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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
F4JI44 | NDX_ARATH | MVRLLQPKHMVQAVNALHWRNSVEFHKLLKDNGDFSICFNSEQVLPQKISVEKMVKMLPRHLIAVVMTPNKDGKSRYILCGIRLLQTLCDLTPRNAKLEQVLLDDVKLSAQMIDLVILVIIALGRNRKESCNSNKESLLEATLVASCLHLFHGFISPNSQDLVLVLLAHPRVDVFIDSAFGAVLNVVISLKAKLLYRQTDSPKKLGASSVEEVNFHCQQAEAALQFLHSLCQHKPFRERVAKNKELCGKGGVLRLAQSILSLTITPEFVGATVTIASTSRMKAKVLSILQHLFEAESVSFLDEVANAGNLHLAKTVASEVLKLLRLGLSKASMATASPDYPMGFVLLNAMRLADVLTDDSNFRSFFTEHFSMVLSAVFCLSHGDFLSMLCSSDLSSREDDANVDYDLFKSAGWILSVFSSSGQSVTPQFKLSLQNNLTMSSYAHQRTSLFIKMIANLHCFVPNVCQEQDRNRFIQNVMSGLRKDPSSILIKMLPGSSYTPVAQRGTGVCRNLGSLLRHAESLIPSSLNEEDFLLLRVFCDQLQPLIHSEFEESQVQVKVKKLFALLYIGFTILWLICLVTLIQDIEGRGGNLSGKLKELLNLNNEEASEDCDVRVEGVMTKQGVNEEIDTVERLKESDADASNLETSGSDTSSNRGKGLVEEGELVQNMSKRFKGSASGEVKEDEKSETFLVFEKQKKKRKRSIMNADQMGMIEKALAEEPDLQRNSASRQLWADKISQKGSEVITSSQLKNWLNNRKAKLARANKQTGPAHDNNSSGDLPESPGDENTWQQKPSTPIKDQTVTETPKTGENLMRTSSSSEEGIKQGQQVRLMDERGDEIGKGTVLRTDGEWNGLSLETRQICVVDVMELSESYDGSKKMIPYGSDDVGRTFTEANSRFGVMRVAWDVNKLQY | null | null | flower development [GO:0009908]; negative regulation of antisense RNA transcription [GO:0060195]; root development [GO:0048364]; seed germination [GO:0009845] | nucleolus [GO:0005730]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; single-stranded DNA binding [GO:0003697] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23641115}. Nucleus, nucleolus {ECO:0000269|PubMed:23641115}. | null | null | null | null | null | FUNCTION: Regulates COOLAIR, a set of antisense transcripts originating from the 3' end of FLOWERING LOCUS C (FLC). Associates with single-stranded DNA that is part of an RNA-DNA hybrid, or R-loop, that covers the COOLAIR promoter. R-loop stabilization mediated by NDX inhibits COOLAIR transcription, which in turn modifies FLC expression. {ECO:0000269|PubMed:23641115}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JIN3 | DNJ29_ARATH | MAESEENSVLFPIFILTMMAIPLVPYTFVKLSRAFSKKQRSIHCQCLECDRSGKYKRSISQSISSFTSCSNLTVVLLWIVMIFLIYHTKNMSRESQLFEPFGILGLEPGASDSEIKKAYRRLSIQYHPDKNPDPEANKYFVESIAKAYQALTDPLSRENFEKYGHPDGRQGYTMGIALPQFILNMNGESGGILLLCTVGLCILLPLVIASIYLWRSSKYTGNHVKLQTRQAYFELLQPSLTPSKVMDIFIRAAEYAEISVRKSDDESLQKLFMSVKSELNLDPKKLKQEEAKFWKKHPATIKTELLIQKQLTRESSVLSPTLQRDFRHVLEFAPRLLEDLIKMAVIPRNEQGRGWLRPALGVMELSQCIVQAVPLSARKSSSEDIAPFLQLPHFNESIAKSIALQVKSFQKFQELSLAERSKLLREVVSLSETDVQDIEKVLEMIPSLKINVTCKTEGEEGIQEGDIMTVQAWITLKRPNGLIGAIPHSPYFPFHKEENFWVLLADSNHVWFFQKVKFMDEAGAIAAASNTITETMEPLGASVKETNDAVKEAVEKVKSGSRLVMGRLLAPGEGTYNLTCFCLSDTWIGCDQKTSLKVEVLKRTRDVEGENAEEGLEEEDDEIEEEDYESEYSEDEEDKKRGSKKKVNKESSSEESGSDEE | null | null | post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Sec62/Sec63 complex [GO:0031207] | protein transmembrane transporter activity [GO:0008320]; RNA binding [GO:0003723] | PF00226;PF02889; | 1.10.150.20;2.60.40.150;1.10.287.110;1.10.3380.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:18718935}; Multi-pass membrane protein {ECO:0000305|PubMed:18718935}. | null | null | null | null | null | FUNCTION: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane. {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JJL0 | ENDO4_ARATH | MSSSLRQWFARVLVLTQLINGALCWGKEGHYTVCKIAESYFEEETVAAVKKLLPKSADGDLASVCSWPDEIKHHWQWRWTSPLHYVDTPDYRCNYEYCRDCHDTHKNQDRCVTGAIFNYTMQLMSASENSDTIVHYNLTEALMFLSHFIGDIHQPLHVGFLGDEGGNTITVRWYRRKTNLHHVWDNMIIESALKTYYNKSLPLMIEALQANLTNDWSNDVPLWESCQLNQTACPNPYASESINLACKYAYRNATPGTTLGDDYFLSRLPIVEKRLAQGGIRLAATLNRIFSSKPKHAGS | 3.1.30.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23620482}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23620482}; Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:23620482}; | DNA catabolic process [GO:0006308] | null | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA endonuclease activity [GO:0004521]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF02265; | 1.10.575.10; | Nuclease type I family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.30.1; Evidence={ECO:0000269|PubMed:23620482}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with RNA and ssDNA as substrates. {ECO:0000269|PubMed:23620482}; | null | FUNCTION: Endonuclease that can use single-stranded RNA and DNA as substrates (PubMed:23620482). In contradiction with PubMed:23620482, cannot hydrolyze single-stranded DNA and does not cleave mismatches (PubMed:17651368). {ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:23620482}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JJL3 | ENDO5_ARATH | MRLWIVSVLVLTHLVHGALCWGKDGHYTVCKLAEGFFEDDTIAAVKKLLPESVDGGGLADFCSWPDEIKKLSQWQWTSTLHYVNTPEYRCNYEYCRDCHDTHKHKDWCVTGAIFNYTNQLMSASENSQNIVHYNLTEALLFLSHYMGDVHQPLHTGFLGDLGGNTIIVNWYHNKSNLHHVWDNMIIDSALETYYNSSLPHMIQALQAKLKNGWSNDVPSWKSCHFHQKACPNLYASESIDLACKYAYRNATPGTTLGDEYFLSRLPVVEKRLAQGGIRLAATLNRIFSAKPKLAGL | 3.1.30.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23620482}; Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:23620482}; | DNA catabolic process [GO:0006308] | null | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA endonuclease activity [GO:0004521]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]; T/G mismatch-specific endonuclease activity [GO:0043765] | PF02265; | 1.10.575.10; | Nuclease type I family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.30.1; Evidence={ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:23620482}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with RNA and ssDNA as substrates. {ECO:0000269|PubMed:23620482}; | null | FUNCTION: Hydrolyzes, with low efficiency, only single-stranded DNA and RNA without apparent specificity for bases (PubMed:17651368, PubMed:23620482). Endonuclease that recognizes and cleaves some mismatches with high efficiency, including heteroduplex double-stranded DNA; mostly efficient on T/G, A/G and G/G mismatches, less efficient for T/T and poorly efficient for C/C, A/A, T/C and A/C (PubMed:17651368). {ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:23620482}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JKB6 | PRRP3_ARATH | MKLKKPSLPSSLLCAVPPCLSQIRLLIPRRVRVSSSTFANAKLVTLRNHTVNLHIYYCSMAGTDNRRSRHDDESPKNPNKKKKGNRNPEKSLLINLHSCSKRKDLSAALALYDAAITSSDIRLNQQHFQSLLYLCSAFISDPSLQTVAIDRGFQIFDRMVSSGISPNESSVTAVARLAAAKGDGDYAFKLVKDLVAVGGVSVPRLRTYAPALLCFCDTLEAEKGYEVEDHMDASGIVLEEAEISALLKVSAATGRENKVYRYLQKLRECVGCVSEETSKAIEEWFYGVKASEVSDNGIGSDIELLRAAVLKNGGGWHGLGWVGEGKWIVKKGNVSSAGKCLSCDEHLACVDTNEVETEDFVNSLVTLAMERKAKMNSCEPMADFSEFQEWLEKHGDYEAILDGANIGLYQQNFADGGFSLPQLEAVVKELYNKSGSKKQPLILLHKKRVNALLENPNHRNLVEEWINNNVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLSNSFFQKWKERHQVRFTFVKGCLKLEMPPPFSVVIQESEKGSWHVPITSQDKEESLRSWMCITRQSS | 3.1.26.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q66GI4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q66GI4}; Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q66GI4}; | mRNA processing [GO:0006397]; sno(s)RNA processing [GO:0043144]; tRNA 5'-leader removal [GO:0001682] | nucleus [GO:0005634] | metal ion binding [GO:0046872]; ribonuclease P activity [GO:0004526] | PF17177;PF16953; | 3.40.50.11980;1.25.40.10; | PPR family, P subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20473316}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000269|PubMed:22549728}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 uM for tRNA(Gln) precursor {ECO:0000269|PubMed:22549728}; | null | null | null | FUNCTION: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA). {ECO:0000269|PubMed:22549728}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JKH6 | REC2_ARATH | MAPKAGKTKPHKSKGEKKKKEEKVLPTVIEISVETPDESQVTLKGISTDRILDVRKLLAVHVQTCHFTNFSLSHQVRGTKLKDSVDIVSLKPCHLTIVEEDYTEEQATAHIRRLLDIVACTTAFGPSKPPVSRTLPKDSEKKESGSTDGDSPTEKDAGDSNSGLSPKPKESEKKSVGACEAQSAEGAAKSDIDMCPPTRLGQFYEFFSFSYLTPPIQYIRRSVRPSKEDKGLDDLFQIDIKVSSGKPFTVVASRTGFYPPGKQQLLCHSLVELLQQISRPFDAAYDALMKAFIEHNKFGNLPYGFRANTWVVPPVVADSPSTFPSLPVEDETWGGDGGGVGRSGKYDKRKWAKEFAILAAMPCKTPEERQVRDRKAFLLHSLFVDVSVFKAVEIIKKIVENNQCSLKDPAALGFHEERIGDLIVRVARDDPDASAKLDRKSDGTQVLEISQEELAQRNLLKGITADESATVHDTSTLGVVVVRHCGCTAIVKVASEFKLNDGHILQDIDIEDQSEGGANALNVNSLRTLLHKSSTPSSLAQRSPNADSEQIRVAKSLVRKVIEDSLKKLEIEPSRYSKPIRWELGACWVQHLQNQASSKSESKKTEDPKPEPAVKGLGKQGALLKEIKRKIDVKANKTEQGKEAPANDTDNTSETEDQKELEKQNEEIEKMWKELVTETAYQRLKESETGFHLKSPKELIEMARKYYTDTALPKLVADFGSLELSPVDGRTLTDFMHTRGLQMHSLGRVVELAEKLPHVQSLCVHEMIVRAYKHILQAVVAAVENTADVATSIATCLNVLLGTPSDTESVYDEKIKWTWVETFISKRFGWDWKHEGCQELRKFSILRGLSHKVGLELVPKDYEMDTSYPFKKFDIISMVPVYKHVACSSADGRTLLESSKTSLDKGKLEDAVNYGTKALAKLVAVCGPYHRMTAGAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLAVFYYRLQHTELALKYVNRALYLLHLTCGPSHPNTAATYINVAMMEEGMKNAHVALRYLHEALKCNQRLLGADHIQTAASYHAIAIALSLMDAYSLSVQHEQTTLQILQAKLGPEDLRTQDAAAWLEYFESKALEQQEAARNGTPKPDASISSKGHLSVSDLLDYITPDSGIKARDAQRKARPKVKGKPGQSPGPVSEENQKDDEILSPAHLTGESSSDKENKSETKSEEKKVENFDLEQSKPQDQLKLVKPEATVHEDDDSDEGWQEAVPKNRFSSGRRTRPSLAKLNTNFMNVTQQPSRSRGKSTNFTSPRTSSNELSISVAGSTSSPASKMFVKSPLNKKQNNSSVVGERPVNDKSALASSACTEQINKPTPMLSPVSVKAGKLFSYKEVALAPPGTIVKIVAEQLPEETKAPQNLDAAKIAVDGPEKVNAQDAESENKHVATETEAENTDCNEQGRVVVGGSELTSSPKEIKNVEVEKAAEKAFPIETAVSNARPGKSKSAQMAEDSDTCLLNKSPTANDSNGSESVIGVKLQKDLCDAELKTVDGETENLPNGDSSPKSSVAADGEKQDACEAQKEMSKKLSASAPPYTPTTIPIFGSIAVPGFKDHGGILPSPLNMPPMLPINHVRRSTPHQSVTARVPYGPRLSGGGYNRSGNRVPRNKPSFPNSTESNGEANQFNGPRIMNPHAAEFIPSQPWVSNGYPVSPNGYLASPNGAEITQNGYPLSPVAGGYPCNMSVTQPQDGLVSEELPGAGSSEEKSGSEEESNNDKNAGEDDEAVGQETTDTPENGHSTVGEVETTSHETCDEKNGERQGGKCWGDYSDNEIEQIEVTS | null | null | cell cycle [GO:0007049]; chloroplast localization [GO:0019750]; organelle organization [GO:0006996] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | mRNA binding [GO:0003729] | PF15044;PF12807;PF13424; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:F4HS99}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:F4HS99}. | null | null | null | null | null | FUNCTION: Negatively regulates meristematic tissue proliferation by integrating developmental signals with carbon source availability (PubMed:21185286). 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 (PubMed:21185286). Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment (PubMed:26862170). {ECO:0000269|PubMed:21185286, ECO:0000269|PubMed:26862170}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JKK0 | SUD1_ARATH | MEISPADSLSISGAAASEVVSEPSVSSSSSSSSPNQASPNPFSNMDPAVSTATGSRYVDDDEDEEDVCRICRNPGDADNPLRYPCACSGSIKFVHQDCLLQWLNHSNARQCEVCKHPFSFSPVYADNAPSRLPFQEFVVGIAMKACHVLQFFLRLSFVLSVWLLTIPFITFWIWRLAFVRTFGEAQRLFLSHISTTVILTDCLHGFLLSASIVFIFLGATSLRDYFRHLRELGGQEERDDDVDRNGARAARRPAGQANRNLAGEGNGEDAGDQGAAVGQIARRNPENVLARLDIQAARLEAQVEQMFDGLDDADGAEDVPFDELVGMQGPVFHLVENAFTVLASNMIFLGVVIFVPFTLGRIILYHVSWLFAAARGPAVAASLHLTDTGLSLENITLKSALTAVSNLTSEGQGNGLLGQLTEMMKVNGSELNGANNTLSVATDLLKGSTVGASKLSDITTLAVGYMFIVFLVFLYLGIIALIRYAKGEPLTVGRFYGIASIVEAVPSLLRQFLAAMRHLMTMIKVAFLLVIELGVFPLMCGWWLDVCTVRMFGKTMSHRVQFLSISPLASSLVHWVVGIMYMLQISIFVSLLRGVLRPGVLYFLRDPADPNYNPFRDLIDDPVHKHARRVLLSVAVYGSLIVMLVFLPVKLAIRMAPSIFPLDISVSDPFTEIPADMLLFQICIPFIIEHFRLRTTIKSLLRCWFTGVGWALGLTDFLLPRPEDNIGQDNGNGEPGRQNRAQVLQVGGPDRAMAALPVADDPNRSRLRAGNVNTGEEYEDDDEQSDSDRYNFVVRIILLLLVAWVTLLLFNSALIVVPVSLGRALFSAIPILPITHGIKCNDLYAFVIGTYAFWTTISGARYAIEHVKSKRTSVLLNQIWKWCGIVFKSSVLLAIWVFIIPVLIGLLFELLVIVPMRVPVDESPVFLLYQDWALGLIFLKIWTRLVMLDHMLPIVDDSWRAKFERVREDGFSRLQGLWVLREIVFPIVMKLLTALCVPYVLARGVFPMLGYPLVVNSAVYRFAWIGCLSVSLFCFCAKRCHVWFRNLHNSIRDDRYLIGRRLHNFGEAALANQNQNQSSEDAGDGVLIGREGDVDNGLRLRRAIQQEA | 2.3.2.27 | null | cuticle development [GO:0042335]; cutin biosynthetic process [GO:0010143]; isoprenoid biosynthetic process [GO:0008299]; positive regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:1900486]; protein ubiquitination [GO:0016567]; response to water deprivation [GO:0009414]; suberin biosynthetic process [GO:0010345]; wax biosynthetic process [GO:0010025] | membrane [GO:0016020] | ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF12906; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | 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: Probable E3 ubiquitin ligase acting as a positive post-transcriptional regulator of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity. Might be involved in the quality control that degrades misfolded proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:22635115, ECO:0000269|PubMed:23404890}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JL11 | IMPA2_ARATH | MSLRPNAKTEVRRNRYKVAVDAEEGRRRREDNMVEIRKSKREESLQKKRREGLQANQLPQFAPSPVPASSTVEKKLESLPAMVGGVWSDDRSLQLEATTQFRKLLSIERSPPIEEVIDAGVVPRFVEFLTREDYPQLQFEAAWALTNIASGTSENTKVVIEHGAVPIFVQLLASQSDDVREQAVWALGNVAGDSPRCRDLVLGQGALIPLLSQLNEHAKLSMLRNATWTLSNFCRGKPQPPFDQVRPALPALERLIHSTDEEVLTDACWALSYLSDGTNDKIQSVIEAGVVPRLVELLQHQSPSVLIPALRSIGNIVTGDDLQTQCVISHGALLSLLSLLTHNHKKSIKKEACWTISNITAGNRDQIQAVCEAGLICPLVNLLQNAEFDIKKEAAWAISNATSGGSPDQIKYMVEQGVVKPLCDLLVCPDPRIITVCLEGLENILKVGEAEKVTGNTGDVNFYAQLIDDAEGLEKIENLQSHDNSEIYEKAVKILETYWLEEEDETLPPGDPSAQGFQFGGGNDAAVPPGGFNFQ | null | null | NLS-bearing protein import into nucleus [GO:0006607] | cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasmodesma [GO:0009506] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}. | null | null | null | null | null | FUNCTION: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as a cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JL28 | EBS_ARATH | MAKTRPGVASKIKTGRKELDSYTIKGTNKVVRAGDCVLMRPSDAGKPPYVARVEKIEADARNNVKVHCRWYYRPEESLGGRRQFHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENVGAEDYYCRFEYKAATGAFTPDRVAVYCKCEMPYNPDDLMVQCEGCKDWYHPACVGMTIEEAKKLDHFVCAECSSDDDVKKSQNGFTSSPADDVKVRLSLFSHLLYRCSITYL | null | null | flower development [GO:0009908]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of long-day photoperiodism, flowering [GO:0048579]; post-embryonic development [GO:0009791]; regulation of photoperiodism, flowering [GO:2000028]; seed germination [GO:0009845] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; molecular function inhibitor activity [GO:0140678]; transcription cis-regulatory region binding [GO:0000976] | PF01426;PF00628; | 2.30.30.490;3.30.40.10; | SHL1/EBS protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837946}. | null | null | null | null | null | FUNCTION: Chromatin remodeling factor that binds to methylated histone (e.g. H3K4me2/3) to prevent their acetylation (e.g. H3K9K14Ac), likely by recruiting histone deacetylase (HDAC) complexes, and thus regulating the transcription of target genes (PubMed:25281686). Negative regulator in developmental processes in a gibberellic acid- (GA-) dependent manner, such as germination, flowering induction, and flower organ specification, probably by modulating developmental gene expression (PubMed:11340178, PubMed:25281686). Involved in the chromatin-mediated repression of floral initiation and controls genes regulating flowering (PubMed:25281686). Negatively regulates the expression of the floral integrator FT epigenetically, by preventing high levels of H3 acetylation, thus maintaining an inactive chromatin conformation at FT locus (PubMed:12837946, PubMed:25281686). {ECO:0000269|PubMed:11340178, ECO:0000269|PubMed:12837946, ECO:0000269|PubMed:25281686}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JLC1 | MRL7_ARATH | MSFFAVACSAPRSSMLLTGLNSSFSDMHRSPLFVFPVTISSRSVKRFAAVSSDSVLDPESKNQTRSRRKNKEAVTPIAETENNEKFPTKVPRKSKRGRRSEADAVEDYVRSSLERTFSTIKEQNPEVFENKEKANFIKDRGVDEEEEEEEEMVVEEEDPDWPVDTDVGWGIKASEYFDTHPIKNVVGDDGSEIDWEGEIDDSWVKEINCLEWESFAFHPSPLVVLVFERYKRASDNWKTLKELEKAIKVYWDAKDRLPPRAVKIDLNIETDLAYALKAKECPQILFLRGNRILYREKDFRTADELVHMIAHFYYKAKRPSCVDKANVTPYC | null | null | chloroplast organization [GO:0009658]; regulation of DNA-templated transcription [GO:0006355]; response to temperature stimulus [GO:0009266] | chloroplast nucleoid [GO:0042644]; nucleus [GO:0005634] | null | null | 3.40.30.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:21220584, ECO:0000269|PubMed:24111559}. Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:24132784, ECO:0000269|PubMed:31201314}. Nucleus {ECO:0000269|PubMed:31201314}. Note=Associated with punctuate structures in chloroplasts. {ECO:0000269|PubMed:21220584}. | null | null | null | null | null | FUNCTION: Plays an essential role in early steps of chloroplast development (PubMed:21220584, PubMed:21515910, PubMed:23956074, PubMed:24111559, PubMed:33824329). Involved in the regulation of plastid gene expression (PubMed:21515910, PubMed:23956074, PubMed:24111559). May positively regulate plastid-encoded RNA polymerase (PEP) activity through binding to FSD3 and CITRX/TRXZ (PubMed:23956074). Involved in redox-mediated regulation of chloroplast development (PubMed:23956074, PubMed:24132784). Possesses disulfide reductase activity in vitro (PubMed:23956074). Required for the proper function of the plastid transcriptional machinery and protein accumulation in thylakoid membranes. May function as molecular chaperone to ensure proper organization of the nucleoids in chloroplasts (PubMed:24111559). May mediate some aspect of thylakoid structure or function that controls non-photochemical quenching (NPQ) (PubMed:21220584, PubMed:21515910, PubMed:23956074, PubMed:24111559, PubMed:24132784). Participates in the early light signaling events of photobody biogenesis in chloroplasts (PubMed:31201314). May mediate the degradation of two repressors of chloroplast biogenesis, PIF1 and PIF3 in nucleus (PubMed:31201314). Collaboratively with PTAC12/HMR/PAP5, involved in the regulation of thermoresponsive responses via the stabilization of PIF4 in the daytime to initiate thermomorphogenesis (PubMed:33824329). {ECO:0000269|PubMed:21220584, ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:23956074, ECO:0000269|PubMed:24111559, ECO:0000269|PubMed:24132784, ECO:0000269|PubMed:31201314, ECO:0000269|PubMed:33824329}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JLE5 | SFH1_ARATH | MAETKPEIEMSEEERKIVKISSLKKKAINASNRFKNSFKKKGRRSSSRVMSVPIEDDIDAEDLQALDAFRQALILDELLPSKLDDLHMMLRFLRARKFDIEKAKQMWSDMIQWRKDFGADTIIEDFDFEEIDEVMKHYPQGYHGVDKEGRPVYIERLGQIDANKLLQVTTMDRYVKYHVKEFEKTFKVKFPSCSVAANKHIDQSTTILDVQGVGLKNFSKSARELLQRLCKIDNENYPETLNRMFIINAGSGFRLLWSTVKSFLDPKTTAKIHVLGNKYHSKLLEVIDASELPEFFGGACTCEDKGGCMRSDKGPWNDPEVLKIAINREAKCSPISEDEHKHVDQGRSTSGFESLERIKKKTDEDNVYEKQIATIDKSMDMAWLAKTQKAENFPISKGLECYVRKGAPKKGDGLLVGGVMAFVMGIVAMVRLSKDVPRKLTEAALYGNSVCYEESTKSKQNQGQFAAPVSSSEYMLMVKRMAELEDKCMFLDLKPAHVESEKEEKLQAALNRVQVLEQELTETKKALEEALVSQKEILAYIEKKKKKKKLFFGF | null | null | cell tip growth [GO:0009932]; protein transport [GO:0015031]; root epidermal cell differentiation [GO:0010053]; root hair cell tip growth [GO:0048768]; root hair elongation [GO:0048767] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; root hair tip [GO:0035619] | null | PF00650;PF03765; | 3.40.525.10;1.10.8.20; | SFH family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:15728190}; Peripheral membrane protein {ECO:0000269|PubMed:15728190}. | null | null | null | null | null | FUNCTION: Required for transport of secretory proteins from the Golgi complex (By similarity). Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Plays a role in root hair tip elongation as a key regulator of polarized membrane trafficking. May promote the PtdIns(4,5)P2 synthesis and organization in root hair membrane. {ECO:0000250, ECO:0000269|PubMed:15546352, ECO:0000269|PubMed:15728190, ECO:0000269|PubMed:17335879, ECO:0000269|PubMed:23456248, ECO:0000269|PubMed:9390433}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JLP5 | PLPD2_ARATH | MQSVLSLSFSQASLPLANRTLCSSNAAPSTPRNLRFCGLRREAFCFSPSKQLTSCRFHIQSRRIEVSAAASSSAGNGAPSKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKAFGLQVSAAGYDRQGVADHASNLATKIRNNLTNSMKALGVDILTGFGAVLGPQKVKYGDNIITGKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINTRKIDYHTGVFASKITPAKDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENINVTTQRGFIPVDERMRVIDGNGKLVPHLYCIGDANGKLMLAHAASAQGISVVEQVTGRDHVLNHLSIPAACFTHPEISMVGLTEPQAREKAEKEGFKVSIAKTSFKANTKALAENEGEGLAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVVDELFKAAKVDSPASVTAQSVKVTV | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; | response to arsenic-containing substance [GO:0046685] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829] | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC). {ECO:0000269|PubMed:11056213}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JLZ6 | SMO13_ARATH | MIPYPTVEDASVALGRNLTWFETVWFDYSATKSNFHVYCHTILVLFLVFSLAPFPLVIVEWTGWFDQFKIQKKVKYSLSDMFQCYKEVMKLFLLVVGTLQIVSYPSIQMVGIRSGLPLPSLMEIVAQLVVYFLIEDYTNYWIHRWMHCKWGYEKIHRIHHEYTSPIGYASPYAHWAEILILGIPTFLGPAIAPGHIMTFWLWISLRQFEAIETHSGYDFPWSVTKLIPFYGGPEYHDYHHYVGGQSQSNFASVFTYCDYIYGTDKGYRIHKKLLHHQIKEEAEEKRVRKHD | 1.14.18.11; 1.14.18.9 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045}; | sterol biosynthetic process [GO:0016126] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | C-4 methylsterol oxidase activity [GO:0000254]; iron ion binding [GO:0005506] | PF04116; | null | Sterol desaturase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31341004}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58387; EC=1.14.18.9; Evidence={ECO:0000250|UniProtKB:Q8L7W5}; CATALYTIC ACTIVITY: Reaction=24-methylidenelophenol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-ergosta-7,24(24(1))-dien-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:58868, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29107, ChEBI:CHEBI:142850; EC=1.14.18.11; Evidence={ECO:0000250|UniProtKB:Q8L7W5}; | null | null | null | null | FUNCTION: Non-heme iron oxygenase involved in sterols biosynthesis by catalyzing the removal of the first methyl group at the C-4 position (By similarity). 