entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
F4IYM4
|
DEX1_ARATH
|
Protein DEFECTIVE IN EXINE FORMATION 1
|
MKSRARQCLLVCLLCLSLTNLSYGENKFRERKATDDELGYPDIDEDALLNTQCPKKLELRWQTEVTSSVYATPLIADINSDGKLDIVVPSFVHYLEVLEGADGDKMPGWPAFHQSNVHSSPLLFDIDKDGVREIALATYNAEVLFFRVSGFLMSDKLEVPRRKVHKNWHVGLNPDPVDRSHPDVHDDVLEEEAMAMKSSTTQTNATTTTPNVTVSMTKEVHGANSYVSTQEDQKRPENNQTEAIVKPTPELHNSSMDAGANNLAANATTAGSRENLNRNVTTNEVDQSKISGDKNETVIKLNTSTGNSSETLGTSGNSSTAETVTKSGRRLLEEDGSKESVDSHSDSKDNSEGVRMATVENDGGLEADADSSFELLRENDELADEYSYDYDDYVDEKMWGDEEWVEGQHENSEDYVNIDAHILCTPVIADIDKDGVQEMIVAVSYFFDPEYYDNPEHLKELGGIDIKNYIASSIVVFNLDTKQVKWIKELDLSTDKANFRAYIYSSPTVVDLDGDGYLDILVGTSFGLFYAMDHRGNIREKFPLEMAEIQGAVVAADINDDGKIELVTTDSHGNIAAWTTQGVEIWEAHLKSLVPQGPSIGDVDGDGHTEVVVPTSSGNIYVLSGKDGSIVRPYPYRTHGRVMNQLLLVDLNKRGEKKKGLTIVTTSFDGYLYLIDGPTSCTDVVDIGETSYSMVLADNVDGGDDLDLIVSTMNGNVFCFSTPSPHHPLKAWRSSDQGRNNKANRYDREGVFVTHSTRGFRDEEGKNFWAEIEIVDKYRYPSGSQAPYNVTTTLLVPGNYQGERRITQSQIYDRPGKYRIKLPTVGVRTTGTVMVEMADKNGLHFSDEFSLTFHMYYYKLLKWLLVLPMLGMFGLLVILRPQEAVPLPSFSRNTDL
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Required for exine pattern formation during pollen development, especially for primexine deposition.
|
F4IZR5
|
XPO1B_ARATH
|
Protein EXPORTIN 1B
|
MAAEKLRDLSQPIDVVLLDATVEAFYSTGSKEERASADNILRDLKANPDTWLQVVHILQNTSSTHTKFFALQVLEGVIKYRWNALPVEQRDGMKNYISDVIVQLSRDEASFRTERLYVNKLNIILVQIVKQEWPAKWKSFIPDLVIAAKTSETICENCMAILKLLSEEVFDFSKGEMTQQKIKELKQSLNSEFQLIHELCLYVLSASQRQELIRATLSALHAYLSWIPLGYIFESPLLEILLKFFPVPAYRNLTLQCLSEVASLNFGDFYDMQYVKMYSIFMNQLQAILPLNLNIPEAYSTGSSEEQAFIQNLALFFTSFFKLHIKILESAPENISLLLAGLGYLISISYVDDTEVFKVCLDYWNSLVLELFGTRHHACHPALTPSLFGLQMAFLPSTVDGVKSEVTERQKLYSDPMSKLRGLMISRTAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHEDTEKQMLSKLSKQLSGEEWAWNNLNTLCWAIGSISGSMVVEQENRFLVMVIRDLLSLCEVVKGKDNKAVIASNIMYVVGQYSRFLRAHWKFLKTVVHKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGESEPFVSELLSGLATIVGDLQPHQIHTFYESVGSMIQAESDPQKRGEYLQRLMALPNQKWAEIIGQARQSADILKEPDVIRTVLNILQTNTRVATSLGTFFLSQISLIFLDMLNVYRMYSELVSSSIANGGPYASRTSLVKLLRSVKREILKLIETFLDKAENQPHIGKQFVPPMMDQVLGDYARNVPDARESEVLSLFATIINKYKVVMRDEVPLIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFRALIQLSSEQLKLVMDSVIWAFRHTERNIAETGLNLLLEMLKNFQKSDFCNKFYQTYFLQIEQEVFAVLTDTFHKPGFKLHVLVLQHLFSLVESGSLAEPLWDAATVPHPYSNNVAFVLEYTTKLLSSSFPNMTTTEVTQFVNGLYESRNDVGRFKDNIRDFLIQSKEFSAQDNKDLYAEEAAAQMERERQRMLSIPGLIAPSEIQDDMADS
|
Receptor for the leucine-rich nuclear export signal (NES). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (By similarity). Required for the maternal-to-embryonic transition and during gametophyte development.
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F4J061
|
IQD5_ARATH
|
Protein IQ-DOMAIN 5 (AtIQD5)
|
MGASGRWIKALVGFTKSDKSRSSKKDENVKVATKSRFGRKNSVDFDFEKFQDGFEDSNTRSMVDTGVSTSTSLQSYGGVAYDEQSRENRAATRIQTAYRGFLARRALRALKGLVRLQALVRGHAVRKQAAVTLRCMQALVRVQARVRARRVRLALELESETSQQTLQQQLADEARVREIEEGWCDSIGSVEQIQAKLLKRQEAAAKRERAMAYALTHQWQAGTRLLSAHSGFQPDKNNWGWNWLERWMAVRPWENRFLDSNLRDDAKLGENGMEQSENVPKTQIKSVSKMPNTSNLVSGVSSQMTGPCQSDGDSSSPGISSSIPVVSKAKSKPAKDDLAVEVNSRPGAGPRSHSNPKERSREPNRSSKERLSLPNSGKSLGSQSTKANRAGKLTPASQKVVEEKSAQNQRRRNSDPIKQRLA
|
May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin (CaM) calcium sensor proteins to cortical microtubule arrays, thus being a potential scaffold in cellular signaling and trafficking. Binds to microtubules (MTs) and promotes MT assembly and dynamics to modulate pavement cell (PC) morphogenesis via cellulose deposition-dependent anisotropic cell expansion triggered by cellulose synthase complexes (CSCs). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
|
F4J077
|
PATH1_ARATH
|
Protein PAT1 homolog 1 (AtPAT1H1) (Protein ROOT STEM CELL DEFECTIVE 2)
|
MERSDSRDLYNFVRASSLDKNSTLFDASQYEFFGQNLDDMELGGLDDDGVIAPVLGHADDDEYHLFDKGEGAGLGSLSDMDDLATTFAKLNRVVTGPKHPGVIGDRGSGSFSRESSSATDWTQDAELTSWLDEQDQEAKRWSSQPQSFAHSKPLYRTSSYPQQQPQLQHYNSEPIILPESNFTSFPPPGNRSPQASPGNLHRAPSLPGGSQLTYSAPSPLSNSGFHLSGLSQGPHYGGNLTRYASCGPTLGNMVQPHWVTDPGHLHGDHSGLLHNLVQQQHQQLPPRNAIMSQHLLALQQRQSYAQLAALQSQLYSSYPSPSRKVPFGVGEVREHKHKSSHRSRKNRGLSQQTSDAASQKSETGLQFRSKHMTSEEIESILKMQHSNSHSNDPYVNDYYHQAKLAKKSAGSKAISHFYPAQLKDHQPRSRNSSEQHPQVHVDALGKITLPSVRRPHALLEVDSSPGFNDGSGDHKGSGKHLEQEPLVAARVTIEDALGVLIDIVDIDRTLQNTRPQDGGAQLKRKRQILLEGLATALQLADPFSKTGQKSGMTAKDDIVFLRIATLPKGRKLLTKYLQLLVPGTENARVVCMAIFRHLRFLFGGLPSDTLAAETISNLAKAVTVCVQAMDLRALSACLAAVVCSSEQPPLRPIGSSAGDGASVVLISLLERAAEVVVVPRVMHGNSNDGLWRASFDEFFNLLTKYCRSKYDTIRGQNQGSAADVLELAIKREMPAELLRASLRHTNDDQRNYLLNFGRKPSAISESASHARGGQINSESVRG
|
Activator of mRNA decapping. Involved in mRNA decay via decapping (By similarity). Involved in the regulation of root stem cell niche identity. Maintains root stem cell niche stability through the interaction with the negative regulator of jasmonate signaling AFPH2/NINJA, and the regulation of cell division.
