARATH | MSINMRTLTQALAKTAAVIEKTVQTTVQEVTGPKPLQDYELLDQIGSGGPGLAWKLYSAKARDSTRPQQYPTVCVWVLDKRALSEARARAGLSKAAEDAFLDLIRADSGKLVRLRHPGVVHVVQALDENKNAMAMVTEPLFASVANALGNVENVDNVPKDLKSMEMSLLEVKHGLLQIAETLNFLHNNAHLIHRAVSPENVFITSAGSWKLAGFGFAISQAQDGNLDNLQSFHYSEYDVEDSILPLQPSLNYTAPELVRSKTSSAGVSSDIFSFGCLTYHLVARKPLFDCHNNVKMYMNTLNYLTNETFSSIPSDLVSDLQRMLSMNESYRPTALDFTGSSFFRSDTRLRALRFLDHMLERDNMQKSEFLKALSDMWKDFDSRVLRYKVLPPLCAELRNLVMQPVILPMVLTIAESQDKNDFELTTLPALVPVLSTATGDTLLLLIKRAELIINKTNAEHLVSHVLPLLLRAYNDNDVRIQEEVLKRSTSVAKQLDGQVVRQAILPRVHGLALKTTVAAVRVNALLCLAELVQTLDKLAVTEILQTIQRCTAVDRSAPTLMCTLAIANAILKQYGVEFTSEHVLPLIIPLLTAQQLNVQQFAKYILFVKDILRKIEEKRGVTVNDSGVPEVKPGCVADGLQFQTPTKKTEKVASAAKNSPAWDEDWALPTKISAPRDPGPANSPQFNNSTVQSQSSNRTSVPTTCPAVDLEWPPRQSFNATAQPANDETRINAAGTPTTPSFDELDPFANWPPRPNSASTASGGFHNSTTTQPPINNSGSGLRNNLTDGRQFQTTNNDFWAFGNASLSSMKSQQETSGIRASNADPLTSFGIQNQNQGMPSFGSSSYGNQKPQADISSIFSSSRTEQSAMKLAPPPSIAVGRGRGRGRSGTSISKPNGSKQQQTEQPSLLDLL | null | null | null | Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; trans-Golgi network membrane [GO:0032588] | ATP binding [GO:0005524]; clathrin heavy chain binding [GO:0032050]; protein kinase activity [GO:0004672] | PF00069; | 1.25.10.10;1.10.510.10; | Protein kinase superfamily | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:28751315}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28751315}. Prevacuolar compartment membrane {ECO:0000269|PubMed:28751315}. Note=Colocalizes with the clathrin heavy chain 1 (CHC1). {ECO:0000269|PubMed:28751315}. | null | null | null | null | null | FUNCTION: Probably inactive kinase (PubMed:28751315). Component of the AP2-containing clathrin coat that regulates clathrin-dependent trafficking at plasma membrane, TGN and endosomal system (PubMed:28751315). Together with SCYL2B, required for cell growth, plant growth and development (PubMed:28751315). {ECO:0000269|PubMed:28751315}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I316 | SUN3_ARATH | MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPLSLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINNTGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNSRNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTIKIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGVDAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSEPVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQEGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTGSGAWLLLLISSTFIMFVLSL | null | null | defense response to bacterium [GO:0042742]; protein folding in endoplasmic reticulum [GO:0034975]; regulation of bone remodeling [GO:0046850]; response to cold [GO:0009409]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | protein self-association [GO:0043621] | PF07738; | 2.60.120.260; | null | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR]. | Arabidopsis thaliana (Mouse-ear cress) |
F4I3P9 | MURE_ARATH | MAFTFLSPHPVFLSLTGTTSSFSYKPVLLPFSRNSRTLTVAAGPARRNSYPNPADDDPPEAPEDSMHGVSKFQQIQRQAARARKLEEEDFEKNRNTYLSAIADVEDAAETGRDDEESGGDLFSDIDRAISMKRSEFVKQGLLKPNPPKTASLKKIGEEGNEEEGDVTDDVDELDEEEVVDLDEIDKLTGLTEISDEEDWVDEEGNTRINKKKEFGSDHQFEFDLDDFGESKARIVEPKFKMCLAELLDESKVVPISVYGDLDVEITGIQHDSRGVSAGDLFVCCLGSENFLSEADKRGAVAVVASKEIDIEDTLGCRALVIVEDTNAVLAALASSFYRHPSKNMSVIGVTGTDGKTTTTYLIKSLYEAMGVRTGMFSTVSCYIHGDNKLDTPNATMNPDAVLVQSLMAKMLHNGTESLVMEASPQELALGKCDEVDFDIAVFTNLTRENTDFRGTDEEYRDAEAKLFSRMVDPERHRKVVNIDDPNAAFFVQQGNPNVPVVTFAMENTKADVHPLKFELSLFETQVLVNTPQGILEISSGLLGRHNIYNILAAVAVGIAVGAPLEDIVRGVEEVDAVPGRCELIDEEQAFGVIVDHANTPDGLSRLLDSIRELKPRRIITVIGCEGENERGKRPLMTKIATEKSDVTMLTSDNPRNEDPLDILDDMLSGIGWTMQEYLKHGEHDYYPPLANGHRLFLHDIRRVAVRCAVAMGEEGDMVVVAGKGHEAYQLEGEKKEFYDDREECREALQYVDELHQAGIDTSEFPWRLPESH | null | null | biosynthetic process [GO:0009058]; cell division [GO:0051301]; chloroplast fission [GO:0010020]; chloroplast organization [GO:0009658]; regulation of cell shape [GO:0008360] | chloroplast [GO:0009507]; chloroplast nucleoid [GO:0042644] | acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524] | PF01225;PF02875;PF08245; | 3.90.190.20;3.40.1190.10;3.40.1390.10; | MurCDEF family, MurE subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18036201}. | null | null | null | null | null | FUNCTION: Involved in chloroplast biogenesis. Required for thylakoid membrane development. Seems to be required for plastid-encoded plastid RNA polymerase (PEP)-dependent gene expression. {ECO:0000269|PubMed:18036201}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I3V6 | SHW1_ARATH | MAAATTTLSSSSSSPSLTLINASHRFVSVTPFSSNSIFLRRRFRRLNRSLASSSSHSRRRYESDDRFFGGGDNYDVVPDDDGFSDDDDEEDERESSVDLLIRFLRSMFKKVSKRTKKASRRILPAAMSPRLVSFAVDGILLLGSLSITRAFLEVICNLGGTVFTVILLIRLFWAAASFFQTYGNSFGPNPVN | null | null | abscisic acid-activated signaling pathway [GO:0009738]; flower development [GO:0009908]; negative regulation of photomorphogenesis [GO:0010100]; positive gravitropism [GO:0009958]; positive regulation of lateral root development [GO:1901333]; positive regulation of long-day photoperiodism, flowering [GO:0048578]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; regulation of anthocyanin biosynthetic process [GO:0031540]; regulation of chlorophyll biosynthetic process [GO:0010380]; regulation of red or far-red light signaling pathway [GO:0090227]; response to light intensity [GO:0009642]; response to light stimulus [GO:0009416] | nuclear membrane [GO:0031965]; nucleus [GO:0005634] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:26474641}; Multi-pass membrane protein {ECO:0000255}. Note=Constitutively localized in the nucleus of hypocotyl cells. {ECO:0000269|PubMed:18375596}. | null | null | null | null | null | FUNCTION: Negative regulator of photomorphogenesis modulating both light and abscisic acid (ABA) signaling pathways (PubMed:18375596, PubMed:19704523, PubMed:26474641). Negatively regulates the light-mediated inhibition of hypocotyl elongation, probably in a PHYB-mediated signaling pathway, but promotes flowering time (especially in long days) and lateral root formation (PubMed:18375596, PubMed:19704523). Enhances light-regulated gene expression (PubMed:18375596). Promotes COP1-mediated degradation of HY5 during seedling development (e.g. hypocotyl growth) through enhanced ubiquitination in the darkness. Also involved in root gravitropism (PubMed:18375596, PubMed:26474641). {ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:19704523, ECO:0000269|PubMed:26474641}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I443 | BARD1_ARATH | MAEFTNMLMNPWVLHLQKLELELKCPLCLKLLNRPVLLPCDHVFCDSCVHKSSQVESGCPVCKSKHPKKARRDLRFMESVISIYKSLNAAVSVHLPQLQIPNDCNYKNDALNNSNSPKHGESEDSEMTDKDVSKRSGGTDSSSRDGSPLPTSEESDPRPKHQDWTEKQLSDHLLLYEFESEYDAANHTPESYTEQAAKNVRDITASEQPSNAARKRICGDSFIQESSPNPKTQDPTLLRLMESLRSDDPTDYVKAQNHQQLPKSHTEQDSKRKRDITASDAMENHLKVPKRENNLMQKSADIDCNGKCSANSDDQLSEKISKALEQTSSNITICGFCQSARVSEATGEMLHYSRGRPVDGDDIFRSNVIHVHSACIEWAPQVYYEGDTVKNLKAELARGMKIKCTKCSLKGAALGCFVKSCRRSYHVPCAREISRCRWDYEDFLLLCPAHSSVKFPNEKSGHRVSRAEPLPKINPAELCSLEQTPAFTKELVLCGSALSKSDKKLMESLAVRFNATISRYWNPSVTHVIASTDEKGACTRTLKVLMGILNGKWIINAAWMKASLKASQPVDEEPFEIQIDTQGCQDGPKTARLRAETNKPKLFEGLKFYFFGDFYKGYKEDLQNLVKVAGGTILNTEDELGAESSNNVNDQRSSSIVVYNIDPPHGCALGEEVTIIWQRANDAEALASQTGSRLVGHTWVLESIAGYKLHPVIG | null | null | DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; leaf development [GO:0048366]; maintenance of root meristem identity [GO:0010078]; maintenance of shoot apical meristem identity [GO:0010492]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fatty acid biosynthetic process [GO:0045717]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-DNA complex assembly [GO:0065004]; regulation of meristem structural organization [GO:0009934] | BRCA1-A complex [GO:0070531]; BRCA1-BARD1 complex [GO:0031436]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842] | PF00533;PF13923;PF13771; | 3.40.50.10190;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16957774, ECO:0000305|PubMed:18591352}. | null | null | null | null | null | FUNCTION: Binds specifically to H3K4me3 regions of target genes (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. Required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem (PubMed:18591352, PubMed:25631790). Plays a role in DNA repair and in cell-cycle control. Required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR) (PubMed:16957774). {ECO:0000269|PubMed:16957774, ECO:0000269|PubMed:18591352, ECO:0000269|PubMed:25631790}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I460 | MYO8_ARATH | MVATFNPAVGSHVWVEDPDEAWLDGEVVEINGDQIKVLCASGKQVVVKDSNIYPKDVEAPASGVEDMTRLAYLHEPGVLQNLQSRYDINEIYTYTGSILIAVNPFRRLPHLYSSHMMTQYKGASLGELSPHPFAVADAAYRQMVNEGVSQSILVSGESGAGKTESTKLLMRYLAFMGGRGAATEGRTVEQKVLESNPVLEAFGNAKTVKNNNSSRFGKFVEIQFDQSGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEEDAKKFKLGDPKIYHYLNQSKCIQLDAMNDAEEYHATKKAMDVVGISSEEQDAIFRVVASILHLGNIEFAKGTEIDSSIPRDEKSWFHLKTAAELLMCNEKSLEDSLCKRIMATRDETITKTLDPEAALLSRDALAKVMYSRLFDWLVEKINTSIGQDPDSKYLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYKKEEINWSYIEFVDNQDILDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTYKNHKRFTKPKLARSDFTICHYAGDVTYQTELFLDKNKDYVIAEHQALLNASTCSFVANLFPPVSDDSKQSKFSSIGTRFKQQLVSLLEILNTTEPHYIRCIKPNNLLKPGIFENQNVLQQLRCGGVMEAIRISCAGYPTRKHFDEFLNRFGIIAPQVLDKNSNEPAACKKLLDKAGLEGYQIGKSKVFLRAGQMADLDTRRTEILGRSASIIQRKVRSYLAQKTFIQLRISATQIQAVCRGYLARSIYEGMRREAAALKIQRDLRKFLARKAYTELFSATILIQAGMRGMVSRKELCLRRQTKAATIIQTRCRVYLARLHYRKLKKAAITTQCAWRGKVARKELKNLKMAARETGALQEAKNKLEKQVEELTWRLQLEKRMRTDLEEAKKQENAKYESSLEEIQNKFKETEALLIKEREAAKTVSEVLPIIKEVPVVDQELMEKLTNENEKLKGMVSSLEIKIDETAKELHETARISQDRLKQALAAESKVAKLKTAMQRLEEKISDMETEKQIMLQQTILNTPVKSVAGHPPTATIKNLENGHRTNLENQFNEVEVNGNAGKSAAERQLENVDTLIDCVKENIGFSNGKPIAAFTIYKCLLHWKCFESEKTSAFDRLIEMIGSAIENEDDNGHLAYWLTNTSALLFLLQKSLKPAGAGATASKKPPITTSLFGRMALSFRSSPNLAAAAEAAALAVIRPVEAKYPALLFKQQLAAYVEKIFGMIRDNLKKELSALISMCIQAPRISKGGIQRSARSLGKDSPAIHWQSIIDGLNSLLAILKDNYVPLVLIQKIHTQTFSFVNVQLFNSLLLRKECCTFSNGEFVKSGLAELELWCGQVNEYAGPSWDELKHIRQAVGFLVIHQKYRVSYDDIVHDLCPILSVQQLYRICTLYWDDCYNTRSVSQEVISSMRALMTEESNDADSNSFLLDDNSSIPFSIDEISNSMHEKDFASVKPAKELLENPEFVFLH | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; root hair elongation [GO:0048767]; vesicle transport along actin filament [GO:0030050] | cytoplasm [GO:0005737]; myosin complex [GO:0016459]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146] | PF01843;PF00612;PF00063;PF02736; | 1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family, Plant myosin class XI subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617}. Note=Colocalizes with cytoplasmic vesicles and/or organelles. | null | null | null | null | null | FUNCTION: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. {ECO:0000269|PubMed:20581304}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I4F2 | RHS3_ARATH | MLLKPGNKLVSPETSHHRDSASNSSNHKCQQQKPRKDKQKQVEQNTKKIEEHQIKSESTLLISNHNVNMSSQSNNSESTSTNNSSKPHTGGDIRWDAVNSLKSRGIKLGISDFRVLKRLGYGDIGSVYLVELKGANPTTYFAMKVMDKASLVSRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCSGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVNPTLVKSFNGGGTTGIIDDNAAVQGCYQPSAFFPRMLQSSKKNRKSKSDFDGSLPELMAEPTNVKSMSFVGTHEYLAPEIIKNEGHGSAVDWWTFGIFIYELLHGATPFKGQGNKATLYNVIGQPLRFPEYSQVSSTAKDLIKGLLVKEPQNRIAYKRGATEIKQHPFFEGVNWALIRGETPPHLPEPVDFSCYVKKEKESLPPAATEKKSKMFDEANKSGSDPDYIVFEYF | 2.7.11.1 | null | phosphorylation [GO:0016310]; root hair cell development [GO:0080147] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Autophosphorylated and phosphorylated by PDPK1/PDK1. {ECO:0000269|PubMed:16973627}. | null | 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:16973627}; 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:16973627}; | null | null | null | null | FUNCTION: Involved in root hair growth and morphogenesis. {ECO:0000269|PubMed:19448035}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I562 | AP3M_ARATH | MLQCIFLISDSGEVMLEKQLTGHRVDRSICAWFWDQYISQGDSFKALPVIASPTHYLFQIVRDGITFLACSQVEMPPLMAIEFLCRVADVLSEYLGGLNEDLIKDNFIIVYELLDEMIDNGFPLTTEPSILKEMIAPPNLVSKMLSVVTGNASNVSDTLPSGAGSCVPWRPTDPKYSSNEVYVDLVEEMDAIVNRDGELVKCEIYGEVQMNSQLTGFPDLTLSFANPSILEDMRFHPCVRYRPWESHQVLSFVPPDGEFKLMSYRVKKLKNTPVYVKPQITSDSGTCRISVLVGIRSDPGKTIESITLSFQLPHCVSSADLSSNHGTVTILSNKTCTWTIGRIPKDKTPCLSGTLALEPGLERLHVFPTFKLGFKIMGIALSGLRIEKLDLQTIPPRLYKGFRAQTRAGEFDVRL | null | null | endocytosis [GO:0006897]; gravitropism [GO:0009630]; intracellular protein transport [GO:0006886] | clathrin adaptor complex [GO:0030131]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794] | null | PF00928; | 3.30.450.60;2.60.40.1170; | Adaptor complexes medium subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Part of the AP-3 complex, an adaptor-related complex which seems to be clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. It also functions in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles. {ECO:0000269|PubMed:21670741}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I5N6 | RIC3_ARATH | MATVKGLLKGLRYITQIFDEEKDKDMQIGFPTDVKHVAHIGSDGPATNVPSWMGDFKPQENENGQVVSRADANNNQIGEGVGLQELLPPTDKPKHKKTRRKSETVSQNGSPPRRNSSASASDMQPKNTRRHHRSRHGSIDSSNDPSVRRRRVVSVTTNDMEGSYPLSDSSTHSRKSTSRHRKPKGSGGGELSMKKTKGKTENPIVESVDTCNDNNISDKE | null | null | establishment of vesicle localization [GO:0051650]; pollen tube growth [GO:0009860]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of actin filament depolymerization [GO:0030834]; regulation of calcium-mediated signaling [GO:0050848]; regulation of exocytosis [GO:0017157] | cytoplasm [GO:0005737] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15824136}. | null | null | null | null | null | FUNCTION: Functions as a downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Functions as a downstream effector of ARAC11/ROP1 to activate calcium signaling that leads to F-actin disassembly associated with exocytosis in the tip of the growing pollen tube. Counteracts the ARAC11/ROP1-RIC4 pathway, which promotes apical F-actin assembly associated with vesicle accumulation, to control actin dynamics and pollen tube apical growth. {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15824136, ECO:0000269|PubMed:18591430}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I6G4 | JMJ18_ARATH | MENPPLESEIKEDMSLKNHPPDKDKDKDTIMEQPSSPRHRKVVARWLPDEAQRPIINDAPVFTPSLEEFVDPLAYIEKIRPLAEPYGICRIIPPSTWKPPCRLKEKSIWEQTKFPTRIQTVDLLQNREPMKKKPKSRKRKRRRNSRMGSSKRRSGSSPAESTSSPEAEEKFGFNSGSDFTLDEFEKYALHFKDSYFEKKDSGGDIVKWTPSVDDIEGEYWRIVEQPTDEVEVYYGADLENGVLGSGFYKRAEKFTGSDMEQYTLSGWNLNNLPRLPGSVLSFEDCDISGVLVPWLYVGMCFSSFCWHVEDHHLYSLNYHHFGEPKVWYGVPGSNATALEKAMRKHLPDLFEEQPDLLHGLVTQFSPSILKDEGVQAYRVVQNSGEYVLTFPRAYHAGFNCGFNCAEAVNVAPVDWLAHGQNAVELYSKETRKTSLSHDKLLLGAAYEAVKALWELSASEGKENTTNLRWKSFCGKNGTLTNAIQARLQMEEGRITALGRDSSSLKKMEKDFDSNCERECFSCFYDLHLSASGCKCSPEEYACLKHADDLCSCDVKDGFILLRYTMDELSSLVRALEGESDDLKIWASKVLGIEHSDEDQTKTSSVISEEKKLKEGSFDLNIDLEMDYQEDVKEEASTSGGELTASENLGVSVEPINLGFLIFGKLWCNKYAIFPKGFRSRVKFYNVLDPTRMSNYISEVLDAGLMGPLFRVTLEESPDESFFNVSAQQCWEMVMRRVKDTSTSLGLPILPQFESINGLQMFGFLSPSIVQAIEALDPNHRLVEYWNHKNQTSSDSKDHFISSNCSASLTKGKLFGVDLM | 1.14.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8GUI6}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6}; | photoperiodism, flowering [GO:0048573]; regulation of DNA-templated transcription [GO:0006355] | chromatin [GO:0000785]; nucleus [GO:0005634] | histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976] | PF05965;PF05964;PF02373;PF02375;PF02928; | 3.30.160.360;2.60.120.650; | JARID1 histone demethylase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:22536163}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:22536163}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213; Evidence={ECO:0000269|PubMed:22536163}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60216, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:22536163}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217; Evidence={ECO:0000269|PubMed:22536163}; | null | null | null | null | FUNCTION: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 and H3K4me2. No activity on H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC. {ECO:0000269|PubMed:22536163}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I6M1 | POLIA_ARATH | MAMGVSLTSHNNPLLRHLSPSSSWVSRSSSRLSSSPLPSFLFPCRRTLLQRKLASTDGNVGYCTTTVCQGFQHSVHQRSSSVVFNGEWELRSESNKVRMVPKIIKVGNQTEVAETHQVPGTVSAWREEANKLRERNGQIARNLDDNGYFNGSVPIISSAPSYETSQKIDYEFKPRGTTRSTTATLNKELIGITQSEPVVSLPRKGLDVGDNMDVNPKGEGIQRPLISDKSSGTANGNKNTVAISKVERSTEPSNVRENLGKIYDKVLIVDNVQAAKDTVAKLVNQFRNHVHSCDTEVSGIEVKEETPVDHGELICFSIYCGPEADFGNGKSCIWVDVLGENGREVLAEFKPYFEDSFIRKVWHNYSFDSHIIRNHGIEISGFHADTMHMARLWDSARRIKGGYSLEALTSDPKVLGGTQTKEEAEFLGKISMKTIFGKRKLKKDGSEGKIVVIPPVEELQREDREAWISYSALDAISTLKLYESMTKKLQLMDWHLDGKPVLGRTMLDFYHEFWRPFGELLVKMEAEGILVDREYLAEIEKVAKAEQQVAGSRFRNWASKYCPDAKYMNIGSDTQLRQLFFGGISNSHDEVLPVEKLFKVPNIDKVIEEGKKTPTKFRNIKLHRISDSPLSTENFTASGWPSVGGDVLKELAGKVSAEYDFMDDVSDISLEEVVEDDDVETSETQKSKTDDETDTSAYGTAYVAFGGGERGKEACHAIASLCEVCSIDSLISNFILPLQGSNVSGKDGRVHCSLNINTETGRLSARRPNLQNQPALEKDRYKIRKAFVASPGNTLVVADYGQLELRILAHLTGCKSMMEAFKAGGDFHSRTAMNMYPHVREAVENGQVILEWHPEPGEDKPPVPLLKDAFGSERRKAKMLNFSIAYGKTAVGLSRDWKVSTKEAQETVDLWYNDRQEVRKWQEMRKKEAIEDGYVLTLLGRSRRFPASKSRAQRNHIQRAAINTPVQGSAADVAMCAMLEISINQQLKKLGWRLLLQIHDEVILEGPIESAEIAKDIVVDCMSKPFNGRNILSVDLSVDAKCAQNWYAAK | 2.7.7.7 | null | double-strand break repair [GO:0006302]; mitochondrial DNA replication [GO:0006264]; plastid