4,4-dimethyl-9-beta,19-cyclopropylsterols such as 24-methylenecycloartanol are the preferred substrates (By similarity). {ECO:0000250|UniProtKB:Q8L7W5}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JN35 | NTL9_ARATH | MGAVSMESLPLGFRFRPTDEELVNHYLRLKINGRHSDVRVIPDIDVCKWEPWDLPALSVIKTDDPEWFFFCPRDRKYPNGHRSNRATDSGYWKATGKDRSIKSKKTLIGMKKTLVFYRGRAPKGERTNWIMHEYRPTLKDLDGTSPGQSPYVLCRLFHKPDDRVNGVKSDEAAFTASNKYSPDDTSSDLVQETPSSDAAVEKPSDYSGGCGYAHSNSTADGTMIEAPEENLWLSCDLEDQKAPLPCMDSIYAGDFSYDEIGFQFQDGTSEPDVSLTELLEEVFNNPDDFSCEESISRENPAVSPNGIFSSAKMLQSAAPEDAFFNDFMAFTDTDAEMAQLQYGSEGGASGWPSDTNSYYSDLVQQEQMINHNTENNLTEGRGIKIRARQPQNRQSTGLINQGIAPRRIRLQLQSNSEVKEREEVNEGHTVIPEAKEAAAKYSEKSGSLVKPQIKLRARGTIGQVKGERFADDEVQVQSRKRRGGKRWKVVATVMVAVMVGVGMGIWRTLVSS | null | null | cellular response to osmotic stress [GO:0071470]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of defense response to bacterium [GO:1900426]; regulation of defense response [GO:0031347]; regulation of DNA-templated transcription [GO:0006355] | endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF02365; | 2.170.150.80; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18443413}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24329768}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17947243, ECO:0000269|PubMed:18443413}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon osmotic stress or pathogen attack, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:18443413, ECO:0000269|PubMed:24329768}. | null | null | null | null | null | FUNCTION: Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (PubMed:18443413, PubMed:24329768). Calmodulin-regulated transcriptional repressor. Binds several synthetic promoters with randomly selected binding sites (PubMed:17947243). Functions synergistically with SNI1 as negative regulator of pathogen-induced PR1 expression and basal resistance to a virulent strain of P.syringae. Binds directly to the promoter of the PR1 gene (PubMed:22826500). Acts as a positive regulator of innate immunity. Involved in the effector-triggered immunity (ETI) induction of immunity-related gene expression (PubMed:24329768). Mediates osmotic stress signaling in leaf senescence by up-regulating senescence-associated genes (PubMed:18443413). {ECO:0000269|PubMed:17947243, ECO:0000269|PubMed:18443413, ECO:0000269|PubMed:22826500, ECO:0000269|PubMed:24329768}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JNX3 | CMKMT_ARATH | MDPTSSSSSALRWKILRQALLRRSDSQSQTETKRISRKATQGFNLIPCQVVDSSPQSDKSREASVCYTLPITGSPKLYLTQRVDNCSDLNDFEISNRYNIDNTGLVCQWPSEEVLAYFCKSQPERFRGKRVIELGSGYGLAGLVIAAATEASEVVISDGNPQVVNYIKRNIETNSMAFGGTSVKAMELHWNQHQLSELTNTFDIIVASDCTFFKEFHKDLARTIKMLLKAKKASEALFFSPKRGDSLEKFMKEIKDIGLHYILTENYDAQVWKRHETLVKGDEAWPNYDKNHCYPLLIQITNQI | 2.1.1.60 | null | abscisic acid-activated signaling pathway [GO:0009738]; auxin-activated signaling pathway [GO:0009734]; gravitropism [GO:0009630]; methylation [GO:0032259]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; regulation of auxin mediated signaling pathway [GO:0010928]; regulation of response to salt stress [GO:1901000]; regulation of response to water deprivation [GO:2000070]; regulation of root development [GO:2000280]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to oomycetes [GO:0002239]; response to osmotic stress [GO:0006970]; response to salt [GO:1902074]; response to salt stress [GO:0009651]; root hair cell development [GO:0080147] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | calmodulin-lysine N-methyltransferase activity [GO:0018025] | PF10294; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, CLNMT methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z624}. Nucleus {ECO:0000250|UniProtKB:Q7Z624}. | CATALYTIC ACTIVITY: Reaction=[calmodulin]-L-lysine + S-adenosyl-L-methionine = [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21556, Rhea:RHEA-COMP:11360, Rhea:RHEA-COMP:11361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.60; Evidence={ECO:0000250|UniProtKB:Q6GQ33}; | null | null | null | null | FUNCTION: Catalyzes the trimethylation of calmodulin (PubMed:24285794). Regulates roots development probably by modulating auxin signaling responses. May be involved in gravitropism. Involved in abscisic acid (ABA)-mediated and abiotic stress responses, including salt (NaCl), cold, drought and heat stresses (PubMed:24285794). {ECO:0000269|PubMed:24285794}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JNY0 | APE2_ARATH | MKIVTYNVNGLRQRVSQFDSLLKLLDSFDADIICFQETKLRRQELTADLAIADGYESFFSCTRTSEKGRTGYSGVATFCRVKSASSSCETALPVTAEEGITGLVNSNSRGGKSETSTVAEGLEEYEKEELLMIDQEGRCVITDHGHFVVFNVYGPRAVADDADRIEFKHRFYGVLERRWECLLRQGRRVFVVGDLNIAPFAMDRCEAGPDFEKNEFRKWFRSLLVERGGSFSDVFRSKHPERKDAFTCWSSSSGAEQFNYGSRIDHILVAGSCLHQDEDKQGHSFLACHVKECDILTEYKRFKNENMPTRWKGGLVTKFKGSDHVPVFISFDDLPDIPEHSTPPLASRYLPMIYGFQQTLVSVFKKRRANEEAKAIEVSCSSSTQSNTSSICGDISTGPLRNCGSMGISLEKSCSFENKSTSGVTEAETVAATGSIDNLSDGIRASSVRALNISRDGDRKKARKIQSSQLSLKSFFTTNSKVNNVEDSSSSYVSSSPSSQVESITEPNVSGKEDSEPTTSTQEQDQTGSSAKQKNDAALMEWQRIQNLMQNSIPLCKGHKEACVARVVKKPGPTFGRRFYVCSRAEKQTVVISNGLHQNSETSKRVMRSK | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25228464}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA demethylation [GO:0080111]; DNA repair [GO:0006281] | nucleus [GO:0005634] | DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; phosphoric diester hydrolase activity [GO:0008081]; polynucleotide 3'-phosphatase activity [GO:0046403]; zinc ion binding [GO:0008270] | PF03372;PF06839; | 3.60.10.10; | DNA repair enzymes AP/exoA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764}. | null | null | null | null | null | FUNCTION: Exhibits apurinic/apyrimidinic (AP) endonuclease activity in vitro (PubMed:25569774). By contrast, another report show that APE2 has no biochemical activity (PubMed:25228464). Unable to catalyze the conversion of 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) to 3'-OH (PubMed:25228464, PubMed:25569774). Has no in vitro 3'-phosphatase activity (PubMed:25228464, PubMed:25569774). Redundant with APE1L and at least one functional allele is required for seed viability (PubMed:19172180). Has a strong non-specific affinity to DNA (PubMed:25228464). {ECO:0000269|PubMed:19172180, ECO:0000269|PubMed:25228464, ECO:0000269|PubMed:25569774}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JP36 | HAP2_ARATH | MVNAILMACILAGIFVGMFNEVDGIQILSKSKLEKCEKTSDSGNLNCSTKIVLNLAVPSGSSGGEASIVAEIVEVEDNSSSNMQTVRIPPVITVNKSAAYALYDLTYIRDVPYKPQEYHVTTRKCEHDAGPDIVQICERLRDEKGNVLEQTQPICCPCGPQRRMPSSCGDIFDKMIKGKANTAHCLRFPGDWFHVFGIGQRSLGFSVRVELKTGTRVSEVIIGPENRTATANDNFLKVNLIGDFGGYTSIPSFEDFYLVIPREAAEAGQPGSLGANYSMWMLLERVRFTLDGLECNKIGVGYEAFNTQPNFCSSPYWSCLHNQLWNFRESDINRIDRHQLPLYGLEGRFERINQHPNAGPHSFSIGVTETLNTNLMIELRADDIEYVFQRSPGKIINIAIPTFEALTQFGVAAVIIKNTGEVEASYSLTFDCSKGVAFVEEQFFIIKPKAVTTRSFKLYPTKDQAAKYICTAILKDSQFSEVDRAECQFSTTATVLDNGTQVTNPFQIPETQPKGFFDSIRILWTKIINGLVDFITGDTCRNKCSSFFDFSCHIQYVCLSWMVMFGLLLALFPITCLLLWLLHQKGLFDPCYDWWEDHFDLDHHRRLLPSRADVVNRHHHHHKHRHHHNHHRRTHQRHKHHHGQDDDVLQKMMLERDHSDSHYYHQLHRVHKDSKQKQRRRAKHGIVLPRDVHVERQRKQRLRES | null | null | double fertilization forming a zygote and endosperm [GO:0009567]; fusion of sperm to egg plasma membrane involved in double fertilization forming a zygote and endosperm [GO:0061936]; plasma membrane fusion [GO:0045026]; pollen sperm cell differentiation [GO:0048235]; pollen tube guidance [GO:0010183] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | lipid binding [GO:0008289] | PF10699; | null | HAP2/GCS1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17079265, ECO:0000305|PubMed:23180860}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16378100, ECO:0000269|PubMed:17079265, ECO:0000269|PubMed:23180860, ECO:0000269|PubMed:28137780}; Single-pass type I membrane protein {ECO:0000269|PubMed:28137780}. Note=Predominantly localized in a perinuclear ring (PubMed:17079265). Redistribution to the cell membrane is mediated by EC1 peptides after their secretion upon sperm arrival (PubMed:23180860). {ECO:0000269|PubMed:17079265, ECO:0000269|PubMed:23180860}. | null | null | null | null | null | FUNCTION: Required for male fertility (PubMed:17079265, PubMed:20333238). Plays a role in pollen tube guidance and successful gamete attachment (PubMed:17079265). Essential for the fusion of gametes during double fertilization, where one male gamete fuses with the egg to produce a zygote, and another male gamete fuses with the central cell to produce the endosperm (PubMed:17079265, PubMed:20333238, PubMed:21209845). Mediates the fusion of cell membranes (PubMed:28137780). Not required for pollen tube outgrowth (PubMed:17079265, PubMed:20333238). {ECO:0000269|PubMed:16378100, ECO:0000269|PubMed:17079265, ECO:0000269|PubMed:20333238, ECO:0000269|PubMed:21209845, ECO:0000269|PubMed:23180860, ECO:0000269|PubMed:28137780}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JP52 | PQT3_ARATH | MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA | 2.3.2.27 | null | cellular response to paraquat [GO:0072756]; negative regulation of response to oxidative stress [GO:1902883]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of response to oxidative stress [GO:1902884]; protein ubiquitination [GO:0016567]; response to cadmium ion [GO:0046686]; response to hydrogen peroxide [GO:0042542]; response to mannitol [GO:0010555]; response to oxidative stress [GO:0006979]; response to paraquat [GO:1901562]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634] | ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein ligase activity [GO:0061659]; zinc ion binding [GO:0008270] | PF08783;PF13696; | 4.10.60.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:27676073}. | 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:27676073}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase acting as a negative regulator of oxidative stress tolerance, probably by mediating 26S proteasome-mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and GPX1 accumulation via the reduction of histone H3 methylation (H3R17me2a). Confers sensitivity to cadmium CdCl(2) and salt NaCl stresses. {ECO:0000269|PubMed:27676073}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JPW1 | BASS5_ARATH | MGVISPTETLFLKSQHRLLQPRNYSYALAFHSTRRVANFPRNSFSSLGSCSVDFPLRSNPISQNSKSIHPWRRYVSESDSNELYHKKVSSIMETLKQAYSFIPHGILLSTILALVYPPSFTWFKPRYFVPGLGFMMFAVGINSNERDFLEALKRPDAIFAGYIGQYLIKPLLGYIFGVIAVSLFNLPTSIGAGIMLVSCVSGAQLSNYTTFLTDPSLAALSIVMTSISTATAVLVTPMLSLLLIGKKLPVDVFGMISSILQVVITPIAAGLLLNRLFPRLSNAIKPFLPALTVIDMSCCIGAPLALNIDSILSPFGATILFLVITFHLLAFVAGYFFTGFFFSKAPDVKALQRTISYETGMQSSLLALALATKFFQDPLVGVPPAISTVVMSLMGVSLVTIWKNRKE | null | null | glucosinolate biosynthetic process [GO:0019761]; glucosinolate biosynthetic process from homomethionine [GO:0033506]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611] | chloroplast envelope [GO:0009941]; membrane [GO:0016020]; plastid [GO:0009536] | monocarboxylic acid transmembrane transporter activity [GO:0008028] | PF01758; | 1.20.1530.20; | Bile acid:sodium symporter (BASS) (TC 2.A.28) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19542295}; Multi-pass membrane protein {ECO:0000305|PubMed:19542295}. Plastid, chloroplast envelope {ECO:0000305|PubMed:19542295}. | null | null | null | null | null | FUNCTION: Plastidic transporter involved in the biosynthesis of aliphatic glucosinolates by translocating the biosynthetic intermediates of Met-derived glucosinolates across chloroplast membranes. Transports short chain (C2) alpha-keto acids, such as 4-methylsulfanyl-2-oxobutanoic acid, from the cytosol to the chloroplast where they are subjected to chain elongation cycles. Functions also in the transport of chain-elongated (C3 to C8) Met derivatives from the chloroplast to the cytosol. Does not seem to be involved in the transport of indole-derived glucosinolates. {ECO:0000269|PubMed:19542295, ECO:0000269|PubMed:19633020}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JQH3 | AMPP1_ARATH | MSEILSSLRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKKEARLWTDGRYFLQALQQLSDEWTLMRMGEDPLVEVWMSDNLPEEANIGVDSWCVSVDTANRWGKSFAKKNQKLITTTTDLVDEVWKSRPPSEMSPVVVHPLEFAGRSVSHKFEDLRAKLKQEGARGLVIAALDEVAWLYNIRGTDVAYCPVVHAFAILTTDSAFLYVDKKKVSDEANSYFNGLGVEVREYTDVISDVALLASDRLISSFASKTVQHEAAKDMEIDSDQPDRLWVDPASCCYALYSKLDAEKVLLQPSPISLSKALKNPVELEGIKNAHVRDGAAVVQYLVWLDNQMQELYGASGYFLEAEASKKKPSETSKLTEVTVSDKLESLRASKEHFRGLSFPTISSVGSNAAVIHYSPEPEACAEMDPDKIYLCDSGAQYLDGTTDITRTVHFGKPSAHEKECYTAVFKGHVALGNARFPKGTNGYTLDILARAPLWKYGLDYRHGTGHGVGSYLCVHEGPHQVSFRPSARNVPLQATMTVTDEPGYYEDGNFGIRLENVLVVNDAETEFNFGDKGYLQFEHITWAPYQVKLIDLDELTREEIDWLNTYHSKCKDILAPFMNQTEMEWLKKATEPVSVSA | 3.4.11.9 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11891249}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11891249}; Note=Binds 2 manganese or zinc ions per subunit. {ECO:0000269|PubMed:11891249}; | auxin polar transport [GO:0009926]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886] | aminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; N-1-naphthylphthalamic acid binding [GO:0010013]; zinc ion binding [GO:0008270] | PF01321;PF16189;PF00557;PF16188; | 3.90.230.10;3.40.350.10; | Peptidase M24B family | PTM: Glycosylated. Also present in a non-glycosylated form. {ECO:0000269|PubMed:11891249}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891249}. Cell membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}. Microsome membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}. | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:11891249}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=36 nmol/min/mg enzyme for Tyr-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=20 nmol/min/mg enzyme for Trp-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=74 nmol/min/mg enzyme for Ala-Pro-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=29 nmol/min/mg enzyme for Pro-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; | null | null | null | FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). Aminopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins (PubMed:11891249). {ECO:0000250|UniProtKB:Q9VJG0, ECO:0000269|PubMed:11891249}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JQZ3 | REN1_ARATH | MANKNAESSSQPPPHVQPNQQQQQQPPIANEQEQEPHGDTCSIPPAQSGNTDSRSRGGNTVFKSGPLSISSKGIGWTSWKKRWFILTRTSLVFFRSDPSAVQQKGSEVNLTLGGIDLNNSGSVVVKADKKLLTVLFPDGRDGRAFTLKADTMEDLHEWKAALENALTQAPSASHVMGQNGIFRNDHADPAVGVDEKKDETPTKSTVLGRPVLLALEDVDGAPSFLEKALRFVENHGVRIEGILRQAADVDDVEHRIREYEKGKNEFSPEEDAHIIADCLKYFLRELPSSPVPASCCNALLEACRTDRGNRVNAMRAAICESFPEPNRRLLQRILMMMQTVASNKTVNRMNTNAVAACMAPLLLRPLLAGDCEIENDFDVGGDGSMQLLQAAAAANHAQAIVITLLEEYESIFGEGSLSPGLYSDSEESGSGTEEGSDDEEYDDDDDGSQGSEDYTDEEEDLENESNGSYSESAASEDKYADSIDPDDHKINDNLSTESKSPKRSKEPKKLLSGSRRSSLPRHDDGKKDEDIVVKGVNNTEVKAVVEVSTSEDKNSSTSDVASDTQKPSKLSDAPGGSKRHWGRTPGKKNLSMESIDFSVEVDEDNADIERLESTKLELQSRITEEVKSNAVLQASLERRKKALYGRRQALEQDVGRLQEQLQQERDRKLALETGLNMSKGNQPIPETIDENLKKDLQEVAQAEADIAKLEHKVDDLENRLGHHDGKASGSTHSASKESRKLPEHNAKMKEKQKDTEAASTHISERSTSKDGQGAARENETEKQQDSRSKSSQQETSRGSSKLVGLSKRSGTKGEGSTTTTSALSKLTMRLNFLKERRSQIANELQNMDKGKTLGQPSPTSGQNRVSEETEKGSGSNQDPDSSKLQSPHILDRGRSENGGDRGRGSSGGNHPNTTPRTFSR | null | null | activation of GTPase activity [GO:0090630]; negative regulation of Rho protein signal transduction [GO:0035024]; pollen germination [GO:0009846]; pollen tube adhesion [GO:0009865]; pollen tube development [GO:0048868]; pollen tube growth [GO:0009860]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; exocytic vesicle [GO:0070382]; pollen tube [GO:0090406] | GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267] | PF14389;PF00169;PF00620; | 2.30.29.30;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19108776}; Peripheral membrane protein {ECO:0000305|PubMed:19108776}. Note=Localizes to the apical plasma membrane and accumulates in the clear zone of growing pollen tubes. | null | null | null | null | null | FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Maintains the global inactivation of ARAC11/ROP1 at the apex in pollen tubes in order to regulate the polar cell growth. {ECO:0000269|PubMed:19108776}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JRB0 | HHO5_ARATH | MVQTETDQRMGLNLNLSIYSLPKPLSQFLDEVSRIKDNHSKLSEIDGYVGKLEEERNKIDVFKRELPLCMLLLNEEIVFLCVAIGALKDEARKGLSLMASNGKFDDVERAKPETDKKSWMSSAQLWISNPNSQFRSTNEEEEDRCVSQNPFQTCNYPNQGGVFMPFNRPPPPPPPAPLSLMTPTSEMMMDYSRIEQSHHHHQFNKPSSQSHHIQKKEQRRRWSQELHRKFVDALHRLGGPQVATPKQIRDLMKVDGLTNDEVKSHLQKYRMHIRKHPLHPTKTLSSSDQPGVLERESQSLISLSRSDSPQSPLVARGLFSSNVGHSSEEDEEEEDEEEEKSDGRSSCRNDETKKKRQVLDLEL | null | null | floral organ formation [GO:0048449]; negative regulation of gene expression [GO:0010629]; regulation of DNA-templated transcription [GO:0006355]; specification of plant organ identity [GO:0090701] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:26903506}. Cytoplasm, cytosol {ECO:0000269|PubMed:26903506}. Note=Localizes in cytosolic foci. {ECO:0000269|PubMed:26903506}. | null | null | null | null | null | FUNCTION: Transcriptional repressor that functions with ULT1 in a pathway which regulates floral meristem homeostasis and organ number in the flower. Binds specifically to the DNA sequence motif 5'-GTAGATTCCT-3' of WUS promoter, and may be involved in direct regulation of WUS expression. Binds specifically to the DNA sequence motif 5'-AAGAATCTTT-3' found in the promoters of AG and the NAC domain genes CUC1, CUC2 and CUC3, and may be involved in direct regulation of these gene expressions. | Arabidopsis thaliana (Mouse-ear cress) |
F4JRS4 | MORC7_ARATH | MDNSIHVKREIQLPSTSPAGFPGRESVTVVDLCSSDDDSDIGEVAGGLEKVGNNFVGLKRGRDTFGGSSEVDRNNVKKVTTLAELGVGLPEGFGQSNPPESLTHPIPANPCNVFRPVPPPPPPPYAGTSGKIGGCKQFWKAGDYEGAAGDNWDLSSGGFDHVRVHPKFLHSNATSHKWALGAFAELLDNALDEVASGATYVKVDMLENNKGGNRMLLIEDNGGGMDPEKMRQCMSLGYSAKSKLANTIGQYGNGFKTSTMRLGADVIVFSRCPGKDGKSSTQSIGLLSYTFLRSTGKEDIVVPMLDYERRDPEWSKIIRSSTRDWDKNVETIIQWSPFSSEEDLLHQFDLMKDRGTRIIIYNLWEDDQGMLELDFDADPYDIQLRGVNREERNIKMASQFPNSRHFLTYKHSLRSYVSILYLRIPPGFRIILRGIDVEHHSVVNDMMQTEQITYRPQSESYGVVTNMSAIVIIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNATGSDGRGVIGVLEANFVEPAHDKQGFERTTVLARLESRLVQMQKTYWSTNCHKIGYAPRRREKSAYGYDNRDSSPENDREGPSSIKTPTPASDKFYSSSYPNHNGDNGVSGKDGARLQEELRREKERRKALEVEVQLSRQKIEEMKKEQENLIEIFSEERDRRDGEEEVLRNKLEEASNTIDDLLNKIKKMEGSKVPSWRH | 3.6.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q84WV6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q84WV6}; | defense response [GO:0006952]; DNA repair [GO:0006281]; gene silencing by RNA-directed DNA methylation [GO:0080188]; phosphorylation [GO:0016310]; positive regulation of defense response to oomycetes [GO:1902290]; regulation of DNA repair [GO:0006282]; regulation of gene silencing by regulatory ncRNA [GO:0060966] | nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; kinase activity [GO:0016301]; protein self-association [GO:0043621]; RNA binding [GO:0003723] | PF13589;PF17942; | 3.30.565.10; | MORC ATPase protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}. | null | null | null | null | null | FUNCTION: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC4, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulators of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) (PubMed:27171361). {ECO:0000250|UniProtKB:Q84WV6, ECO:0000269|PubMed:27171361}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JS25 | SRFR1_ARATH | MATATATSERFELAKHCSSRNWSKAIRVLDSLLAKESSILDICNRAFCYNQLELHKHVIKDCDKALLLEPFAIQAFILKGRALLALGRKQEAVLVLEQGYKSALQQTADVKQLLELEELLKDARREIDGILKSHATESPQETPAYHSEKSDEKSDKLDNHESGASSNGNSHESSSELGEQSKIVSFSKVASKASKQSDGNSDLCNGSVYKEKENGKCGSQINGYYESCKPCNGSDLHDNLAESSDRFGELSINGNKISIKSSKMSHKAEARCGISDESRKNKKYTIARISGTHSISVDFRLSRGIAQVNEGNYTKAISIFDKVLKEEPTYPEALIGRGTAYAFQRELESAIADFTKAIQSNPAASEAWKRRGQARAALGEYVEAVEDLTKALVFEPNSPDVLHERGIVNFKSKDFTAAVKDLSICLKQEKDNKSAYTYLGLAFASLGEYKKAEEAHLKSIQLDSNYLEAWLHLAQFYQELADHCKALECIEQVLQVDNRVWKAYHLRGLVFHGLGEHRKAIQELSIGLSIENTIECLYLRGSCYHAVGEYRDAVKDYDATVDVELDAVEKFVLQCLAFYQKELALYTASKVSSEFLCFDIDGDIDPMFKEYWCKRLHPKNVCEKVYRQPPLRESLKKGKLKKQDLAITKQKANILRFADLIGKRIQYDCPGFLPNKRQHRMAGLAVIEIAQKVSKAWRIEWRNSTKGTTKNGKKNRRRERTNILSQNRGGAGCSSSSFSETSTGYASLEDRSSGRSILSWQDVYSPAVRWRQISEPCDPVVWVNKLSEEFNSGFGSHTPMVLGQAKVVRYFPNYERTLTLAKSIIKDKLSVRSKKDKVIDLSKDEKIEKIMRAETCDELHNIVGEDFWVATWCDSTGSEGKRLEGTRITCIQKPGRLGYDFSIRTPCTPARWSDFDEEMTSAWEALCTAYCGENYGSTELDALETVRDAILRMTYYWYNFMPLARGTAVTGFVVLLGLLLAANMEFTETIPKGLQIDWEAILNVEPGSFVDSVKSWLYPSLKINTSWRDHTEISSAFSTTGAVVAALSTYND | null | null | defense response to bacterium [GO:0042742]; negative regulation of defense response [GO:0031348]; negative regulation of DNA-templated transcription [GO:0045892] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | molecular adaptor activity [GO:0060090] | PF13432;PF13181; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:21079790}. Cytoplasm {ECO:0000269|PubMed:18774967}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18774967}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:21079790}. Note=Found in microsomes when interacting with SNC1 and RPS4. {ECO:0000269|PubMed:21079790}. | null | null | null | null | null | FUNCTION: Negative regulator of effector-triggered immunity associated with the EDS1 resistance pathway (PubMed:15469494, PubMed:18774967, PubMed:19525323, PubMed:19649196, PubMed:20862316, PubMed:21079790). May localize its interactors to a microsomal membrane (PubMed:22158819). May therefore negatively regulate RPS4 and SNC1 translocation to the nucleus (PubMed:21079790). Contributes to the regulation of RPS2 and RPS4 protein levels and negatively regulates SNC1 stability (PubMed:20862316). {ECO:0000269|PubMed:15469494, ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:19525323, ECO:0000269|PubMed:19649196, ECO:0000269|PubMed:20862316, ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22158819}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JSE7 | EDR2_ARATH | MSKVVYEGWMVRYGRRKIGRSYIHMRYFVLEPRLLAYYKKKPQDYQVPIKTMLIDGNCRVEDRGLKTHHGHMVYVLSVYNKKEKSHRITMAAFNIQEALMWKEKIESVIDQHQESQVPNGQQYVSFEYKSGMDTGRTASSSDHESQFSAAEDEEDSRRSLMRRTTIGNGPPESVLDWTKEFDAELANQNSDNQAFSRKHWRLLQCQNGLRIFEELLEVDYLPRSCSRAMKAVGVVEATCEEIFELLMSMDGTRYEWDCSFQFGSLVEEVDGHTAVLYHRLLLDWFPMIVWPRDLCYVRYWRRNDDGSYVVLFRSREHENCGPQPGCVRAHLESGGYNISPLKPRNGRPRTQVQHLIQIDLKGWGAGYLPAFQQHCLLQMLNSVAGLREWFSQTDERGVHTRIPVMVNMASSSLSLTKSGKSLHKSAFSLDQTNSVNRNSLLMDEDSDDDDEFQIAESEQEPETSKPETDVKRPEEEPAHNIDLSCFSGNLKRNENENARNCWRISDGNNFKVRGKNFGQEKRKIPAGKHLMDLVAVDWFKDSKRIDHVARRKGCAAQVAAEKGLFSMVVNVQVPGSTHYSMVFYFVMKELVPGSLLQRFVDGDDEFRNSRLKLIPLVPKGSWIVRQSVGSTPCLLGKAVDCNYIRGPTYLEIDVDIGSSTVANGVLGLVIGVITSLVVEMAFLVQANTAEEQPERLIGAVRVSHIELSSAIVPNLESE | null | null | ethylene-activated signaling pathway [GO:0009873]; negative regulation of leaf senescence [GO:1900056]; plant-type hypersensitive response [GO:0009626]; regulation of defense response to fungus [GO:1900150]; response to ethylene [GO:0009723]; response to salicylic acid [GO:0009751] | endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886] | phosphatidylinositol-4-phosphate binding [GO:0070273] | PF07059;PF00169;PF01852; | 3.30.530.20;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17612410}; Single-pass membrane protein {ECO:0000269|PubMed:17612410}. Cell membrane {ECO:0000269|PubMed:17612410}; Single-pass membrane protein {ECO:0000269|PubMed:17612410}. Endosome membrane {ECO:0000269|PubMed:17612410}; Single-pass membrane protein {ECO:0000269|PubMed:17612410}. | null | null | null | null | null | FUNCTION: Negative regulator of the salicylic acid- (SA-) mediated resistance to pathogens, including the biotrophic powdery mildew pathogens Golovinomyces cichoracearum and Blumeria graminis, and the downy mildew pathogen Hyaloperonospora parasitica, probably by limiting the initiation of cell death and the establishment of the hypersensitive response (HR). Prevents ethylene-induced senescence. Binds to phosphatidylinositol-4-phosphate (PtdIns(4)P) in vitro. {ECO:0000269|PubMed:16212604, ECO:0000269|PubMed:17612410}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JSH1 | APY7_ARATH | MVFGRITELFTAASSRLPAGSQSSVPYMPTGSSPDVGTSVSDSISIGNGGRKNCLRHSASLQDFSSYHGFDPEESILPREAISWGQNGSSFSKEKGSVPNGTNPSTRRKLIRAVMIVMCLFLFAFLVYIVSMYIYTNWSRGASRYYVVFDCGSTGTRAYVYQASINYKKDSSLPIVMKSLTEGISRKSRGRAYDRMETEPGFDKLVNNRTGLKTAIKPLIQWAEKQIPKNAHRTTSLFVYATAGVRRLRPADSSWILGNVWSILAKSPFTCRREWVKIISGTEEAYFGWTALNYQTSMLGALPKKATFGALDLGGSSLQVTFENEERTHNETNLNLRIGSVNHHLSAYSLAGYGLNDAFDRSVVHLLKKLPNVNKSDLIEGKLEMKHPCLNSGYNGQYICSQCASSVQGGKKGKSGVSIKLVGAPNWGECSALAKNAVNSSEWSNAKHGVDCDLQPCALPDGYPRPHGQFYAVSGFFVVYRFFNLSAEASLDDVLEKGREFCDKAWQVARTSVSPQPFIEQYCFRAPYIVSLLREGLYITDKQIIIGSGSITWTLGVALLESGKALSSTLGLKSYETLSMKINPIALISILILSLLLLLCALSRVSNCLPRFFRKSYLPLFRHNSTSASSVLNIPSPFRFQRWSPMSTGVKTPLSPTVRGSPRRPFSFGSSIQLMESSLYSSSSCVMHSCSSDSLGDIQYDSTGSFWSSPRRSQMRLQSRRSQSREDLSSSLADSHMLKM | 3.6.1.5 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | anther dehiscence [GO:0009901]; pollen exine formation [GO:0010584] | membrane [GO:0016020] | apyrase activity [GO:0004050]; ATP binding [GO:0005524] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (By similarity). Involved in the regulation of pollen and anther development. {ECO:0000250, ECO:0000269|Ref.1}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JT76 | VPS54_ARATH | MDSHPSLMGRSITNSNRSSLDLGRPSSSSSSSPSPLTKSISDASSQSLSSILNNPHGGKSGVYGSDASWVGWWSSSTFVAPAEFAPVASTKLPGSELTRSDFHGYVSSISESHGRFEDIRKHTREESCGFDQESHVSGLAACLREVPSLYFKEDFALEDGATFRSACPFSSLNENLALQEKLSQYLDVVELHLVKEISVRSDSFFEAQGQLQDLNVKIVEGCSRIRELKETIRLLDRNLVDSARQIQELSSTRINMLELQRKLRLILYVNQALSALKLLVASADCAGALDITDDLQNLLAGDELTGLYCFRHLRDHVTSSIDSINSILTSEFMRISIHDTGEIDVLILSAANIRGSISSNGNTGEEVKLEEEDTSTLCDRLLPLVIGLLRTAKFPSILRMYRDTLTSEMKNAIKKAVADLLPILVARSLESDFSHGERSVDDGGGLSLASKLRTLSSEAFVNLLTAIFKIVQAHLVRASEVKKAIEWILCNIDGHYAADSVAAAIAVGAVAAETAQEIGFQGGSLVSSPLGKATSKAPPLQGKSSDASSLMNMSRNFRADVLRENTEAVFAACEVTHGRWAKLLGVRALLHPKLKLQEFMSIYDLTQEFITSTEKIGGRLGSSIRGTLQSQAKAFVDSQHESRMTKLKAVLDQETWDEIDVPEEFQSIISSLFASQRLISGKVDDADLNSYHSNRLPLNGSLTSGSGDQNSELRNEKSESSEGSVVSDAQVKPTVSPESLERSKAGVSSATNNQSNQKAHGKSNLFYQGVGYHMVNCGLILLKMLSEYIDMNNSLPALSSEIVLRVVEVLRFFNTRTCQLVLGAGAMQVSGLKSIKAKHLALASQVIDFTYTIIPETRRILFSKVPETRKPLLSVEIDKVAQDFRIHRDEIYTKLVQIMRERLLAHLHGLPKVVEGWNRPPDTNKQTKEFAWPLTREVGYLHRVLSETLHEADVQAIFRQVISIIHTQTSQTLTNLEISSTEAKKRLKLHVELILKCIRSLPSDNANQSDIPNWGQLDEFFAEHFREEEAGEAE | null | null | Golgi to vacuole transport [GO:0006896]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147] | chloroplast [GO:0009507]; cytosol [GO:0005829]; GARP complex [GO:0000938]; Golgi membrane [GO:0000139] | syntaxin binding [GO:0019905] | PF07928; | 6.10.250.860; | VPS54 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Plastid, chloroplast. Note=Localized in the GARP complex in the Golgi and post-Golgi compartments. | null | null | null | null | null | FUNCTION: Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (By similarity). Probably involved in pollen tube elongation and other polar growth. {ECO:0000250, ECO:0000269|PubMed:18583349}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JTE7 | GPP1_ARATH | MLTTPTRFVALRIPFRSSNKIPISIAPSPKVFPRKPVIRVPASLRFVATMSTPAAAVNATVTVTDAGRGSITHVIFDMDGLLLDTEKFYTEVQEKILARYNKTFDWSLKAKMMGRKAIEAARLFVDESGISDSLSAEDFIVERESMLQDLFPTSDLMPGASRLLRHLHGKGIPICIATGTHTRHFDLKTQRHRELFSLMHHVVRGDDPEVKEGKPAPDGFLAASRRFEDGPVDPRKVLVFEDAPSGVQAAKNAGMNVIMVPDSRLDKSYCNVADQVLASLLDFKPEEWGLPSFQDSHN | 3.1.3.104; 3.1.3.