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F4J0D2
|
PBL36_ARATH
|
Serine/threonine-protein kinase PBL36 (EC 2.7.11.1) (PBS1-like protein 36) (Receptor-like cytoplasmic kinase PBL36)
|
MATKLESFKVVEKLGVEKGEKGKMMSKKKNVKKDGDESESGFWFRFKFIFSCISSRSKVDSSMNATAVIAEPKKVIEKLEGHPAPTKDTGCAESGSSTPLMSGELKYSSKLRIFMFNDLKLATRNFRPESLLGEGGFGCVFKGWIEENGTAPVKPGTGLTVAVKTLNPDGLQGHKEWLAEINFLGNLVHPSLVKLVGYCMEEDQRLLVYEFMPRGSLENHLFRRTLPLPWSVRMKIALGAAKGLAFLHEEAEKPVIYRDFKTSNILLDGEYNAKLSDFGLAKDAPDEKKSHVSTRVMGTYGYAAPEYVMTGHLTTKSDVYSFGVVLLEILTGRRSVDKSRPNGEQNLVEWVRPHLLDKKRFYRLLDPRLEGHYSIKGAQKATQVAAQCLNRDSKARPKMSEVVEALKPLPNLKDFASSSSSFQTMQPVAKNGVRTQGGGFVSRNGPPMRSLSSLNLPQASPYRYARQSPKPKGKEP
|
Involved in chitin-triggered immune signaling and is required for reactive oxygen species (ROS) production. Acts downstream of SD129 in defense signaling triggered by the pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty acid.
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F4J0W4
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MIRO2_ARATH
|
Mitochondrial Rho GTPase 2 (AtMIRO2) (EC 3.6.5.-) (Calcium-binding GTPase) (AtCBG) (Miro-related GTPase 2)
|
MMLGGKSSAGGRTSLRVAVAGDKGTGKSSLISAVASETFPDNVPRVLPPITLPADAFPDYIPITIVDTPSSIDNRIKLIEEFRKADVVLLTYACDQPSTLDRLSSYWLPELRRLEIKAPVIVVGCKLDLRDERSPARLEDIMSPIMKEYREIETCIECSALTLIQVPDVFYFASKAVLHPTFPLFDQEKQCLKPRLRRAVQRIFNLCDHDLDGALNDAELNDFQVNCFGAPLDPVELMGVKKVVQERQPDGVTDLGLTLPGFLFLFSLFIERGRPETAWAILRKCGYNDSLELHAELLPVPAKQSPDQSIELTNEAMDFLSGIFQLYDLDNDGALQPAELDDLFQTAPDSPWLEDPYKEAAEKTPGGSLTINGFLSEWALMTLLDPRKSLANLTYIGYGHDPASTFSVTRKRSVDRKKQRTERNVFQCFVFGPKKSGKSALLDSFLGRKFSNSYKATMGERYAANVIDQPGGSKKTLILREIPEDRVKKFLTNKESLAACDVAVVVYDSSDVYSWRKAREILMEVARRGEERGYGTPCLLVAAKDDLDPYPMSVQESDRVCMELGIDIPVSLSMKLGEPNSLFSRIVSTAENPHMSIPETESGRRSRNIRQLVNSSLLFVSVGTAVGFAGLAAYRAYSARKNA
|
Calcium-binding mitochondrial GTPase involved in calcium signaling during salt stress response. May play a role in the progression of embryonic cell division, development of haploid male and female gametes, and pollen tube growth.
|
F4J117
|
LSF1_ARATH
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Phosphoglucan phosphatase LSF1, chloroplastic (EC 3.1.3.-) (Phosphoglucan phosphatase like sex Four1) (Protein LIKE SEX4 1)
|
MAFLQQISGLGALERSCPSIMIGSSFRSGNGRVFDGRGIAYLGSREKFGFNRRRRVVLRVVAMSSSSTPFKMNLNEYMVTLEKPLGIRFALSADGKIFVHAIKKGSNAEKARIIMVGDTLKKASDSSGGTLVEIKDFGDTKKMLVEKTGSFSLVLERPFSPFPIQYLLHLSDLDLLYNRGRVSFVTWNKNLLSSNLRASSQGSGNSGYAAFSSKFFTPQGWKLLNRQSNSFQSGTKKNILSPPISPLVSVFSEDVPGDGEWGYGNFPLEEYIKALDRSKGELSYNHALGMRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAWATWDLIAMVDDGKHDGTPTHSVTFVWNGHEGEEVLLVGDFTGNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVVGDVANVRPTIQQPRKDANIIKVIERVLTESERFRLAKAARCIAFSVCPIRLCPKS
|
Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Participates in the regulation of the initial steps of starch degradation at the granule surface. May release a different set of phosphate groups from those removed by DSP4.
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F4J220
|
LPPE1_ARATH
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Lipid phosphate phosphatase epsilon 1, chloroplastic (AtLPPE1) (EC 3.1.3.-) (Phosphatidic acid phosphatase epsilon 1) (Plastidic phosphatidic acid phosphatase epsilon 1)
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MAASSSLLLLLHCPTCNFYFDSSSYLKRSRLSSYSSIISRGSPLFVSSFGSMTVKRFSSRVGSRSNDGNEQFGALEQESFINNSSEIRKDLVTGGGIEAIVNRLSKWVVSVLFGSIILLRHDGAALWAVIGSISNSALSVVLKRILNQERPTTTLRSDPGMPSSHAQSISFISVFAVLSVMEWLGTNGVSLFLSGLILALGSYFIRLRVSQKLHTSSQVVVGAIVGSLFCILWYTMWNSLLREAFEASLLVQISVFLFAATFALAFAAYVVLNWFKDER
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Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a secondary role as PAP in plastids.
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F4J264
|
PRFB3_ARATH
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Peptide chain release factor PrfB3, chloroplastic (AtPrfB3)
|
MAAKIIGGCCSWRRFYRKRTSSRFLIFSVRASSSMDDMDTVYKQLGLFSLKKKIKDVVLKAEMFAPDALELEEEQWIKQEETMRYFDLWDDPAKSDEILLKLADRAKAVDSLKDLKYKAEEAKLIIQLGEMDAIDYSLFEQAYDSSLDVSRSLHHYEMSKLLRDQYDAEGACMIIKSGSPGAKSQIWTEQVVSMYIKWAERLGQNARVAEKCSLLSNKSGVSSATIEFEFEFAYGYLLGERGVHRLIISSTSNEECSATVDIIPLFLRASPDFEVKEGDLIVSYPAKEDHKIAENMVCIHHIPSGVTLQSSGERNRFANRIKALNRLKAKLLVIAKEQKVSDVNKIDSKNILEPREETRSYVSKGHKMVVDRKTGLEILDLKSVLDGNIGPLLGAHISMRRSIDAI
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Involved in the light- and stress-dependent regulation of stability of 3' processed petB transcripts, thus regulating cytochrome b6 accumulation, a rate-limiting step in photosynthetic electron transport. May be recruited to specifically protect petB transcripts against 3'-5' exonucleolytic attack by masking the 3' ends. Does not function as release factor.