DNA replication [GO:0033259] | chloroplast [GO:0009507]; mitochondrion [GO:0005739] | 3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887] | PF00476;PF01612; | 3.30.70.370;1.10.150.20;3.30.420.10; | DNA polymerase type-A family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion. Note=Targeted to chloroplast when translation is initiated at the AUG initiator start, and to mitochondrion when it is initiated at a non-canonical CTG leucine codon located 21-bp upstream of the initiator methionine codon. {ECO:0000269|PubMed:16169894}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; | null | null | null | null | FUNCTION: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity (By similarity). Required for DNA replication and accumulation in plastids and mitochondria. May be required for DNA repair in both organelles. {ECO:0000250, ECO:0000269|PubMed:21427281, ECO:0000269|PubMed:23167278}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I718 | CSI3_ARATH | MLKAFLPGTQEEETLSSLQSGKVDAKMEMDDPEKAMATVAQLIEQLHAKTSSPQDKELTTARLLGIAKGKREARRLIGSYGQAMPLFISMLRNGTTLAKVNVASILCVLCKDKDLRLKVLLGGCIPPLLSVLKSGTMETRKAAAEAIYEVSSAGISNDHIGMKIFITEGVVPTLWDQLSLKGNQDKVVEGYVTGALRNLCGVDDGYWRLTLEGSGVDIVVSLLSSDNPNSQANAASLLARLVLSFCDSIQKILNSGVVKSLIQLLEQKNDINVRASAADALEALSANSDEAKKCVKDAGGVHALIEAIVAPSKECMQGKHGQSLQEHATGALANVFGGMRHLIIYLGQVSQSPRLTEPIGDVIGALAYALMIFKQPESSENIFDPSVIESILVKLLKPRDTKLIQERILEAMASLYGNSSLSCYLDDAEAKRVLIALITMASADVRERLIICLSGLCHDKVGIWEAIGKREGIQLFISFLGLSSEQHQEYAVEMLKILTAQVDDSKWAVTAAGGIPPLVQLLETGSQKAKEDAACILWNLCCHSEEIRDCVERAGGIPAFLWLLKTGGPNSQETSAKTLVKLVHTADPATINQLLALLLGDDPTSKIQVIEVLGHVLSKASQEDLVHRGCAANKGLRSLVESLTSSREETKEHTASVLADLFSSRQDICGHLATDDIINPWIKLLTNNTQNVAKQVARALDALSRPVKNNNNKKKSYIAEGDIKSLIKLAKNSSIESAENAVSALANLLSDPDIAAEALAEDVVSAFTRILADGSPEGKRNASRALHQLLKNFPVCDVLKGSAQCRFAILSLVDSLKSIDVDSADAFNILEVVALLAKTKSGVNFSYPPWIALAEVPSSLETLVQCLAEGHTLVQDKAIEVLSRLCSDQQFLLSELIVSRPKSMLVLADRIVNASSLEVRVGSTALLLCAAKEKKQLITETLDQSGFLKLLLHALVDMIKHNSTSFSLETEVQTPKGFLEKNVFQDTGSFYFPDPAKILGGTVALWLLCILTSVDAKSKVIVMEAGGLEVLVGKLARYTSSAQAEFEDTEGIWISALLLAIMFQDDNVSFSSTTMRIIPTLAVLLGSDELIDRYFAAHAMASLVCTRNRGINLTIANSGAVSGIINLLGYVESEILNLVALANEFSLVKEPDQVILQHLFEIEDVRLGSTARKSIPLLVDLLRPIPDRPGAPQFAVQILIRIADGSDTNKLLMAEAGAVEALTKYLSLSPQDSTEYAISELLRVLFSNHELRQNEMALSSLNQLIAVLRLGSRSARYSAAGALNELFDAENIRNSEIACQAVQPLMDILGSVSESEQEVALSALIKLSSGNTSNTALLIDVEGSLLENVIKILSSATASEELKINAARLCSVVFSNKNIRTSASASGCMKPLITLMQSERSAAVEAAVFAIKILLDDEQHLELAAAHNIQELLVGLVSGKNYVIIEASLSALIKLGKDRVPRKLDMVEAGIIERCLELLPGASSSLCSAVVELFRILTNSGVIARRPDVAKTVEPLFAVLLRSDLTLWGQHSALQALVNILEKQQTLEAFSFTPSEAIVPLISFLESSSQAIQQLGAELLSHFLTMEDFQQDITTQSAVVPLVRLAGIGILSLQETAIKALEKISASWPKAVLDAEGIFELSKVILQEDPQPPLDLWESAAFVLSNILQYDAECFFRVELPVLVKLLFSTIESTVLLALKALMLHEKNDASSTVQMAELGAIDALLDLLRSHQCEEESGSLLEVIFNNPRVRELKLCKYAIAPLSQYLLDPHTRSEPGRLLAALALGDLSQHEGLSRSSGSVSACRALISVLEEQPTEEMKVVAICALQNFVMNSRTNRRAVAEAGGVLLIQELLLSCNPEVSGQAALMVKFLFSNHTLQEYVSNELIRSLTAALERGLWSTATINIEVLRTLNVIFSNFPKLRASEAATFCIPHLVGALKSGVEDVQGLVLDILYLLRHSWTNMSIDVAKSQAMIAAEAIPVLQMLMKTCPPRFHDKADSLLHCLPGCLTVNVMRANNLKQSMATTNAFCQLTIGNCPPRQTKVVSNSTTPEWKEGFTWAFDVPPKGQKLHIICKSKSTFGKTTLGRVTIQIDKVVTEGEYSGSLSLNHENSKDASSRSLDIEIAWSNRTTDETH | null | null | anisotropic cell growth [GO:0051211]; plant-type cell wall cellulose biosynthetic process [GO:0052324]; protein localization to cortical microtubule cytoskeleton [GO:0072699]; regulation of cell shape [GO:0008360]; regulation of cellulose biosynthetic process [GO:2001006]; unidimensional cell growth [GO:0009826] | cellulose synthase complex [GO:0010330]; cortical microtubule [GO:0055028]; endomembrane system [GO:0012505]; plasma membrane [GO:0005886] | microtubule binding [GO:0008017] | PF00514;PF00168; | 2.60.40.150;1.25.10.