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | dephosphorylation [GO:0016311]; glycerol biosynthetic process [GO:0006114]; riboflavin biosynthetic process [GO:0009231] | mitochondrion [GO:0005739] | 5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity [GO:0043726]; glycerol-1-phosphatase activity [GO:0000121]; glycerol-3-phosphatase activity [GO:0043136]; metal ion binding [GO:0046872] | PF00702; | 3.40.50.1000; | HAD-like hydrolase superfamily, DOG/GPP family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27490826}. | CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:17136424}; CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21; Evidence={ECO:0000269|PubMed:17136424}; CATALYTIC ACTIVITY: Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate; Xref=Rhea:RHEA:25197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58421; EC=3.1.3.104; Evidence={ECO:0000269|PubMed:27490826}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 mM for DL-glycerol-3-phosphate {ECO:0000269|PubMed:17136424}; Vmax=3 nmol/min/mg enzyme toward DL-glycerol-3-phosphate {ECO:0000269|PubMed:17136424}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:17136424}; | null | FUNCTION: Acts as a glycerol-3-phosphatase with higher stereospecificity for L-glycerol-3-phosphate than DL-glycerol-3-phosphate (PubMed:17136424). Can also dephosphorylate in vitro 5-amino-6-(5-phospho-D-ribitylamino)uracil, also known as ARPP (PubMed:27490826). {ECO:0000269|PubMed:17136424, ECO:0000269|PubMed:27490826}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JTN2 | LAZ1_ARATH | MDILKSYHLLAAAYSAPAWASFMAGAFLVLTLSLSLFLVFDHLSTYKNPEEQKFLIGVILMVPCYSIESFASLVKPSISVDCGILRDCYESFAMYCFGRYLVACIGGEERTIEFMERQGRKSFKTPLLDHKDEKGIIKHPFPMNLFLKPWRLSPWFYQVVKFGIVQYMIIKSLTALTALILEAFGVYCEGEFKWGCGYPYLAVVLNFSQSWALYCLVQFYGATKDELAHIQPLAKFLTFKSIVFLTWWQGVAIALLSSLGLFKSSIAQSLQLKTSVQDFIICIEMGIASVVHLYVFPAKPYGLMGDRFTGSVSVLGDYASVDCPIDPDEIRDSERPTKVRLPHPDVDIRSGMTIKESMRDVFVGGGEYIVKDVRFTVTQAVEPMEKSITKFNEKLHKISQNIKKHDKEKRRVKDDSCMSSSPSRRVIRGIDDPLLNGSFSDSGVTRTKKHRRKSGYTSAESGGESSSDQAYGGFEVRGRRWITKD | null | null | negative regulation of brassinosteroid mediated signaling pathway [GO:1900458]; programmed cell death [GO:0012501]; vacuole organization [GO:0007033]; vesicle-mediated transport to the plasma membrane [GO:0098876] | cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; plant-type vacuole membrane [GO:0009705]; plasma membrane [GO:0005886] | null | PF03619; | null | TMEM184 family | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein {ECO:0000269|PubMed:20830211}. Cell membrane {ECO:0000269|PubMed:20830211}; Multi-pass membrane protein {ECO:0000269|PubMed:20830211}. Cytoplasm, cytosol {ECO:0000269|PubMed:20830211}. | null | null | null | null | null | FUNCTION: Required for programmed cell death (PCD) associated with hypersensitive response (HR). Involved both in the induction of EDS1/PAD4 mediated HR and in accelerated cell death in the acd11 mutant. Not required for HR induction elicited through pathways exclusively dependent on CC-NB-LRR resistance proteins. {ECO:0000269|PubMed:20830211}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JTP5 | STY46_ARATH | MVMEDNESCASRVIFDALPTSQATMDRRERIKMEVFDEVLRRLRQSDIEDAHLPGFEDDLWNHFNRLPARYALDVNVERAEDVLMHKRLLHSAYDPQNRPAIEVHLVQVQPAGISADLDSTSNDAGHSSPTRKSIHPPPAFGSSPNLEALALAASLSQDEDADNSVHNNSLYSRPLHEITFSTEDKPKLLFQLTALLAELGLNIQEAHAFSTTDGYSLDVFVVDGWPYEETERLRISLEKEAAKIELQSQSWPMQQSFSPEKENGQTGARTHVPIPNDGTDVWEINLKHLKFGHKIASGSYGDLYKGTYCSQEVAIKVLKPERLDSDLEKEFAQEVFIMRKVRHKNVVQFIGACTKPPHLCIVTEFMPGGSVYDYLHKQKGVFKLPTLFKVAIDICKGMSYLHQNNIIHRDLKAANLLMDENEVVKVADFGVARVKAQTGVMTAETGTYRWMAPEVIEHKPYDHKADVFSYGIVLWELLTGKLPYEYMTPLQAAVGVVQKGLRPTIPKNTHPKLAELLERLWEHDSTQRPDFSEIIEQLQEIAKEVGEEGEEKKKSSTGLGGGIFAALRRSTTHH | 2.7.11.1 | null | cellular response to hypoxia [GO:0071456]; chloroplast organization [GO:0009658]; protein phosphorylation [GO:0006468]; response to abscisic acid [GO:0009737]; signal transduction [GO:0007165] | cytosol [GO:0005829] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712] | PF01842;PF07714; | 3.30.70.260;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated on serine and threonine residues. Autophosphorylated at Thr-443. {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21799034}. | 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:17090544}; 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:17090544}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for ATP {ECO:0000269|PubMed:17090544}; | null | null | null | FUNCTION: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs (PubMed:16429265, PubMed:17090544). Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034). {ECO:0000269|PubMed:17090544, ECO:0000269|PubMed:21799034}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JTS8 | NOV_ARATH | MQGNHDGSWSLHPSTNNGSGRANGNININTVPGGGYLPQANPVFPNFNQPIRYPIPQFPANFYRPNFPDFSLGNPNFQPHQNLNFLHQQIPHQYGSAANHFLQNHNQNSFSFPPQSIPNNDISISQNHGAFENSSLKRRRQEEVVQVTDVVPKSNFASGESANNSFSVSLPIPIATDDSGVSRVHGEKSSGKPKRKVDVLRIDKAVNKTRKLFVAAGESVSSTRVSRAVLEELQADSWRSLGVQMQDVPSLRQLMAIEGKINAFIHCFVGARRIVTLHDLEVAICRNEFVDSFDDLELGPLLQHPLVLLYFPSISSSTGPVKITSEEIISFLDSYLHTYMTEDVKLDEFLNFVASQKSVTSKEKLGVRIQSLRMYVSFILDAKRQEGETLKVLLTELHQKYHIPSSKKQQRDKSLTVSERADSFALHHKDYCGKHIRFDSSSSDENDNVYEVRNLNSSDHINSCPYPSVAEEMKRLGGSNKKRKGERRNHEKSDSSKLLRKSPSKLQGHAKQEIPKLADDSEAKKVFSVDEADFTLSEGDLRLFISTWKDTCKELSISTFVEKMLSFYNLGGSEGRAQIKRAKAMSSFPFVGLLNVAVTSLRRGMWDSIYDNFQMTSLSDTTNTGSGNQVGEINPIENSELSKTQHVMPPTHCNTVEEIIRRLSLYFEHDLSGAKHIGIFRKLQTCENLLAEQFQVQDFESLGWGGFFAFLEKHMLLLPTQLQRFLSRELQEEFPLEVHVNENLLTLLLSQASEFSSDKVLSRQTLARLVAEQFPSISFKVVGRDSEENFSEIIGKKKSSSKCVLFSATLLGAENSLTSKYLEESLTVGNDTEARSTTLNAVASKEVLDVLLRVPLLSDLNSWCHWDLRYAPQFGPLMGCLNEINSTDLLCLVTRDGKIIRADPSATADSFLEAALQGSAYRTAAQLLSLISLNGRTHLPFSLLKCYAKRAFEVFFYNYSEEMELNDRNSLVQMHGPEKLSTSFDKVIVVGEKAKVAKRDYAASKFLLDCLGYLPGEFRSLVVDILLPGLRSVVKDAPTRVLSACEQTEQRIMLHDAGLLLGIVEWISDYHKFCSSCSPNSSIVENASSNLDSGAGFVQNELEDPVQTKQRCMIVSEKSCEYKEEPHESCHTFGGSGILCDSVGEAFTQTAPEFYDNRASVIDSIRRDEFGLDLTSSGSEMSMLQKQHARLGRALQCLSQELYSQDSHFILELVQNADDNKYPEHVEPTLTFILQKTGIVVLNNECGFMPENIRALCDVGQSTKKGSGGYIGKKGIGFKSVFRVSDAPEIHSNGFHFKFDISEGQIGYILPTVVPPHDIESLSSMLSGRALHLKDAGWNTCITLPFRAIDSERTTVNHIEPMFSDLHPSLLLFLHRLQCIVYRNVLDDSLLVMRKEVVSKNIVKVSCGENSMTWFVASEKLKATNLRDDVQTTEISIGFTLDMLEDGTYRSCMIQEPVFAFLPLRTYGLKFIIQGDFILTSSREDVDEDSPWNQWLLSEFPGLFVDALRSFCSLPSFTQNLGKGVSSYMQLVPLVGEVHGFFSSLPRSIISRLRTTNCLLLEGDGEEWVPPCKVLRNWNEKIRVLLKDGLLQEHLALGFLDKDIVLSDSLSRALGIEDYGPKTLVQILSSLSHKNGCLQSMGFTWLSSILTELYLLFRSSGHGNVELGIDKSLIDDLHKIPFIPLSNGKFTSLDEGAVWLHHDTTGLDLGDVFEAFPVLYGNLRTIDHSLLLASSVDEKSSVDDLVNMLCAIGVQKLSAHEIVKAHILPAFEARSTGAVDGLMVDYLCFVMTHLRSGCHICLKERKYIISELRSKALVLSNYGLKQLGEGSIHFGEEYGNQVNMKKLTKNLDISWHVVDGTYLKHPASKFYACGLKEWREFFQEIGIADFVQVVQVEKSIAEFYSVSHCEKYDINLLSPDLTVKDWESPELVDLLSLLHKSNGRKGCKYLLEVLDRLWDDCYYDKTTVNYNSGTHGIIRSSESSFMRVICDSLWIVSSMDSKLHLSKDLYHDCDDVQSILGMNAPYAVPTVTSVKLLSDIGFKTKVSLDDALEVLESWVHCGDSFKSSISQITRFYKYLWNEMADSKQKITEKLHTLPSVFVPHGIASRQNDMISGIFLSLDDVYWNDSAGVLDEIKEISSQISSVVEPLRRKTLGNIYPGLHDFFVNGCGVPETPSFQEYLKILGQFAHNVSPSSAAKAVFKIFLKWSDDLNSGKSSEDVIHFKERLSELEYTVLPTENDKWVSLHSSFGLVCWCDNEKLKKRFKNKDKIEFISFGENDDEGQEVLQTKVSGLMHSLGIPSISEVVKREAKYEGLQDNTVTVSLVNWALPYAQRYIFTLHHEKYTQTKKTVHSQVKRLQVFVVDKLSYRNVIPQYGISSKKEFKCSSLLQDKALYTTPSLDSHSLFMELSRLFFNGVPDLHLANFLHLIKTMAESGLSEEQMESFILNSQKVHQVPDGEEIWSLKSAVKAKKKAGISLSWLPSSSKTRHGSSKTNTDDSKQELDTSSSKEDVTEALEEKIPIEMTNTNLVSGYDNCAGTSSRASEPNPLHSMHMISGSTSGNQAAMHLNPNLPHEWNNSFTANFSDRDQLHTGTPWAAQAQQTGRKGEEIAYRYFVAKYGNEALVKWVNDQSETGLPYDLMIENRGGKKEYVEVKATVSTRKDYFNLTVREWQFANEKGESYIIAHVLLGNSNAILTQHRNPVKLCQEGHLRLLVLMPNQRNEVNVTF | null | null | auxin polar transport [GO:0009926]; cell fate specification [GO:0001708]; embryo development ending in seed dormancy [GO:0009793]; leaf vascular tissue pattern formation [GO:0010305]; root development [GO:0048364]; stem cell population maintenance [GO:0019827] | nucleus [GO:0005634] | null | PF13020; | 3.30.565.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:19880797}. Note=Accumulates in speckles within the nucleus and the nucleolus. {ECO:0000269|PubMed:19880797}. | null | null | null | null | null | FUNCTION: Essential protein required for cell fate determination during embryogenesis (PubMed:15266054). Mediates auxin-dependent coordinated cell-fate specification and patterning in embryos (e.g. cotyledon outgrowth and separation), shoots and roots (e.g. leaf vascular development, cellular patterning and stem cell maintenance in the meristems) (PubMed:19880797, PubMed:20729639). Required for provascular PIN1 expression and region-specific expression of PIN7 in leaf primordia, cell type-specific expression of PIN3, PIN4, and PIN7 in the root, and PIN2 polarity in the root cortex (PubMed:19880797, PubMed:20729639). {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:19880797, ECO:0000269|PubMed:20729639}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JUI3 | BPC5_ARATH | MESGGQYENGRYKPDYYKGTQSVNVMPKKEQHNALVMNKKIISILAERDAAVKERNEAVAATKEALASRDEALEQRDKALSERDNAIMETESALNALRYRENNLNYILSCAKRGGSQRFITEESHLPNPSPISTIPPEAANTRPTKRKKESKQGKKMGEDLNRPVASPGKKSRKDWDSNDVLVTFDEMTMPVPMCTCTGTARQCYKWGNGGWQSSCCTTTLSEYPLPQMPNKRHSRVGGRKMSGSVFSRLLSRLAGEGHELSSPVDLKNYWARHGTNRYITIK | null | null | response to ethylene [GO:0009723] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF06217; | null | BBR/BPC family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes. {ECO:0000269|PubMed:14731261}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JUU5 | S2P_ARATH | MEISGRRMRRFRMRFRRDHLTGGENIENEASCCYCDLKISNFNEPIFRLGRRFSGVLKVWFSIGLGFGVASLILVTVFLLLQFHSNPLFSNRLTSAVFGFSPSTRVSLSGIAYVLVSTVITVSVHELGHALAAASEGIQMEYIAVFIAAIFPGGLVAFDNDVLQSLPSFNALRIYCAGIWHNAVFCALCVFALFLLPVMLSPFYKHGESLTVVDVPSVSPLFGYLSPGDVIVSLDGIQVHKPSEWLELAAILDKENSKTSNGSLYLGGSRRFHHGKGYCVPISLIEEGYKGKMVENQFVCPGDLTAFRTMPCSNAAIREVSVCLDAKDIVKLQKCGDGWVTTSDTDNQSDCVCPQGDLCLQAMQSPGVLWTEITYKRTSSQDCSRLGLDFNTSNCLGTFVFVGDLIAMSHSVHLTAYQPRWLFNFFGKSFPNILERSLTCTFHVSLALVLLNSLPVYYLDGESILESSLQSFTWLSPRKKKKALQVCLVGGSLLSFLAFFRIFLLGLPLSRRW | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; | cellular hyperosmotic salinity response [GO:0071475]; membrane protein intracellular domain proteolysis [GO:0031293]; proteolysis [GO:0006508]; regulation of brassinosteroid mediated signaling pathway [GO:1900457]; regulation of response to endoplasmic reticulum stress [GO:1905897]; response to salt stress [GO:0009651] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF02163; | null | Peptidase M50A family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:20876872}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Metalloprotease that catalyzes the second step (site-2 cleavage) in the proteolytic activation of various factors, after site-1 cleavage. Part of a regulated intramembrane proteolysis (RIP) cascade. After ER stress, cleaves BZIP17 and BZIP28 proteins which function as stress sensors and transducers in ER stress signaling pathway. The N-terminal bZIP component is translocated to the nucleus, where it activates the expression and production of ER chaperones, as well as proteins involved in brassinosteroid (BR) signaling, which is required for stress acclimation and growth. {ECO:0000269|PubMed:20876872}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JUY5 | GAMT1_ARATH | MESSRSLEHVLSMQGGEDDASYVKNCYGPAARLALSKPMLTTAINSIKLTEGCSSHLKIADLGCAIGDNTFSTVETVVEVLGKKLAVIDGGTEPEMEFEVFFSDLSSNDFNALFRSLDEKVNGSSRKYFAAGVPGSFYKRLFPKGELHVVVTMSALQWLSQVPEKVMEKGSKSWNKGGVWIEGAEKEVVEAYAEQADKDLVEFLKCRKEEIVVGGVLFMLMGGRPSGSVNQIGDPDSSLKHPFTTLMDQAWQDLVDEGLIEEEKRDGFNIPVYFRTTEEIAAAIDRCGGFKIEKTENLIIADHMNGKQEELMKDPDSYGRDRANYAQAGLKPIVQAYLGPDLTHKLFKRYAVRAAADKEILNNCFYHMIAVSAVRV | 2.1.1.275 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | methylation [GO:0032259] | null | gibberellin A9 carboxyl methyltransferase activity [GO:0102117]; gibberellin carboxyl-O-methyltransferase activity [GO:0010341]; metal ion binding [GO:0046872]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF03492; | 1.10.1200.270;3.40.50.150; | Methyltransferase superfamily, Type-7 methyltransferase family, SABATH subfamily | null | null | CATALYTIC ACTIVITY: Reaction=gibberellin A9 + S-adenosyl-L-methionine = O-methyl gibberellin A9 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36119, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73255, ChEBI:CHEBI:73256; EC=2.1.1.275; Evidence={ECO:0000269|PubMed:17220201}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.4 uM for GA4 {ECO:0000269|PubMed:17220201}; KM=15.8 uM for GA9 {ECO:0000269|PubMed:17220201}; Note=kcat is 0.01 sec(-1) for GA4. kcat is 0.026 sec(-1) for GA9.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17220201}; | null | FUNCTION: Methylates the carboxyl group of several gibberellins (GAs). Substrate preference is GA9 > GA20 > GA3 > GA4 > GA34 > GA51 > GA1 > GA19 > GA12. No activity with diterpenes abietic acid and ent-kaurenoic acid. {ECO:0000269|PubMed:17220201}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JVH1 | CFM3B_ARATH | MAINSSHHFCPMTTTTTTSAKFVDSLGSSFCKFHGTSSSISLRSYRFGFSFMKNVKRLSCEGSSSSSSSRNENWNRTQKQNQFRPSKVVLNRRKDERFSDLGVISGENSSRSGDVGGGSGSSSTMEKIVEKLKKYGFVDEDQFQDKEVEQERRIEKSSVEERFYVEERRGGFSEESPFGVYGGNDEVKFPWEKVSSMEKKELVNGEWTAKKESRYSLAEMTLSEFELNRLRNVMFRTKSKMRVTGAGVTQAVVDAIQEKWKGSEIVRLKIEGSSALNMRRMHEILERKTGGLVIWRSGTSIALYNYKGGSNRDGSGNMNKQVYRRAERLPSSLPTSTVDQSVQLVNLPQLEKEPTVVGNKDRTSPQEVEYEDEINELLEGLGPRYTDWQGGYPLPVDADLLPGIVPGYEPPFRALPYGVRSTLGTKEATSLRRIATVLPPHFALGRSRQLQGLATAMVKLWQKSLIAKVALKRGVQLTTSERMAEDIKRLTGGMLLSRNKDFLVFYRGKSFLSLEVGEALMEKEMLVRTLQDEEEQARLRASSALVVPSIKANQQLARTLQDKEEQARPSALVLPSTKANQNLVSAGTLGETLDATGKWGKNLDNDDHVEEMKQEVEKVRSAKLVRKLERKLAFAEKKLLKAERALAKVEESLKPAEQRTDLEGITEEERFMFQKLGLKMKAFLLLGRRGVFDGTVENMHLHWKYRELIKILVKAKTLEGAQKVAMALEAESGGILVSVDKISKGYAVIVYRGKDYKRPTTLRPKNLLTKRKALARSLELQKREALIKHIEAIQTRSEQLRAEIEQVELVKDKGDETLYDKLDMAYSSDEETEETDGEEDDVYLDTYEDEGEDDEEGGIQANGSLSETDVEFGSDESDTDFGDNSASSTTPETTFVELQNEELDVQP | null | null | Group II intron splicing [GO:0000373]; mRNA processing [GO:0006397]; plastid rRNA transcription [GO:0042794]; RNA splicing [GO:0008380]; rRNA processing [GO:0006364]; seed development [GO:0048316] | chloroplast [GO:0009507]; plastid [GO:0009536]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729] | PF01985; | 3.30.110.60; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18799595}. Plastid {ECO:0000269|PubMed:32143506}. Note=Localized to root plastids. {ECO:0000269|PubMed:32143506}. | null | null | null | null | null | FUNCTION: Binds specific group II introns in chloroplasts and facilitates their splicing (PubMed:18799595, PubMed:32143506). Exhibits non-specific action during plastid rRNA biogenesis; RFC3 prevents unaccurate splicing to improve the accuracy of plastid rRNA processing (PubMed:32143506). Acts on subgroup IIB introns (PubMed:18799595). The substrates of the subgroup IIB also require the CRM domain proteins CAF1 or CAF2, with a simultaneous binding of CFM3B and CAF1 or CAF2 (PubMed:18799595). Required for seed development (PubMed:18799595). {ECO:0000269|PubMed:18799595, ECO:0000269|PubMed:32143506}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JVI3 | MTEF5_ARATH | MQSLSQLGPSEIFLVARREKPSTRAQLWFTGRLSFRQETNGIRLKNRVEFSPRPVPPNLIAAEKEEAKAVLTLFFKKQGLSNSLSSRLINKSDLFIDHLVSRLHSVHKARYLVGRELTTLEIRDSLIPYLEQLHEEHGDLLAELVVSFPDPPAEPRLVASSPVSVLPPRGDTDSAADTRKLRAVSRVSELDTEGALRPQTLYLLDLGLNLEQIKTITRKFAAFPYYSLDGKIKPVVEFLLDLGIPKSDIPTILCKRPQICGISLTDNLKPTMAFLETLGIDKNQWAKIISRFPAILTYSRQKLTSTVEFLSQTGLTEEQIGRILTRCPNIMSYSVEDKLRPTMEYFRSLNVDVAVLLHRCPQTFGLSIESNLKPVTEFFLEKGFGLDEIGIMISRYGALYTFSLKENVMPKWDYFQTMDYPKSELVKFPQFFGYSLQERIKPRYELVQRSGVRLLLNQVLSLSGIEFEKVVKKKMMKLVSNNVIAEQSSGGLL | null | null | chloroplast organization [GO:0009658]; DNA-templated transcription termination [GO:0006353]; plastid transcription [GO:0042793]; regulation of DNA-templated transcription [GO:0006355]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651] | chloroplast [GO:0009507] | sequence-specific double-stranded DNA binding [GO:1990837] | PF02536; | 1.25.70.10; | MTERF family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:21464319, ECO:0000269|PubMed:31128276}. | null | null | null | null | null | FUNCTION: Transcription termination factor required for processing and steady-state levels of plastid transcripts (PubMed:22905186). Involved also in chloroplast transcriptional pausing, a general feature of chloroplast genes (PubMed:31128276). Specifically and positively regulates the transcription of chloroplast psbEFLJ encoding for photosystem II (PSII) core subunits psbE, psbF, psbL and psbJ; causes the plastid-encoded RNA polymerase (PEP) complex to pause at psbEFLJ by binding to the +30 to +51 region of double-stranded DNA, and recruits additional pTAC6 to the transcriptionally paused region of psbEFLJ (PubMed:31128276). May play a role in response to abiotic stresses (PubMed:22905186). {ECO:0000269|PubMed:22905186, ECO:0000269|PubMed:31128276}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JVN6 | TPPII_ARATH | MDLSLQLQIHGALINKGPSCTSYWASSSSLSLPRDFISSSTFLLHRRLRRRSCSRSRGIRLRRSGFSAMPCSSSDTLTASRVGCGGGGGGGAVGGGAENASVANFKLNESTFIASLMPKKEIRADCFIEAHPEYDGRGVVIAIFDSGFDPSAAGLHVTSDGKPKVLDVIDCTGSGDIDTSTVVKANEDGHIRGASGATLVVNSSWKNPTGEWRVGSKLVYQLFTDDLTSRVKKERRKSWDEKNQEEIAKAVNNLYDFDQKHSKVEDAKLKKTREDLQSKVDFLKKQADKYEDKGPVIDAVVWHDGEVWRVALDTQSLEEDPDSGKLADFSPLTNYRIERKYGVFSRLDACSFVANVYDEGKVLSIVTDSSPHGTHVAGIATAHHPEEHLLNGVAPGAQIISCKIGDSRLGSMETGTGLTRALIAALEHNCDLVNMSYGEPALLPDYGRFVDLVTEAVNKRRLIFVSSAGNSGPALTTVGAPGGTTSSIIGVGAYVSPAMAAGAHSVVEPPSEGLEYTWSSRGPTSDGDLGVCISAPGGAVAPVPTWTLQRRMLMNGTSMASPSACGAIALLLSAMKAEGIPVSPYSVRRALENTSTPVGDLPEDKLTTGQGLMQVDKAYEYLKQFQDYPCVFYQIKVNLSGKTIPTSRGIYLREGTACRQSTEWTIQVDPKFHEGASNLKELVPFEECLELHSTDEGVVRVPDYLLLTNNGRGFNVVVDPTNLGDGVHYFEVYGIDCKAPERGPLFRIPVTIIIPKTVANQPPVISFQQMSFISGHIERRYIEVPHGATWAEATMRTSGFDTTRRFYIDTLQVCPLRRPIKWESAPTFASPSAKSFVFPVVSGQTMELAIAQFWSSGLGSREPTIVDFEIEFHGVGVDKEELLLDGSEAPIKVEAEALLASEKLVPIAVLNKIRVPYQPIDAQLKTLSTGRDRLLSGKQILALTLTYKFKLEDSAEVKPYIPLLNNRIYDTKFESQFFMISDTNKRVYAMGDVYPESSKLPKGEYKLQLYLRHENVELLEKLKQLTVFIERNMGEIRLNLHSEPDGPFTGNGAFKSSVLMPGVKEAFYLGPPTKDKLPKNTPQGSMLVGEISYGKLSFDEKEGKNPKDNPVSYPISYVVPPNKPEEDKKAASAPTCSKSVSERLEQEVRDTKIKFLGNLKQETEEERSEWRKLCTCLKSEYPDYTPLLAKILEGLLSRSDAGDKISHHEEIIEAANEVVRSVDVDELARFLLDKTEPEDDEAEKLKKKMEVTRDQLADALYQKGLAMARIENLKGEKEGEGEEESSQKDKFEENFKELTKWVDVKSSKYGTLTVLREKRLSRLGTALKVLDDLIQNENETANKKLYELKLDLLEEIGWSHLVTYEKQWMQVRFPKSLPLF | 3.4.14.10 | null | proteolysis [GO:0006508] | chloroplast [GO:0009507]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; plant-type vacuole [GO:0000325]; vacuole [GO:0005773] | aminopeptidase activity [GO:0004177]; mRNA binding [GO:0003729]; salicylic acid binding [GO:1901149]; serine-type endopeptidase activity [GO:0004252]; tripeptidyl-peptidase activity [GO:0008240] | PF00082;PF12580;PF21316;PF21223; | 1.25.40.710;2.60.40.3170;6.10.250.3080;3.40.50.200; | Peptidase S8 family | null | null | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; Evidence={ECO:0000269|PubMed:15908606, ECO:0000269|PubMed:19822524}; | null | null | null | null | FUNCTION: Serine protease of the proteasome pathway that may function with the 20S proteasome to degrade oxidized proteins generated by environmental stress. {ECO:0000269|PubMed:15908606, ECO:0000269|PubMed:19822524}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JW79 | RDM3_ARATH | MDRKGKGKQVAGSDSYSGGQKRKNSVEFRDEGLRIKKRKNPEVLQFFEESAEVGYYGGSSDEDDDGLGFLNDMEDEPEVEESSKAGKGEKGKSSFVFPKEEDLNEEEFDRIMEERYKPGSGFLRYADDDIKDAIEMDALAPTSKDPPIWKVKCAIGRERRSVFCLMHKFVELRKIGTKLEIISVFSVDHVKGFIFIEADKEHDVLEACKSLVGIYATRMVLLPKAETPNLLTVQKKTKKVSEGTWARVKNGKYKGDLAQIVAVSDTRNKALIKLIPRIDIQALTQKYGGGVTVQKGQTPAPRLISSSELEEFRPLIQVRRDRDTGITFEHLDSLMLKDGYLYKKVSLDSISSWGVIPTKDELLKFTPVDRKETGDVEWISEIYGEERKKKILPTCREGGKGEGSGGGKGEGSGGGKGEGSRGGKGEGSSDFKSESSYELYNLVCFSRKDFGLIVGVDDKGDGYKVLKEGIDGPVVVTVGKKEMQNGPFDSKFTALDLNKKQISVNDVVKISKGPSEGKQGVVRQVYRGIIFLYDESEEENGGYFCCKSQSCEKVKLFTEESNEKTGGFDGTAFEDFVSSPKSPLSPEKEWQPRERYNSSNQGDIGSTYSIGQKLRIRVGPLKGYLCRVIALRYSDVTVKLDSQHKIFTVKSEHLAEVRDRNTVLSTSGDAGTGSFQPFGMLGTESSTGDWAIGAGTSSEGGNWNIGGPSTDSHESLNIERNMVQLCREKNPWGGSKPTSDVSPTVADDNTSAWANAAAENKPASASDQPGGWNPWGKTPASEAGTVSGWGDTSASNVEASSWEKQGASTSNVADLGSWGTHGGSSGGNKQDEDSVWGKLCEASESSQKKEESSWGKKGGSDGESSWGNKDGNSSASKKDGVSWGQQDKGSDESKGGSAWSNQCGDFGSGKKKDGSSGWNKSAEDSNANSKGVPDWGQPNDGSSWGKKGDGAASWGKKDDGGSWGKKDDGNKDDGGSSWGKKDDGQKDDGGSSWEKKFDGGSSWGKKDDGGSSWGKKDDGGSLWGKKDDGGSSWGKEDDGGSLWGKKDDGESSWGKKDDGESSWGKKDDGGSSWGKKDEGGYSEQTFDRGGRGFGGRRGGGRRGGRDQFGRGSSFGNSEDPAPWSKPSGGSSWGKQDGDGGGSSWGKENDAGGGSSWGKQDNGVGSSWGKQNDGSGGGSSWGKQNDAGGGSSWGKQDSGGDGSSWGKQDGGGDSGSAWGKQNNTSGGSSWGKQSDAGGGSSWGKQDGGGGGSSWGKQDGGGGSGSAWGKQNETSNGSSWGKQNDSGGGSSWGKQDGGGGGSSWGKQNDGGGGSSWGKQGDGGSKPWNEHSGGGRGFGERRGGGGFRGGRNQSGRGGRSFDGGRSSSWKTDNQENTWKSDQSGGSDWKKGWGEDSNNSKPSGSSAGGCAGNWPSWDTNSKKETNDKPGDDSKSAWGTSNDQVNTDNNNDSWNKKPNNDVGTSGEADNAWGGKTNAVAPSPSGSAAWGTGDKKTGW | null | null | gene silencing by RNA-directed DNA methylation [GO:0080188]; heterochromatin formation [GO:0031507]; regulation of DNA-templated transcription elongation [GO:0032784]; regulation of transcription by RNA polymerase II [GO:0006357]; siRNA processing [GO:0030422]; transcription elongation by RNA polymerase II [GO:0006368] | DSIF complex [GO:0032044]; nucleoplasm [GO:0005654] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF03439; | 2.30.30.30;3.30.70.940; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19410546}. Note=Localized at punctate nuclear foci. Colocalizes with AGO4 and polymerase V in the nucleoplasm. {ECO:0000269|PubMed:19410546}. | null | null | null | null | null | FUNCTION: Effector of RNA-directed DNA methylation (RdDM) triggered by small interfering RNAs (siRNAs, 24-nt RNAs). Functions as an adapter protein that binds scaffold transcripts generated by polymerase V and recruits AGO4 and AGO4-bound siRNAs to form an RdDM effector complex (PubMed:19343051, PubMed:19410546). Promotes the expression of 24-nt RNAs (PubMed:19343051). Required for the initial establishment of DNA methylation (PubMed:21150311). Together with AGO4, required for transcriptional gene silencing (TGS) by DNA methylation and repressive histone modifications (H3K9me2) of several chromatin loci (PubMed:21738482). {ECO:0000269|PubMed:19343051, ECO:0000269|PubMed:19410546, ECO:0000269|PubMed:21150311, ECO:0000269|PubMed:21738482}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JWB3 | MYTM2_ARATH | MTALRPLSGRSRSLRCSSEKMEGTGSWDVLEWTKLDSASWSGSYSNLDCLLESERIIFEACGVILINTDEAGTLLLSNFRILFLSEGTRKLVPLGTIPFVAIEKFNKLAPKVQSNKYHNNENAPTRLLQVTGKDMRIVVYGFRPGTKQRHTVVDTLLRCNKPERVWDLYAFTCGPSQFGNTNPKERLLNEYFRLLGKSSQRASMNMIEDGSFTLSNDLWRITNLNSNYDLCQSYPFALMVPKSISDEELLQTSTFRARCRLPVISWCHPGSGAVIARSSQPLVGLMMNMRSNSDEKLVASFCTQLAGHKGARRKLYIVDARPRKNALANGAKGGGSESSSNYLQSEIVFLGIDNIHAMRESFSRLRDYLDMHGTTSSDGTSSFLRHGGWTWGGGNLSSMSASVSVLGDSGWLSHIQSILAGVAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFSGFQALVEKDWLSFGHPFSDRVGMPNVSESGNFELPIQSSSARSFPSSPVRQSPGSAAAQSSSSSYGLNNYSPIFLQWLDCISQLMRMYPSAFEFSPTFLVDFIDCLLSCRFGNFLCNSEKERQQCGISETCGCIWAYLADLRSSSGTSHVHCNPFYDPSRYDGPLLPPAAALAPTLWPQFHLRWACPVEPNVTETEDQCRAMTVKYSEMKKEKEEAERKVDELSSAMESLNEELLNERDISRAARESAKRATKERAVISRAVQSLGCKVKFTRNGDCTVEVEDGPQKCSHSIPQKQSEDNTTDVSESISSVTEQNVCEAVCPLRTREGTCRWPDAGCARIGNQFLGLKTNFEAFDNLCVYDSYFTAE | 3.1.3.64; 3.1.3.95 | null | dephosphorylation [GO:0016311]; intracellular signal transduction [GO:0035556]; lipid metabolic process [GO:0006629] | cytoplasm [GO:0005737] | phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721] | PF06602; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22324391}. Note=Highly concentrated at the peripheral lobes of the epidermal cells. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; Evidence={ECO:0000269|PubMed:22324391}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000269|PubMed:22324391}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=216.5 uM for PtdIns3P {ECO:0000269|PubMed:22324391}; KM=158.2 uM for PtdIns3,5P(2) {ECO:0000269|PubMed:22324391}; Vmax=15.4 pmol/min/mg enzyme with PtdIns3P as substrate {ECO:0000269|PubMed:22324391}; Vmax=28.4 pmol/min/mg enzyme with PtdIns3,5P(2) as substrate {ECO:0000269|PubMed:22324391}; | null | null | null | FUNCTION: Phosphatase with phosphoinositide 3'-phosphatase activity that can use phosphatidylinositol-3-phosphate (PtdIns3P) and phosphatidylinositol-3,5-diphosphate (PtdIns3,5P(2)) as substrates and produces phosphatidylinositol-5-phosphate (PtdIns5P); participates in pathway(s) that transfer gene regulatory signals to the nucleus. {ECO:0000269|PubMed:22324391}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JXF1 | GAF1_ARATH | MGFFDLSIPYNEPPRSGGKEIAGGKTLRLKLATKAMELGYVGIAHNRSIKGVMSDKDSCTIPLLTLGSLIKVAPRLASSVGFHRDLLGVPRTTPFRQYTRLTVHVESNAQCQSLNSGNPILKSYDIIAVRPMNQNAFDYACEKAEVDLISIDFTDKMLFRLKHPMVKAAIQRGIYFEIKYSDILMDAQTRRQVISNAKLLVDWTRGKNLIISSGAPSVTELRGPNDVINLMFLLGLSAERARAAISKNCRNMIAKVLKKKRFHKEAVRVELLSAGDTFSLEQPLSEDCMKWDRLSSGEGDMLLDDLAKAFDATNVVAHKSSKAIDFTSVLDGLPKHGFRVKDIVGTESVTQPSAAKVIDTQVHSSNQVSELRMATASSDDNLREIETISQIDMLMSEDDNKVEPTTNVLKEEAFALRKCSASHGQGILVQNQTATPFTLTRCTKSEAASDVSMNIESTSEGGSMSPSKSDHGIPQSPVEVNNMGNAAFEEEASVDENSKERATTGHASNDEMHITESGHHASIDDEKHIPEPEHLTSIADEMKIDCSSEANHDEYMEVTMEDQMHETVQMRLCKTMTKHQD | 3.1.26.