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F4J2K2
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FPGS2_ARATH
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Folylpolyglutamate synthase (EC 6.3.2.17) (DHFS-FPGS homolog C) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase)
|
MLVCGKGFLKCRAPGVPFFCDKRKSFFTKTKRGFHSLPLGTGVRVYFNNNLRYSSNSIEVVEKAAINMGSKEDKADNPALSSYDDAMEALSTLISRRNRGDRTPTKGNRDKLEQVVTYLKILDLEDKIKELKVIHVAGTKGKGSTCVFSEAILRNCGFRTGMFTSPHLIDVRERFRIDGLDISEEKFLQYFWECWKLLKEKAVDGLTMPPLFQFLTVLAFKIFVCEKVDVAVIEVGLGGKLDSTNVIQKPVVCGIASLGMDHMDILGNTLADIAFHKAGIFKPQIPAFTVPQLSEAMDVLQKTANNLEVPLEVVAPLEPKKLDGVTLGLSGDHQLVNAGLAVSLSRCWLQRTGNWKKIFPNESKETEIPVAFCRGLATARLHGRAQVVHDVVSDPQDSSDSMETPCGDLIFYLDGAHSPESMEACGRWFSSAVRGDKSLSTAVNGYMRHGEYGTDLNRVSKQILLFNCMEVRDPQVLLPKLVTTCASSGTHFSRALFVPSMSTYNKVISGASAIPSDTRRKDLTWQFRLQRLWEKSIQGTDAGLDHTLKPDGITALPPHDFLCGDAPQCGGPAGTPVTSSAVMPSLPLTINWLRDCVRRNPSLKLEVLVTGSLHLVGDVLRLLKR
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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.
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F4J2U9
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CFM3A_ARATH
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CRM-domain containing factor CFM3A, chloroplastic/mitochondrial (Protein CRM FAMILY MEMBER 3A) (AtCFM3a)
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MAMKPSLHFCPTTVTKKFVYSFQSSFCFRFLRYSSSISLGSCKGVTFSSRNDQIASRRFSFSRDCNNGVWLENWNRIQKRNQPKPPKVVVNYRKEGRFSGSEIVSGDDNRSRDGDGSTMEKIVEKLKKYGYMEEVQNKEIEQERRIEKGSVEDIFYVEEGKLPNTRGGFTEESLLGGENVIGSNGDVGFPWEKMSAKEKKELEAEWTAKKENRYSLAEMTLPESELRRLRNLTFRTASKMRIRGGGVTQVAVDAIKEKWKSAEIVRLKIEGASALNMRKMHEILEKKTGGLVIWRSGTSISLYRGVSYELPSGKWNKQRREETPPEAVIENHDETTTMVDKSDEKVHLPQLEQETTSVEKKDQTSPVVEYEDELDELLDDLGPRFMDWPGDNPLPVDADLLPGAIPDYEPPFRVLPYGVRSSLGPKEATALRRLARSIPPHFALGRSRQLQGLATAMVRLWEKSMLAKIAIKRGVQSTTSERMAEDLKKLTGGIMLSRNKDFLVFYRGKNFLSREVADALVEQERFVRTLQDEEEQARLRGSSALIVPSTEPANKLVSAGTLGETLDATGKWGKNLDDDDHSDEVKQEVEILRHENLVRKLERKLAFAERKLLKAERGLAKVEVCLKPAEQREDPESITDEERFMFRKLGLKMKAFLLLGRRGVFDGTVENMHLHWKYRELVKIIVKAKTFDGVKKVALALEAESGGILVSIDKVTKGYAIIVYRGQDYKRPTMLRPKNLLTKRKALARSIELQRREGLLKHISTMQAKAKQLRAEIEQMEKVTDKGDEELYNKLDMAYASSDEETDEEDDDDAFPETYAEGEDGEEGEILAGELSETEDKDLDSNESETGFGDDSVLFAEDLHTKSEDLPNKKVRLQHQS
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Binds specific group II introns in chloroplasts and facilitates their splicing. Acts on subgroup IIB introns. The substrates of the subgroup IIB also require the CRM domain proteins CAF1 or CAF2, with a simultaneous binding of CFM3A and CAF1 or CAF2. Required for seed development. May influence the biogenesis of the mitochondrial small ribosomal subunit.
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F4J339
|
RPP1_ARATH
|
Probable disease resistance protein RPP1 (Probable NAD(+) hydrolase RPP1) (EC 3.2.2.6) (Protein RECOGNITION OF PERONOSPORA PARASITICA 1)
|
MGSVMSLGCSKRKATNQDVDSESRKRRKICSTNDAENCRFIQDESSWKHPWSLCANRVISVAAVALTNFRFQQDNQESNSSSLSLPSPATSVSRNWKHDVFPSFHGADVRRTFLSHIMESFRRKGIDTFIDNNIERSKSIGPELKEAIKGSKIAIVLLSRKYASSSWCLDELAEIMKCRQMVGQIVMTIFYEVDPTDIKKQTGEFGKAFTKTCRGKPKEQVERWRKALEDVATIAGYHSHSWRNEADMIEKISTDVSNMLNSFTPSRDFDGLVGMRAHMDMLEQLLRLDLDEVRMIGIWGPPGIGKTTIARFLFNQVSDRFQLSAIMVNIKGCYPRPCFDEYSAQLQLQNQMLSQMINHKDIMISHLGVAQERLRDKKVFLVLDEVDQLGQLDALAKETRWFGPGSRIIITTEDLGVLKAHGINHVYKVEYPSNDEAFQIFCMNAFGQKQPHEGFDEIAWEVTCLAGELPLGLKVLGSALRGKSKREWERTLPRLKTSLDGKIGSIIQFSYDVLCDEDKYLFLYIACLFNGESTTKVKELLGKFLDVKQGLHLLAQKSLISFDGERIHMHTLLEQFGRETSRKQFVHHGFTKRQLLVGARGICEVLDDDTTDSRRFIGIHLELSNTEEELNISEKVLERVHDFHFVRIDASFQPERLQLALQDLIYHSPKIRSLNWYGYESLCLPSTFNPEFLVELDMRSSNLRKLWEGTKQLRNLKWMDLSYSSYLKELPNLSTATNLEELKLRNCSSLVELPSSIEKLTSLQILDLENCSSLEKLPAIENATKLRELKLQNCSSLIELPLSIGTATNLKQLNISGCSSLVKLPSSIGDITDLEVFDLSNCSSLVTLPSSIGNLQNLCKLIMRGCSKLEALPININLKSLDTLNLTDCSQLKSFPEISTHISELRLKGTAIKEVPLSIMSWSPLADFQISYFESLMEFPHAFDIITKLHLSKDIQEVPPWVKRMSRLRDLSLNNCNNLVSLPQLSDSLDYIYADNCKSLERLDCCFNNPEIRLYFPKCFKLNQEARDLIMHTCIDAMFPGTQVPACFIHRATSGDSLKIKLKESPLPTTLRFKACIMLVKVNEELMSYDQTPMIVDIVIRDEHNDLKEKIYPSIYPSIYPLLTEHIYTFELDVEEVTSTELVFEFPQLNKRNWKIGECGILQRETRSLRRSSSPDLSPESSRVSSYDHCLRGD
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TIR-NB-LRR receptor-like protein that confers resistance to the pathogen Hyaloperonospora arabidopsis (By similarity). Probably acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide NAD(+) cleavage triggering a defense system that promotes cell death.