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24368796}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:F4IIM1}. Endomembrane system {ECO:0000269|PubMed:24368796}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24368796}. Note=Colocalizes with cellulase synthase (CESA) complexes (CSCs) in a CSI1-dependent dynamic way. Present with cortical microtubules. {ECO:0000269|PubMed:24368796}. | null | null | null | null | null | FUNCTION: Regulator of the microtubular cytoskeleton (By similarity). Microtubule-associated protein involved in the association of cellulase synthase (CESA) complexes (CSCs) and cortical microtubules. Promotes dynamics of CSCs in the plasma membrane in both microtubules-dependent and microtubules-independent manners. Regulates primary cell wall biosynthesis and cellulose microfibrils organization (PubMed:24368796). {ECO:0000250|UniProtKB:F4IIM1, ECO:0000269|PubMed:24368796}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I735 | PDS5B_ARATH | MEKTPTQIVSELCSRLLQLSRPNKDSLVKLLREVANTLSKIDQPSATNKEKGLKLIEAELRPLKKSIIKHALLKNRDNDVSLLVTVCVSELFRILAPHLPFEDEYLRDIFTLFIAEFSELSDTVSPYFSKRAKILETVSRLKFCLLMLDEDCQDLVHEMFNMFFSLVREHHQQSLINQKSMKTQQRKANTQQTQHSLFNNILAIMSDVLEEEANSSFVVVILENLVKEGEDTTSGADKLASSLIERCADRLEPLICSFLTSCFMEKDSIQTNLKDSYHEIIFKISLIAPQMLLAVIPKLTQELLTDQVDVRIKALNLAGRIFAQPKHCLSSYVETYQDLYAEFLRRFSDKSAEVRMAALKCGKQCYFANPSGNKASGVLTAIQERLLDFDDRVRTQALIVACDIMKFNMKYVPLNLISEASERLRDKKISVRKKALQKLTEVYQDYCDKCSEGDMTITDNFEQIPCKILLLCCEKNCEEFRSQNLELVLSDDLFPRLLPVEERMRHWVQCFAIMNHIHLKSLNSILSQKRRLQNELRHCLTLWRKAKVDNIEEAQRKKKSYFVKLSACFPDASEAEDLFEKLDRMRDASIFDVLTLLLEELSSTNAQIIKEKFLKMIGVKHSLFEFLRILSTKCSPSIFSSEHVQCLLNQLCGSTSANTQLKAPSIKLLLVILNMFPSYLRGSEKQFLKLLEENDSAADELIVVLSKAAPYISVNFGDYYPVLEKVCLEGTRSQTKCAVSAISSLAGSSEKSVFSELCEMLMDSLLCGRNIPTTLQSLACVGQYSVLEYDNIYEDITSYIYRVFQAEPSDNQLPCDQSSGCCNSCKLKIYGLKTLVKSFLPRHGQVVRKIDDLLNILKKTLKSQGHDGIKSCEDTGANVRLAAAKAVLLLSRKWDLHISPEVFRLTILMAKDSNAFITKTFLTKLYKLLTEHMIPSRYACAFSFSLSSPCRDLHDDSFRYINGFINKATRESRTCRDLDQGESLTDSPVYMTVFLIHVLAHDPEFPSEDCRDEHIYARFCGPLFSVLQVLLSINNNGFTIKETAPFLFCIFRAIKRAEDAVDSRKTPRLHILADIGYSAVNILNSIVVTSPQAPRSILLPSSLYSLTSITDNQNKAKSRTRNALEQSFIERIVHIFQSQISMHDQRCQKDSLAVGSEDKVLPPLLGNQIETSITGSTEASQNNTRCSRKRTHLGEHISCNSLSLRTVESEIPIKKLERHTTCAKESVKASVSNKITSSKHSGVVSALKDISNHGEAIIGQRIKLLSPTDGCFYPGTVEKFNSKSNSHKIIFDNGDVELVCLDSESWETLSHESMGQQERLGKETESYGSRNCVPEISHTLAKVTAQKQTTTTKQQNKKVPAKLNPPAVPCFMMSAKSKKGNSDSGEGSVSEVTDTSDNIGPRRSRRQRIS | null | null | cell division [GO:0051301]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; homologous recombination [GO:0035825]; leaf morphogenesis [GO:0009965]; mitotic sister chromatid cohesion [GO:0007064]; proximal/distal pattern formation [GO:0009954] | chromatin [GO:0000785]; nucleus [GO:0005634] | null | PF20168; | 2.30.30.140;1.25.10.10; | PDS5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | null | null | null | null | null | FUNCTION: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex (PubMed:26648949). Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin (PubMed:26648949). May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (PubMed:26648949). Required for proximal-distal cell cycle-driven leaf growth in both lamina and petiole (PubMed:24946828). {ECO:0000250|UniProtKB:Q29RF7, ECO:0000269|PubMed:24946828, ECO:0000269|PubMed:26648949}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I7C7 | WAPL1_ARATH | MIIVKLTANRICCSLLQLRRSYEHFYIFVFLPEIPLFRFSHLKLFPKNLQIQRLVSAMMERTYGRRKPGIPRTLSDSLNDSVSQTEYLSSSSSPDIEPIDYSLLPFSSQESSSLWHSSSRSNFREDYPQNGGVVRRAKRVRNGAEAAAFTSTLLEAQEFGELMEHEDEVNFALDGLRKGHQLRIRRASLSSLLSICASQHQRRSLRAQGISQSIIDAILVLSLDDIPSNLAAATLFFALTADGQDEHFMESPKCIKFLIKLLKPVIVTSTEGKPRNIGFKLLSLLKDVDAARDPVKMDDPSSSDILSRVQELLVNCKEMRLNDSYITETTRPELSTKWVALLAMERACVSKISFDDTSGSVKKTGGNFKEKLRELGGLDAVLEVVMDCHAVMERWVEYDALSVQEKKDNLHKQSLMLLLKCLKIMENATFLSTDNQNHLLGFKKCLGSHDSRMSFTELTISVIKMLSGLHLRGGFSSPNTNNVNSHYSNGGNHDSVLEANRKVTNEVVTISSDTYSTVGSISTRNGSVSQRSQSIIHLDFSPTSMSGSQSSVSGNEPTTSKTRVGSTISGSFAGRLASLGSDIARTTLRTTQAGEPICKKFGEFAPPEESEDPFAFDLEDYKPSKWAVVSVNQKKSRAQKKKGCYKQSKDESLYQLFSSQEESSNHRLNSQEESSNRDCSTSLQPSHCTNDIDEECLCLLFDCLLTAVKVLMNLTNDNVVGCRQVGGCRGLESMAELIARHFPSFTRSQLFSEMEKTGSSHQKKDKYLTDQELDFLVAILGLLVNLVERDGVNRSRLASASVPITKPEELQESEQEMIPLLCSIFLTNQGSAETKEETTTFTLDDEEAVLEGEKEAEKMIVEAYSALLLAFLSTESRSIRNSIKDYLPKRNLAILVPVLERFVAFHMTLNMIPPETHKAVMGVIESCKSP | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; embryo development ending in seed dormancy [GO:0009793]; meiotic chromosome segregation [GO:0045132]; meiotic sister chromatid cohesion [GO:0051177]; meiotic sister chromatid cohesion involved in meiosis I [GO:0010789]; meiotic sister chromatid segregation [GO:0045144]; mitotic sister chromatid cohesion [GO:0007064]; mitotic sister chromatid segregation [GO:0000070]; regulation of cohesin loading [GO:0071922] | chromosome [GO:0005694]; nucleus [GO:0005634] | null | PF07814; | 1.25.10.10; | WAPL family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z5K2}. Chromosome {ECO:0000250|UniProtKB:Q7Z5K2}. | null | null | null | null | null | FUNCTION: Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of CTF7 (PubMed:25033056, PubMed:26813623). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). Essential for the prophase removal of cohesin during meiosis thus determining the timely release of meiotic cohesion (PubMed:25033056). Important for proper spindle attachment and assembly during meiosis (PubMed:25033056). Helps to prevent abnormal centromere association during prophase I in meiocytes (PubMed:25033056). Required for early embryonic patterning (PubMed:25033056). Also involved in chromosome segregation during mitosis (PubMed:25033056). {ECO:0000250|UniProtKB:Q7Z5K2, ECO:0000269|PubMed:25033056, ECO:0000269|PubMed:26813623}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I7I0 | ALAT1_ARATH | MRRFVIGQAKNLIDQSRRRQLHHHKNLSFVSLIPPFSAPSDSSSRHLSSSSSSDMSASDSSSSLPVTLDTINPKVIKCEYAVRGEIVNIAQKLQEDLKTNKDAYPFDEIIYCNIGNPQSLGQQPITFFREVLALCSYTALLDESATHGLFSSDSIERAWKILDQIPGRATGAYSHSQGIKGLRDAIADGIEARDGFPADPNDIFMTDGASPGVHMMMQLLITSEKDGILCPIPQYPLYSASIALHGGTLVPYYLDEASGWGLEISELKKQLEDARSKGITVRALAVINPGNPTGQVLSEENQRDVVKFCKQEGLVLLADEVYQENVYVPDKKFHSFKKVARSMGYGEKDLALVSFQSVSKGYYGECGKRGGYMEVTGFTSDVREQIYKMASVNLCSNISGQILASLIMSPPKPGDDSYESYIAEKDGILSSLARRAKTLEEALNKLEGVTCNRAEGAMYLFPCLHLPQKAIAAAEAEKTAPDNFYCKRLLKATGIVVVPGSGFRQVPGTWHFRCTILPQEDKIPAIVDRLTAFHQSFMDEFRD | 2.6.1.-; 2.6.1.2 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q93ZN9}; | biosynthetic process [GO:0009058]; cellular response to hypoxia [GO:0071456]; L-alanine catabolic process, by transamination [GO:0019481]; response to cadmium ion [GO:0046686]; response to hypoxia [GO:0001666] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; L-alanine:2-oxoglutarate aminotransferase activity [GO:0004021]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 1.10.287.1970;3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family, Alanine aminotransferase subfamily | PTM: The N-terminus is blocked. {ECO:0000250}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate; Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2; Evidence={ECO:0000269|PubMed:17319845}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19454; Evidence={ECO:0000269|PubMed:17319845}; | null | PATHWAY: Photosynthesis; C4 acid pathway. {ECO:0000305}.; PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Is the major alanine aminotransferase in roots that catalyzes the conversion of alanine to pyruvate (PubMed:17319845). Involved in the rapid conversion of alanine to pyruvate during recovery from low-oxygen stress (PubMed:17319845). {ECO:0000269|PubMed:17319845}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I7Y4 | BSK11_ARATH | MGCCQSSFLKPSSLHDKKITSDDLSGRRGKGAKRGNRHRHANINEGRGWHFSDVPDFSEFSASVLRDATNNFNKNAVVSVCSDQEPNLVYQGCIRSDKDKRLIAVKKFSKTTWPDPKQFATEARAIGSLRHVRLVNLIGYCCEGDERLLVSEYMPNESLTKHLFHWEKQTMEWAMRLRVALYVAEALEYCRQSGLKLYHDLNTCRVLFDENGSPRLSCFGWMKNSKDGKNFSTNLAYTPPEYLRSGTLIPESVVFSFGTFLLDLLSGKHIPPSHAVGTIQKQNLNVLMDSHLEGNYPEEDAAMVFDLASKCLHNNPNERPEIGDIISVITTLQQKLDVPSYTMLGISKLEKLEMEHPKSLIYDACHQMDLAALHQILEAMEYKEDEVTCELSFQQWAQQIKDVCNTRQQGDSAFRNKHFESAIDKYTQFIEIGIMISPTVYARRSMCYLFCDQPDAALRDAMQAQCVYSDWPTAFYLQAVALSKLNMVEDSATMLKEALILEDKRGS | 2.7.11.1 | null | brassinosteroid mediated signaling pathway [GO:0009742]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF07714; | 1.25.40.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2. {ECO:0000269|PubMed:23496207}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12912986}; Lipid-anchor {ECO:0000305|PubMed:12912986}. | 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}; 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}; | null | null | null | null | FUNCTION: Probable serine/threonine kinase that acts as a positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. {ECO:0000250|UniProtKB:Q944A7}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I893 | ILA_ARATH | MSYSMVNASSAVSSPETAKNSDEPPPISSEAVNVLFPSVDPNSKLFRNSLNITISREAPPLTTSRIDFLSLFIFCKLTHWLSLNPSSHRDEEEEEASPFYPFTIVLTYQPGPGQSPWKEMASPLESLLSISGSVSTSSTLIRLRIFRHDIPEILQNSDMTSDIAPVIVDMIFQTLAIYDDRASRKAVDDLIVKGLGNVTFMKTFAAMLVQVMEKQLKFCFDTVCYRLLIWSCLLLEKSQFATVSKNAFVRVASTQASLLRIIMESSFRMRRACKRFMFHLFSQSQAIYSLYMDEVKGSRIPYKDSPELLGLLLEFSCSSPALFEQSKAIFVDIYVKDVLNSREKQKPNLSNCFKPLLQRLSHEEFQTVILPAAVKMLKRNPEIVLESVGFLLANVNIDLSKYALELLPVILPQARHTDEDRRLGALSMVMCLSEKSSNPDTIEAMFASVKAIIGGSEGRLQSPHQRIGMLNAVQELASAPEGKYIGSLSRTICSFLIACYKDEGNEDVKLSILSAVASWASRSSVAIQPNLVSFIAAGLKEKEALRRGHLRCVRIICRNPDTISQISDLLSPLIQLVKTGFTKAVQRLDGIYALLIVSKIAACDIKAEDTMVKEKLWTLISQNEPSLVQITLASKLSSDDCVVCVDLLEVLLVEHSSRVLEAFSLKSLSQLLLFLLCHPSWNVRKTAYNSVTKIFLATSQLATTLLDEFSDFLSITGDQIVSSRTSDADNPADHQAPFVPSVEVLVKALIVISSAAVAGPPSSWIVRAIFCSHHPSIVGTGKRDAVWKRLQKCLKTCGFDVATFLSTNGESVCKSLLGPMGLTSAKTPEQQAAVYSLSTMMSLAPEDTFTVFKMHLQDLPDRLSHDMLSETDIKIFHTPEGMLLSEQGVYVAQTIGAKYTKQEPSSNHSLKKGLASRETANSGRRDTAKLTKKADKGKTAKEEARELMLKEEASTRENVHRIQKSLSLVLHALGEMGLANPVFCHSQLPFLATFLDPLLRSPIVSAAAFENLVKLARCTVQPLCNWALEISTALRLIAIDEVDTSFDFRPSVDKAGKTYEGLFERIVNGLSISCKSGPLPVDTFTFIFPVLYHVLGVVPAYQASVGPALNELCLGLQADDVANALYGVYSKDVHVRLACLNAVKCIPAVSKCSLPQNVKIATNIWIALHDPEKSVAESADDLWARYGHDLGTDYSGIFKALSHINLNVRLAAAEALADALHESPSSIQLSLSTLFSLYIRDATSGEDVFDAGWIGRQGIALALQSAADVLTTKDLPAVMTFLISRALADPNTDVRGKMINAGIMIIDKHGKENVSLLFPIFENYLNKEASDEEEYDLVREGVVIFTGALAKHLARDDPKVHNVVEKLLEVLNTPSESVQRAVSTCLSPLVLSKQEEAPALFLRLLDKLMKSDKYGERRGAAFGLAGVVMGFGISSLKKYGLIVTLQEALIDRNSAKRREGALLAFECLCEKLGKLFEPYVIKMLPLLLVSFSDQVGAVREAAECAARAMMSQLSAYGVKLVLPSLLKGLEDKAWRTKQSSVQLLGAMAFCAPQQLSQCLPRVVPKLTEVFKTIQVLTDTHPKVQSAGQLALQQVGSVIKNPEISSLVPTLLLALTDPNEYTRHALDTLLQTTFVNSVDAPSLALLVPIVHRGLRERSSETKKKASQIVGNMCSLVTEPKDMIPYIGLLLPEVKKVLVDPIPEVRSVAARAVGSLIRGMGEDNFPDLVPWLFETLKSDTSNVERYGAAQGLSEVIAALGTDYFENILPDLIRHCSHQKASVRDGYLTLFKFLPRSLGAQFQKYLQLVLPAILDGLADENESVRDAALGAGHVLVEHHATTSLPLLLPAVEDGIFNDNWRIRQSSVELLGDLLFKVAGTSGKALLEGGSDDEGASTEAQGRAIIDILGMDKRNEVLAALYMVRTDVSLSVRQAALHVWKTIVANTPKTLKEIMPILMSTLISSLASPSSERRQVAGRSLGELVRKLGERVLPLIIPILSKGLKDPDVDKRQGVCIGLNEVMASAGRSQLLSFMDQLIPTIRTALCDSALEVRESAGLAFSTLYKSAGLQAMDEIIPTLLEALEDDEMSTTALDGLKQIISVRTAAVLPHILPKLVHLPLSALNAHALGALAEVAGAGFNTHLGTILPALLSAMGGENKEVQELAQEAAERVVLVIDEEGVETLLSELLKGVSDSQASIRRSSAYLIGYFFKSSKLYLIDEAPNMISTLIVMLSDSDSTTVAVSWEALARVIGSVPKEVLPSYIKLVRDAVSTARDKERRKRKGGYVVIPGLCLPKSLKPLLPVFLQGLISGSAELREQAAIGLGELIEVTSEQALKEFVIPITGPLIRIIGDRFPWQVKSAILATLIILIQRGGMALKPFLPQLQTTFVKCLQDSTRTIRSSAAVALGKLSALSTRIDPLVGDLMTSFQAADSGVREAILSAMRGVIKHAGKSIGPAVRVRIFDLLKDLMHHEDDQVRISATSMLGVLSQYLEAAQLSVLLQEVNDLSASQNWGARHGSVLCISSLLKHNPSTIMTSSLFSSMLNSLKSSLKDEKFPLRESSTKALGRLLLKQLATDPSNTKVVIDVLSSIVSALHDDSSEVRRRALSSLKAFAKDNPSATMANISVIGPPLAECLKDGNTPVRLAAERCALHVFQLTKGAENVQAAQKYITGLDARRLSKFPEQSDDSESDDDNVSG | null | null | cellular response to amino acid starvation [GO:0034198]; defense response to bacterium [GO:0042742]; induced systemic resistance [GO:0009682]; innate immune response [GO:0045087]; regulation of translation [GO:0006417]; systemic acquired resistance [GO:0009627] | nucleus [GO:0005634] | protein kinase regulator activity [GO:0019887] | null | 1.25.10.10; | GCN1 family | null | null | null | null | null | null | null | FUNCTION: Involved in immunity against bacterial infection and in non-host resistance (PubMed:20360018). Required for embryo development (PubMed:17915010). Required for systemic acquired resistance, but functions in an salicylic acid-independent manner (PubMed:20360018). Required for bacterium-triggered stomatal closure response (PubMed:21998587). {ECO:0000269|PubMed:17915010, ECO:0000269|PubMed:20360018, ECO:0000269|PubMed:21998587}. | Arabidopsis thaliana (Mouse-ear cress) |
F4I8I0 | SUN4_ARATH | MQRSRRALLVRRRVSETTSNGRNRFYKVSLSLVFLIWGLVFLSTLWISHVDGDKGRSLVDSVEKGEPDDERADETAESVDATSLESTSVHSNPGLSSDVDIAAAGESKGSETILKQLEVDNTIVIVGNVTESKDNVPMKQSEINNNTVPGNDTETTGSKLDQLSRAVPLGLDEFKSRASNSRDKSLSGQVTGVIHRMEPGGKEYNYAAASKGAKVLSSNKEAKGASSIICRDKDKYLRNPCSTEGKFVVIELSEETLVNTIKIANFEHYSSNLKDFEILGTLVYPTDTWVHLGNFTALNMKHEQNFTFADPKWVRYLKLNLLSHYGSEFYCTLSLLEVYGVDAVERMLEDLISIQDKNILKLQEGDTEQKEKKTMQAKESFESDEDKSKQKEKEQEASPENAVVKDEVSLEKRKLPDPVEEIKHQPGSRMPGDTVLKILMQKIRSLDVSLSVLESYLEERSLKYGMIFKEMDLEASKREKEVETMRLEVEGMKEREENTKKEAMEMRKWRMRVETELEKAENEKEKVKERLEQVLERLEWMEKKGVVVFTICVGFGTIAVVAVVFGMGIVRAEKQGGLAWLLLLISSTFVMFILSL | null | null | nucleus organization [GO:0006997]; protein folding in endoplasmic reticulum [GO:0034975] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965] | protein self-association [GO:0043621] | PF07738; | 2.60.120.260; | null | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR]. | Arabidopsis thaliana (Mouse-ear cress) |
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