- | null | rRNA processing [GO:0006364]; tRNA processing [GO:0008033] | mitochondrion [GO:0005739]; nucleolar ribonuclease P complex [GO:0005655]; nucleus [GO:0005634] | hydrolase activity [GO:0016787]; RNA binding [GO:0003723] | PF01876; | 3.20.20.140; | Eukaryotic/archaeal RNase P protein component 3 family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P38786}. Nucleus {ECO:0000269|PubMed:22509260}. Mitochondrion {ECO:0000269|PubMed:22509260}. | null | null | null | null | null | FUNCTION: Probable component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (By similarity). May also be a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (By similarity). Required for female gametophyte development and male competence (PubMed:22509260). {ECO:0000250|UniProtKB:P78346, ECO:0000269|PubMed:22509260}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JY12 | GFS12_ARATH | MRGEDSDLCFDCLDQRINSDFSDQIVFSYGVSDSPLPFGSSAVVKVSDSSEEFSASCSSCESTSSQFILEYLRKDEHGCLAKYVDKFVVKDREGNSNDAVESDECLDCSTSGSQATEDDDTENITCGSVTCEHSGSFSCWRTVAALLPIAQIRKCSASELQKLASSFHYECPEDQILASLHRLIDGKSSGQATHSFLCLLLGLPLLEEKSKLRCLRHPNLSPVLGLLTSSDCLVSVLPKAPYTLENILYYSPSAIKSEWHRNFIIYQLLSALAHLHGLKVSHGDIRPSNILLSDSLWSWLTIYSKPDLGSVDANSSASRRRWCVEGCYSYGLYADLKISSHLDWQTHFDKWWKGELSNFEYLLVLNKLAGRRWGDHTFHPVMPWVIDFSKKPENDSDSGWRDLRKSKWRLAKGDEQLDFTYSTFEFPHHVSDECLSELAVCSYKARRLPLSVLRKAVRSVYEPNEYPSDMQRLYDWTPDECIPEFYCDPRIFCSLHPSMSDLAVPPWASSPDEFIRLHRDALESPHVSSLIHHWIDITFGYKMSGHAAITAKNVMLSSSEPTVPRSVGRRQLFFRPHPVRLGFSREKEQSRNELEMHTFHGFGVDNKRSVILLADEYLEETEEASAFSDHATHLCPKYHLRENLVESPLHVSYSENTKKVNTSLPGTSKNKGLSSRISLNYLLEHMEVRDEASTELQELLQWRQDFCTGNISKDIAGDIFSIGCVLAELYLMKPLFNSVSLATYLEGGDLPELIKELPPPTQVIVEACIEQDWRRRPSAKSLLDSPYFSATVRSAHLFAAPLQLLAKGQTRLCYAASFAKQGVLKVMGTFVAEMCAVYCLPLVTTPLSEDECELAYVLLKEFTKSLTPMAVQRLVLPSIQKILLTTGYSHLKVSLLQDSFVRELWNQIGKRVYLEMIHPLVISNLYNSPDKISASAASVLLIGSSEELGAPVTVHQTILPLISYFGKGICTDGIDVLVRIGRLLGVNFIVKQMLPLLEHVVCFCIDLSSMKKPEPVHSWCSLALSDCLITLDGLVALISDELLIHELTKGRLCLHVRVLMQKNLELRVLQFAATSLMSICQRIGQEMTALHVLPQLKELFDEFAFSEKSTDASDSLSWKIRTAEQKFHPESPIKSRMDLVLLLYPSFASLLGMEKLRQGCPTWLLLEQYLLKHHNWKWEYTGRSSRYNMEARPVLKQGPASKHTPKVLLNGSGRSVPQSQGLRNSNHLKLHIHVPVEGQEAVLNPLVHEPWSWFPSPVTCWDGLDIGRFGNPKDENRWKIRASVLSSARAHHGALRSLVVSEDECTVFTSGIDPGFKGSVQKWELASLSCVSSYHAHEEVVNDIGILSSTGKVASCDGTIHVWNSQTGKLISLFSESPSDQDQASSDPSSKNNSNPCNRHASHGLSSGIFDENLYTCMHYLEYMDQLIVGTGFGALRFIDLARGQKLELWGGEAIESGFTSLVSALCSGGSQTKHGDGASVSPSWIAAGFSSGQCRLFDLRENGFISSWRAHDGYVTKLVAPESHLLVSSSLDKTLRIWDLRKSWTPQPFVVKGHNDGVSGFSIWGKDVISISRNNIGIFSLAKSQDEEEQQQQRIIPQKLYMAEKGGRVKSDLSTICVLPFSRLFIVGAHDGHLRICC | 2.7.10.- | null | defense response to bacterium [GO:0042742]; phosphorylation [GO:0016310]; protein targeting to vacuole [GO:0006623] | Cul4-RING E3 ubiquitin ligase complex [GO:0080008] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672] | PF02138;PF00069;PF00400; | 1.10.1540.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | null | null | null | null | null | null | null | FUNCTION: May act predominantly to suppress BCHC1, which itself is a negative factor in protein storage vacuole (PSV) trafficking regulation and plant effector triggered immunity (ETI). Required for ETI, but not for cell death. {ECO:0000269|PubMed:25618824}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JY24 | CHR17_ARATH | MARASKREVSSDEAYSSEEEEQVNDQANVEEDDDELEAVARSAGSDEEDVAPDEAPVSDDEVVPVEDDAEEDEEDEEKAEISKREKARLKEMQKMKKQKIQQILDSQNASIDADMNNKGKGRIKYLLQQTELFAHFAKSDPSPSQKKGKGRGRHSSKLTEEEEDEECLKEEEGGIVGSGGTRLLTQPACIQGKLRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPEERRHIREELLVAGKFDICVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLEVVNGGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLVTNAGKMVLLDKLLPKLKDRDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTENAIEAKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDSADFYDFDDDNKDESKVDFKKIVSENWNDPPKRERKRNYSEVEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQAHQKTQMKDTIEVDEPEEVGDPLTAEEVEEKELLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAQVFQVRYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGNWDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLIEKENQEFDERERQARKEKKLSKSATPSKRPSGRQANESPSSLLKKRKQLSMDDYGKRRK | 3.6.4.- | null | nucleosome organization [GO:0034728]; positive regulation of cellular response to heat [GO:1900036]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; histone binding [GO:0042393]; nucleosome array spacer activity [GO:0140750]; nucleosome binding [GO:0031491] | PF09110;PF00271;PF09111;PF00176; | 1.10.10.60;1.20.5.1190;1.10.1040.30;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family, ISWI subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}. | null | null | null | null | null | FUNCTION: Possesses intrinsic ATP-dependent nucleosome-remodeling activity. Constitutes the catalytic subunit of several complexes capable of forming ordered nucleosome arrays on chromatin (By similarity). Involved in the formation of nucleosome distribution patterns (PubMed:24606212). Required for the maintenance of the plant vegetative phase. In association with RLT1 or RLT2 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 (PubMed:22694359). Necessary to acquire heat stress (HS) memory (PubMed:27680998). {ECO:0000250|UniProtKB:O60264, ECO:0000269|PubMed:22694359, ECO:0000269|PubMed:24606212, ECO:0000269|PubMed:27680998}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JY37 | RUK_ARATH | MNQYHIYEAIGHGKCSTVYKGRKKKTIEYFACKSVDKSRKNKVLQEVRILHSLNHPNVLKFYAWYETSAHMWLVLEYCVGGDLRTLLQQDCKLPEESIYGLAYDLVIALQYLHSKGIIYCDLKPSNILLDENGHIKLCDFGLSRKLDDISKSPSTGKRGTPYYMAPELYEDGGIHSFASDLWALGCVLYECYTGRPPFVAREFTQLVKSIHSDPTPPLPGNASRSFVNLIESLLIKDPAQRIQWADLCGHAFWKSKINLVQLPTQPAFDDMIGINTKPCLSERNGDRPNKTPPKYREKDRKGGSKQNENSIQGSKGHETPIKGTPGGSKAQAKLPSRATEEKHGGRPAANRQVNILRLSRIAKANLQKENEKENYRRPLPNSNENCAEVKIDNTDMELDFDENNDDEGPDESEGTENTSCAQEERVMSHNENHRRQRVVSSNVPDENSSANETPTLGEARDCHEDQSEPMDMSAAPPSASPQLKTHRGRETSGVAVNHDSSKAPTSLTDVFWHISDLSVRPVMPSRKSDKEAVHSLSFETPQPSDFSKKGKQELEPLNNRIITVLSGSSSGLSEKQNLIRYLETLSTNADAANILTNGPIMLVLVKVLRLSKTPAFRVQIASLIGLLIRHSTSIEDDLANSGILDSLTNGLRDKHEKVRRFSMAALGELLFYISTQNEHKDFKPPESPSKETRSASGWQVSNALISLVSSVLRKGEDDLTQVYALRTIENICSQGAYWATRFSSQDLISNLCYIYKATGKQESMRQTAGSCLVRLARFNPPCIQTVVEKLSLKEIASSFVKGSAREQQVCLNLLNMAMIGSHTFTSFGRHLVTLTEEKNLFPSLLSIIEQGTEVLRGKALLFVAFLCKNSRRWLTNFFCNARFLPVVDRLAKEKDSYLQQCLEAFVNVIASIIPGMLDTITNDIQQLMTGRRHGPVSPLNSRAPVKTNAHLFPVVLHLLGSSSFKNKMVTPQVLRQLANLTKLVEASFQGRDDFRVTLLQVLECITGDAPLVTQNGEIIIREILPSLAAIYNGNKDGDARFLCLKIWFDSLTILLTECTEIEQQISEDLKSISNSHFLPLYPALIQDEDPIPAYAQKLLVMLVEFDYIKISNLLRHNTVSQCFEFLLGDLSSANVNNVKLCLALASAPEMESKLLSQLKVVRRIGNLLEFVNAKDMEDFLEPTLSLCRAFLLRSLGNKKGLSSNYTKEPTLLSEASFTFEVDPQECIRDIADFGSNIGLFLHFAGLDDDTSIAVADIASECVVLLLKAASREATTGFLTNLPKITPILDSWRRRKSTELHLLVLKRVLHCLGYACKQYLSQAMILSISGHDVSKINAIVSEMKNSDAAGLNSIASLVAMELQRLPR | 2.7.11.1 | null | cellularization [GO:0007349]; cytokinesis by cell plate formation [GO:0000911]; endosperm cellularization [GO:0010342]; microsporogenesis [GO:0009556]; phosphorylation [GO:0016310]; phragmoplast assembly [GO:0000914]; pollen development [GO:0009555]; radial microtubular system formation [GO:0010245] | microtubule [GO:0005874]; phragmoplast [GO:0009524]; plasmodesma [GO:0009506]; preprophase band [GO:0009574]; spindle [GO:0005819] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; transferase activity [GO:0016740] | PF00069; | 1.25.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:19268593}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19268593}. Note=Colocalizes also with mitotic preprophase band. {ECO:0000269|PubMed:19268593}. | 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: Essential protein that regulates phragmoplast microtubule organization during cell plate expansion in cytokinesis during cell division, both somatic and syncytial (PubMed:11089872, PubMed:19268593, PubMed:23451828). Required for endosperm cellularisation (PubMed:12421698, PubMed:23451828). In pollen development, involved in cellularisation during microsporogenesis by regulating radial microtubules (MT) organization in microspore mother cells (PubMed:23451828). Seems to not have kinase activity (PubMed:19268593). {ECO:0000269|PubMed:11089872, ECO:0000269|PubMed:12421698, ECO:0000269|PubMed:19268593, ECO:0000269|PubMed:23451828}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JYC8 | PTM_ARATH | MEAKVPRPRGRPRKRQRLEDDNRKLNNRGKKQVLEVEPAVPISLLGCYMLKDFDDNEVFLGKIVSYDTGLYRVIYEDGDCEELESGDLRRLIISDSYLDDELRVRRKKLDKLILKKEEKKKRNSPENKAVELPNQVNGVQARAVTNSEDGDSYSDSESSESGDKRGSDLEIEAPLVPPVDLPPSSGTIGIPEEAVAHLLSVYGFLRSFSFQLYICPFELNDFVGALYFSGPNSLLDAVHVALLRALKGHLERLSSSKSVLASKCLRCIDWSLLDVLTWPVYLVQYFTAMGHASGPQWNIFNKFVVEIEYYSLPIGMKLKILQILCDDIFDVADLRDEIDAREESEIGFDPDRVATGLLENVPRRVHPRFAKTSAYKEKEVTDSSTNESKDLDSRCTNGGSNEVSSDLDGNSDECRICGMDGTLLCCDGCPLAYHSRCIGVVKMYIPDGPWFCPECTINKKGPKIAHGTSLRGAVQFGMDPHGRLFLGTCNHLLVLNISVNGDAVVKYYNVNDISKVVLVLISASSHTLEYVEICKAITQYWDLPEGISLREGEIGLTQAKDREDGKVSEITKSDSANISNRSHTQTVFDLPTSTLGNTNSAVTGGSCGIQGKKLAARVTYLGLSFKPNTYNNHYTNGELAVSAAASLAVLSSEETHEPDLRKYNSAKKAASSNILEQMKAFSLVAPRFFWPSPDKKEITRERCGWCHSCRLTSASRRGCMLNAAVAGATKGAMKIFSGLFPLKNGEGVLSSIAAYILYLEESLRGLIAGPFLSESPRKQWRKQVEEASTCKALKAPLLELEENICSIALSCDWFKQMDDWLIEHSIFQSAPVTLGVPQRRGPGRTKQNTQAEVTAEGSDADSFTWWRGGKLSKVILLKAVLSQPATKKAAWQGGSKKIPGLNYGDASYIPRRSRRSFWKAAVESSKNISQLALQVRYLDMSLRWRELVRPDQNLQNVKGPETDVAIFRNARICDKKLSDNKVSYGVFFGNQKHLPSRVMKNIMEVEKTQDRNEKYWLQEAHVPLYLIKEFEESLHRVQMPSSTKKPSKKLSKLQRKQLKASLMDIFSYIASRRDKMEKCSCASCDHDVLLRDTTTCSSCHGFCHKDCTSMSQHTNGNVEVLVTCKRCYLSKTRVPTNINHRQSTAPQFTINVRHQNAVIPVIKVKPPSQQLSSQKPRENTSGVKQVTPDSSVSKSKQKTLSCGVIWRKKNVEDTGVDFRNQNILLAGRSDKPSLEPVCGICLLPYNPGLTYIHCTKCEKWFHTEAVKLKDSQIPEVVGFKCCKCRRIRSPDCPYMDPKLKEQKQIKRIVFTNQKQRQGNSGLDSDSERMSEQKDSKPSTPLPATPLYPPDDVFIPEDDPLLVSVSKVKQITPSSFDLEWSTTAFAPGPQKLPVRRQVKREDSDAAYPELHPIVKPEAEEQALPVLTEWDLSGELLFDYEDMEFEPQTYFSLTELLTADDSGGGQYQENGDMVVSGNPQFEPTEKEECEDDMGPCQRCLQMDPAPDLLCTVCGLLIHSHCSPWSALPGSSWSCGQCRIRALGSITLGSFGAITQFKSILPDRSTKVDISLAGPFAGAALSVSMFAVGLFLSTEPDAANDLVQVPSMLFQGSLLLGLISRATLGYAALHAATVSIHPLVIAGWCGLTTTAFNMLPVGCLDGGRAVQGAFGKNALVTFGLSTYVMLGLRVLGGPLALPWGLYVLICRNT | null | null | chloroplast-nucleus signaling pathway [GO:0010019]; positive regulation of DNA-templated transcription [GO:0045893]; proteolysis [GO:0006508] | chloroplast envelope [GO:0009941]; chloroplast outer membrane [GO:0009707]; ISWI-type complex [GO:0031010]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; methylated histone binding [GO:0035064] | PF02791;PF02163;PF00628;PF21743;PF15612; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:21934661}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:21934661}. Note=Localized primarily in the chloroplast outer membrane as dormant form and, upon specific stimulation, is released from the membrane through proteolytic cleavage, and its cleaved fragment containing the transcription factor domain is redistributed to the nucleus, where it regulates the expression of particular nuclear genes. {ECO:0000269|PubMed:21934661}. | null | null | null | null | null | FUNCTION: Membrane-bound transcription factor required for the plastid-to-nucleus retrograde signaling. Functions in multiple retrograde pathways. The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. In the nucleus, activates ABI4 transcription in a PHD-dependent manner associated with histone modifications. Localized primarily in the chloroplast outer membrane as dormant form and, in response to retrograde signals, is released from the membrane through proteolytic cleavage and its cleaved fragment containing the transcription factor domain is redistributed to the nucleus, where it regulates the expression of particular nuclear genes. {ECO:0000269|PubMed:21934661}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JYE9 | DHFS_ARATH | MRTLWNHFSTISYIKISPRMRRISAANLISNRNLSTISSTEDPELRDFVGFLESLKNYEKSGVPKGAGTDSDDGFDLGRMKRLMLRLRNPHYKYKVVHVAGTKGKGSTSAFLSNILRAGGYSVGCYSSPHILSIKERISCNGEPVSASTLNDLFYSVKPILEQSIQEENGSLSHFEILTGIAFSLFEKENVDIAVIEAGLGGARDATNVIESSNLAASVITTIGEEHMAALGGSLESIAEAKSGIIKHGRPVVLGGPFLPHIEGILRSKAASVSSSVILASNIGSSSSIKGIINKNGIGLCQSCDIVIQNEKDDQPIVELSDVNLRMLGHHQLQNAVTATCVSLCLRDQGCGRVTDEAIRIGLENTRLLGRSQFLTPKEAETLLLPGATVLLDGAHTKESARALKEMIKKDFPEKRLVFVVAMASDKDHVSFAKELLSGLKPEAVILTEADIGGGKIRSTESSVLKESWIKAADELGSRSMEASENKTVLGSLKLAYKILSDDTTSSDSGMVIVTGSLHIVSSVLASLQH | 6.3.2.12 | null | embryo development ending in seed dormancy [GO:0009793]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate biosynthetic process [GO:0046654] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759] | ATP binding [GO:0005524]; dihydrofolate synthase activity [GO:0008841]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326] | PF08245; | 3.90.190.20;3.40.1190.10; | Folylpolyglutamate synthase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11752472}. | CATALYTIC ACTIVITY: Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216; EC=6.3.2.12; Evidence={ECO:0000269|PubMed:11752472}; | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from folate: step 1/1. {ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:12535338}. | null | null | FUNCTION: Conversion of folates to polyglutamate derivatives, including tetrahydrofolate (PubMed:11752472, PubMed:12535338). Required during embryogenesis; from maternal tissues until the globular stage, and from the embryo after the globular stage (PubMed:12535338). {ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:12535338}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JYG0 | PIAL2_ARATH | MSTAAAARPVAGTGLREKTAASLVNSFRLASVTQRLRYHIQDGAKVDPKEFQICCISFAKGIDFAIANNDIPKKVEEFPWLLKQLCRHGTDVYTKTALMVLMISVKHACHLGWFSDSESQELIALADEIRTCFGSSGSTSPGIKSPGSTFSQIMERFYPFVKLGHVLVSFEVKAGYTMLAHDFYISKNMPHSLQEKIRLFVAQTDNIDTSACISNPPEVSFLLNGKGVEKRVNIAMDTGPQLPTNVTAQLKYGTNLLQVMGNFKGNYIIIIAFTGLVVPPEKPVLKDYLQSGVIEASPDSDIIEGPSRVSLSCPISRKRIKLPVKGQLCKHLQCFDFSNYVHINMRNPTWRCPHCNQPVCYPDIRLDQNMAKILKDVEHNAADVIIDAGGTWKVTKNTGETPEPVREIIHDLEDPMSLLNSGPVVFDLTGDDDAELEVFGDNKVEDRKPCMSDAQGQSNNNNTNKHPSNDDYSSIFDISDVIALDPEILSALGNTAPQPHQASNTGTGQQYSNLSQIPMSIDPMPVPVPFSQTPSPRDRPATTSTVFTIPNPSPQYSQVHASPVTPTGTYLGRTTSPRWNQTYQSQAPPMTTPYTSRKVSVPVTSQSPANVSSFVQSQHVPRVLSQPNNYGVRGLTSSHASTSRQHPSGPTVQSVSRLSDLVDVDLTVPDTSNWRPRMRGSLVPGSHSTALDHMIIRPSQQSQTSTRLNSSQPVQTPSVQTSQAQSPFTTAAYRTETVLGNRNHPVPAPPGIVRPTGPTS | 2.3.2.- | null | positive regulation of sulfur metabolic process [GO:0051176]; protein sumoylation [GO:0016925]; regulation of gene silencing by regulatory ncRNA [GO:0060966]; regulation of transcription by RNA polymerase II [GO:0006357]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; ligase activity [GO:0016874]; protein homodimerization activity [GO:0042803]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270] | PF02891; | 3.30.40.10; | PIAL protein ligase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:25415977}. | null | null | FUNCTION: Together with MOM1 and PIAL1, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation (PubMed:27113777). E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates (PubMed:25415977). Involved in stress responses and sulfur metabolism (PubMed:25415977). {ECO:0000269|PubMed:25415977, ECO:0000269|PubMed:27113777}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JZC2 | ENAS1_ARATH | MSVAPPAPSPPPFDPTKPSTPISFPIKTLQDLKSRSYFDSFHYPFNRSSVPLRRNIGALSDRPRLLVCHDMKGGYVDDKWVQGCGNNAGYAIWDWYLMDVFVYFSHSLVTLPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKELLATKESAQMYAERLAELAAALGFDGWLINIENVIDEVQIPNLMVFVSHLTKVMHSSVPGGLVIWYDSVTIDGHLAWQDQLTENNKPFFDICDGIFMNYTWKENYPKASAEIAGDRKYDVYMGIDVFGRGTYGGGQWTANVALDLLKSSNVSAAIFAPGWVYETEQPPDFYTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGLGSHTSLGGRKLSEAPWYNISCQSLQPFLEFNEGRNSETIQVTVDGREASYNGGGNVSFRGKLKRNAHFTARLFKPQLQLSAAPISIFFSVKSDKRSELSILLHFSSPSQEKKSMLMVPNESINRFGDMFLPCLLTSKQTTSGWTVHETNLVLDGHTLTEISAFCSRPDDLTEETNTLEYFALLGHISIKSQQKAKVYPLASSWVIEAHHVKFVPGDSGSKTLSCKLEWRLKHPEEDSVFPKYNVYAENLSSSEYRPRKVMEEPRSEKVFLGTAHVDAYYVSEMVVGSDVKGVRFVVQTCGEDGSWQELDASPNLVVEVERVSSKLCCCGLI | 3.2.1.96 | null | N-glycan processing [GO:0006491]; protein deglycosylation [GO:0006517] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; vacuole [GO:0005773] | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity [GO:0033925] | PF03644; | 2.60.120.260;3.20.20.80; | Glycosyl hydrolase 85 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21796445}. | CATALYTIC ACTIVITY: Reaction=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603, Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248, ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; EC=3.2.1.96; Evidence={ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for dabsyl-Asn-Man5 {ECO:0000269|PubMed:21796445}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:21796445}; | null | FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the production of high-mannose type N-glycans during plant development and fruit maturation. {ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JZG9 | TERC_ARATH | MSLASVIHHGILPPAKSDRIFLTIPVFPPDFRARGWTKSPFSLLINPSLASAANRRLSHLPPIACSRGIDQEDEEKESRELLPHKNDENATTSRSSSSVDSGGLKDYQQEETYKTSFKTVALCVGTAVAFGIGIGLKEGVGKASEFFAGYILEQSLSVDNLFVFVLVFKYFKVPLMYQNKVLTYGIAGAIVFRFTLILLGTATLQKFEAVNLLLAAVLLYSSFKLFASEEDDTDLSDNFIVKTCQRFIPVTSSYDGNRFFTKHDGILKATPLLLTVAVIELSDIAFAVDSIPAVFGVTRDPFIVLTSNLFAILGLRSLYTLISEGMDELEYLQPSIAVVLGFIGVKMILDFFGFHISTEASLGVVALSLSTGVLLSLTNKSSDS | null | null | seedling development [GO:0090351]; thylakoid membrane organization [GO:0010027] | chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535] | null | PF03741; | null | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18429937, ECO:0000269|PubMed:24612058}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Integral thylakoid membrane protein that plays a crucial role in thylakoid membrane biogenesis and thylakoid formation in early chloroplast development (PubMed:18429937). Is essential for de novo synthesis of photosystem II (PSII) core proteins and required for efficient insertion of thylakoid membrane proteins, presumably via interaction with ALB3. May assist synthesis of thylakoid membrane proteins at the membrane insertion step (PubMed:24612058). {ECO:0000269|PubMed:18429937, ECO:0000269|PubMed:24612058}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JZN6 | KDSRB_ARATH | MAAIFSLFLFFILFIVSLLIILSFIVRPRSVTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAKICFDGIKAGKFTVTCHFIGFLLSIASTGMSPQGSFWLALTEVMFGGLIRLASLVFQWQWYKTIEKWSQRNKKEVNSKLA | 1.1.1.102 | null | 3-keto-sphinganine metabolic process [GO:0006666]; sphingolipid biosynthetic process [GO:0030148] | endoplasmic reticulum membrane [GO:0005789] | 3-dehydrosphinganine reductase activity [GO:0047560] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:21421810}; Multi-pass membrane protein {ECO:0000305|PubMed:21421810}. | CATALYTIC ACTIVITY: Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH; Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349; EC=1.1.1.102; Evidence={ECO:0000269|PubMed:21421810}; | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. | null | null | FUNCTION: Catalyzes the reduction of 3'-oxosphinganine (3-ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis. In plants, sphingolipids seems to play a critical role in mineral ion homeostasis, most likely through their involvement in the ion transport functionalities of membrane systems in the root. Is stereospecific for D-erythro-DHS production and does not produce L-threo-DHS. {ECO:0000269|PubMed:21421810}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JZW1 | PBL13_ARATH | MVLCFQDPDNIYSPKKTKKDDGERVITKQKSFLGLSILDISNPSSTTLSEDLSISLAGSDLHVFTQAELRVITQSFSSSNFLGEGGFGPVHKGFIDDKLRPGLKAQPVAVKLLDLDGLQGHREFMTEVMCLGKLKHPNLVKLIGYCCEEAHRLLVYEFMPRGSLESQLFRRCSLPLPWTTRLNIAYEAAKGLQFLHEAEKPIIYRDFKASNILLDSDYTAKLSDFGLAKDGPQGDDTHVSTRVMGTQGYAAPEYIMTGHLTAKSDVYSFGVVLLELLTGRKSVDIARSSRKETLVEWARPMLNDARKLGRIMDPRLEDQYSETGARKAATLAYQCLRYRPKTRPDISTVVSVLQDIKDYKDDIPIGIFTYTVPTKPRREVKETSLQNFDKPRRETKVTSLQNFDKTRREVKDTSLQNFDKTRREVKETSLQNFDKTRREVKETSLQNFDKPRNVSTTDNHQKFRSPAHTARNHRITLRNGYNSPMRNEAGGERY | 2.7.11.1 | null | defense response [GO:0006952]; negative regulation of immune response [GO:0050777]; protein phosphorylation [GO:0006468] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26432875}. | 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:26432875}; 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:26432875}; | null | null | null | null | FUNCTION: Involved in defense responses. Acts as a negative regulator of plant immune responses. {ECO:0000269|PubMed:26432875}. | Arabidopsis thaliana (Mouse-ear cress) |
F4JZY1 | CIP1_ARATH | MKKHKFRETLKSFFEPHFDHEKGEMLKGTKTEIDEKVNKILGMVESGDVNEDESNRQVVADLVKEFYSEYQSLYRQYDDLTGEIRKKVNGKGESSSSSSSDSDSDHSSKRKVKRNGNGKVEKDVELVTGALKQQIEAANLEIADLKGKLTTTVEEKEAVDSELELALMKLKESEEISSKLKLETEKLEDEKSIALSDNRELHQKLEVAGKTETDLNQKLEDIKKERDELQTERDNGIKRFQEAEKVAEDWKTTSDQLKDETSNLKQQLEASEQRVSELTSGMNSAEEENKSLSLKVSEISDVIQQGQTTIQELISELGEMKEKYKEKESEHSSLVELHKTHERESSSQVKELEAHIESSEKLVADFTQSLNNAEEEKKLLSQKIAELSNEIQEAQNTMQELMSESGQLKESHSVKERELFSLRDIHEIHQRDSSTRASELEAQLESSKQQVSDLSASLKAAEEENKAISSKNVETMNKLEQTQNTIQELMAELGKLKDSHREKESELSSLVEVHETHQRDSSIHVKELEEQVESSKKLVAELNQTLNNAEEEKKVLSQKIAELSNEIKEAQNTIQELVSESGQLKESHSVKDRDLFSLRDIHETHQRESSTRVSELEAQLESSEQRISDLTVDLKDAEEENKAISSKNLEIMDKLEQAQNTIKELMDELGELKDRHKEKESELSSLVKSADQQVADMKQSLDNAEEEKKMLSQRILDISNEIQEAQKTIQEHMSESEQLKESHGVKERELTGLRDIHETHQRESSTRLSELETQLKLLEQRVVDLSASLNAAEEEKKSLSSMILEITDELKQAQSKVQELVTELAESKDTLTQKENELSSFVEVHEAHKRDSSSQVKELEARVESAEEQVKELNQNLNSSEEEKKILSQQISEMSIKIKRAESTIQELSSESERLKGSHAEKDNELFSLRDIHETHQRELSTQLRGLEAQLESSEHRVLELSESLKAAEEESRTMSTKISETSDELERTQIMVQELTADSSKLKEQLAEKESKLFLLTEKDSKSQVQIKELEATVATLELELESVRARIIDLETEIASKTTVVEQLEAQNREMVARISELEKTMEERGTELSALTQKLEDNDKQSSSSIETLTAEIDGLRAELDSMSVQKEEVEKQMVCKSEEASVKIKRLDDEVNGLRQQVASLDSQRAELEIQLEKKSEEISEYLSQITNLKEEIINKVKVHESILEEINGLSEKIKGRELELETLGKQRSELDEELRTKKEENVQMHDKINVASSEIMALTELINNLKNELDSLQVQKSETEAELEREKQEKSELSNQITDVQKALVEQEAAYNTLEEEHKQINELFKETEATLNKVTVDYKEAQRLLEERGKEVTSRDSTIGVHEETMESLRNELEMKGDEIETLMEKISNIEVKLRLSNQKLRVTEQVLTEKEEAFRKEEAKHLEEQALLEKNLTMTHETYRGMIKEIADKVNITVDGFQSMSEKLTEKQGRYEKTVMEASKILWTATNWVIERNHEKEKMNKEIEKKDEEIKKLGGKVREDEKEKEMMKETLMGLGEEKREAIRQLCVWIDHHRSRCEYLEEVLSKTVVARGQRRVSQRT | null | null | abscisic acid-activated signaling pathway [GO:0009738]; cellular response to abscisic acid stimulus [GO:0071215]; positive regulation of abscisic acid-activated signaling pathway [GO:0009789]; regulation of protein import into nucleus [GO:0042306]; response to abscisic acid [GO:0009737]; response to osmotic stress [GO:0006970] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plastid [GO:0009536] | actin binding [GO:0003779] | null | 1.10.287.1490;1.10.287.2610; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27372427}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7753789}. Note=Associated to the cytoskeleton in hypocotyl and cotyledon cells, but not in root cells, where observed as disconnected cytoplasmic speckles (PubMed:7753789). Localized to the plasma membrane in the epidermal cells of cotyledons and roots, including root hairs (PubMed:27372427). {ECO:0000269|PubMed:27372427, ECO:0000269|PubMed:7753789}. | null | null | null | null | null | FUNCTION: Positive regulator of abscisic acid (ABA)-mediated signaling pathways involved in abiotic stress responses (e.g. osmotic stress) and leading to various plant adaptation (e.g. stomata closure). {ECO:0000269|PubMed:27372427}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K0A6 | MYO2_ARATH | MMLSASPNTLAKSSLEEMLESLRQKDECDRPKDMPPALPSRPNSRARLPSARRSLPANFNVSSVMEDQNGSVVSVTPAVEAESERKEEGVKRKEKDLGVKRNSFGSKKMRTGLRSESPYAAEKEEEGVKISIAKVSLVENTEEHNKPESEWNNNVEYFIKKKLRVWCRVSNGQWQLGKIQSTSADTSLVMLSTANVVKVSTEELFPANPDILEGVEDLIQLSYLNEPSVLYNLRVRYLQDVIYSKAGPVLIAVNPFKNVEIYGNDVISAYQKKVMDAPHVYAVADAAYDEMMREEKNQSLIISGESGAGKTETAKFAMQYLAALGGGSCGVEYEILKTTCILEAFGNAKTSRNANSSRFGKLIEIHFSAMGKICGAKLETFLLEKSRVVQLFNGERSYHIFYELCAGASPILKERLKLKTASEYTYLSQSDCLTIAGVDDAQKFHKLLEAFDIVQIPKEHQERAFALLAAVLWLGNVSFRVTDNENHVEVVADEAVANAAMLMGCNTEELMVVLSTRKLQAGTDCIAKKLTLRQATDMRDGIAKFIYANLFDWLVEQINIALEVGKSRTGRSISILDIYGFESFKNNSFEQFCINYANERLQQHFNRHLFKLEQEEYEEDGIDWTKVEFVDNQECLDLIEKKPIGLLSLLDEESNFPKATDLTFANKLKQHLKTNSCFKGERGRAFRVNHYAGEVLYDTNGFLEKNRDPLPADLINLLSSCDCQLLKLFSTKMRGKSQKPLMLSDSTNQTVGTKFKGQLFKLMNKLENTSPHFIRCIKPNSKQLPRVYEEDLVLQQLRCCGVLEVVRISRSGYPTRLTHQEFAGRYGFLLSDKKVAQDPLSVSIAVLKQYDVHPEMYQVGYTKLYLRTGQIGIFEDRRKKVLQGIVGLQKHFRGHLSRAYFQNMRKVTLVLQSYIRGENARRLFDTEAKFHADSVSEASTDELSAVIHLQSAVRGWLARKHFNSMQRQKELRNVATKSKRKAGRRISEDKDIPLEQPQVQPTSMSDLQKRILKSEAALSQKEEENTALREQLRQFEERWSEYDIKMKSMEETWQKQMSSLQMSLAAARKSLAAESITGQAGGRQDTSISPFGYDSEDTMSTGTPGVRTPTNKFTNGNTPELRIRELNGSLNAVNHLAREFDQRRLNFDEDARAIVEVKLGPQATPNGQQQQHPEDEFRRLKLRFETWKKDYKARLRDTKARLHRVDGDKGRHRKWWGKRG | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; endocytosis [GO:0006897]; vesicle transport along actin filament [GO:0030050] | endosome [GO:0005768]; myosin complex [GO:0016459]; plasmodesma [GO:0009506] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146] | PF00612;PF00063; | 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 VIII subfamily | null | SUBCELLULAR LOCATION: Cell junction, plasmodesma. Endosome. | 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 (By similarity). Involved in endocytosis via its action in endosomal trafficking. {ECO:0000250, ECO:0000269|PubMed:18393384}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K0E8 | ISPG_ARATH | MATGVLPAPVSGIKIPDSKVGFGKSMNLVRICDVRSLRSARRRVSVIRNSNQGSDLAELQPASEGSPLLVPRQKYCESLHKTVRRKTRTVMVGNVALGSEHPIRIQTMTTSDTKDITGTVDEVMRIADKGADIVRITVQGKKEADACFEIKDKLVQLNYNIPLVADIHFAPTVALRVAECFDKIRVNPGNFADRRAQFETIDYTEDEYQKELQHIEQVFTPLVEKCKKYGRAMRIGTNHGSLSDRIMSYYGDSPRGMVESAFEFARICRKLDYHNFVFSMKASNPVIMVQAYRLLVAEMYVHGWDYPLHLGVTEAGEGEDGRMKSAIGIGTLLQDGLGDTIRVSLTEPPEEEIDPCRRLANLGTKAAKLQQGVAPFEEKHRHYFDFQRRTGDLPVQKEGEEVDYRNVLHRDGSVLMSISLDQLKAPELLYRSLATKLVVGMPFKDLATVDSILLRELPPVDDQVARLALKRLIDVSMGVIAPLSEQLTKPLPNAMVLVNLKELSGGAYKLLPEGTRLVVSLRGDEPYEELEILKNIDATMILHDVPFTEDKVSRVHAARRLFEFLSENSVNFPVIHHINFPTGIHRDELVIHAGTYAGGLLVDGLGDGVMLEAPDQDFDFLRNTSFNLLQGCRMRNTKTEYVSCPSCGRTLFDLQEISAEIREKTSHLPGVSIAIMGCIVNGPGEMADADFGYVGGSPGKIDLYVGKTVVKRGIAMTEATDALIGLIKEHGRWVDPPVADE | 1.17.7.