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F4J3N2
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FTSI5_ARATH
|
Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic (AtFTSHI5) (Protein EMBRYO DEFECTIVE 2458) (Protein FTSH INACTIVE PROTEASE 5)
|
MDFISASSLSSPFSTQLSPIYLSSGIVSLKPRHRVKNRNFGSRESNNKSRKIVPIRGCFGFSGSFLRSKQSDYGSEAVSESLRLCGEGNELVLSSEYNSAKTRESVIQFVTKPLVYALFCIAIGLSPIRSFQAPALAVPFVSDVIWKKKKERVREKEVVLKAVDHEFSDYTRRLLETVSVLLKTIEIVRKENGEVAEVGAALDAVKVEKEKLQKEIMSGLYRDMRRLRKERDLLMKRADKIVDEALSLKKQSEKLLRKGAREKMEKLEESVDIMESEYNKIWERIDEIDDIILKKETTTLSFGVRELIFIERECVELVKSFNRELNQKSFESVPESSITKLSRSEIKQELVNAQRKHLEQMILPNVLELEEVDPFFDRDSVDFSLRIKKRLEESKKLQRDLQNRIRKRMKKFGEEKLFVQKTPEGEAVKGFPEAEVKWMFGEKEVVVPKAIQLHLRHGWKKWQEEAKADLKQKLLEDVDFGKQYIAQRQEQVLLDRDRVVSKTWYNEDKSRWEMDPMAVPYAVSRKLIDSARIRHDYAVMYVALKGDDKEFYVDIKEYEMLFEKFGGFDALYLKMLACGIPTSVHLMWIPMSELSLQQQFLLVTRVVSRVFNALRKTQVVSNAKDTVLEKIRNINDDIMMAVVFPVIEFIIPYQLRLRLGMAWPEEIEQTVGSTWYLQWQSEAEMNFKSRNTEDFQWFLWFLIRSSIYGFVLYHVFRFLKRKVPRLLGYGPFRRDPNVRKFWRVKSYFTYRKRRIKQKRKAGIDPIKTAFDRMKRVKNPPIPLKNFASIESMREEINEVVAFLQNPKAFQEMGARAPRGVLIVGERGTGKTSLALAIAAEARVPVVNVEAQELEAGLWVGQSAANVRELFQTARDLAPVIIFVEDFDLFAGVRGKFVHTKQQDHESFINQLLVELDGFEKQDGVVLMATTRNHKQIDEALRRPGRMDRVFHLQSPTEMERERILHNAAEETMDRELVDLVDWRKVSEKTTLLRPIELKLVPMALESSAFRSKFLDTDELLSYVSWFATFSHIVPPWLRKTKVAKTMGKMLVNHLGLNLTKDDLENVVDLMEPYGQISNGIELLNPTVDWTRETKFPHAVWAAGRALITLLIPNFDVVENLWLEPSSWEGIGCTKITKVTSGGSAIGNTESRSYLEKKLVFCFGSHIASQMLLPPGDENFLSSSEITKAQEIATRMVLQYGWGPDDSPAVYYATNAVSALSMGNNHEYEMAGKVEKIYDLAYEKAKGMLLKNRRVLEKITEELLEFEILTHKDLERIVHENGGIREKEPFFLSGTNYNEALSRSFLDVGDPPETALLSAPT
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Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (Probable).
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F4J3R7
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SPD1_ARATH
|
Protein SEEDLING PLASTID DEVELOPMENT 1
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MRALNSRLVLIDINSSWQASRRLISATATAFSSDSSSSFRRTRGARQRIASSKSPASSPSPVRRPSDGFSFDVRSPSSDSSISSRKSPTTAPPTVELDAFLEILPPATRKELVKHEAIEELIEVVMDLGRKPLARFPSGDWVISEQPVTHQDLELAVSKVGDFSDDNRSGIDRSLHRISAIRNRKLQVIGLTCRVGRVVSGSAEIIRDLIEGGGSILVIGSPGVGKTTLIREIARMLADEHRKRVVIVDTSNEIGGDGDVPHSGIGRARRMQVPNVNLQHDVMIEAVENHMPETIIIDEIGTELEALAASTIAQRGVQLVATAHGMTIDNIIKNPSLQILIGGIESVTLGDEEARKRKVQKTILERKGPPTFTCAVEMISRTECRVHQRLDVTVDAILAGKSAPFEIRQIRGEDDVPHKLVTPIPLENLEEEPAPLLNRDFVSELLSDDEDEDFLLIRSNKARSNTYTSPRSSPVHVYTYNVLEADLLQVAEVMGLDDEIEVTDDVGEADVILASSSELKQNSSIRRVAKLHKLPIFVIKSTTMAQMVKAVRMILGRESFGSAPKAIEKSSVDDIEIKDDAPESKPSLEELDALEEVRLAIEYIVIPGGEPVELLPRRSDIIVRQLELVESYQLAVENLGTHLNPRLQILPRRSTKKTLTSSSPQKSADGSMGTTGTRLPFLKD
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Required during eoplast (a highly reduced plastid type present during the degreening and dehydration stages of seed maturation) development in embryos and early stages of eoplast redifferentiation during seedling growth.
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F4J3T8
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MYTM1_ARATH
|
Phosphatidylinositol-3-phosphatase myotubularin-1 (AtMTM1) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
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MTPPRPPSGRVRSLRDYSSESEKMDGTGSWDTLEWTKLDSTSGSGSFSNLSCLLESERVIVEGYGVVLINTDEAGTLLVTNFRILFLSEGTRKVIPLGTIPLATIEKFNKMVLKVQSSPRQSDKIPPRRLLQVTGKDMRIIVYGFRPRTKQRRNVFDALLKCTKPERVWDLYTFACGPSKFGNANPKERLLNEYFRLLGKSSIRASMDMIEDGAFTLSNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLMMNMRSNLDEKLVAAFCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHGTTSSDGRSSFLRHGGWTWGGGNLSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSGNFDFPRQSSSAGSFPSSPVRQSSGSAASQSSSSSHGHNNYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLSCRFGNFLCNSEKEREQCGIADACGCLWAYLTDLRSFSATSHVHCNPFYDPLKYDGPLLPPAASLAPTLWPQFHLRWACPEEAKAADIGVQCRAMTVKYSEMQKEKEAAERRVDEISFAMESLSAELLRERHLSWVARESANRATKEYAALTRAVQSLGCKINFTTSDVEDDPRSSLENNPRRRNRHGNNSDVSVSISLMPEENTSGNPKGRVCEALCPLRTREGVCRWPEVGCAHVGSQFVGLKANFDAFDRLAIYDSYFQPK
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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. Required for recovery after water deprivation, via the accumulation of PtdIns5P upon dehydration high PtdIns5P levels mediate ATX1 cytoplasmic localization, thus down-regulating the expression of ATX1-dependent genes. Confers sensitivity to soil-water-deficit stress.
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F4J4C8
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EVN_ARATH
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Dolichol kinase EVAN (EC 2.7.1.108)
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MKTTATSFVTGERVVVFVVVSRILLSLPLSLISHGFSLFLLSLSAFLVEIRVETSPFLLSHFSSRRGASSGILLGAVTLPSVMISKLVQLSRAISIHEAEQDELAHVTMQYWAASASCCAILIYLSVIMSQVRKDESLSSSSIWLTRVSLTGTVLYGVACFVSLSMISHTGLNTSLKMLWMLFHGLAAVKLIRHLLCTFPSCASIGEALLVTSGLVLYFGDFLACTIAKIFEKLIPVDLVSISYGIKRTETGIIVQGLLLGLLLFPMVFRFVLHIYESSLRKRDARQRNCSDAAKSVLFFVSLLFFMVVAVPSWMQFVHDFNQHPFLWVLTFVFSEPLKRLSLCIYWILLIVVSVSRFYNISRSSKVERILLRKYYHLMAVLMFLPALVLQPKFLDLAFGAALAVFVALEIIRIWRIQPLGEPLHQFMNAFTDHRDSEHLIVSHFSLLLGCALPIWMSSGFNDRALSPFAGILSLGIGDTMASMVGHKYGVLRWSKTGKKTVEGTAAGITSMMAVCFVLVPILASMGYILSQGWWSLLVAVTATGMLEAYTAQLDNAFIPLVFYSLLCL
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Essential for pollen development. Involved in protein N-glycosylation in the endoplasmic reticulum (ER), especially in the female gametophyte. Mediates pollen tube (PT) reception in synergids through protein glycosylation.
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F4J7T2
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EAF1B_ARATH
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Chromatin modification-related protein EAF1 B (ESA1-associated factor 1 B)
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MHGSVSGYLLVNAEVDSMGGVIDSGGGIGVKTSPRRTAIEKAQAELRQEYDVREERRRELEFLEKGGNPLDFKFGIATSHSVQSTSLTDQQAEHFVNSEVKDSFALTASPHGDSVESSGRPGVPTISEPNTADNLLLFDSENKSVEGERNLRHPNRQNRTSESERSSKAHTNQNTKETEDSAIFRPYARRNRSKISRDPARSSSTDLVQNRGGLATSISIRRGSVEGKGCIPEAANQKDMHTTSVSCPVFANSNGNIVPKNRVSSNSLNTKVDGEPVVRESTAGSKTSLLKDEADISYSKSSAYLPVGESGLAGEKAQLVSTGGSPKAATIAGQKNSSTQLNGLRDSTVEEESLTNRGATGTNGLESESSHANNVEVNVDNERDLYKVDKLDSDEISMQKTLRVEGLLDQTVGEMTKTKIEDETGQSTTIISECIPECEMQMKSVKIENQSHRSTAEMQTKEKSSETEKRLQDGLVVLENDSKVGSILSENPSSTLCSGIPQASVDTSSCTVGNSLLSGTDIEALKHQPSSDAVMLDTVKEDAILEEARIIQAKKKRIAELSCGTAPVEVREKSQWDFVLEEMAWLANDFAQERLWKMTAATQICHRVALTCQLRFEERNQHRKLKKIASVLSYAILQFWSSVEAEVPGELEETSLGIVKETCQESNCLNGIRCLAAGVKEYASRFLKYNNSSISYHSAALSTPDNMCDPEILDISMVDQLTEASLFYSVPSGAMEVYLKSIESHLTRCEKSGSSMQEEVDTSAYDTAGDIGYNVTAFDEDEGETSTYYLPGAFESSRSFNISHKKRKNLMKSHSARSYDLGDDLPYVNNTGGSNSSSLIVKRPDSNINAGSVPTRRVRTASRHRVVSPFGCATTGNLPVPSKTDASSGDTSSFQDEYSSLHGGSAVQKGTEVESSVNFEKLLPYDMAETSGKPKKKKKTHQGSAYDQTWHLNPSVHVEQKDHWKKRPENNFDMNGLYGPHSAKKQKTTKQLVENNFDMAIPHTGSIPSPAASQMSNMSNPNKSIKFIGGRDRGRKIKGLKISPGQHGSGNPWSLFEDQALVVLVHDMGPNWELISDAMNSTLKIKYIYRNPTECKDRHKILMDKTAGDGADSAEDSGNSQSYPSTLPGIPKGSARQLFQRLQGPMEEDTLKSHFEKICLIGKKLHYRKTQNDGRDPKQIVPVHNSQVMALSQVFPNNLNGGVLTPLDVCDASTSGQDVFSLENPGLPMLNQGTPVLPTSGAHPSTPGSSGVVLSNNLPTTSGLQSASVRDGRFNVPRGSLPLDEQHRLQQFNQTLSGRNLQQPSLSTPAAVSGSDRGHRMVPGGNAMGVSGMNRNTPMSRPGFQGMASAAMPNTGNMHTSGMVGIPNTGNIHSGGGASQGNSMIRPREAVQHMMRMQAAQGNSPGIPAFSNLSSGFTNQTTPVQAYPGHLSQQHQMSPQSHVLGNSHHPHLQSPSQATGAQQEAFAIRQRQIHQRYLQQQQQQFPASGSMMPHVQQPQGSSVSSSSQNSPQTQPPVSPQPLSMPPVSPSPNINAMAQQKPQKSQLALHGLGRSPQSGTSGVNNQAGKQRQRQLQQSARQHPHQRQPTQGQQLNKQLKGMGRGNMIHQNITVDQSHLNGLTMPQGNQATEKGEIAVSVRPDQQSSVGTTTSTDLQSKPFVSPLSSNHSQQLPKSFPGALSPSPQQQMQLHSDNSIQGQSSPATPCNILSTSSLSIAPAVAPSNHQHLLIHQKQRNQVQSTAQRVVQHNHLGNSELSKKSQAECMPRVPQSVTNTTQTASMGTTKGMPQASNDLKNIKAVGSTAVPALEPPSCVASVQSTASKVVNNSNTDSAGNDPVSTPNQGLAQKHGIKGVTQRQQQSLPSEEKRPKLPEKPTVQNQKHLASEEQPHLEEAQELSSSKPPDTKVE
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Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. {ECO:0000269|Ref.3}.