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:15650872}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:15650872}; | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0019288]; response to bacterium [GO:0009617]; systemic acquired resistance, salicylic acid mediated signaling pathway [GO:0009862]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; plastid [GO:0009536] | 4 iron, 4 sulfur cluster binding [GO:0051539]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity [GO:0046429]; iron ion binding [GO:0005506] | PF04551; | 3.20.20.20;3.30.413.10; | IspG family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000305|PubMed:11943178, ECO:0000305|PubMed:18236010}. | CATALYTIC ACTIVITY: Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:26119, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58483, ChEBI:CHEBI:128753; EC=1.17.7.1; Evidence={ECO:0000269|PubMed:15650872}; | null | PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6. | null | null | FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Is essential for chloroplast development and required for the salicylic acid (SA)-mediated disease resistance to biotrophic pathogens. {ECO:0000269|PubMed:11943178, ECO:0000269|PubMed:15133149, ECO:0000269|PubMed:15650872, ECO:0000269|PubMed:16167903, ECO:0000269|PubMed:16480720}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K128 | CHR23_ARATH | MVKQLQEQEENDPVEKTKSLISALNYLSRDLLLPSHLYASVSSIYHASVSDLSPSPPLRGNSYTPNRGDLMSEFEDALLQQRLNYESGSRLAELKETRYKNRIHNRLSQLEGLPSNRGEDLQEKCLLELYGLKLQELQCRVRGEVSAEYWLRLNCADPERQLYDWGMMRLPRRMYGVGDSFVMEADDQFRNKRDAERLLRLEEEEKNLIETTQRKFFAEVLNAVREFQLQIQASHRRCKQRNDGVQAWHGKQRQRATRAEKLRIMALKSDDQEEYMKLAKESKNEKLTLFLEETNKIFVSLGAAVQRQKDAKLSENTKLLKGSESDLSDVDAPEDVLPAQDIEIIDSDNNDDSNDLLEGERQFNLAIHSIQEKVTKQPSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVIRPFLLRRKKSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGNGKSKSLQNLTMQLRKCCNHPYLFVGADYNMCKKPEIVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLLSTRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLFNTTSTAQDRREMLEEIMSKGTSSLGEDVPSEREINRLAARTEEEFWMFEQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDKTNAKNHFGSLTGKRKRKEAVYSDSLSDLQWMKAMESEDEDASKVSQKRKRTDTKTRMSNGSKAEAVLSESDEEKEEEEEERKEESGKESEEENEKPLHSWKTNKKKRSRYPVMTSSPNSRGKGSSKGSKRN | 3.6.4.12 | null | maintenance of root meristem identity [GO:0010078]; maintenance of seed dormancy [GO:0010231]; maintenance of shoot apical meristem identity [GO:0010492]; positive regulation of transcription by RNA polymerase II [GO:0045944]; unidimensional cell growth [GO:0009826] | nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin DNA binding [GO:0031490]; helicase activity [GO:0004386]; histone binding [GO:0042393] | PF00271;PF14619;PF00176; | 3.40.50.300;3.40.50.10810; | Helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23062007}. | 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; | null | null | null | null | FUNCTION: Probable chromatin-remodeling factor that is functionally redundant with CHR12 in root and shoot stem cell initiation and root apical meristem (RAM) and shoot apical meristem (SAM) maintenance. Can associate with the promoter region of WOX5 (PubMed:23062007). May promote seed maturation and repress initiation of germination (PubMed:24839909). May repress plant growth (PubMed:24666886). {ECO:0000269|PubMed:23062007, ECO:0000269|PubMed:24666886, ECO:0000269|PubMed:24839909}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K1J4 | ATXR7_ARATH | MVAVDSTFPSHGSSYSSRRKKVSALEPNYFGSMCMGVYSDDVSISAREVAQDYSCDSCGDLATVSSACCNFDELCGLDSALEMGCRSNEDCRAGQEASGSGIASGLDKSVPGYTMYASGWMYGNQQGQMCGPYTQQQLYDGLSTNFLPEDLLVYPIINGYTANSVPLKYFKQFPDHVATGFAYLQNGIISVAPSVTSFPPSSSNATVHQDEIQTEHATSATHLISHQTMPPQTSSNGSVLDQLTLNHEESNMLASFLSLGNEHACWFLVDGEGRNHGPHSILELFSWQQHGYVSDAALIRDGENKLRPITLASLIGVWRVKCGDANCDEPVTGVNFISEVSEELSVHLQSGIMKIARRALLDEIISSVISDFLKAKKSDEHLKSYPPTSAVESISSRVINAEKSVVSNTESAGCKNTMNEGGHSSIAAESSKYTKSVGSIENFQTSCSAVCRTLHHHCMQIMWNAVFYDTVATHSSCWRKNKIWFRSSDISTVNYCKGSHTKYSDKPESFESFTCRVDSSSSKTAYSDEFDLATNGARVRGLSSDTYGTESVIASISEHVENELFLSLKTHLTDYTSILIKDGANNTTSSARDGKMHEGSFREQYNLEGSSKKKNGLNVVPAKLRFSNDFSDSQRLLQEGESSEQITSEDIIANIFSTALETSDIPVNDELDALAIHEPPPPGCESNINMPCLRYKYQPVRSKESIPEIKAYVSMALCRQKLHNDVMRDWKSLFLKCYLNEFLASLKGSHQVSRKETLALKKRKTVTRNKKLVQSNISNQTAEKLRKPCVGASEKVLVKRSKKLSDSHSMKEVLKVDTPSIDLSVRKPSQQKMRNTDRRDHCIIKDATKLHKEKVGKDAFSKVICDKSQDLEMEDEFDDALLITRLRRISRNKTKELRECRNAAKSCEEISVTAEESEETVDCKDHEESLSNKPSQKVKKAHTSKLKRKNLSDARDEGTKSCNGAVKSFTEISGKEGDTESLGLAISDKVSHQNLSKRRKSKIALFLFPGFENTSRKCFTKLLSPEDAAKNGQDMSNPTGNPPRLAEGKKFVEKSACSISQKGRKSSQSSILKRKHQLDEKISNVPSRRRLSLSSTDSEDAVIKEDYDVRNEEKLPCHTSDKLQKGPNKLIRRRKPLAKHTTERSPIKDLSVDDGRPKPIALKPLEKLSSKPSKKKLFLSIPKSDGCARTSINGWHWHAWSLKASAEERARVRGSSCVHMQHFGSKSSLTQNVLSARTNRAKLRNLLAAADGADVLKMSQLKARKKHLRFQQSKIHDWGLVALEPIEAEDFVIEYVGELIRSSISEIRERQYEKMGIGSSYLFRLDDGYVLDATKRGGIARFINHSCEPNCYTKIISVEGKKKIFIYAKRHIDAGEEISYNYKFPLEDDKIPCNCGAPNVYCFCEQVPWIAKLKRRTWFSRRN | 2.1.1.354; 2.1.1.357 | null | flower development [GO:0009908]; methylation [GO:0032259]; regulation of flower development [GO:0009909]; vegetative to reproductive phase transition of meristem [GO:0010228] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | histone H3K36 dimethyltransferase activity [GO:0140954]; histone H3K4 trimethyltransferase activity [GO:0140999] | PF00856; | 3.30.1490.40;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19726574}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354; Evidence={ECO:0000305|PubMed:19855050}; CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357; Evidence={ECO:0000305|PubMed:19726574}; | null | null | null | null | FUNCTION: Histone methyltransferase involved in regulation of flowering time. Required for the expression of the flowering repressors FLC and MADS-box genes of the MAF family (PubMed:19726574, PubMed:19855050). Required for histone H3 dimethylation on 'Lys-36' H3K36me2 at the FLC locus (PubMed:19726574). Required for histone H3 trimethylation on 'Lys-4' (H3K4me3) at the FLC locus. Prevents trimethylation on 'Lys-27' (H3K27me3) at the same locus (PubMed:19855050). Involved in the control of seed dormancy and germination (PubMed:21799800). {ECO:0000269|PubMed:19726574, ECO:0000269|PubMed:19855050, ECO:0000269|PubMed:21799800}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K2A1 | FPGS1_ARATH | MFAVSIVPRTTSCRLSSAFLCQLSIPLTLRLHHHYQHHQPHLPSPLSFQIHSLRKQIDMAAQGGDSYEEALAALSSLITKRSRADKSNKGDRFELVFDYLKLLDLEEDILKMNVIHVAGTKGKGSTCTFTESIIRNYGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLGYFWWCYNRLKERTNEEIPMPTYFRFLALLAFKIFAAEEVDAAILEVGLGGKFDATNAVQKPVVCGISSLGYDHMEILGDTLGKIAGEKAGIFKLGVPAFTVPQPDEAMRVLEEKASETEVNLEVVQPLTARLLSGQKLGLDGEHQYVNAGLAVSLASIWLQQIGKLEVPSRTQMSILPEKFIKGLATASLQGRAQVVPDQYTESRTSGDLVFYLDGAHSPESMEACAKWFSVAVKGDNQSGSSGHLVNGSAGSSHDKWSNETCEQILLFNCMSVRDPNLLLPHLKNMCAKYGVNFKKALFVPNMSVYHKVGTAADLPENDPQVDLSWQFTLQKVWESLVQSERDGEKDGESDGNSEVFTSLPMAIKCLRDTVHESSSATRFQVLVTGSLHLVGDVLRLIRK | 6.3.2.17 | COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000250|UniProtKB:Q05932}; Note=A monovalent cation. {ECO:0000250|UniProtKB:Q05932}; | lignin biosynthetic process [GO:0009809]; one-carbon metabolic process [GO:0006730]; quiescent center organization [GO:1904961]; root development [GO:0048364]; root hair elongation [GO:0048767]; root meristem growth [GO:0010449]; tetrahydrofolylpolyglutamate biosynthetic process [GO:0046901] | chloroplast [GO:0009507]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326] | null | 3.90.190.20;3.40.1190.10; | Folylpolyglutamate synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:11752472}. | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738, Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005, ChEBI:CHEBI:456216; EC=6.3.2.17; Evidence={ECO:0000269|PubMed:11752472}; | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. {ECO:0000250|UniProtKB:Q05932}. | null | null | FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Essential for organellar and whole-plant folate homeostasis. Required for postembryonic root development. Generates polyglutamylated folate cofactors to support C1 metabolism required for meristem maintenance and cell expansion during postembryonic root development. {ECO:0000250|UniProtKB:Q05932, ECO:0000269|PubMed:11752472, ECO:0000269|PubMed:21070407, ECO:0000269|PubMed:21233333}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K2E9 | PRP16_ARATH | MGVDPFKTTETLEADKETNGGVPVKDKLTFKAPERKSRLGLDARAIEKKDNAKTEGEFKVPKKSAISVTSSLDEEDKSDVSGLDFGTENTRPVHSSRRYREKSSRSQSAQESTVTTENAGTSDISITPRTLSCTSSYERGGSNRHREEHRRDRSETPRSRQRNTYDEMDHYRRRESYRQSDRDYHGEKRRRYNSDWRTPGRSDWDDGQDEWERSPHGDRGSSYSRRPQPSPSPMLAAASPDARLASPWLDTPRSTMSSASPWDMGAPSPIPIRASGSSIRSSSSRYGGRSNQLAYSREGDLTNEGHSDEDRSQGAEEFKHEITETMRVEMEYQSDRAWYDTDEGNSLFDADSASFFLGDDASLQKKETELAKRLVRRDGSKMSLAQSKKYSQLNADNAQWEDRQLLRSGAVRGTEVQTEFDSEEERKAILLVHDTKPPFLDGRVVYTKQAEPVMPVKDPTSDMAIISRKGSGLVKEIREKQSANKSRQRFWELAGSNLGNILGIEKSAEQIDADTAVVGDDGEVDFKGEAKFAQHMKKGEAVSEFAMSKTMAEQRQYLPIFSVRDELLQVIRENQVIVVVGETGSGKTTQLTQYLHEDGYTINGIVGCTQPRRVAAMSVAKRVSEEMETELGDKIGYAIRFEDVTGPNTVIKYMTDGVLLRETLKDSDLDKYRVVVMDEAHERSLNTDVLFGILKKVVARRRDFKLIVTSATLNAQKFSNFFGSVPIFNIPGRTFPVNILYSKTPCEDYVEAAVKQAMTIHITSPPGDILIFMTGQDEIEAACFSLKERMEQLVSSSSREITNLLILPIYSQLPADLQAKIFQKPEDGARKCIVATNIAETSLTVDGIYYVIDTGYGKMKVFNPRMGMDALQVFPISRAASDQRAGRAGRTGPGTCYRLYTESAYLNEMLPSPVPEIQRTNLGNVVLLLKSLKIDNLLDFDFMDPPPQENILNSMYQLWVLGALNNVGGLTDLGWKMVEFPLDPPLAKMLLMGERLDCIDEVLTIVSMLSVPSVFFRPKERAEESDAAREKFFVPESDHLTLLNVYQQWKEHDYRGDWCNDHYLQVKGLRKAREVRSQLLDILKQLKIELRSCGPDWDIVRKAICSAYFHNSARLKGVGEYVNCRTGMPCHLHPSSALYGLGYTPDYVVYHELILTTKEYMQCATSVEPHWLAELGPMFFSVKDSDTSMLEHKKKQKEEKSGMEEEMEKLRRDQVESELRSKERERKKRAKQQQQISGPGLKKGTTFLRPKKLGL | 3.6.4.13 | null | defense response to fungus [GO:0050832]; embryo development ending in seed dormancy [GO:0009793]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of RNA splicing [GO:0033120]; primary miRNA processing [GO:0031053]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; RNA splicing [GO:0008380]; root development [GO:0048364]; root hair elongation [GO:0048767]; xylem and phloem pattern formation [GO:0010051] | nucleus [GO:0005634]; spliceosomal complex [GO:0005681] | 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723] | PF00270;PF21010;PF04408;PF00271;PF07717; | 1.20.120.1080;3.40.50.300; | DEAD box helicase family, DEAH subfamily, PRP16 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25384462, ECO:0000269|PubMed:25902521}. Note=Binds to the spliceosome. {ECO:0000250|UniProtKB:P15938}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing by mediating structural transitions of the spliceosome during the catalytic step. Facilitates expression of genes involved in auxin-mediated development including male-gametophyte transmission, apical-basal patterning of embryonic and gynoecium development, stamen development, phyllotactic flower positioning, and vascular development (PubMed:25384462). Also involved in root-meristem maintenance and planar polarity of root-hair positioning (PubMed:26237376). Acts as a component of RNA silencing that regulates distinct classes of endogenous small RNAs. Functions as a positive regulator of plant immunity (PubMed:25902521). {ECO:0000269|PubMed:25384462, ECO:0000269|PubMed:25902521, ECO:0000269|PubMed:26237376}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K2R6 | CB60G_ARATH | MKIRNSPSFHGGSGYSVFRARNLTFKKVVKKVMRDQSNNQFMIQMENMIRRIVREEIQRSLQPFLSSSCVSMERSRSETPSSRSRLKLCFINSPPSSIFTGSKIEAEDGSPLVIELVDATTNTLVSTGPFSSSRVELVPLNADFTEESWTVEGFNRNILTQREGKRPLLTGDLTVMLKNGVGVITGDIAFSDNSSWTRSRKFRLGAKLTGDGAVEARSEAFGCRDQRGESYKKHHPPCPSDEVWRLEKIAKDGVSATRLAERKILTVKDFRRLYTVNRNELHNIIGAGVSKKTWNTIVSHAMDCVLDETECYIYNANTPGVTLLFNSVYELIRVSFNGNDIQNLDQPILDQLKAEAYQNLNRITAVNDRTFVGHPQRSLQCPQDPGFVVTCSGSQHIDFQGSLDPSSSSMALCHKASSSTVHPDVLMSFDNSSTARFHIDKKFLPTFGNSFKVSELDQVHGKSQTVVTKGCIENNEEDENAFSYHHHDDMTSSWSPGTHQAVETMFLTVSETEEAGMFDVHFANVNLGSPRARWCKVKAAFKVRAAFKEVRRHTTARNPREGL | null | null | abscisic acid-activated signaling pathway [GO:0009738]; cellular response to hypoxia [GO:0071456]; cellular response to molecule of bacterial origin [GO:0071219]; defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; plant-type hypersensitive response [GO:0009626]; positive regulation of abscisic acid-activated signaling pathway [GO:0009789]; positive regulation of response to water deprivation [GO:1902584]; regulation of DNA-templated transcription [GO:0006355]; regulation of salicylic acid biosynthetic process [GO:0080142]; regulation of systemic acquired resistance [GO:0010112]; response to bacterium [GO:0009617]; response to fungus [GO:0009620]; response to molecule of bacterial origin [GO:0002237]; response to UV-B [GO:0010224]; salicylic acid biosynthetic process [GO:0009697] | nucleus [GO:0005634] | calmodulin binding [GO:0005516]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF20452;PF20451;PF07887; | null | Plant ACBP60 protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22466450}. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA in a sequence-specific manner, 5'-GAAATTTTGG-3', to promote the expression of target genes (PubMed:20921422, PubMed:21615571, PubMed:23153277, PubMed:29757140). Recruited to the promoter of ICS1 and other defense-related genes (e.g. PR1, PR2 and EDS5) in response to both biotic (e.g. Pseudomonas syringae pv. maculicola ES4326, P. syringae pv. tomato DC3000, and microbe-associated molecular patterns (MAMPs) such as flg22) and abiotic stresses (e.g. UV-B, drought and abscisic acid), thus triggering rapid defense responses by stimulating salicylic acid (SA) biosynthesis. Involved in basal and systemic acquired resistance to P. syringae and Hyaloperonospora arabidopsidis (PubMed:19214217, PubMed:20921422, PubMed:21615571, PubMed:22466450). Mediates resistance to drought and sensitivity to abscisic acid (ABA), especially for ABA-mediated signaling process that regulates early seedling growth (PubMed:22466450). {ECO:0000269|PubMed:19214217, ECO:0000269|PubMed:20921422, ECO:0000269|PubMed:21615571, ECO:0000269|PubMed:22466450, ECO:0000269|PubMed:23153277, ECO:0000269|PubMed:29757140}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K3G5 | EDM2_ARATH | MTFVDDDEEEDFSVPQSASNYYFEDDDKEPVSFARLPIQWSVEEKVDGSGLGFYLRGRSDNGLLPLHKLVKAWRYDLSNFQPEISVLTKDNIWIKLEEPRKSYGELIRTVLVTLHSIQFLRRNPQASEKALWEKLTRSLRSYDVKPSQNDLVDHIGLIAEAAKRDRNLANSKFILAFLTKKPTKRRLPDEDNAKDDFIVGDEDTYVASDEDELDDEDDDFFESVCAICDNGGEILCCEGSCLRSFHATKKDGEDSLCDSLGFNKMQVEAIQKYFCPNCEHKIHQCFICKNLGSSDNSSGAAEVFQCVSATCGYFYHPHCVTRRLRLGNKEESEALERQIIAGEYTCPLHKCSVCENGEVKTDSNLQFAVCRRCPKSYHRKCLPREISFEDIEDEDILTRAWDGLLHNRVLIYCQEHEIDEELLTPVRDHVKFPFTEEQKVFVKEQRRILESHVGRDKARLKVKDPALQDTCGKASKNSFRSSFPSSKDGFSTKKHGLVSSVPDHSRKRKDIDPSIKHKMVPQKSQKMMEDSREAGKNKLGVKEARDAGKSKISLGERLFSYTQEPNPVKPGRVIPVDSKHNKTDSIASKEPGSEIPTLDNDSQRRLLAVMKKATEEITMGTILKKFKIQSTMSTHSTRNVVDKTITMGKVEGSVQAIRTALKKLEEGGNIEDAKAVCEPEVLSQILKWKDKLKVYLAPFLHGARYTSFGRHFTNPEKLQQIVDRLHWYADDGDMIVDFCCGSNDFSCLMNAKLEETGKKCLYKNYDLFPAKNNFNFERKDWMTVSKDELEPGSKLIMGLNPPFGVNASLANKFITKALEFRPKILILIVPPETERLDKKKSSYVLIWEDKTFLSGNSFYLPGSVNEEDKQLEDWNLVPPPLSLWSRSDFAAKHKKIAEKHCHLSRDVGSSKLKIVEEEANASLHPLGASDGMCDDIPMEKDELEVAECVNKILVSEKIDTVETVARVHQSDHLSRRSQLKKEGKTKDYSGRKLGKSMDSNNVDWKSNDMEEDQGELSRAPESIKVKIPEMTSDWQSPVRSSPDDIYAVCTSISTTTPQRSHEAVEASLPAITRTKSNLGKNIREHGCKVQGTGKPEVSRDRPSSVRTSREDIYTVRPSPENTGQKPFEAFEPSYGASLSHFDDGLAAKYGGFGGGYRMPDPPFLPDQFPLRNGPNEMFDFRGYSDLDRGIGQREYPQQYGGHLDPMLAPPPPPNLMDNAFPLQQRYAPHFDQMNYQRMSSFPPQPPLQPSGHNLLNPHDFPLPPPPPSDFEMSPRGFAPGPNPNYPYMSRSGGWIND | null | null | defense response to fungus [GO:0050832]; epigenetic regulation of gene expression [GO:0040029]; leaf pavement cell development [GO:0090436]; negative regulation of heterochromatin formation [GO:0031452]; positive regulation of defense response to oomycetes [GO:1902290]; positive regulation of flower development [GO:0009911]; regulation of defense response [GO:0031347]; regulation of DNA-templated transcription [GO:0006355]; regulation of leaf development [GO:2000024]; regulation of post-transcriptional gene silencing [GO:0060147]; retrotransposon silencing by heterochromatin formation [GO:0141005]; signal transduction [GO:0007165]; stomatal lineage progression [GO:0010440]; vegetative to reproductive phase transition of meristem [GO:0010228] | heterochromatin [GO:0000792]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | DNA-binding transcription factor activity [GO:0003700]; histone reader activity [GO:0140566]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; sequence-specific DNA binding [GO:0043565] | PF12047; | 3.30.40.10; | null | PTM: Phosphorylated by WNK8. {ECO:0000269|PubMed:20149132}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:20149132, ECO:0000269|PubMed:21830950}. | null | null | null | null | null | FUNCTION: Cellular antisilencing factor and regulator of genome DNA methylation patterns involved in the regulation of chromatin states (PubMed:32925902). Together with SUVH4, monitors repressive epigenetic marks H3K27me1, H3K9me2, and prevents DNA-methylation at CHG sites, affecting especially the expression of transposons and developmentally important genes (PubMed:21830950, PubMed:23609044, PubMed:24248388). Collaboratively with ASI1 and AIPP1/EDM3, the AAE complex regulates alternative RNA processing (e.g. alternative splicing) and epigenetic silencing (e.g. H3K9me2) of intronic heterochromatin-containing genes as well as genic heterochromatin-containing genes by promoting distal 3' polyadenylation (PubMed:24248388, PubMed:28808009, PubMed:33438356). Epigenetic reader that binds DNA and contributes to transcriptional transposable element (TE) silencing by modulating levels of the repressive post-translational histone modifications (PHM) H3K9me2 (PubMed:23609044, PubMed:28808009, PubMed:32925902, PubMed:33438356). In cv. Columbia, required for RPP7-dependent disease resistance against the Hyaloperonospora arabidopsidis isolate Hiks1, by promoting levels of RPP7 via alternative polyadenylation (APA), resulting from cooption of epigenetic information at the TE insertion locus COPIA-R7 (PubMed:17253987, PubMed:20149132, PubMed:23940361, PubMed:30407670). Exhibits a global role in NLR (nucleotide-binding, leucine-rich repeat) defense genes epigenetic (e.g. H3K9me2 hallmarks) expression control; promotes the accumulation of RPP7, RPP4 and some other proteins, but mediates the repression of several other NLR products, probably to compensate for fitness penalties caused by defense mechanisms (PubMed:32925902). Regulates development processes such as the formation of leaf pavement cells, leaf expansion, fertility and flowering (PubMed:20149132, PubMed:20840782, PubMed:23609044). Prevents FLC accumulation to control flowering (PubMed:23976921). Modulates stomatal development by regulating the methylation-mediated silencing of ERECTA receptor genes (e.g. ER, ERL1 and ERL2) and preventing cell divisions (PubMed:27697902). {ECO:0000269|PubMed:17253987, ECO:0000269|PubMed:20149132, ECO:0000269|PubMed:20840782, ECO:0000269|PubMed:21830950, ECO:0000269|PubMed:23609044, ECO:0000269|PubMed:23940361, ECO:0000269|PubMed:23976921, ECO:0000269|PubMed:24248388, ECO:0000269|PubMed:27697902, ECO:0000269|PubMed:28808009, ECO:0000269|PubMed:30407670, ECO:0000269|PubMed:32925902, ECO:0000269|PubMed:33438356}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K410 | SVR3_ARATH | MELSLSTSSASPAVLRRQASPLLHKQQVLGVSFASALKPGGGALRFPSRRPLPRPITCSASPSTAEPASEVKKKQLDRRDNVRNIAIVAHVDHGKTTLVDSMLRQAKVFRDNQVMQERIMDSNDLERERGITILSKNTSITYKNTKVNIIDTPGHSDFGGEVERVLNMVDGVLLVVDSVEGPMPQTRFVLKKALEFGHAVVVVVNKIDRPSARPEFVVNSTFELFIELNATDEQCDFQAIYASGIKGKAGLSPDDLAEDLGPLFEAIIRCVPGPNIEKDGALQMLATNIEYDEHKGRIAIGRLHAGVLRKGMDVRVCTSEDSCRFARVSELFVYEKFYRVPTDSVEAGDICAVCGIDNIQIGETIADKVHGKPLPTIKVEEPTVKMSFSVNTSPFSGREGKYVTSRNLRDRLNRELERNLAMKVEDGETADTFIVSGRGTLHITILIENMRREGYEFMVGPPKVINKRVNDKLLEPYEIATVEVPEAHMGPVVELLGKRRGQMFDMQGVGSEGTTFLRYKIPTRGLLGLRNAILTASRGTAILNTVFDSYGPWAGDISTRDLGSLVAFEDGTSTSYALASAQERGQMFVGSGVDVYKGQIVGIHQRPGDLGLNICKKKAATNIRSNKDVTVILDTPLTYSLDDCIEYIEEDELVEVTPSSIRMCKNQKMAKKGRQ | null | null | protein stabilization [GO:0050821]; response to cold [GO:0009409]; rRNA processing [GO:0006364] | chloroplast [GO:0009507]; cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746] | PF21018;PF00679;PF00009;PF03144; | 3.30.70.240;2.40.50.250;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, BipA subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:21187014}. | null | null | null | null | null | FUNCTION: Putative chloroplastic elongation factor involved in response to chilling stress. Required for proper chloroplast rRNA processing and/or translation at low temperature (PubMed:21187014). Involved in plastid protein homeostasis (PubMed:21208309). {ECO:0000269|PubMed:21187014, ECO:0000269|PubMed:21208309}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K4E3 | LSM4_ARATH | MLPLSLLKTAQGHPMLVELKNGETYNGHLVNCDTWMNIHLREVICTSKDGDRFWRMPECYIRGNTIKYLRVPDEVIDKVQEEKTRTDRKPPGVGRGRGRGVDDGGARGRGRGTSMGKMGGNRGAGRGRG | null | null | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; mRNA splicing, via spliceosome [GO:0000398]; P-body assembly [GO:0033962]; spliceosomal snRNP assembly [GO:0000387] | cytosol [GO:0005829]; Lsm1-7-Pat1 complex [GO:1990726]; Lsm2-8 complex [GO:0120115]; nucleus [GO:0005634]; P-body [GO:0000932]; plastid [GO:0009536]; spliceosomal complex [GO:0005681]; spliceosomal tri-snRNP complex [GO:0097526]; U6 snRNP [GO:0005688] | U6 snRNA binding [GO:0017070] | PF01423; | 2.30.30.100; | SnRNP Sm proteins family | PTM: Methylated by PMRT15/SKB1 in response to salt stress or abscisic acid (ABA) treatment. {ECO:0000269|PubMed:21258002}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}. | null | null | null | null | null | FUNCTION: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression. {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K5J1 | MYO17_ARATH | MVGPVNIIVGSHVWIEDPGAAWIDGEVVKINGEEVHAHTTNGKTVVANIANVFPKDTEAPPGGVDDMTKLSYLHEPGVLNNLAMRYELNEIYTYTGNILIAVNPFQRLPHLYDTHMMEQYKGAGFGELSPHVFAIAEVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVELQFDNCGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPPEEREKFKLGDPKLFHYLNQSKCYKLDGVDDTEEYLATRRAMDIVGISEEEQDAIFRVVAAILHLGNVNFAKGKEIDSSVLKDEKSRYHLDVCAELLRCDAKKMEDALIKRVMVTPEEVITRTLDPDSATGSRDALAKTIYSRLFDWLVDKINNSIGQDPNSKTIIGVLDIYGFESFKINSFEQFCINFTNEKLQQHFNQHVFKMEQEDYTKEEINWSYIEFVDNKDVLELIEKKPGGVIALLDEACMFPKSTHETFAQKLYQTFKNYKRFTKPKLSRTSFAISHYAGEVTYQADLFLDKNKDYVVAEHQDLLIASSDTFVAGLFPRLPEETSSKTKFSSIGSRFKLQLQSLMETLSSTEPHYIRCVKPNNVLKPAIFENVNVIQQLRCGGVLEAIRISCAGYPTKRTFYEFLNRFGVLAPEVLEGNYDDKVACKMLLDKIGLKGYELGKTKVFLRAGQMAELDARRAEVLGNAARRIQRQSRTFIACKEFRALRGAAIVLQSNCRGKLACNLYEEMRRQAAAVKIQKIFRRHIARESYLRIRHSTITVQTALRGMVARNEFRFRKQMKAATIIQARLRSHLTHSYYKQLQKAALSTQCGWRSRVARKELRTLKMAARDTGALREAKDKLEKRVEELTWRLQLEKRQRTELEEAKTQEYAKQQEALETMRLQVEEANAAVIREREAARKAIEEAPPVIKETPVLVEDTEKINSLTSEVEALKASLQAERQAAENLRKAFSEAEARNSELATELENATRKADQLHESVQRLEEKLSNSESEIQVLRQQALAISPTSRTMATRSKTMLLPRTPENGNYLNGGTKTTPDMTLAVREPESEEKPQKHLNEKQQENQDLLVKCISQNLGYNGDKPVAACVIYKCLLHWRSFEVERTSVFDRIIQTIATAIEVPDNNEVLAYWLSNSATLLLLLQRTLKATGAASLTPQRRRTTSASLFGRMSQGLRGSPQSAGLSFLNRQGLTKLDDLRQVEAKYPALLFKQQLTAFLEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGRAQANAVAQQALIAHWQSIRKSLNSYLNLMKANNAPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEQWCIEATDEYAGSAWDELRHIRQAVGFLVIHQKPKKTLDEITRELCPVLSIQQLYRISTMYWDDKYGTHSVSSDVIANMRVMMTEDSNNAVSSSFLLDDDSSIPFTVEDISKSMQQVDVNDIEPPQLIRENSGFGFLLTRKEGSTS | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cell division [GO:0051301]; fruit development [GO:0010154]; Golgi localization [GO:0051645]; gynoecium development [GO:0048467]; leaf pavement cell development [GO:0090436]; mitochondrion localization [GO:0051646]; peroxisome localization [GO:0060151]; post-embryonic development [GO:0009791]; root hair cell tip growth [GO:0048768]; root hair elongation [GO:0048767]; trichome branching [GO:0010091]; trichome morphogenesis [GO:0010090]; unidimensional cell growth [GO:0009826]; vesicle transport along actin filament [GO:0030050] | myosin complex [GO:0016459]; plasmodesma [GO:0009506]; root hair tip [GO:0035619]; transport vesicle [GO:0030133] | 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 | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056, ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:20351265, ECO:0000269|PubMed:22969781}. Note=Colocalizes with peroxisome, cytoplasmic vesicles, endomembrane vesicles, endoplasmic reticulum 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 the tip growth of root hair cells and in the elongation of trichome stalk and branches. Plays a major role in trafficking of Golgi stacks, mitochondria and peroxisomes during root hair development. Acts as the primary contributor to ER streaming with a major role in the movement of Golgi bodies. Required for development of pavement cells, trichomes, and stigmatic papillae. {ECO:0000269|PubMed:17458634, ECO:0000269|PubMed:18178669, ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:19060218, ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:20351265, ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656, ECO:0000269|PubMed:22672737}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K5T2 | CGL_ARATH | MEDRVLIKNDVTELIGNTPMVYLNKIVDGCVARIAAKLEMMEPCSSIKDRIAYSMIKDAEDKGLITPGKSTLIEATGGNTGIGLASIGASRGYKVILLMPSTMSLERRIILRALGAEVHLTDISIGIKGQLEKAKEILSKTPGGYIPHQFINPENPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTVTGTGKFLKEKNKDIKVCVVEPSESAVLSGGKPGPHLIQGIGSGEIPANLDLSIVDEIIQVTGEEAIETTKLLAIKEGLLVGISSGASAAAALKVAKRPENVGKLIVVIFPSGGERYLSTELFESVRYEAENLPVE | 2.5.1.47; 4.4.