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F4J7T3
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EAF1A_ARATH
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Chromatin modification-related protein EAF1 A (ESA1-associated factor 1 A)
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MHGSVSGYLLVNAEVDSMGGVIDSGGGIGVKTSPRRTAIEKAQAELRQEYDVREERRRELEFLEKGGNPLDFKFGIATSHSVQSTSLTDQQAEHFVNSEVKDSFALTASPHGDSVESSGRPGVPTISEPNTADNLLLFDSENKSVEGERNLRHPNRQNRTSESERSSKAHTNQNTKETEDSAIFRPYARRNRSKISRDPARSSSTDLVQNRGGLATSISIRRGSVEGKGCIPEAANQKDMHTTSVSCPVFANSNGNIVPKNRVSSNSLNTKVDGEPVVRESTAGSKTSLLKDEADISYSKSSAYLPVGESGLAGEKAQLVSTGGSPKAATIAGQKNSSTQLNGLRDSTVEEESLTNRGATGTNGLESESSHANNVEVNVDNERDLYKVDKLDSDEISMQKTLRVEGLLDQTVGEMTKTKIEDETGQSTTIISECIPECEMQMKSVKIENQSHRSTAEMQTKEKSSETEKRLQDGLVVLENDSKVGSILSENPSSTLCSGIPQASVDTSSCTVGNSLLSGTDIEALKHQPSSDAVMLDTVKEDAILEEARIIQAKKKRIAELSCGTAPVEVREKSQWDFVLEEMAWLANDFAQERLWKMTAAAQICHRVALTCQLRFEERNQHRKLKKIASVLSNAILQFWSSVEAEVPGELEETSLGIVKETCQESNCLNGRRCLAAGVKEYASRFLKYNNSSISYHSAAPSTPDNMCDPEILDISMVDQLTEASLFYSVPSGAMEVYLKSIESHLTRCEKSGSSMQEEVDTSAYDTAGDIGYNVTAFDEDEGETSTYYLPGAFESSRSFNISHKKRKNLMKSHSARSYDLGDDLPYVNNTGGSNSSSLMAKRPDSNINAGSVPTRRVRTASRQRVVSPFGCATTGNLPVPSKTDASSGDTSSFQDEYSSLHGGSAVQKGTEVESSVNFEKLLPYDMAETSGRPKKKKKTHQGSAYDQTWHLDPSVHVEQKDHWKKRPENNFDMNGLYGPHSAKKQKTTKQLVENNFDMAIPHTGSIPSPAASQMSNMSNPNKSIKFIGGRDRGRKIKGLKISPGQHGSGNPWSLFEDQALVVLVHDMGPNWELISDAMNSTLKIKCIYRNPTECKDRHKILMDKTAGDGADSAEDSGNSQSYPSTLPGIPKGSARQLFQRLQGPMEEDTLKSHFEKICLIGKKLHYRKTQSVIGVSVVSFVHGIQFSSCTGAGISQSLDIPGLHVSKYSCKSWLGFPENDGRDSKQIVPVHNSQVMALSQVFPNNLNGGVLTPLDVCDASTSGQDVFSLENPGLPMLNQGTPVLPTSGAHPSTPGSSGVVLSNNLPTTSGLQSASVRDGRFNVPRGSLPLDEQHRLQQFNQTLSGRNLQQPSLSTPAAVSGSDRGHRMVPGGNAMGVSGMNRNTPMSRPGFQGMASSAMPNTGSMLSSGMVEIPNTGNIHSGGGASQGNSMIRPREAVQHMMRMQAAQGNSPGIPAFSNLSSGFTNQTTPVQAYPGHLSQQHQMSPQSHVLGNSHHPHLQSPSQATGAQQEAFAIRQRQIHQRYLQQQQQQQQFPASGSMMPHVQQPQGSSVSSSPQNSPQTQPPVSPQPLSMPPVSPSPNINAMAQQKPQKSQLALHGLGRSPQSGTSGVNNQAGKQRQRQLQQSARQHPHQRQPTQGQQLNKQLKGMGRGNMIHQNITVDQSHLNGLTMPQGNQATEKGEIAVPVRPDQQSSVGTTTSTNLQSKPFVSPLSSNHSQQLPKSFPGALPPSPQQQMQLHSDNSIQGQSSPATPCNILSTSSPSIAPAVAPSNHQHLLIHQKQRNQVQSTAQRVVQHNHLGNSELSKKSQAERMPRVPQSVTNTTQTVSMGTTKGMPQASNDLKNIKAVGSTAVPALEPPSCVASVQITASKVVNSSNTDSAGNDPVSTPNQGLAQKHGIKGVTQRQQQSLPSEEKRPKLPEKPTVQNQKHLASEEQPHLEEAQELSSSKPPDTKVE
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Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. {ECO:0000269|Ref.3}.
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F4J8C6
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VIP1L_ARATH
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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP1 (EC 2.7.4.24) (Probable protein QUANTITATIVE VITAMIN E-7) (Protein VIP HOMOLOG 2) (VIP1 homolog protein 1) (Arabidopsis homolog protein of yeast VIP1 1) (AtVIP1)
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MEMEEGASGVGEKIKIGVCVMEKKVFSAPMGEILDRLQSFGEFEILHFGDKVILEDPIESWPICDCLIAFHSSGYPLEKAQAYAALRKPFLVNELDPQYLLHDRRKVYEHLEMYGIPVPRYACVNRKVPNQDLHYFVEEEDFVEVHGERFWKPFVEKPVNGDDHSIMIYYPSSAGGGMKELFRKIGNRSSEFHPDVRRVRREGSYIYEEFMATGGTDVKVYTVGPEYAHAEARKSPVVDGVVMRNTDGKEVRYPVLLTPAEKQMAREVCIAFRQAVCGFDLLRSEGCSYVCDVNGWSFVKNSYKYYDDAACVLRKMCLDAKAPHLSSTLPPTLPWKVNEPVQSNEGLTRQGSGIIGTFGQSEELRCVIAVVRHGDRTPKQKVKLKVTEEKLLNLMLKYNGGKPRAETKLKSAVQLQDLLDATRMLVPRTRPGRESDSDAEDLEHAEKLRQVKAVLEEGGHFSGIYRKVQLKPLKWVKIPKSDGDGEEERPVEALMVLKYGGVLTHAGRKQAEELGRYFRNNMYPGEGTGLLRLHSTYRHDLKIYSSDEGRVQMSAAAFAKGLLDLEGQLTPILVSLVSKDSSMLDGLDNASIEMEAAKARLNEIVTSGTKMIDDDQVSSEDFPWMTDGAGLPPNAHELLRELVKLTKNVTEQVRLLAMDEDENLTEPYDIIPPYDQAKALGKTNIDSDRIASGLPCGSEGFLLMFARWIKLARDLYNERKDRFDITQIPDVYDSCKYDLLHNSHLDLKGLDELFKVAQLLADGVIPNEYGINPQQKLKIGSKIARRLMGKILIDLRNTREEALSVAELKESQEQVLSLSASQREDRNSQPKLFINSDELRRPGTGDKDEDDDKETKYRLDPKYANVKTPERHVRTRLYFTSESHIHSLMNVLRYCNLDESLLGEESLICQNALERLCKTKELDYMSYIVLRLFENTEVSLEDPKRFRIELTFSRGADLSPLRNNDDEAETLLREHTLPIMGPERLQEVGSCLSLETMEKMVRPFAMPAEDFPPASTPVGFSGYFSKSAAVLERLVNLFHNYKNSSSNGRS
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Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Probably involved in vitamin E homeostasis via the regulation of gamma-tocopherol biosynthesis. Catalyzes the conversion of InsP7 to InsP8. Regulates jasmonic acid (JA) perception and plant defenses against herbivorous insects (e.g. P.rapae) and necrotrophic fungi (e.g. M.brassicae, B.cinerea and A.brassicicola) by triggering the production of jasmonate-induced pools of InsP8 and subsequent activation of SCF(COI1) E3 ubiquitin ligase complexes with JAZ proteins (e.g. TIFY10A/JAZ1).