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:19955263}; | cysteine biosynthetic process from serine [GO:0006535]; intracellular cysteine homeostasis [GO:0080145]; response to oxidative stress [GO:0006979]; stress response to cadmium ion [GO:1990170] | cytoplasm [GO:0005737] | cystathionine gamma-lyase activity [GO:0004123]; cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146]; L-cystine L-cysteine-lyase (deaminating) [GO:0044540]; pyridoxal phosphate binding [GO:0030170] | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine + NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1; Evidence={ECO:0000269|PubMed:19955263}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:19955263}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for L-cysteine for the cystathionine gamma-lyase activity {ECO:0000269|PubMed:19955263}; KM=5.2 mM for O(3)-acetyl-L-serine for the cysteine synthase activity {ECO:0000269|PubMed:19955263}; Vmax=0.04 umol/min/mg enzyme for the DES reaction {ECO:0000269|PubMed:19955263}; Vmax=1.8 umol/min/mg enzyme for the OASTL reaction {ECO:0000269|PubMed:19955263}; | PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. | null | null | FUNCTION: Involved in maintaining Cys homeostasis through the desulfuration of L-cysteine. Modulates the generation of the signaling molecule sulfide in plant cytosol. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein. {ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:19955263, ECO:0000269|PubMed:23428891}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K5X6 | RVE2_ARATH | MAMQERCESLCSDELISSSDAFYLKTRKPYTITKQREKWTEAEHEKFVEALKLYGRAWRRIEEHVGTKTAVQIRSHAQKFFTKVARDFGVSSESIEIPPPRPKRKPMHPYPRKLVIPDAKEMVYAELTGSKLIQDEDNRSPTSVLSAHGSDGLGSIGSNSPNSSSAELSSHTEESLSLEAETKQSLKLFGKTFVVGDYNSSMSCDDSEDGKKKLYSETQSLQCSSSTSENAETEVVVSEFKRSERSAFSQLKSSVTEMNNMRGFMPYKKRVKVEENIDNVKLSYPLW | null | null | circadian rhythm [GO:0007623]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; seed germination [GO:0009845] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. | null | null | null | null | null | FUNCTION: Positive regulator for cold-responsive gene expression and cold tolerance. Part of a regulatory feedback loop that controls a subset of the circadian outputs and modulates the central oscillator. Negatively self-regulates its own expression. {ECO:0000269|PubMed:17587236, ECO:0000269|PubMed:23371945}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K6B8 | RGI4_ARATH | MPRNPRFCFFLFLLFHSSLFFSIPCFSIDEQGLALLSWKSQLNISGDALSSWKASESNPCQWVGIKCNERGQVSEIQLQVMDFQGPLPATNLRQIKSLTLLSLTSVNLTGSIPKELGDLSELEVLDLADNSLSGEIPVDIFKLKKLKILSLNTNNLEGVIPSELGNLVNLIELTLFDNKLAGEIPRTIGELKNLEIFRAGGNKNLRGELPWEIGNCESLVTLGLAETSLSGRLPASIGNLKKVQTIALYTSLLSGPIPDEIGNCTELQNLYLYQNSISGSIPVSMGRLKKLQSLLLWQNNLVGKIPTELGTCPELFLVDLSENLLTGNIPRSFGNLPNLQELQLSVNQLSGTIPEELANCTKLTHLEIDNNQISGEIPPLIGKLTSLTMFFAWQNQLTGIIPESLSQCQELQAIDLSYNNLSGSIPNGIFEIRNLTKLLLLSNYLSGFIPPDIGNCTNLYRLRLNGNRLAGNIPAEIGNLKNLNFIDISENRLIGNIPPEISGCTSLEFVDLHSNGLTGGLPGTLPKSLQFIDLSDNSLTGSLPTGIGSLTELTKLNLAKNRFSGEIPREISSCRSLQLLNLGDNGFTGEIPNELGRIPSLAISLNLSCNHFTGEIPSRFSSLTNLGTLDVSHNKLAGNLNVLADLQNLVSLNISFNEFSGELPNTLFFRKLPLSVLESNKGLFISTRPENGIQTRHRSAVKVTMSILVAASVVLVLMAVYTLVKAQRITGKQEELDSWEVTLYQKLDFSIDDIVKNLTSANVIGTGSSGVVYRVTIPSGETLAVKKMWSKEENRAFNSEINTLGSIRHRNIIRLLGWCSNRNLKLLFYDYLPNGSLSSLLHGAGKGSGGADWEARYDVVLGVAHALAYLHHDCLPPILHGDVKAMNVLLGSRFESYLADFGLAKIVSGEGVTDGDSSKLSNRPPLAGSYGYMAPEHASMQHITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVQWVRDHLAGKKDPREILDPRLRGRADPIMHEMLQTLAVSFLCVSNKASDRPMMKDIVAMLKEIRQFDMDRSESDMIKGGKCEKWQPQPLPPEKIVSTPRGSSNCSFAYSDESV | 2.7.11.1 | null | maintenance of meristem identity [GO:0010074]; phosphorylation [GO:0016310]; regulation of pollen tube growth [GO:0080092]; regulation of root meristem growth [GO:0010082]; response to temperature stimulus [GO:0009266] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; 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 | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}.; PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus leading to activation a subsequent degradation. {ECO:0000250|UniProtKB:Q9LHP4}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ZWC8}; Single-pass type I 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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159}; | null | null | null | null | FUNCTION: Receptor with a serine/threonine-protein kinase activity (By similarity). Together with SKM1, LRR-rich receptor-like kinase (LRR-RLK) required for male fertility by the perception of CLE43 and CLE45 peptides and the transduction of their promoting action in pollen tubes, especially under relatively high temperature (at 30 degrees Celsius), thus conferring tolerance against high temperature probably through the maintenance of mitochondrial activity (PubMed:23910659). Seems to not be involved in the perception of CLE45 peptide in roots (PubMed:27354416). Together with RGI1, RGI2, RGI3, RGI4 and RGI5, acts as receptor of RGF1, a peptide hormone that maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT) (PubMed:27229311, PubMed:27229312). Links RGF1 signal with its downstream components (PubMed:27229311). {ECO:0000250|UniProtKB:Q9ZWC8, ECO:0000269|PubMed:23910659, ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312, ECO:0000269|PubMed:27354416}. | Arabidopsis thaliana (Mouse-ear cress) |
F4K933 | ET2_ARATH | MEFGDGVSFAVVPTVFKREDYKRTKHDTVFSKWQVLIGSNDWEDFKNGKDGVGRYRVQNLPRKSCPGLYELGVAVIGQEQCRKLEPDIVLASYLGQAESVRSRLQRYGRSGAHLRNVNNLNDCETIESPVKAVTGGLFEDIFSKGGSILYRWAPMGSKREAEATEGMLLSTFDYAWNKGSNGERRQLDLLKKLGDREFMSKRKSGISRMLFPFLRNQVGIRIKGEKHVLKEERKLTCDVDEEKSNNFLTSILKLTRSRPQPVSDRFDEVDGSCSDIVCGVLLEDGGCCIRSPVKGRKRCIEHKGQRVCRVSPEKQTPPKSEIFTGQDHHNHKDSDVVCGVILPDMEPCNKRPVPGRKRCEDHKGMRINAFLFLLNQTDREKTVKDEKPDPESHTESIEEEALTRFCEATTKNGLPCTRSSPKGSKRCWQHKEKTSSDTSPVYFQPEAAKNVACGVKLGNGLICERSPVKGRKRCEEHKGMRIT | null | null | negative regulation of DNA-templated transcription [GO:0045892]; regulation of seed dormancy process [GO:2000033]; xylem development [GO:0010089] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | supercoiled DNA binding [GO:0097100] | PF19239; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17991462}. Nucleus {ECO:0000269|PubMed:17991462}. Note=Localizes to the cytoplasm in non-differentiating cells and to the nucleus in differentiating cells. {ECO:0000269|PubMed:17991462}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in the regulation of cell differentiation in meristems. Probably regulates the expression of various KNAT genes involved in the maintenance of the cells in an undifferentiated, merismastic state. Plays a role in the regulation of gibberellin 20 oxidase and the gibberellin-regulated protein GASA4. Localizes in the nucleus during the cellular differentiation state and may act via a single strand cutting domain (PubMed:17991462). Transcriptional regulator required for the induction of dormancy during late seed development. Interacts genetically with FUS3 and may be component of the same regulatory pathway during embryogenesis. Binds both linear and supercoiled DNA without sequence preference (PubMed:22226340). {ECO:0000269|PubMed:17991462, ECO:0000269|PubMed:22226340}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KAB8 | MCM6_ARATH | MEAFGGFVMDEQAIQVENVFLEFLKSFRLDANKPELYYEAEIEAIRGGESTMMYIDFSHVMGFNDALQKAIADEYLRFEPYLRNACKRFVIEMNPSFISDDTPNKDINVSFYNLPFTKRLRELTTAEIGKLVSVTGVVTRTSEVRPELLYGTFKCLDCGSVIKNVEQQFKYTQPTICVSPTCLNRARWALLRQESKFADWQRVRMQETSKEIPAGSLPRSLDVILRHEIVEQARAGDTVIFTGTVVVIPDISALAAPGERAECRRDSSQQKSSTAGHEGVQGLKALGVRDLSYRLAFIANSVQIADGSRNTDMRNRQNDSNEDDQQQFTAEELDEIQQMRNTPDYFNKLVGSMAPTVFGHQDIKRAVLLMLLGGVHKTTHEGINLRGDINVCIVGDPSCAKSQFLKYTAGIVPRSVYTSGKSSSAAGLTATVAKEPETGEFCIEAGALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPVGGRYDKSKPLKYNVNLPPAILSRFDLVYVMIDDPDEVTDYHIAHHIVRVHQKHEAALSPEFTTVQLKRYIAYAKTLKPKLSPEARKLLVESYVALRRGDTTPGTRVAYRMTVRQLEALIRLSEAIARSHLEILVKPSHVLLAVRLLKTSVISVESGDIDLSEYQDANGDNMDDTDDIENPVDGEEDQQNGAAEPASATADNGAAAQKLVISEEEYDRITQALVIRLRQHEETVNKDSSELPGIRQKELIRWFIDQQNEKKKYSSQEQVKLDIKKLRAIIESLVCKEGHLIVLANEQEEAAEAEETKKKSSQRDERILAVAPNYVIE | 3.6.4.12 | null | DNA replication initiation [GO:0006270]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication [GO:1902969] | MCM complex [GO:0042555]; THO complex [GO:0000347] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; single-stranded 3'-5' DNA helicase activity [GO:1990518]; single-stranded DNA binding [GO:0003697] | PF00493;PF18263;PF17855;PF14551;PF17207; | 1.20.58.870;2.20.28.10;3.30.1640.10;2.40.50.140;3.40.50.300; | MCM family | 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; | null | null | null | null | FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KAF2 | MORC4_ARATH | MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNVETVVQWSPYATEEELLCQFNLMKKHGTRIIIYNLWEDDEGMLELDFDTDPHDIQLRGVNRDDKNIVMASQFPNSRHYLTYKHSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADVSQLSAVVTIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYWRSKCHKIGYAKRQGRKSAKDTEKDTEDRESSPEFDPKGSASSRKRTVPSSFKTPTAAPRFNTPTAASEKFNPRSNVNGGGKGSVKVSKDIGYKSSEKGGKLGNSFSKSNKRAKPQGARAVEVTNSDDDYDCDSSPERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDGKARGR | 3.6.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q84WV6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q84WV6}; | defense response [GO:0006952]; DNA repair [GO:0006281]; gene silencing by RNA-directed DNA methylation [GO:0080188]; phosphorylation [GO:0016310]; positive regulation of defense response to oomycetes [GO:1902290]; regulation of DNA repair [GO:0006282]; regulation of gene silencing by regulatory ncRNA [GO:0060966] | nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; kinase activity [GO:0016301]; protein self-association [GO:0043621]; RNA binding [GO:0003723] | PF13589;PF17942; | 3.30.565.10; | MORC ATPase protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}. | null | null | null | null | null | FUNCTION: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC7, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa) (PubMed:27171361). {ECO:0000250|UniProtKB:Q84WV6, ECO:0000269|PubMed:27171361}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KAK5 | PSD2_ARATH | MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRNSAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSNVVGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQINMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTLI | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03209}; | phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540] | plant-type vacuole membrane [GO:0009705] | calcium ion binding [GO:0005509]; phosphatidylserine decarboxylase activity [GO:0004609] | PF00168;PF13499;PF02666; | 2.60.40.150;1.10.238.10; | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type II sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03209}. | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:17449644}; Peripheral membrane protein {ECO:0000305|PubMed:17449644}. Note=Tonoplast. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}. | null | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:17449644}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KB17 | KTN83_ARATH | MNTKRAYKLQEFVAHSAAVNCLKIGRKSSRVLVTGGEDHKVNLWAIGKPNAILSLYGHSSGIDSVTFDASEGLVAAGAASGTIKLWDLEEAKVVRTLTGHRSNCVSVNFHPFGEFFASGSLDTNLKIWDIRKKGCIHTYKGHTRGVNVLRFTPDGRWIVSGGEDNVVKVWDLTAGKLLHEFKSHEGKIQSLDFHPHEFLLATGSADKTVKFWDLETFELIGSGGTETTGVRCLTFNPDGKSVLCGLQESLKIFSWEPIRCHDGVDVGWSNLSDMNVHEGKLLGCSYNQNCVGVWVVDLSRTEPMSGGATQSNSHPEKTSGSGRDQAGLNDNSSKVILGKLPGSQKVDPLLKETKSLGKLSVSQNSDPLPKDTKSTGRSSVSQSSDPLVKEPKPLGRFSATHSSDTVKESRTLSSTGSVSDSPHRVTLTSAPKSASGISTVVPNAAASKRNFGKANPKANPPVVNKEDYFPVIVPRTEPIIEQASESRAELDIIGRTMPYSLQSKAADSRRLSSSRNEPDLPTSSLLERSQSQPIEPITLQDGNTYPSDEGGSWDTAERTNKESKCRVFGRFNSRSLVRSPPRNHDENSDLISYNANRDSSPTESRKGGRLHSLVLNRERRGRFSNFEGPVSSSSGGNMTAPNSRPSNMLKQRGNHVPVDQGITSASEEDIVADIMGQHDQFVSSMHSRLAKLQVVRRYWERNDIKNSISSIEKMADNAVIADVLLIVNERPEILTLDTCTSLLPLLTALLGSNMDSHLSVCLDLLLKLVRMYGSQIYSSLSAPSSVGVDIEAEQRMERYSCCFVEFEKIKACLPSLARRGNLVAKTLHELNLTFQEVSS | null | null | microtubule depolymerization [GO:0007019]; microtubule severing [GO:0051013]; regulation of unidimensional cell growth [GO:0051510] | 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). {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KBF5 | KITHB_ARATH | MFGVSMRTLISPSLAPFSLHLHKPSLFSTALRFSFSINNITPTNSPPSTISTRKLQTKATRVTSSSSSQPLSSSSPGEIHVVVGPMFSGKTTTLLRRILAERETGKRIAIIKSNKDTRYCTESIVTHDGEKYPCWSLPDLSSFKERFGFDDYENRLDVIGIDEAQFFGDLYEFCREAADKEGKTVIVAGLDGDFMRRRFGSVLDLIPIADTVTKLTSRCEVCGKRALFTMRKTEEKETELIGGAEVYMPVCRSHYVCGQNVLETARAVLDSSNNHSVVASSL | 2.7.1.21 | null | DNA biosynthetic process [GO:0071897]; phosphorylation [GO:0016310]; response to cold [GO:0009409]; seedling development [GO:0090351]; thymidine metabolic process [GO:0046104] | chloroplast [GO:0009507] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; thymidine kinase activity [GO:0004797] | PF00265; | 3.30.60.20;3.40.50.300; | Thymidine kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04183}. | CATALYTIC ACTIVITY: Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; Evidence={ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:23351158}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for deoxyuridine {ECO:0000269|PubMed:22897443}; KM=1.4 uM for deoxythymidine {ECO:0000269|PubMed:22897443}; KM=0.38 uM for AZT {ECO:0000269|PubMed:22897443}; KM=0.9 uM for thymidine (in the absence of ATP) {ECO:0000269|PubMed:23351158}; KM=0.9 uM for thymidine (in the presence of ATP) {ECO:0000269|PubMed:23351158}; Vmax=0.7 umol/min/mg enzyme with thymidine as substrate (in the absence of ATP) {ECO:0000269|PubMed:23351158}; Vmax=0.8 umol/min/mg enzyme with thymidine as substrate (in the presence of ATP) {ECO:0000269|PubMed:23351158}; Note=kcat is 0.045 sec(-1) with deoxyuridine (dU) as substrate. kcat is 0.02 sec(-1) with deoxythymidine (dT) as substrate. kcat is 0.009 sec(-1) with 3'-azido-3'-deoxythymidine (AZT) as substrate. {ECO:0000269|PubMed:22897443}; | PATHWAY: Purine metabolism. {ECO:0000269|PubMed:22897443}.; PATHWAY: Pyrimidine metabolism. {ECO:0000269|PubMed:22897443, ECO:0000269|PubMed:23351158}. | null | null | FUNCTION: Part of the salvage pathway for purine and pyrimidine deoxyribonucleotide synthesis. Phosphorylates preferentially purines over pyrimidines. {ECO:0000269|PubMed:22897443}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KBP5 | CHR4_ARATH | MKDSGSEMIKRDWVMKQKRRKLPSILDILDQKVDSSMAFDSPEYTSSSKPSKQRLKTDSTPERNSSKRKGNDGNYFECVICDLGGDLLCCDSCPRTYHTACLNPPLKRIPNGKWICPKCSPNSEALKPVNRLDAIAKRARTKTKKRNSKAGPKCERASQIYCSSIISGEQSSEKGKSISAEESKSTGKEVYSSPMDGCSTAELGHASADDRPDSSSHGEDDLGKPVIPTADLPSDAGLTLLSCEDLSESKLSDTEKTHEAPVEKLEHASSEIVENKTVAEMETGKGKRKKRKRELNDGESLERCKTDKKRAKKSLSKVGSSSQTTKSPESSKKKKKKNRVTLKSLSKPQSKTETPEKVKKLPKEERRAVRATNKSSSCLEDTNSLPVGNLQVHRVLGCRIQGLTKTSLCSALSDDLCSDNLQATDQRDSLVQDTNAELVVAEDRIDSSSETGKSSRDSRLRDKDMDDSALGTEGMVEVKEEMLSEDISNATLSRHVDDEDMKVSETHVSVERELLEEAHQETGEKSTVADEEIEEPVAAKTSDLIGETVSYEFLVKWVDKSNIHNTWISEAELKGLAKRKLENYKAKYGTAVINICEDKWKQPQRIVALRVSKEGNQEAYVKWTGLAYDECTWESLEEPILKHSSHLIDLFHQYEQKTLERNSKGNPTRERGEVVTLTEQPQELRGGALFAHQLEALNWLRRCWHKSKNVILADEMGLGKTVSASAFLSSLYFEFGVARPCLVLVPLSTMPNWLSEFSLWAPLLNVVEYHGSAKGRAIIRDYEWHAKNSTGTTKKPTSYKFNVLLTTYEMVLADSSHLRGVPWEVLVVDEGHRLKNSESKLFSLLNTFSFQHRVLLTGTPLQNNIGEMYNLLNFLQPSSFPSLSSFEERFHDLTSAEKVEELKKLVAPHMLRRLKKDAMQNIPPKTERMVPVELTSIQAEYYRAMLTKNYQILRNIGKGVAQQSMLNIVMQLRKVCNHPYLIPGTEPESGSLEFLHDMRIKASAKLTLLHSMLKVLHKEGHRVLIFSQMTKLLDILEDYLNIEFGPKTFERVDGSVAVADRQAAIARFNQDKNRFVFLLSTRACGLGINLATADTVIIYDSDFNPHADIQAMNRAHRIGQSKRLLVYRLVVRASVEERILQLAKKKLMLDQLFVNKSGSQKEFEDILRWGTEELFNDSAGENKKDTAESNGNLDVIMDLESKSRKKGGGLGDVYQDKCTEGNGKIVWDDIAIMKLLDRSNLQSASTDAADTELDNDMLGSVKPVEWNEETAEEQVGAESPALVTDDTGEPSSERKDDDVVNFTEENEWDRLLRMRWEKYQSEEEAALGRGKRLRKAVSYREAYAPHTSGPVNESGGEDEKEPEPELKKEYTPAGRALKEKFTKLRERQKNLIARRNSVEESLPSGNVDQVTEVANQDEESPTSMDLDDSKASQQCDAQKRKASSSDPKPDLLSQHHHGAECLPSLPPNNLPVLGLCAPNFTQSESSRRNYSRPGSRQNRPITGPHFPFNLPQTSNLVEREANDQEPPMGKLKPQNIKEEPFQQPLSNMDGWLPHRQFPPSGDFERPRSSGAAFADFQEKFPLLNLPFDDKLLPRFPFQPRTMGTSHQDIMANLSMRKRFEGTGHSMQDLFGGTPMPFLPNMKIPPMDPPVFNQQEKDLPPLGLDQFPSALSSIPENHRKVLENIMLRTGSGIGHVQKKKTRVDAWSEDELDSLWIGIRRHGYGNWETILRDPRLKFSKFKTPEYLAARWEEEQRKFLDSLSSLPSKSSRTDKSTKSSLFPGLPQGIMNRALHGKYATPPRFQSHLTDIKLGFGDLASPLPLFEPSDHLGFRSEHFPPMANLCTDNLPGEPSAGPSERAGTSTNIPNEKPFPLNSLGMGNLGSLGLDSLSSLNTLRAEEKRDAIKRGKLPLFLDMPLPQMLDSSNNVFLGRSANPSFLHPNRGLNPSNPMGRDIMGISSSENKLPHWLRNVVTVPTVKSPEPPTLPPTVSAIAQSVRVLYGEDSTTIPPFVIPEPPPPAPRDPRHSLRKKRKRKLHSSSQKTTDIGSSSHNAVESSSQGNPQTSATPPLPPPSLAGETSGSSQPKLPPHNLNSTEPLSSEAIIIPPPEEDSVIAAAPSEAPGPSLEGITGTTKSISLESQSSEPETINQDGDLDPETDEKVESERTPLHSDEKQEEQESENALNKQCEPIEAESQNTNAEEEAEAQEEDEESMKMVTGNSLSDD | 3.6.4.- | null | null | chromatin [GO:0000785]; endosperm protein body [GO:0042735]; nucleus [GO:0005634]; plasmodesma [GO:0009506] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; metal ion binding [GO:0046872] | PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | null | null | null | null | null | FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 (By similarity). Probable chromatin remodeling factor. {ECO:0000250|UniProtKB:Q8TDI0, ECO:0000303|PubMed:16547115}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KCC2 | PRT6_ARATH | METNSSLFGLVSPSSHDLVIERLASVGVPKKYRSKRGLVEFVRANPAKISELVSALLPTDDDVKLGLKEARERPRKSAVSPTMKKRFRESMNMLQWLMFQDEPDVSLRNLAKLNLDQRGVCGSVWGQNDIAYRCRTCENDPTCAICVPCFQNGDHNSHDYSIIYTGGGCCDCGDETAWKPDGFCSNHKGSEQIRPLSENLANSVGPILDALFTCWNNKLLSAESSGQKGARSNDTLVILQKMSNELTFIVVEMLLEFSMSSESLLSFVSRRIISSSGLLSILLKAERFLDQDVMKKLHDLFLKLIGDPVFKCEFAKAFVSYYPVVISEVVKQGTDNAFKKYPLLSTFSVQILTVPTLTPFLVKEMNLLAMLLGCLSDIFVSCSGEDGLLQATKLERLCETSERVIGDLKFVMSHAIVSKYATHEHRELSRSWLTLLTFAQGMNPLKRETGIPIDEENDYMHLFFVLGHSIAVIHSLLVNGTYSAASDEEIENDRNAKEEFDKCDGDGERYAKVGRLSHEDSVCTAIVSSSSFDSSMASEVHKIDPFHALLPSSAIYLIRECLKVLETCLGNDEGISKFLCKLSSSSGRNIPESKMSWPRRDLLNVETGGSVSSNLASSSRDPSTGLSPLCGDIQTNLSLDNVCGPYGVVQTDVTADSKRVSCNSADLTKNASGLRILGLCDWPDIHYDVSSQAISVHLPLHRLLSLLIQKALRICYGESASYNGVSISHEIPHADFFSSVIGDFHPCGFSALVMEHVLQIRVFCAQVIAGMWKKNGDSALVSCEWYRSVRWSEQGLELDLFLLQCCAALAPADSYVDKLLSRFGLSSYLSLNPDITNEYEPVLVQEMLGLLIQILQERRFCGLSTAESLRREIIFKLATGDFTHSQLVKSLPRDLSKSDELQEVLDDVSVYCNPSGMNQGKYSLQSSCWKELDLYHPRWQSRDLQSAEERFSRYCGVSALTTQLPRWRMIYPPLKGLARIGTCKATFQIISSALYYALQSGTSVKSRAPDGVLITALQLLSLSLDICTQQRQSNSQDCCLENSIPILELAGLEIIGIAQGTEKESLLSLLVSLMKTRMGDGRHQFPEPGSCNISSWIGNLLKKFSAIDSVCMNLLQSLAPEVVGQSGFDKVMSGSTSDEKRKAKAKERQAAIMAKMKAEQSKFLSTLSSSMDDDDPRSEFETSDSVMEHDSEIAVREVCSLCHDPDSKDPVSFLIFLQKSKLLSFVDRGPPSWDQCPQSEKKISVDGAPDLLRMNASSDSLRISSPLMLQLSDDTISESANMIESIKARLIGNGQTEKRSSDGRGKDESNMESLEIAMYQTVRNKIENMINQSLTRVDHQPHEAENCSEKNSVGGPSTLQGRFPDIRSRQTSRRPDAGSDGFHPIDCDGVYLSSCGHAVHQSCLERYLKSLKERSGRRTVFEGAHIVDLKKKEFLCPVCRRLANSVLPECPGDLCSVSKLQDSPRTKLRRKDALQPSLWLSEALCLLRSAAEVIEDGDRGKTVTPQGDGPRRKDLKSVSKMLWDFYFPKPEDKTLKRLWLPPQSIVMWDTLKYSLISMEIGTRFAKNSMLPVYCIDSLYEELKTSKGTILSVLLRVVQSSRTKNTIHVRQRFVGMKHLAESICYGVSSSSSSSIFGSEGTTGSLKNIDLLWNRASDPVLAHDPFSSLMWALFCLPFPFLTCEESLLSLVHIFHSVSLVQTVIAYCACRPSELSELNFGENLLNDISNALRESGGWEYFRSNNMDLSCDIKDTIRKYSLPFLRRCALLWKLLKSTPRKLHEESDMFDLPSDPTTDNMDFIYSPQSELNHVQELEKMFNIPPIDIILNDELLRSSTQIWLQHFQREYRVNRVKRSLCITPVVPFQLMKLPNLYQDLLQRCIKKRCVNCTKVIEEPVLCLLCGSLCSPIWSPCCRESGCPNHAITCGAGTGVFLLIRRTTILLQRFARQSPWPSPYLDTFGEEDIDMIRGKRLYLNEERYAALTYLVGSHGLDRSSKVLGQTTIGAVLH | 2.3.2.27 | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; protein ubiquitination [GO:0016567]; regulation of lipid catabolic process [GO:0050994]; regulation of seed germination [GO:0010029]; response to abscisic acid [GO:0009737]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596] | cytoplasm [GO:0005737]; ubiquitin ligase complex [GO:0000151] | ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF18995;PF02207; | 2.10.110.30;1.10.10.2670;3.30.40.10; | UBR1 family | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Ubiquitin protein ligase which is a component of the N-end rule pathway with arginine specificity, and functions with the arginyltransferases ATE1 and ATE2. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed:17572409, PubMed:19255443, PubMed:19620738, PubMed:22020282). Does not participate in degradation of proteins with N-terminal Phe or Leu (PubMed:17572409). The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination (PubMed:19255443). The N-end rule pathway regulates various aspects of leaf and shoot development (PubMed:19620738). Involved in the ubiquitination and subsequent degradation of RAP2-12, an activator of hypoxic gene expression. The ubiquitination occurs after the N-arginylation of RAP2-12 by ATE1 or ATE2 under aerobic conditions (PubMed:22020282). The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato (PubMed:27173012, PubMed:30117535). Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity (PubMed:27173012). Controls the expression of specific defense-response genes, activates the synthesis pathway for the phytoalexin camalexin, and influences basal resistance to the hemibiotroph pathogen Pseudomonas syringae pv tomato (PubMed:30117535). Coordinates the mobilization of seed storage reserves and regulates the abundance and activities of several proteases following seed germination (PubMed:29168982). {ECO:0000269|PubMed:17572409, ECO:0000269|PubMed:19255443, ECO:0000269|PubMed:19620738, ECO:0000269|PubMed:22020282, ECO:0000269|PubMed:27173012, ECO:0000269|PubMed:29168982, ECO:0000269|PubMed:30117535}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KCE9 | KNL2_ARATH | MTEPNLDEDGSKSSFQKTVVLRDWWLIKCPKEFEGKQFGVAGFEESVETRAMRVFTSSPITKALDVFTLLASDGIYITLRGFLNKERVLKNGFNPEISREFIFGFPPCWERVCNSCFEGDSFGTDVNTVPSTIEKACPPILSPCKYSNRNLKDNPAESREKSNVTETDIAEINDKGGSGARDIKTARRRSLHLQIKRILESSKVRKTANDGDHGSEFLNTAKRGDVERDGCEVINNEDSEWKLDESEVQNLCNDGDNGSEGFIKAKSSDVEKDKSEAIDNDVISPAVGSGIKHTGADNVDKVTSASATGESLTSEQQNGLLVTTASPHSLLKDLAKSSKPEKKGISKKSGKILRSDDNVVDPMNYSGTKVKSAENKRKIDASKLQSPTSNVAEHSKEGLNNAKSNDVEKDVCVAINNEVISPVKGFGKRLSGTDVERLTSKNATKESLTSVQRKGRVKVSKAFQDPLSKGKSKKSEKTLQSNSNVVEPMNHFRSEAEEAEENLSWEKIKRKIDFDVEVTPEKKVKQQKTNAASTDSLGQKRSRSGRVLVSSLEFWRNQIPVYDMDRNLIQVKDGSETNSAPSKGKGSDSRKRRNLKIK | null | null | cell division [GO:0051301]; meiotic cell cycle [GO:0051321] | chromocenter [GO:0010369]; chromosome, centromeric region [GO:0000775]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; RNA binding [GO:0003723] | PF09133; | null | KNL2 family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:24014547}. Nucleus, nuclear body {ECO:0000269|PubMed:24014547}. Nucleus, nucleolus {ECO:0000269|PubMed:24014547}. Chromosome, centromere {ECO:0000269|PubMed:24014547, ECO:0000269|PubMed:28062749}. Note=Localizes at centromeres during all stages of the mitotic cell cycle, except from metaphase to mid-anaphase (PubMed:24014547). Colocalizes with CENH3 at centromeres in interphase nuclei (PubMed:24014547, PubMed:28062749). {ECO:0000269|PubMed:24014547, ECO:0000269|PubMed:28062749}. | null | null | null | null | null | FUNCTION: Involved in recognition of centromeres and centromeric localization of the centromere-specific histone CENH3. Required for normal progression of mitosis and meiosis. May play a role in the determination of the epigenetic status of centromeres (PubMed:24014547). Binds DNA and RNA in vitro (PubMed:28062749). {ECO:0000269|PubMed:24014547, ECO:0000269|PubMed:28062749}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KCH3 | SOP15_ARATH | MSKEKSYVIALLLSLLLCLSFQVGVSEANYNAVTTRYSDSPRCANGSSASPPTRHCPRGRPRPPTPRVAVHSNSTKGKGP | null | null | response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651] | apoplast [GO:0048046]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612] | null | null | Serine rich endogenous peptide (SCOOP) phytocytokine family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Endoplasmic reticulum {ECO:0000269|PubMed:31001913}. Golgi apparatus {ECO:0000269|PubMed:31001913}. Note=Observed in a reticular pattern and a perinuclear ring (PubMed:31001913). The precursor of SCOOP15, PROSCOOP15, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP15 in the apoplasm (PubMed:31001913). {ECO:0000269|PubMed:31001913}. | null | null | null | null | null | FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (PubMed:34535661). Inhibits root growth (PubMed:34535661). {ECO:0000269|PubMed:34535661}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KDA5 | MIP_ARATH | MWKLTRRLQPHINSTRWLVRNFRNGGAGDATGLYGFDHLKTAKGFQRFVADAIERSGELVSYISGMPSSPEIIKAMDEISDTVCCVVDSAELCRQTHPDREFVEEANKAAIEMNDYLHHLNTNHTLYAAVKKAEQDSNLLTKEASRTAHHLRMDFERGGIHLDPEKLDKVNNLTTNIFQLCREFSENIADDPGHVDIFPGSRIPRHLHHLLNPTYRSTSGGSRGSTRSAHKSKQKGFRINTDPRTVSSILQWTSDEEVRKMVYIQGNSVPHANHGVLEKLIAARHELSQMMGCNSYADIMVEPNLAKSPKVVTSFLQELSKTVKPKADEEFIAIRDFKREKCGNPSAELEPWDETYYTSMMKSSINDVDTAVVASYFPLPQCIEGLKVLVESLFGATFHTIPLAPGESWHPNVVKLSLHHPDEGDLGYLYLDLYSRKGKYPGCASFAIRGGRKISETEYQLPVIALVCNFSRACDSSIVKLNHSEVEVLFHEFGHALHSLLSRTDYQHFSGTRVALDLAEMPSNLFEYYAWDYRLLKRFARHYSTGETIPEKLVNSLQGARNMFAATEMQRQVFYALIDQMLFGEQPETARDVSHLVAELKRQHTSWNHVEGTHWYIRFSHLLNYGAGYYSYLYAKCFASTIWQSICEEDPLSLNTGTLLREKFFKHGGAKDPAELLTDLAGKEIISVHGEGIVPATTYLLNELRL | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion. {ECO:0000305}; | peptide metabolic process [GO:0006518]; protein processing involved in protein targeting to mitochondrion [GO:0006627] | chloroplast thylakoid membrane [GO:0009535]; mitochondrion [GO:0005739] | aminopeptidase activity [GO:0004177]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01432; | 3.40.390.10;1.10.1370.10; | Peptidase M3 family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25732537, ECO:0000269|PubMed:28936218}. | null | null | null | null | null | FUNCTION: Aminopeptidase which cleaves preproteins, imported into the mitochondrion, to their mature size. Could cleave both preproteins and preprotein intermediates already cleaved by the mitochondrial processing peptidase (MPP). {ECO:0000269|PubMed:25732537}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KDF5 | MUPS1_ARATH | MSSSVAEANHTEKEESLRLAIAVSLLRSKFQNHQSSSSTSRCYVSSESDALRWKQKAKERKKEIIRLQEDLKDAESSFHRDLFPANASCKCYFFDNLGVFSGRRIGEASESRFNDVLRRRFLRLARRRSRRKLTRSSQRLQPSEPDYEEEAEHLRISIDFLLELSEADSNDSNFSNWSHQAVDFIFASLKKLISMGRNLESVEESISFMITQLITRMCTPVKGNEVKQLETSVGFYVQHLIRKLGSEPFIGQRAIFAISQRISILAENLLFMDPFDESFPEMDECMFILIQLIEFLICDYLLPWANEAFDNVMFEEWIASVVHARKAVKALEERNGLYLLYMDRVTGELAKRVGQITSFREVEPAILDKILAYQEIE | null | null | chiasma assembly [GO:0051026]; chromosome segregation [GO:0007059]; embryo sac development [GO:0009553]; male meiotic nuclear division [GO:0007140]; meiotic DNA double-strand break formation [GO:0042138]; meiotic spindle organization [GO:0000212]; plant-type sporogenesis [GO:0048236]; pollen development [GO:0009555] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle [GO:0005819] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytoskeleton, spindle {ECO:0000305|PubMed:19500302}. | null | null | null | null | null | FUNCTION: Involved in meiotic spindle organization in meiocytes thus regulating chromosome segregation (PubMed:19500302). Required for formation of meiotic DNA double-strand breaks (DSBs) during early recombination processes (PubMed:19763177). {ECO:0000269|PubMed:19500302, ECO:0000269|PubMed:19763177}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KDH9 | FIPS5_ARATH | MEEDDEFGDLYSDVLQPFQPPVVLPPPPPLPHRSIDLNLRSQDQDVSEPNSAPISRVSDNDAVKLSTQDATRQAIVDGGGDDKDMSFDIEEPDADSTPTIPGLFVTGALPGLATDRGVSQVTTRIEQQVGGGGDGGYGGQGEGDDWDSDSEDDLQIVLNDSSRNVMIGGADRRSRMGDNEDDDDEDDEDPLVIVADTDPNQPMEEQMWGEDGLQGIEGDGKDGGEAGKGSGPGGATGPPKAGYSSHGYHPFHSQFKYVRPGAAPIPGGAASVGGPSSGQVRPPANLGPMAGRGRGDWRPLGMRNASAAQKGFHQPWGSNTAGRGLDFTLPSHKTIFEVDIDSFEEKPWRYPGVEMTDYFNFGLNEESWKDYCKQLDQHRIQTTMQSRIRVYESGRTDQGYDPDLPPELAAATGAQGVPVDSSNLVKPDSVQGDSAKVPANVRPTLPPGRPIPVETGSGERLPSIDTRAPRMRDLDAIIEIVCQDSHEDEPSGENGTDQADSSLPGENVPVETSYVNNKRPDTESAEHSPAQDEPHKNLLKKQDDEISRSTDSGQSFRSSSPVGDRGTRSSSVDREDVGGEAGKDAEMGEELKMSFTSPQSAVQEDDGGESKTERSSESSKARSGSHRDFQQEEDVIQDKHSSRPANNRKQYDNNAPHQSRKNQDRGKEMERTRAASKGGRENSNPHMELDSTYIYSIASREDFDKRKERDVDGAVWRRKEDDPYSRRGGDEGSRKRDREDDPGFRQRGKMRENEIRSKDDQVPSRKHMDDAGMRNIYEPDDHINKRRKDEEYLRRSRPEKNEISYGQRESMSRVKRERDDRLEHQKRDVQHKIRDDFDDHGSLRQRDDIYMQRDGNERLRERDVLDKLKLPHEDGISARGRERQVAVRGHRGSEDRSSRMKDEYKASDKEHVTKDTLRHAKQTKRRDYPGEESSSHHRGHEDFSARTDNIVNNEKKPRQERTGAKIDKFIDTLDGQRLQDRKHKDSRRKIKEQREGTESLSKQGEQNGSSVVTGSKGTNDARNCRSEIPHQPNTAKRHKENASSGDEIHDSKRGRTKLERWASHKEREDAVSAKSSSISSKLEEKENNTNGRLSEPVHGSIGKSRDVTEEKIGHDLADTKDGSEKGPGDRHLDTVEKLKKRSERFKLPMPTEKDTTGVKKMESETLPSAKIEGPVDSEGEYVWDERSCVRIGREYA | null | null | mRNA processing [GO:0006397] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF05182; | null | FIP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UN15, ECO:0000255|PROSITE-ProRule:PRU00768}. | null | null | null | null | null | FUNCTION: Essential gene (PubMed:16282318). Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex (By similarity). {ECO:0000250|UniProtKB:Q6UN15, ECO:0000269|PubMed:16282318}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KDN0 | HEN4_ARATH | MERNSVKFHAEKRSGAFDPGSGFGSSKRVKTHHTQLLSALVVPVGHAAFRLLCPLSHVGAVIGKSGNVIKQLQQSTGAKIRVEEPPSGSPDRVITIIAQADSKSRVKLGANNNGNAEGEKKEEEVEVSKAQGALIKVFELLAAEADSDTVVCRLLTESSHAGAVIGKGGQMVGSIRKETGCKISIRIENLPICADTDDEMVEVEGNAIAVKKALVSISRCLQNCQSIDKVRMVGNRPLEKEFQASLHRPIETIIQESLPRSVEVNPYDYRLRNDEIFPRGTVARANDVIPHDTLHLRRIEAVPQGALRMHIEADRQDVLRRHVEADRQDALRRRIDVVPQETLYMPSDVLRGDCFRQHRERDDSHDSLHRPFEMVPRDAMGMPFESFPRDAYGRPIETMTQETLRGQSADYLAHRYSTLDTHPHSFTTSASMANTATMKPPPSEVEVGNQDVVFKILCSTENAGGVIGTGGKVVRMLHSETGAFINVGNTLDDCEERLIAVTASENPECQSSPAQKAIMLIFSRLFELATNKILDNGPRSSITARLVVPTSQIGCVLGKGGVIVSEMRKTTGAAIQILKVEQNPKCISENDQVVQITGEFPNVREAIFHITSRLRDSVFSNSMKNSLAKSSSALTTERFYDRQSDNPLSIGSHQSVSNPATNSSSLHRRSEDSFLSGSHSSVNYSRSVGTDPYIRPEDPFPDRFNPSAGYSHNFGRRFTMDHSDNSHHLTEAPSRLWASPPPAAPRGLSDASGGLSSARAGHVLGSGHKSAIVTNTTVEIRVPANAMSFVYGEQGYNLEQLRQISGARVIIHEPPLGTSDRIIVISGTPDQTQAAQNLLHAFILTGETSLSKKYNLN | null | null | cell differentiation [GO:0030154]; maintenance of floral organ identity [GO:0048497]; mRNA processing [GO:0006397]; positive regulation of flower development [GO:0009911]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | mRNA binding [GO:0003729] | PF00013; | 3.30.310.210;3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15310842}. | null | null | null | null | null | FUNCTION: Functions in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. Functions in association with HUA1 and HUA2. {ECO:0000269|PubMed:15310842}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KE59 | PAIP2_ARATH | MADRRVGKRQMGQRGFSKVESGTCNVCSAPCSSCMHRNVGFTGSKLDESSDENCHGVVGSQCSVNEDDLLPSSMVNAHKSLNNTASEASNLVNSSHDALSENAESKETIRCSGISDDSGAAAMTSKPSLSGSRMKHKVSASANMLDQSSNCIEDQEDGILSADRAKQLKSGCSNNEIGNKDLADGSALNSDPIPGGSRKDEVKLESLQNPSSNHDDRVSSEKGNFKEKSRPGGNKERQEPSVEGSTRSGENRKDGKSSKSSSSNSSAVSESESDDSEMVEHDVKVCDICGDAGREDLLAICSGCSDGAEHTYCMREMLDEVPEGDWLCEECAEEAEKQKQEAKRKRETEVTFNTYSSGKRHADKIEAAPDAKRQVVEASTGSPKKSILPRVGALSRETSFKGLDRLRGKLNHQTSFSDDTESARSAGSQLQPPKGAFLKSSSFNCSSSKPKVQLMDDAIHPRQKTGKEDTALDLKVGGFRNVGKSMPSRTTDAGNSGGSDSQAKMLGSKVYHSQEGKSLKQVKDRNREANASASSIDQKLKSRGNSSVSHANNNRDLKGLQSDGKRGNLTKQVSNLSRNRLENSVVSGGDISTNEKCSASEQSSSQADCKDELPSTSCTGEGMPNHGTVALQDGLPRSRVPREVGKKSKEAFSKRQRSSLLAGAKGLPSSQKGGQTAESSDTSGVSDSDLSTTKNVKEDLNKGNRLRAAVDAALRKKPSFGKNRVLEQSDASLVANVDSSSEKTLRNQLPSKMHKNHVSHEGLQGGHPILWPTSDPYKQTIVTNEKQLIFPGADTIPSRLVEPEVSFPAVKPVMRDLPLVPSPVMLRSSAIPDHEFIWQGDLEVRKIINQSAMHSGIQAHLSTLASPRVAEVVNKFPETFSLNEVPRKSTWPTQFEKLGTKEAHIALFFFAKDTESYERNYKPLVDNMIKNDLALKGNLDNVDLLIFASNQLPSNCQRWNMLYFLWGVFQGRKETNPQKNTSLPTSNVLPRDRDPKELCQTSSPSKHLEKGSSLRESSSNGIETRNGTDARSHENPNNRESSIERSPSKKEDIALKVEEAGVNHIPPQVTGSNSGDSLVRKVQKVEEQELGGRKDLPLTVMGSGIQSHGQDNPLEKDLNSSQASHRKRPLWELSNPANENSSAINQKVELNNDGLCEGSPNKKLKTENGSSSLCRDTSGHDSGIMKKSPKVVFPLDLNDDSEMVDNLSPLGNDENNNNRRLISGTVPNLELALGAEETTEATMGLLPFLSRSSNSGEQSNNSMNKEKQKADEEEEDDAEVAASLSLSLSFPGTEERKNVNTPLFLFRDLPR | null | null | negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; regulation of photoperiodism, flowering [GO:2000028] | null | histone binding [GO:0042393]; histone reader activity [GO:0140566]; metal ion binding [GO:0046872] | PF00628; | 3.30.40.10; | null | null | null | null | null | null | null | null | FUNCTION: Together with AIPP2 and AIPP3/BDT1, cooperates to form a BAH-PHD bivalent histone reader complex able to read histone H3 lysine 27 trimethylation (H3K27me3) and low-methylated H3K4 histone marks in order to regulate transcription, especially to prevent early flowering; promotes AIPP3/BDT1 binding to H3K27me3 (PubMed:33277495, PubMed:33433058). CPL2 is subsequently recruited to form a BAH-PHD-CPL2 complex (BPC) in order to silence several H3K27me3 and low-methylated H3K4 enriched loci, including AGO5, via the phosphorylation state-dependent inhibition of Pol II release from the transcriptional start site (e.g. Ser5P-Pol II dephosphorylation) (PubMed:33277495). The BPC complex represses flowering by inhibiting the expression of several genes, including AGL6, FT, FUL and SOC1 (PubMed:33277495). {ECO:0000269|PubMed:33277495, ECO:0000269|PubMed:33433058}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KEV7 | FHIT_ARATH | MLNLQVTGKTILSSIRCQRKMSSTCSSYAFGPYKIDPREVFYATPLSYAMVNLRPLLPAHVLVCPRRLVPRFTDLTADETSDLWLTAQKVGSKLETFHNASSLTLAIQDGPQAGQTVPHVHIHILPRKGGDFEKNDEIYDALDEKEKELKQKLDLDKDRVDRSIQEMADEASQYRSLFDC | 2.7.7.51; 3.6.1.29; 3.6.2.1; 3.9.1.- | null | null | null | adenosine 5'-monophosphoramidase activity [GO:0043530]; adenylylsulfatase activity [GO:0047627]; adenylylsulfate-ammonia adenylyltransferase activity [GO:0047352]; bis(5'-adenosyl)-triphosphatase activity [GO:0047710]; nucleotide binding [GO:0000166] | PF01230; | 3.30.428.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.29; Evidence={ECO:0000269|PubMed:18694747}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + H2O = AMP + 2 H(+) + sulfate; Xref=Rhea:RHEA:17041, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215; EC=3.6.2.1; Evidence={ECO:0000269|PubMed:18694747}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + NH4(+) = adenosine 5'-phosphoramidate + 2 H(+) + sulfate; Xref=Rhea:RHEA:19197, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:28938, ChEBI:CHEBI:57890, ChEBI:CHEBI:58243; EC=2.7.7.51; Evidence={ECO:0000269|PubMed:26181368}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+); Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57890, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18694747}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for adenosine 5'-phosphoramidate (at pH 6.8) {ECO:0000269|PubMed:18694747}; | null | null | null | FUNCTION: Possesses dinucleoside triphosphate hydrolase activity (PubMed:18694747). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:18694747). Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747). Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747). Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (PubMed:26181368). {ECO:0000269|PubMed:18694747, ECO:0000269|PubMed:26181368}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KF14 | FTSI4_ARATH | MTFYISSSLTPTHFSKPLNPSNTLFPSQFRGSLSSFVRRRKPTEAKLSSKFNLFPSRRNGLITCCSTSSFESTESSVSQEEDAESNRLFEKLRETERERLSNMEELERKANVQLERQLVMASDWSRTLLTMRGKLKGTEWDPETSHRINFSDFMKLLDSNSVQYMEYSNYGQTISVILPYYKDGEPLGEEEDSKKEIIFRRHIVDRMPIDGWNDVWKKLHQQIVNVEVFNVDVVPAEVYTTVATFVVWSMRLALFVSLYVWIDSITRPIYAKLIPCDLGTPTKKIRQPLKRQALGSLGKSRAKFISAEEKTGVTFDDFAGQEYIKRELQEIVRILKNDEEFQNKGIYCPKGVLLHGPPGTGKTLLAKAIAGEAGLPFFAANGTDFVEMFVGVAASRVKDLFASSRSYAPSIIFIDEIDAIGSKRGGPDIGGGGAEREQGLLQILTEMDGFKVTTSQVLVIGATNRLDILDPALLRKGRFDKIIRVGLPSKDGRLAILKVHARNKFFRSEDEKEELLQEVAENTEDFTGAELQNVLNEAGILTARKDLDYIGREELLEALKRQKGTFETGQEDSTEVPEELKLRLAYREAAVAVLACYLPDQYRPISETDINSIRSQPNMRYSETSGRVFARKSDYVNSIIRACAPRVVEEEMFGIENLCWISAKSTLEASQRAEFLILQTGMTAFGKAYYRNQRDLVPNLVPKLEALRDEYMRFAVEKCSSILQEYQSALEEITDVLLEKGEIKADEIWNIYNTAPRIPQKPVRPVDEYGALIYAGRWGIHGVSLPGRVTFSPGNIGFATFGAPRPMETQIISDDTWKLVDEIWDKKVEEIKAEAVIQIEEEKKKPQILMATHFF | null | null | embryo development ending in seed dormancy [GO:0009793]; protein import into chloroplast stroma [GO:0045037]; proteolysis [GO:0006508] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; chloroplast thylakoid membrane [GO:0009535]; plastid [GO:0009536]; Ycf2/FtsHi complex [GO:0062091] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; chloroplast protein-transporting ATPase activity [GO:0016464]; metalloendopeptidase activity [GO:0004222] | PF00004;PF17862; | 1.10.8.60;3.40.50.300;1.20.58.760; | AAA ATPase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24964212}; Single-pass membrane protein {ECO:0000269|PubMed:24964212}. | null | null | null | null | null | FUNCTION: Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis (PubMed:24964212). Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (PubMed:12185496). {ECO:0000269|PubMed:24964212, ECO:0000303|PubMed:12185496}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KFS7 | MEB2_ARATH | MEKSNQPVHVTLSELKDGDKEIVDAEFLVDLLESYRFGKDNVPAREFRSKAAATAPAPVNTTEIELEEDNDGSQAQGNNSVSESTSSLFSDSDPIVLESTVSETGSNEESETGSNEENGNNWLESSSTNLPNVENKRQRNGEDCEIEEEEENNERSLSDSEEKSNLEKLLGTQENYELGNEDEEKNERSSSDSEEKSNLENLLATQENYELYCPSCSTCITRNVVLKKRKRGKHVNSSLDLKPDIPVVEPDEPSDIEEMESPVKVYVPETRIEDDQEDKEGTIFTCLVCDLKYFIRLGTKFLQLDYIRGKPVEKSVEEYIDVRKSINTTQSPPQIQPDGERFAIELLKSTVYGGLTETITSLGVVSSASASGSSTMNILALAVANLAGGLIVLAQNFQDLRNSSDQEKDRYEELLGRRTKSRIHILVAVMSYIFFGLIPPLVYAFSFYETGIKNYKLISVFLGSLVCVILLGSIKVYVRKPTNSCGSTKAYLKSAAYYTSIVVASCGISYVVGDIMGEYIEKLSLVGLDQISITSPCYGIKPEECRFTSF | null | null | null | endoplasmic reticulum membrane [GO:0005789]; ER body [GO:0010168] | iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384] | null | null | CCC1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23166355}; Multi-pass membrane protein {ECO:0000269|PubMed:23166355}. Note=Located in ER bodies. | null | null | null | null | null | FUNCTION: May sequester excess cytosolic iron and manganese into endoplasmic reticulum to reduce metal ion toxicity. Not essential for the accumulation of ER body components, including PYK10. {ECO:0000269|PubMed:23166355}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KFT7 | TENAC_ARATH | MRFLFPTRLINNSSLGLLRSPHTTAPIRSLWFRTKSPVFRSATTPIMTAVAFSSSLSIPPTSEEALPGKLWIKFNRECLFSIYSPFAVCLAAGNLKIDTFRQYIAQDVHFLKAFAHAYELAADCADDDDDKLAISDLRKSVMEELKMHDSFVQDWDLDINKEVSVNSATLRYTEFLLATASGKVEGCKAPGMLDTPFEKTKVAAYTLGAVTPCMRLYAFLGKEFGSLLDLSDVNHPYKKWIDNYSSDAFQASAKQTEDLLEKLSVSMTGEELDIIEKLYQQAMKLEVEFFHAQPLAQPTIVPLLKNHSKDDLVIFSDFDLTCTVVDSSAILAEIAIVTAPKDEQSRSGQQIHRMLSSDLKNTWNLLSKQYTEHYEECIESILNKKKADKFDYEGLCKALEQLSDFEKEANNRVIESGVLKGLNLEDIKRAGERLILQDGCINVFQKILKTENLNAELHVLSYCWCGDLIRAAFSAGGVDAVEVHANEFTFEESISTGEIERKVESPINKAQQFKSILQNRKNENNKKSFLSVYIGDSVGDLLCLLEADIGIVVSSSSSLRRVGSHFGVSFVPLFSGIVQKQKQHTEESSSSAWKGLSGTLYTVSSWAEIHSFALGWE | 3.1.3.100; 3.5.99.2 | null | thiamine biosynthetic process [GO:0009228] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | thiaminase activity [GO:0050334]; thiamine phosphate phosphatase activity [GO:0042131] | PF03070; | 3.40.50.1000;1.20.910.10; | TenA family; HAD-like hydrolase superfamily | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:27677881}. Cytoplasm {ECO:0000269|PubMed:27677881}. Note=Localized to the mitochondrion when the first start codon is preceded by a strong Kozak sequence. {ECO:0000269|PubMed:27677881}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:27677881}. | CATALYTIC ACTIVITY: Reaction=H2O + thiamine phosphate = phosphate + thiamine; Xref=Rhea:RHEA:47948, ChEBI:CHEBI:15377, ChEBI:CHEBI:18385, ChEBI:CHEBI:37575, ChEBI:CHEBI:43474; EC=3.1.3.100; Evidence={ECO:0000269|PubMed:27677881}; CATALYTIC ACTIVITY: Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+); Xref=Rhea:RHEA:31799, ChEBI:CHEBI:15377, ChEBI:CHEBI:16892, ChEBI:CHEBI:28938, ChEBI:CHEBI:63416; EC=3.5.99.2; Evidence={ECO:0000269|PubMed:27677881}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.86 uM for thiamine monophosphate {ECO:0000269|PubMed:27677881}; Note=kcat is 13.5 sec(-1) for thiamine monophosphate. {ECO:0000269|PubMed:27677881}; | null | null | null | FUNCTION: May be involved in the salvage of thiamine breakdown products (PubMed:25014715). This protein has a haloacid dehalogenase family domain fused to its TenA domain (PubMed:25014715). Phosphatase with the highest activity against thiamine monophosphate (ThMP) and, with a lower activity, against thiamine diphosphate (ThDP), flavin mononucleotide, inorganic pyrophosphate, CTP and dATP (PubMed:27677881). Has a thiamine salvage hydrolase activity, but only against 4-amino-5-aminomethyl-2-methylpyrimidine (amino-HMP) and not against N-formylamino-HMP, desthiothiamine, thiamine, ThMP, and ThDP (PubMed:27677881). {ECO:0000269|PubMed:27677881, ECO:0000305|PubMed:25014715}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KGN5 | S40A2_ARATH | MEEETETRVFLSNEQHQEEEEEEEEEPSLPRSMVISLYLGYFLARWGARTWEFSVALYMIYLWPNSLFLTAMYGVVESGSATLFGPIVGQMIDGMSYVKVLRLWLVTQNLSFIVAGGAVVALLVVPDLKSQNFPVFATLVVLTNLSGAIGVLSTLAGTVLIERDWVVVMSEGHSPAVLTRMNSVIRGIDLSSKLLSPVITGLIISFVSLRASAITFAAWATITVWIEYWLFISVYNGVPAIVQSDERRSLRSSQSQAEETDSASSFYVPLLHEEESYRNTQSRSRILRILERISESSFVSAWRNYLNQEIVLPGVSLALLFFTVLSFGTLMTATLEWKGIPTYIIGIGRGISAGVGLAATVLYPLMQSRISPLRTGVWSFWSQWTCLLVCVGSIWVEKEKIASYMLMAGVAASRLGLWMFDLAVIQQMQDLVPESDRCVVGGVQNSLQSALDLMANLLGIIVSNPKDFWMLTLISFATVSLAGILYTIHLYRIRKHLFHLEKIPLLNNFFAS | null | null | cellular response to iron ion starvation [GO:0010106]; cobalt ion transport [GO:0006824]; iron ion transport [GO:0006826]; nickel cation transmembrane transport [GO:0035444]; nickel cation transport [GO:0015675]; transition metal ion transport [GO:0000041] | plant-type vacuole membrane [GO:0009705] | cobalt ion transmembrane transporter activity [GO:0015087]; iron ion transmembrane transporter activity [GO:0005381] | PF06963; | 1.20.1250.20; | Ferroportin (FP) (TC 2.A.100) family, SLC40A subfamily | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:16790430}; Multi-pass membrane protein {ECO:0000305|PubMed:16790430}. Note=Tonoplast. | null | null | null | null | null | FUNCTION: Vacuolar transporter that is involved in the transport of excess nickel into the vacuole under iron deficiency, increasing cellular tolerance to nickel under iron deficiency stress response. {ECO:0000269|PubMed:16790430}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KGQ0 | ALFC4_ARATH | MSCFKSKFAGKSYFRRTFHSSIIQFHPQLSILIWHRRYSIIRTYELIANAAYIGTPGKGILAADESTGTIGKRFVSINVENVESNRRALRELLFTTPGALQYISGIILFEETLYQKTASGKLFVDVMKEAGVLPGIKVDKGTVELAGTNGETTTTGLDGLGDRCKKYYEAGARFAKWRAVLKIGNNEPSELAIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIEKCAYVTERVLAACYKALSDHHVILEGTLLKPNMVTPGSDSGSKVKPEVIAKHTVRALQRTVPAAVPAVVFLSGGQSEEEATVNLNAINQLKGKKPWSLTFSYGRALQQSTLKAWGGKEENVDKAQKAFLARAKANSEATLGGYKGDAQLGEGASESLHVKDYKY | 4.1.2.13 | null | fructose 1,6-bisphosphate metabolic process [GO:0030388]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; mRNA binding [GO:0003729] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | PTM: S-glutathionylated at Cys-207. {ECO:0000250|UniProtKB:Q9SJQ9}.; PTM: S-nitrosylated at Cys-207. {ECO:0000250|UniProtKB:Q9SJQ9}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22561114}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000250|UniProtKB:Q9SJQ9}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000305}. | null | null | FUNCTION: Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:Q9SJQ9}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KH86 | TAD3_ARATH | MDSDAWEIIHIPEKPSLSPDHQPTVKVYASLIKPRFANTIVRHLCKIAPLEDLRHVKRVKKKILPDCGETQLTVILCLAPEHNDQLSDMPPDVQRLVDPYELSPFITQVCKYAAVSKEEWEEQSKIWPTSFHPPTYNIDGIGGFSEEETQSICKFMRVVIDMAVSGHTPLVNAAVIVDPSVRRIIASETDQVYASSAPRDMTSAETRPFEETGEICLNDTLEKQNGSLSALSCLNPWQWSLQPHDTENCSQWHPLRHASMVAIESSSARDRNLFPNPSKIFDQDHVPPSNTDSPAKKQKTSSQSPDVQNDSREETVRDPSMERPYLCTGYDIFLLLEPCTMCAMALVHQRIKRIFYAFPNTTAGGLGSVHRLQGEKSLNHHYAVFRVLLPDDALRQMTTV | 3.5.4.33 | null | tRNA modification [GO:0006400]; tRNA wobble adenosine to inosine editing [GO:0002100] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; tRNA-specific adenosine deaminase activity [GO:0008251]; tRNA-specific adenosine-34 deaminase activity [GO:0052717] | PF14437; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family, ADAT3 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25315605}. Cytoplasm {ECO:0000269|PubMed:25315605}. Note=Localizes predominantly to the nucleus. {ECO:0000269|PubMed:25315605}. | CATALYTIC ACTIVITY: Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33; Evidence={ECO:0000269|PubMed:25315605}; | null | null | null | null | FUNCTION: Involved in RNA editing. Catalyzes the specific deamination of adenosine-34 in several cytosolic tRNA species. Generates inosine at the wobble position of the anticodon loop. {ECO:0000269|PubMed:25315605}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KHI3 | VICTR_ARATH | MASSSSSRNWVYDVFLSFSGKDVRVTFRSHFLKELDRKLISAFRDNEIERSHSLWPDLEQAIKDSRIAVVVFSKNYASSSWCLNELLEIVNCNDKIIIPVFYGVDPSQVRYQIGEFGSIFEKTCKRQTEEVKNQWKKALTDVANMLGFDSAKWDDEAKMIEEIANDVLAKLLLTSSTDSAENSIGIEDHIANMSVLLKLEAEEVRMVGIWGSSGIGKTTIARALFNQLSRHFPVSKFIDRAFVYKSRETYKGANPDDPNMKLHLQGCFLSEILGKKDIKIDHLGALGERLKHQKTLIIIDDLDDLVVLDSLVGKTNWFGCGSRIIVITNNKQFLRAHGIDHIYEVSLPSKERAQEMFCQSAFGENSPPEGFEELVVEIAWLAGSLPLGLTVFGSALRGRKKEYWVKMLPRLQNDLDGNIEETLKVSYDAIGNVKDQALFRLIACLFNHVKVRDIELLLADSGLDVNIALENLVDKSLIHVRNDHVEMHRLLQETGRNIVRSQSTDNPGEREFLVDSNDSRTVLSEGIGTRKVLGISLDTSKVSEFCVHENAFKGMGNLLFLDISSKTFIEEEVKVHLPEKINYYSVQPKQLIWDRFPLKCMPYTFLRNLVKLEMHDSKLEKLWEGAMSFTCLKELDMWASKYLKEIPDLSKATNIEKLDFGHCWSLVELPSSIRNLNKLLELNMEYCGELETLPTGFNLKSLDYLNFNECWKLRTFPEFATNISNLILAETSIEEYPSNLYFKNVRELSMGKADSDENKCQGVKPFMPMLSPTLTLLELWNIPNLVELSSSFQNLNNLERLDICYCRNLESLPTGINLESLVSLNLFGCSRLKRFPDISTNIKYLDLDQTGIEEVPWQIENFFNLTKLTMKGCRELKCVSLNIFKLKHLGEVSFSNCGALTRVDLSCYPSGVEMMKADNADIVSEETTSSLPDSCVLNVNFMDCVNLDREPVLHQQSIIFNSMILPGEEVPSYFTYRTSDSQPFGTSSSLPIPLLPTQLSQPFFRFRVCAVVSASNGVYIGVYSRFKGRIGNKFDSFGEVHNFMEIEKGIHLCIFDCRIRLYKDNVPLSQLNYDHVDINIHITSGDWRSTVVLKEWGIRLLETGSSAENRLGNPNSTLPHVSQAEEGNMGYYTHVQGLVNEIENSEDSGDNNVETERSKKRMRLHHFI | 3.2.2.6 | null | defense response [GO:0006952]; regulation of root meristem growth [GO:0010082]; signal transduction [GO:0007165] | cytosol [GO:0005829]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809] | PF07725;PF00931;PF01582; | 1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140; | Disease resistance NB-LRR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23275581}. Nucleus {ECO:0000269|PubMed:23275581}. | 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:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; | null | null | null | null | FUNCTION: Disease resistance protein of the TIR-NB-LRR-type. Part of the RPS6 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (By similarity). Required for [5-(3,4-dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione-(DFPM-) induced root growth arrest due to reduced number of meristem cells in the division zone of the primary root and inhibition of abscisic acid- (ABA-) induced stomatal closing. {ECO:0000250, ECO:0000269|PubMed:23275581}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KHQ8 | NCER3_ARATH | MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGPAADVNMMGYANMEQVASGVHFRLRARAFIVAEPYKKRIAFVNLDAGMASQLVTIKVIERLKQRYGELYTEENVAISGTHTHAGPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENLRPGSILINKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDKEMTLVKFVDDQWGPVARIMEDWFERENGCRSVDVESPRRVSSIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFRHADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGLPCEFNQSTCGGKNEQCYGRGPGYPDEFESTRIIGERQFKKAADLFTKASEEIQGKVDYRHAYVDFSQLEVTINGQNGGSEVVKTCPAAMGFGFAAGTTDGPGAFDFKQGDDQGNPFWRLVRNLLKNPTEEQVRCQRPKPILLDTGEMKQPYDWAPSILPVQILRIGQLVILCVPGEFTTMAGRRLRDAVKTVLKEGSNGREFSVVIAGLTNSYSQYIATFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLANDLLSAQTTDPGPQPPDLLHKQISLLTPVVADMTPIGTAFGDVTSDVPRLSKFRKGADIVRVQFRSANPRNDLMTEGTFALVERWLEGRETWVPVYDDDDFCLRFKWSRPFKLSTQSTATIEWRIPETASPGVYRITHFGSAKTPISSIHHFSGSSSAFVVY | 3.5.1.23 | null | cellular response to oxidative stress [GO:0034599]; ceramide catabolic process [GO:0046514]; 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] | 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:0000250|UniProtKB:F4HQM3}. 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 (By similarity). Promotes oxidative stress resistance (PubMed:26150824). {ECO:0000250|UniProtKB:F4HQM3, ECO:0000269|PubMed:26150824}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KIX0 | JMJ13_ARATH | MAERRICLSKEAKDGLEFLKRKKLQKMRSDSVNETVGFSTMARSGGDALRPTSASCGMRLRVTSSDTVSKVHGASTVRGGLMKEKVEKLETDDLKWTERLPECPVYRPTKEEFEDPLTYLQKIFPEASKYGICKIVSPLTATVPAGAVLMKEKSNFKFTTRVQPLRLAEWDSDDKVTFFMSGRTYTFRDYEKMANKVFARRYCSGGSLPDSFLEKEFWKEIACGKTETVEYACDVDGSAFSSAPGDPLGSSKWNLNKVSRLPKSTLRLLETSIPGVTEPMLYIGMLFSMFAWHVEDHYLYSINYQHCGASKTWYGIPGSAALKFEKVVKECVYNDDILSTNGEDGAFDVLLGKTTIFPPKTLLDHNVPVYKAVQKPGEFVVTFPRAYHAGFSHGFNCGEAVNFAMGDWFPFGAIASCRYAHLNRVPLLPHEELICKEAMLLNSSSKSENLDLTPTELSGQRSIKTAFVHLIRFLHLARWSLMKSGLCTGLVSNTYGTIVCSLCKRDCYLAFINCECYSHPVCLRHDVKKLDLPCGTTHTLYLRDNIEDMEAAAMKFEKEDGVSDLITTDEDLYKYPSSITLPAAKEDGYTPYSTIYFDFYTEVEMTSHDQLQSGNPVMSYEANASCISSVADDYECSDYVNRRANCSSSSDSKLSEEVACSSSKKTRFFPVVQDEQLVADQESDGSDSECFRVKRRSSLKFENRTVVLDTRESDHHQELKRLKKSHHHEGRYSSSSSVSRQEEEEDELVISNRKETQQQSDVKMQKKRIENHFGGFKRLKVKGLIKP | 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}; | flower development [GO:0009908]; long-day photoperiodism [GO:0048571]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of long-day photoperiodism, flowering [GO:0048579]; negative regulation of short-day photoperiodism, flowering [GO:0048577]; regulation of DNA-templated transcription [GO:0006355]; response to temperature stimulus [GO:0009266] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; histone binding [GO:0042393]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; metal ion binding [GO:0046872] | PF02373;PF02375;PF02928; | 2.60.120.650; | JARID1 histone demethylase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + succinate; Xref=Rhea:RHEA:60228, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15539, 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:30899015}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60229; Evidence={ECO:0000269|PubMed:30899015}; | null | null | null | null | FUNCTION: Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and involved in the regulation of gene expression (PubMed:30899015). Acts as a temperature and photoperiod dependent flowering repressor (PubMed:30899015). {ECO:0000269|PubMed:30899015}. | Arabidopsis thaliana (Mouse-ear cress) |