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F4J8D3
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TPLAT_ARATH
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Protein TPLATE
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MDILFAQIQADLRSNDALRQSSALLQALQQSAAGRDISVIAKSAVEEIVASPASAVCKKLAFDLIRSTRLTPDLWDTVCSGVKTDLHFPDPDVTAAAVSILAALPAFSLPKLISDCSSEIASCFDSPSDNLRFSITETLGCILARDDLVTLCENNVGLLDKVSNWWARIGQNMLDKSDAVSKVAFESVGRLFQEFDSKRMSRLAGDKLVDSENSLAIRSKWVSSMVDIVWRKRSALMARSLVLPVETFRATVFPLVFAVKAVASGSVEVIRQLSKASSAAAAANATVVDSNAEKLVGVSDLVTHLAPFLASSLDPALIFEVGINMLYLADVAGGKPEWASQSIIAILTLWDRQEFSSARESIVRAVVTNLHLLDLHMQVSLFRRLLLMVRNLRAESDRMHALACICRTALCVHLFARESARRGQKPLPGTDIISLFEDARIKDDLNSVTSKSLFREELVAMLVESCFQLSLPLPEQKNSGMESRVIGALAYGTGYGALNWTEPALEVVEVCRPCVKWDCDGRTYAVDCYLKLLVRLCHIYDTRGGVKRLKDGASQDQILNETRLQNLQRELVKDLQEVNTPRILGRLIWTIAEHIDLEGLDPLLADDPDDPLNIIIANIHKVLFNLDAAATTSNRLQDVQAVLLCAQRMGSRHARAGQLLTKELEEYRNHAAADTVSKHQTRLILQRIKYVSNLPERKWAGVSETRGDYPFSHHKLTVQFYEPSAAQDRKLEGLIHKAILELWRPKPTELTLFLTKGVDSTSIKVPPTAYPLTGSSDPCYIEAYHLADTNDGRVTLHLKIINLTELELNRVDIRVGLSGALYFMDGSPQAVRQLRNLVSQDPVQCSVTVGVSQFERCGFWVQVLYYPFRGARGEYDGDYIEEDPQIMKQKRGSKAELGEPVILRCQPYKIPLTELLLPHKISPVEFFRLWPSLPAVAEYTGTYMYEGSGFMATAAQQYGASPFLSGLKSLSSKPFHRVCSHIIRTVAGFQLCYAAKTWHGGFVGMMIFGASEVSRNMDLGDETTTMMCKFVVRASEASITKQIESDIQGWCDDLTDGGVEYMPEDEVKATAAEKLKISMERIALLKAAQPKKTSKIEEESENEEEEEGEEEDDDEEVKEKKEKEEGKDKEEKKKKEKEKGTFSKLTAEETEHMALQAAVLQEWHILCKDRKYTKVN
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Functions in vesicle-trafficking events required for site-specific cell wall modifications during pollen germination and for anchoring of the cell plate to the mother wall at the correct cortical position.
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F4J8G7
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VIR_ARATH
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Protein virilizer homolog (Protein EMBRYO DEFECTIVE 2016)
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MVRSEPCVLFAQTFVHPQLDEYVDEVIFAEPVIITACEFLEQNASSSSQAVSLVGATSPPSFALEVFVRCEGESKFKRLCNPFLYTPSAPYPLEVEAVVTNHLVVRGSYRSLSLIVYGNIVKDLGQYNIILEGRSVTDIVSSTEGNLEDLPLVLHSVNRTIEECLSSLDIVSLPLAAVDLPVEVKRLLQLLLKIFDKLATNDVVNKFVDTVVSGVSSYVTDNVDFFLKNKNCSAVTSSLDSGLFHDIVDRVKEDILDLNEIQESDVALGLFSFLESETYLATSQQLVVMLSPYIQFERDSLCTVLPKLSKGKATLLGLSLAFLLCSGREGCLQFVNSGGMDQLVYLFGHDGQNSTTITLLLLGVVEQATRHSVGCEGFLGWWPREDGSIPSGKSEGYCLLLKLLMQKPCHEIASLAIYILRRLRIYEVISRYEFAVLSALEGLSNSHGAATHNLNMLSDAKSQLQKLQNLMKSLGSVEDPSPSAYAERSLVSDHSEGWLSYKATSKLTSSWTCPFYSSGIDSHILALLKERGFLPLSAALLSMPELHSKVGDIMDVFTDIAMFIGNIILSFMFSRTGLSFLLHHPELTATIIQSLKGSVDLNKEECVPLHYASILISKGFTCSLLEIGINLEMHLRVVSAVDRLLKSIQQTEEFLWILWELRDVSRSDCGREALLTLGVFPEALAVLIEALHSAKDMEPAVENSGISPLNLAICHSAAEIFEVIVSDSTASCLHAWIEHAPVLHKALHTLSPGGSNRKDAPSRLLKWIDAGVVYHKHGVGGLLRYAAVLASGGDAQLSSSSILALDLTPAENGAGESTNVSEMNVLDNLGKVIFEKSFEGVNLSDSSISQLTTALRILALISDNSTVAAALYDEGAVTVVYAILVNCSFMFERSSNIYDYLVDDDHGCSSISDFLSERNREQSLVDLLIPSLVLLISVLQRLQGTKEQYRNTKLMKALLRLHREVSPKLAACAADLSSHYPDSALGFGAVCHLIVSALVCWPVYGWIPGLFHTLLSGVQTSSVPALGPKETCSFLCILSDILPEEGVWFWKSGMPLLSGLRKLAVGTLMGPQKEKQINWYLEPGPLEKLINHLTPNLDKIAKIIQHHAVSALVVIQDMLRVFIVRIACQRVEHASILLRPIFSSIRDGILDQSSTRDTEAYMVYRYLNFLASLLEHPHAKGLLLEEGIVQLLVEVLERCYDATYPSENRVLEYGIVSASSVIQWCIPAFRSISLLCDSQVPLLCFQKKELLASLSAKDCALIFPFVLKFCQVLPVGNELLSCLGAFKDLSSCGEGQDGLVSLLFHLFSGTEESVSERWCDTNSLSLDQLDMKKNPPFLSCWIKLLNSINSKDGLSSLAMKAVNVLSVGSIRLCLDGKSLDSKKVAALKSLFGLPSEFSGTDTFREENIGLIEQMVTLLSSMTSGSDSSATAEMKPYLHEASQSLLSLLKDGNIDDIISCKGVFVSPGNLDMDDLVSRNIEDDLYQRGLEDKFWWECPETLPERLPQSSLPAKRKLPTLESSSRRAKGENSSVDIPTQNSIQRGMGSVSLPPAPTRRDAFRQRKPNTSRPPSMHVDDYVARERSVDTAGNSNAITISRAGSSSGRPPSIHVDEFMARQRERGQNPSTIVVGEAVVQVKNPTPARDTEKVAGKPKQFKADPDDDLQGIDIVFDGEECEGPDDKLPFLQPDENLMQPAPVMVEQNSPHSIVEETESDANGSSQFSHMGTPVASNVDENAQSEFSSRISVSRPEMSLIREPSISSDRKFVEQADEAKKMAPLKSAGISESGFIPAYHMPGSSGQNSIDPRVGPQGFYSKSGQQHTGHIHGGFSGRGVYEQKVMPNQPPLPLVPPPSVSPVIPHSSDSLSNQSSPFISHGTQSSGGPTRLMPPLPSAIPQYSSNPYASLPPRTSTVQSFGYNHAGVGTTEQQQSGPTIDHQSGNLSVTGMTSYPPPNLMPSHNFSRPSSLPVPFYGNPSHQGGDKPQTMLLVPSIPQSLNTQSIPQLPSMQLSQLQRPMQPPQHVRPPIQISQPSEQGVSMQNPFQIPMHQMQLMQQTQVQPYYHPPQQQEISQVQQQQQHHAVQGQQGAGTSQQQESGMSLHDYFKSPEAIQALLSDRDKLCQLLEQHPKLMQMLQEKLGQL
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Subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs. Associates with MTA, MTB, FIP37 and HAKAI to form the m6A writer complex which is essential for adenosine methylation at specific mRNA sequences. N6-methyladenosine (m6A) plays a role in mRNA stability, processing, translation efficiency and editing.