F4KU78 | IYD_HALH1 | MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | null | FMN binding [GO:0010181]; iodotyrosine deiodinase activity [GO:0140616] | PF00881; | 3.40.109.10; | Nitroreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481; Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; CATALYTIC ACTIVITY: Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH; Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:28157283}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455; Evidence={ECO:0000269|PubMed:28157283}; CATALYTIC ACTIVITY: Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459; Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; CATALYTIC ACTIVITY: Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH; Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422; Evidence={ECO:0000250|UniProtKB:B9K712}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345; Evidence={ECO:0000250|UniProtKB:B9K712}; CATALYTIC ACTIVITY: Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH; Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423; Evidence={ECO:0000250|UniProtKB:B9K712}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349; Evidence={ECO:0000250|UniProtKB:B9K712}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for 3,5-diiodo-L-tyrosine {ECO:0000269|PubMed:24153409}; KM=0.012 mM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:28157283}; KM=4.1 mM for 2-iodophenol (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:28157283}; Note=kcat 0.09 sec(-1) for the deiodination of 3,5-diiodo-L-tyrosine (PubMed:24153409). kcat is 0.27 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283). kcat is 0.0029 sec(-1) for the dehalogenation of 2-iodophenol (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283). {ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}; | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:24153409, PubMed:28157283). Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is much stronger than activity towards 3,5-diiodo-L-tyrosine and 2-iodophenol (PubMed:24153409, PubMed:28157283). {ECO:0000250|UniProtKB:B9K712, ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283}. | Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O) |
F4ZGF2 | COMTA_DANRE | MLWVVLAVVVVLASVLVLLRQSSGLLALLWHDVVHQRLLNFFTGLSRPQRILKAVQKNATKGNPESVIAAIDHYCRHSEWAMNVGDEKGLILDSVVTEVNPSTALELGTYCGYSTVRIARLLSPGTKLITLEFNPDYAAIARQIIAYAGLQDKVILVEGPSGDLIPKMKQQHGIKSFDFVFLDHWKDRYVPDTKLLEECGLLRKGSVLLADNVICPGTPEYLKYVRNDPRYESRYFKSNLEYTKVEDGLEKSVFLG | 2.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PIRSR:PIRSR037177-3}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PIRSR:PIRSR037177-3}; | catecholamine catabolic process [GO:0042424]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; methylation [GO:0032259] | axon [GO:0030424]; dendrite [GO:0030425]; extracellular region [GO:0005576]; membrane [GO:0016020] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000269|PubMed:21371608}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-10.5. Active from pH 5.5-11.5. {ECO:0000269|PubMed:21371608}; | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Shows highest activity towards catecholestrogens and dobutamine. Also has lower activity towards L-DOPA, dopamine and epinephrine. Active towards the xenobiotic compounds methyl-DOPA, carbidopa, isoproterenol, and apomorphine. {ECO:0000269|PubMed:21371608}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F5A6E9 | TPIS_PROCL | MANQRKFFVGGNWKMNGDRAGIDSIISFMKGPLSADTEVVVGCPQCYLMYTREHLPSNIGVAAQNCYKVAKGAFTGEISPSMIKDCGCEWVILGHSERRNVFNEPDTLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQEVHAKLRQWLRDNVNAEVADSTRIIYGGSVTPGNCKELAKTGDIDGFLVGGASLKPDFVQIINARD | 4.2.3.3; 5.3.1.1 | null | gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | IgE binding [GO:0019863]; methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000250|UniProtKB:P00939}; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Unstable only at extreme acidic (pH 1.0) or alkaline conditions (pH 11.0). IgE-binding activity is relatively stable under acidic and alkaline conditions, however the activity is increased between pH 2.0-3.0. {ECO:0000269|PubMed:28072528}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable up to 100 degrees Celsius. IgE-binding activity is reduced with increasing temperature higher than 60 degrees Celsius. {ECO:0000269|PubMed:28072528}; | FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}. | Procambarus clarkii (Red swamp crayfish) |
F5BHA2 | T19H_CATRO | MLSSLKDFFVLLLPFFIGIAFIYKLWNFTSKKNLPPSPRRLPIIGNLHQLSKFPQRSLRTLSEKYGPVMLLHFGSKPVLVISSAEAAKEVMKINDVSFADRPKWYAAGRVLYEFKDMTFSPYGEYWRQARSICVLQLLSNKRVQSFKGIREEEIRAMLEKINQASNNSSIINGDEIFSTLTNDIIGRSAFGRKFSEEESGSKLRKVLQDLPPLLGSFNVGDFIPWLSWVNYLNGFEKKLNQVSKDCDQYLEQVIDDTRKRDEENGANNNGGNHGNFVSVLLHLQKEDVKGFPSEKGFLKAIILDMIVGGTDTTHLLLHWVITELLKNKHVMTKLQKEVREIVGRKWEITDEDKEKMKYLHAVIKEALRLHPSLPLLVPRVAREDINLMGYRVAKGTEVIINAWAIARDPSYWDEAEEFKPERFLSNNFDFKGLNFEYIPFGSGRRSCPGSSFAIPIVEHTVAHLMHKFNIELPNGVSAEDFDPTDAVGLVSHDQNPLSFVATPVTIF | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | indole alkaloid biosynthetic process [GO:0035835] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; lyase activity [GO:0016829]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29438577}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = (-)-(R)-19-hydroxytabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61044, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:57893, ChEBI:CHEBI:58210, ChEBI:CHEBI:144372; Evidence={ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61045; Evidence={ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}; CATALYTIC ACTIVITY: Reaction=lochnericine + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + horhammericine + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61048, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144374, ChEBI:CHEBI:144375; Evidence={ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61049; Evidence={ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}; CATALYTIC ACTIVITY: Reaction=(-)-vincadifformine + O2 + reduced [NADPH--hemoprotein reductase] = (-)-minovincinine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61052, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142771, ChEBI:CHEBI:144373; Evidence={ECO:0000269|PubMed:31009114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61053; Evidence={ECO:0000269|PubMed:31009114}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 nM for tabersonine (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:21454651}; Vmax=5 umol/min/ug enzyme with tabersonine as substrate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:21454651}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}. | null | null | FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the conversion of (-)-tabersonine to 19-hydroxytabersonine, of lochnericine to horhammericine and of (-)-vincadifformine to (-)-minovincinine (PubMed:21454651, PubMed:31009114). {ECO:0000269|PubMed:21454651, ECO:0000269|PubMed:31009114}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
F5GUE5 | DAF14_CAEEL | MSNEQEDFGSLFNNQGELGIMDDFAEFGFQTTTTPTNWAAAGNYMYPDQVHLPASINNPNMPINDWLEDAPMPDCYNVPSTSTDENNDPFPFSNISSQSSLKPKTPEKAVVEVRPTGNEMLDPEPKYPKEEKPWCTIFYYELTVRLGKAFEAKVPTITIDGATGASDECRMSLTSQPSSRNSKSSQIRNTVGAGIQLAYENGELWLTVLTDQIVFVQCPFLNQTLNKPLKYVFRLQNKGDQKRMKIFDKEQFEQEKTLALGPLTEKEVADERMRIFSNIRVSFCKGFGETYSRLKVVNLPCWIEIILHEPADEYDTVFRINNERPEIGSRS | null | null | anatomical structure morphogenesis [GO:0009653]; BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; egg-laying behavior [GO:0018991]; negative regulation of dauer larval development [GO:0061067]; pigment accumulation [GO:0043476]; regulation of dauer larval development [GO:0061065]; regulation of transcription by RNA polymerase II [GO:0006357]; SMAD protein signal transduction [GO:0060395]; social behavior [GO:0035176] | heteromeric SMAD protein complex [GO:0071144] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; I-SMAD binding [GO:0070411]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF03166; | 2.60.200.10; | null | null | null | null | null | null | null | null | FUNCTION: Probably an atypical receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta-like daf-7 signaling (PubMed:10625546). Plays a role in TGF-beta-like daf-7 signaling in regulating entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions; partially redundant with R-SMAD daf-8 (PubMed:10625546, PubMed:20081192). {ECO:0000269|PubMed:10625546, ECO:0000269|PubMed:20081192}. | Caenorhabditis elegans |
F5H094 | SO1BT_HUMAN | MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFDISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGYYRYSKETNIDPSENSTSNLPNCLINQMLSLNRTPSEIIERGCVKESGSHMWIYVFMGNMLRGIGETPIVPLGISYIDDFAKEGHSSLYLGTVNVMGMTGLVFAFMLGSLFAKMYVDIGYVDLSTIRITPKDSRWVGAWWLGFLVSGIVSIISSIPFFFLPLNPNKPQKERKVSLFLHVLKTNDKRNQIANLTNRRKYITKNVTGFFQSLKSILTNPLYVIFVIFTLLHMSSYIASLTYIIKMVEQQYGWSASKTNFLLGVLALPAVAIGMFSGGYIIKKFKLSLVGLAKLAFCSATVHLLSQVLYFFLICESKSVAGLTLTYDGNSPVRSHVDVPLSYCNSECNCDESQWEPVCGNNGITYLSPCLAGCKSSSGNKEPIVFYNCSCVEVIGLQNKNYSAHLGECPRDDACTRKSYVYFVIQVLDAFLCAVGLTSYSVLVIRIVQPELKALAIGFHSMIMRSLGGILVPIYFGALIDTTCMKWSTNSCGARGACRIYNSTYLGRAFFGLKVALIFPVLVLLTVFIFVVRKKSHGKDTKVLENERQVMDEANLEFLNDSEHFVPSAEEQ | null | null | sodium-independent organic anion transport [GO:0043252] | plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868] | bile acid transmembrane transporter activity [GO:0015125]; serine-type endopeptidase inhibitor activity [GO:0004867]; sodium-independent organic anion transmembrane transporter activity [GO:0015347] | PF07648;PF03137; | 3.30.60.30;1.20.1250.20; | Organo anion transporter (TC 2.A.60) family | null | SUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane {ECO:0000269|PubMed:29248594}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU362056}. Cell membrane {ECO:0000269|PubMed:29248594, ECO:0000269|PubMed:32818652}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29248594}; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(out) = 17beta-estradiol 17-O-(beta-D-glucuronate)(in); Xref=Rhea:RHEA:72691, ChEBI:CHEBI:82961; Evidence={ECO:0000269|PubMed:29248594, ECO:0000269|PubMed:31509437}; CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905; Evidence={ECO:0000269|PubMed:29248594, ECO:0000269|PubMed:31127008, ECO:0000269|PubMed:31509437, ECO:0000269|PubMed:32818652}; CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:31509437}; CATALYTIC ACTIVITY: Reaction=lithocholate(out) = lithocholate(in); Xref=Rhea:RHEA:73139, ChEBI:CHEBI:29744; Evidence={ECO:0000269|PubMed:31509437}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32.8 uM for 17beta-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:29248594}; KM=34.2 uM for dehydroepiandrosterone sulfate {ECO:0000269|PubMed:29248594}; KM=20.4 uM for dehydroepiandrosterone sulfate {ECO:0000269|PubMed:32818652}; KM=15.99 uM for taurocholate {ECO:0000269|PubMed:31509437}; Vmax=29.7 pmol/min/mg protein with 17beta-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:29248594}; Vmax=300.2 pmol/min/mg protein with dehydroepiandrosterone sulfate {ECO:0000269|PubMed:29248594}; Vmax=264.3 pmol/min/mg protein with dehydroepiandrosterone sulfate {ECO:0000269|PubMed:32818652}; Vmax=17.38 pmol/min/mg protein with taurocholate {ECO:0000269|PubMed:31509437}; | null | null | null | FUNCTION: Mediates the Na(+)-independent uptake of organic anions (PubMed:29248594). Transports the conjugated steroids 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate) or E2G) and dehydroepiandrosterone 3-sulfate (DHEAS) at the smooth endoplasmic reticulum membrane (SER), granting access to metabolizing enzymes (PubMed:29248594, PubMed:31127008, PubMed:32818652). Contributes to the metabolism of bile acids such as taurocholate (cholyltaurine) and lithocholate, by functioning as a doorway between SER and cytosol, thereby decreasing their circulating levels and protecting the organism from their detergent properties (PubMed:31509437). Regulates access or exit of drugs to the SER lumen (PubMed:31127008). {ECO:0000269|PubMed:29248594, ECO:0000269|PubMed:31127008, ECO:0000269|PubMed:31509437, ECO:0000269|PubMed:32818652}. | Homo sapiens (Human) |
F5HCV3 | ORF50_HHV8P | MAQDDKGKKLRRSCVESFVGLSDELKAQLYQCVLLINDAYETIYDPSDLNRVVEDVCIRIMKECSKLGALCGLFTDINMFNLFCFFRASRMRTKGAAGYNVPCAEASQGIIRILTERILFCTEKAFLTAACSGVSLPPAICKLLHEIYTEMKAKCLGAWRRLVCNRRPIMILTSSLLKLYNTYDTAGLLSEQSRALCLLVFQPVYLPRIMAPLEIMTKGQLAPENFYSITGSAEKRRPITTGKVTGLSYPGSGLMPESLILPILEPGLLPASMVDLSDVLAKPAVILSAPALSQFVISKPHPNMPHTVSIIPFNPSGTDPAFISTWQAASQNMVYNTSTAPLKPATGSSQTVSVKAVAQGAVITATTVPQAMPARGTGGELPVMSASTPARDQVAACFVAENTGDSPDNPSSFLTSCHPCDPNTVIVAQQFQPPQCVTLLQVTCAPSSTPPPDSTVRAPVVQLPTVVPLPASAFLPALAQPEASGEELPGGHDGDQGVPCRDSTAAATAAEATTPKRKQRSKERSSKKRKALTVPEADTTPSTTTPGTSLGSITTPQDVHATDVATSEGPSEAQPPLLSLPPPLDVDQSLFALLDEAGPETWDVGSPLSPTDDALLSSILQGLYQLDTPPPLRSPSPASFGPESPADIPSPSGGEYTQLQPVRATSATPANEVQESGTLYQLHQWRNYFRD | 2.3.2.27 | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA-templated viral transcription [GO:0039695]; regulation of DNA-templated transcription [GO:0006355] | host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; transferase activity [GO:0016740] | PF03326; | null | Herpesviridae TAF50 family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:23990779, ECO:0000269|PubMed:35914008}. | 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:23990779, ECO:0000269|PubMed:25320320}; | null | null | null | null | FUNCTION: Transcriptional transactivator that is necessary and sufficient for reactivation of the virus from latency (PubMed:17392367, PubMed:22300411). Acts post-transcriptionally and transcriptionally to regulate viral lytic gene expression and synergistically with ORF57 activates certain early and late viral promoters including its own promoter (PubMed:15269354). Autostimulation on its promoter is mediated by the formation of a ternary complex between ORF50 and the cellular components HGMB1 and POU2F1 (PubMed:17537858). Possesses also a bimodal activity in targeting proteins for degradation through using its own E3 ligase activity or by stabilizing and chaperoning host E3 ligases (PubMed:23990779, PubMed:27912080, PubMed:37888983). These activities help to subvert the host innate and adaptive immune responses while also modulating the host transcriptome and protein landscape to promote virus production. For instance, targets the host SMC5/6 complex for ubiquitination and subsequent degradation through the ubiquitin-proteasome during reactivation while during latency, host SMC5/6 complex binds to the viral episome and condenses viral chromatin, creating a repressive chromatin structure to silence genome transcription (PubMed:35914008). Hijacks the cellular E3 ligase complex RNF20/40 to increase the level of transcriptionally active RNA polymerase II on viral gene promoters thereby facilitating lytic gene expression (PubMed:37888983). Acts as a SUMO-targeting ubiquitin ligase and affects general sumoylation of cellular proteins (PubMed:23990779). Promotes the polyubiquitination and subsequent degradation of host MYD88 and thereby inhibits MYD88-mediated TLR4 signaling (PubMed:25320320). Induces the degradation of vFLIP/ORF71 together with cellular ubiquitin ligase ITCH to prevent vFLIP-induced NF-kappa-B signaling (PubMed:25320320). {ECO:0000269|PubMed:15269354, ECO:0000269|PubMed:17392367, ECO:0000269|PubMed:17537858, ECO:0000269|PubMed:22300411, ECO:0000269|PubMed:23990779, ECO:0000269|PubMed:25320320, ECO:0000269|PubMed:27912080, ECO:0000269|PubMed:35914008, ECO:0000269|PubMed:37888983}. | Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus) |
F5HDE4 | ORF45_HHV8P | MAMFVRTSSSTHDEERMLPIEGAPRRRPPVKFIFPPPPLSSLPGFGRPRGYAGPTVIDMSAPDDVFAEDTPSPPATPLDLQISPDQSSGESEYDEDEEDEDEEENDDVQEEDEPEGYPADFFQPLSHLRPRPLARRAHTPKPVAVVAGRVRSSTDTAESEASMGWVSQDDGFSPAGLSPSDDEGVAILEPMAAYTGTGAYGLSPASRNSVPGTQSSPYSDPDEGPSWRPLRAAPTAIVDLTSDSDSDDSSNSPDVNNEAAFTDARHFSHQPPSSEEDGEDQGEVLSQRIGLMDVGQKRKRQSTASSGSEDVVRCQRQPNLSRKAVASVIIISSGSDTDEEPSSAVSVIVSPSSTKGHLPTQSPSTSAHSISSGSTTTAGSRCSDPTRILASTPPLCGNGAYNWPWLD | null | null | perturbation of host innate immune response [GO:0052167]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity [GO:0039557]; virus-mediated perturbation of host defense response [GO:0019049] | host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | null | null | null | null | PTM: Phosphorylated on Ser-41 and Ser-162 by host IKBKE and TBK1. {ECO:0000269|PubMed:11943871, ECO:0000269|PubMed:22787218}. | SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:12634379}. Host cytoplasm {ECO:0000269|PubMed:19116250}. Host nucleus {ECO:0000269|PubMed:19116250, ECO:0000269|PubMed:35618833}. Host Golgi apparatus {ECO:0000269|PubMed:33315947}. | null | null | null | null | null | FUNCTION: Prevents the establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of host interferon regulatory factor 7/IRF7, a transcription factor critical for the induction of interferons alpha and beta (PubMed:11943871, PubMed:20485504, PubMed:22787218). Mechanistically, ORF45 competes with the associated IRF7 and inhibits its phosphorylation by IKBKE or TBK1 by acting as an alternative substrate (PubMed:11943871, PubMed:22787218). Acts as an activator of the NLRP1 inflammasome via interaction with the N-terminal part of host NLRP1: interaction promotes translocation of the N-terminal part of NLRP1 into the nucleus, relieving autoinhibition of the NLRP1 inflammasome and leading to its activation (PubMed:35618833). Also plays a role in promoting the late transcription and translation of viral lytic genes by constitutively activating host extracellular signal-regulated kinase (ERK)-p90 ribosomal S6 kinase/RPS6KA1 (PubMed:30842327). In addition, supports the viral replication cycle by modulating host p53/TP53 signaling pathway (PubMed:34523970). Interacts with host p53/TP53 and prevents its interaction with the deubiquitinase USP7, leading to sequestration of P53/TP53 in the host cytoplasm thereby diminishing its transcriptional activity (PubMed:34523970). {ECO:0000269|PubMed:11943871, ECO:0000269|PubMed:20485504, ECO:0000269|PubMed:22787218, ECO:0000269|PubMed:30842327, ECO:0000269|PubMed:34523970, ECO:0000269|PubMed:35618833}. | Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus) |
F5HF68 | VIRF1_HHV8P | MDPGQRPNPFGAPGAIPKKPCLSQGSPGTSGSGAPCDEPSRSESPGEGPSGTGGSAAAGDITRQAVVAAITEWSRTRQLRISTGASEGKASIKDWIVCQVNSGKFPGVEWEDEERTRFRIPVTPLADPCFEWRRDGELGVVYIRERGNMPVDASFKGTRGRRRMLAALRRTRGLQEIGKGISQDGHHFLVFRVRKPEEEQCVECGVVAGAVHDFNNMARLLQEGFFSPGQCLPGEIVTPVPSCTTAEGQEAVIDWGRLFIRMYYNGEQVHELLTTSQSGCRISSALRRDPAVHYCAVGSPGQVWLPNVPNLACEIAKRELCDTLDACAKGILLTSSCNGIFCVCYHNGPVHFIGNTVPPDSGPLLLPQGKPTRIFNPNTFLVGLANSPLPAPSHVTCPLVKLWLGKPVAVGKLEPHAPSPRDFAARCSNFSDACVVLEIMPKPLWDAMQ | null | null | immune system process [GO:0002376]; symbiont-mediated perturbation of host cellular process [GO:0044068]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host innate immune response [GO:0052170]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein domain specific binding [GO:0019904]; protein sequestering activity [GO:0140311]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00605;PF10401; | 2.60.200.10;1.10.10.10; | IRF family | PTM: ISGylated. {ECO:0000269|PubMed:26355087}.; PTM: Propionylated in lysine residues Lys-406 and Lys-442, which is required for effective inhibition of IFN-beta production and antiviral signaling. {ECO:0000269|PubMed:26355087}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:35538151, ECO:0000269|PubMed:37459327}. | null | null | null | null | null | FUNCTION: Plays a role in the inhibition of host innate response by repressing the expression of interferon-inducible genes and blocking host IRF1- and IRF3-mediated transcription. Blocks the interaction between host IRF3 and CREBBP. Regulates the host cellular metabolism by increasing glucose uptake, ATP production and lactate secretion through down-regulation of heterogeneous nuclear ribonuclear protein Q1/SYNCRIP. Mechanistically, induces ubiquitination and degradation of SYNCRIP through the ubiquitin-proteasome pathway by recruiting KLHL3/CUL3 ubiquitin ligase complex (PubMed:35538151). Disrupts host TP53 signaling pathway during viral infection by interacting with host USP7 and thereby decreasing the availability of USP7 for deubiquitinating and stabilizing TP53 (PubMed:26786098). Plays a role in the global inhibition of protein ISGylation by interacting with host HERC5 leading to its inhibition (PubMed:26355087). Promotes its own propionylation by blocking SIRT6 interaction with ubiquitin-specific peptidase 10/USP10 leading to SIRT6 degradation via a ubiquitin-proteasome pathway (PubMed:37023208). In turn, propionylation is required to block IRF3-CBP/p300 recruitment and to repress the STING DNA sensing pathway (PubMed:37023208). Plays a role in the activation of mitophagy during infection via interaction with the host proteins NIX/BNIP3L, TUFM and GABARAPL1 thereby inhibiting antiviral responses and contributing to productive replication (PubMed:31324791, PubMed:37459327). {ECO:0000269|PubMed:11314014, ECO:0000269|PubMed:26355087, ECO:0000269|PubMed:26786098, ECO:0000269|PubMed:31324791, ECO:0000269|PubMed:35538151, ECO:0000269|PubMed:37023208, ECO:0000269|PubMed:37459327, ECO:0000269|PubMed:9365244, ECO:0000269|PubMed:9420276}. | Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus) |
F5HKX0 | CLB9_ANOGA | MTSYNRSVAWLTVCVLLALHIGGSHQQQQQCTTPTRLRGRCISIYECDSILDYFKQRILTWEEREFLRKSQCTGATSGRQPFVCCPGNGSKPVVAPATTVPAGTASTTPAGPAATAPSGDAALADQLVGGLLPNPKKNECGVSIGMRIYGGQNADIDEFPWLALLQYENRKGERKYSCGGSLINRRYVLTAAHCVIGEVERKEGKLVSVRLGEYNTKTEIDCVTEEQEEICADPPIDAGIESVIVHPGYQDMAHADDIALLRLAQSIEYTSFVQPVCLPLTDFRASKTGEVNFVTGFGRTLQESRSAVKQKLGIKVYDHARCQEKYATKNSSITTNQLCAGGEYAKDSCHGDSGGPLMKLQKVWYLEGIVSYGNRCGLEDWPGVYTHVPAYMAWVRSNIKE | 3.4.21.- | null | innate immune response [GO:0045087]; positive regulation of melanization defense response [GO:0035008]; protein processing [GO:0016485]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF12032;PF00089; | 3.30.1640.30;2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Proteolytic cleavage is necessary for activation. {ECO:0000269|PubMed:20953892, ECO:0000269|PubMed:25525260, ECO:0000269|PubMed:26926112}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU366078}. | null | null | null | null | null | FUNCTION: Serine protease that functions in the melanization-mediated immune response (PubMed:20953892, PubMed:25525260, PubMed:26926112). Cleaves and activates prophenoloxidase (PPO), which is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products (PubMed:20953892, PubMed:26926112). {ECO:0000269|PubMed:20953892, ECO:0000269|PubMed:25525260, ECO:0000269|PubMed:26926112}. | Anopheles gambiae (African malaria mosquito) |
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