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F4J9M5
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CHR12_ARATH
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Probable ATP-dependent DNA helicase CHR12 (EC 3.6.4.12) (Protein CHROMATIN REMODELING 12) (AtCHR12) (Protein MINUSCULE 1)
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MVAQQLQERCGGTSQEDPVETTKSLICALNYISRDLPLPPHLFTAVSSIYHGASSSSLSDSDVSPPLPTSPPANKAPYGADLMGEFEDALLKQRPDCESGSRLIQLLDNRNKSHIQRRLSELEELPSTRGEDLQAKCLLELYGLKLRELQGKVRTAVSSEFWLRLNCADVSSQVFDWGMMRLPRPFYGVGDPFAMEADDQFRKKRDAERLSRLEEEEKNLIETAKRKFFAEVLNAVREFQLQIQATQKRRRQRNDGVQAWHGRQRQRATRAEKLRLMALKSDDQEAYMKLVKESKNERLTTLLEETNKLLANLGAAVQRQKDAKLPEGIDLLKDSESDLSELDAPRSEPLQDLLPDQDIDITESDNNDDSNDLLEGQRQYNSAIHSIQEKVTEQPSLLEGGELRSYQLEGLQWMVSLFNNNLNGILADEMGLGKTIQTISLIAYLLENKGVPGPYLIVAPKAVLPNWVNEFATWVPSIAAFLYDGRLEERKAIREKIAGEGKFNVLITHYDLIMRDKAFLKKIEWYYMIVDEGHRLKNHESALAKTLLTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSVQNFEEWFNAPFADRGNVSLTDEEELLIIHRLHHVIRPFILRRKKDEVEKFLPGKTQVILKCDMSAWQKVYYKQVTDMGRVGLQTGSGKSKSLQNLTMQLRKCCNHPYLFVGGDYNMWKKPEIVRASGKFELLDRLLPKLRKAGHRILLFSQMTRLIDVLEIYLTLNDYKYLRLDGTTKTDQRGLLLKQFNEPDSPYFMFLLSTRAGGLGLNLQTADTVIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSVGSVEEVILERAKQKMGIDAKVIQAGLFNTTSTAQDRREMLEEIMRKGTSSLGTDVPSEREINRLAARSEDEFWMFERMDEERRRKENYRARLMQEQEVPEWAYTTQTQEEKLNNGKFHFGSVTGKRKRKEIVYSDTLSELQWLKAVESGEDLSKLSMRYNRREENASNTKTSTSKKVIESIQTVSDGTSEEDEEEQEEERAKEMSGKQRVDKSEEEEEEGEEENDGKAIFKWNTHKKKRSRYSFTCSSSDSRAQSSNGSRRK
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Probable chromatin-remodeling factor that is functionally redundant with CHR23 in root and shoot stem cell initiation, and root apical meristem (RAM) and shoot apical meristem (SAM) maintenance. Plays an important role in mediating the temporary plant growth arrest induced upon perception of stress. May promote seed maturation and repress initiation of germination.
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F4JAA5
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SKI2_ARATH
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DExH-box ATP-dependent RNA helicase DExH11 (EC 3.6.4.13) (AtHELPS) (Protein SKI2 homolog) (AtSKI2)
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MNKVEAGNELGFRVGFSGHGGHLRVEPFYTAERDDALNSLPDFVSPPAFAKETKESIKKHIEEKYLIPRLEPDQFSAEKAENQWDFDWFSRVKMPLQPSLPRSVVVPTWELPFRRQKEDTENGAWEPKSVEVDLSEQMYGDQDSGFFPRMVGPPKDFLRGSVNNRPFRPGGLEDSQSSERVLPEGVSSGQWVQELLNGGPAQTVPPSFKQSLDLGDLMPYPQTWSVYEDHSSHGNASDENSSKLSIQFDDLFKKAWEEDTFSELEGDDHTAGSESPKAEAEPDAKASISNEVSKGLETDVTVLDEILSSAKTAIMSEEAVTGSSDKQLRKEGWATKGDSQDIADRFYELVPDMAIEFPFELDNFQKEAICCLEKGESVFVAAHTSAGKTVVAEYAFALATKHCTRAVYTAPIKTISNQKYRDFCGKFDVGLLTGDVSIRPEASCLIMTTEILRSMLYRGADIIRDIEWVIFDEVHYVNDVERGVVWEEVIIMLPRHINFVLLSATVPNTFEFADWIGRTKQKEIRVTGTTKRPVPLEHCLFYSGELYKVCENEVFLSKGIKDAKDSQKKKNSNAVSVAPKQQMGSSAHQDGSKSQKHEAHSRGKQNKHSSVKDVGKSSYSGNSQNNGAFRRSAASNWLLLINKLSKMSLLPVVVFCFSKNYCDRCADALTGTDLTSSSEKSEIRVFCDKAFSRLKGSDRNLPQVLRLQSLLHRGIGVHHAGLLPIVKEVVEMLFCRGVIKVLFSTETFAMGVNAPARTVVFDALRKFDGKEFRQLLPGEYTQMAGRAGRRGLDKTGTVVVMCRDEVPDESDLRRVIVGSATRLESQFRLTYIMILHLLRVEELKVEDMLKRSFAEFHAQKKLPEKQQLLMIKRSLPTKHIECIKGEPAIEDYYDMYMEANEYNNKMSEAVMQSPYAQSFLVQGRVVVMKSGMGIDNLLGIVLKGPSNTNRQYVVLVIKSEIPPPEKNMVSIGKKSSDPSQGYFIAPKSKRGFEEEFYTKPSSRKGPVVIKIELPYHGVAAGVGYEVKGFDNKEFLCICDSKIKIDQVRLLEDGNKAAFSQTVQQLLDLKSDGNKFPPALDPVKDLKLKDAELVETYYKWTNLLQKMSMNKCHGCVKLEEHMKLAREIKKHKTDLKDLEFQMSDEALLQMPAFQGRIDVLKNIGCIDDDLVVQIKGRVACEMNSGEELICTVCLFENQFEELEPEEAVAIMSAFVFQQKNTSAPTLTPKLAKAKQRLYDTAIRLGELQAQYNLQIDPEEYAQENLKFGLVEVVYEWAKGTPFAEICELTDVPEGLIVRTIVRLDETCREFKNAAAIMGNSALHKKMDAASNAIKRDIVFAASLYVTGV
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Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). Involved in the regulation of potassium deprivation stress response.
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F4JAU3
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P4H2_ARATH
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Prolyl 4-hydroxylase 2 (AtP4H-2) (AtP4H2) (EC 1.14.11.2)
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MSMSRLGLLLFVAILLVLLQSSTCLISSPSSIINPSKVKQVSSKPRAFVYEGFLTDLECDHLISLAKENLQRSAVADNDNGESQVSDVRTSSGTFISKGKDPIVSGIEDKLSTWTFLPKENGEDLQVLRYEHGQKYDAHFDYFHDKVNIARGGHRIATVLLYLSNVTKGGETVFPDAQEFSRRSLSENKDDLSDCAKKGIAVKPKKGNALLFFNLQQDAIPDPFSLHGGCPVIEGEKWSATKWIHVDSFDKILTHDGNCTDVNESCERWAVLGECGKNPEYMVGTPEIPGNCRRSCKAC
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Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins. Has low affinity for the substrates tested in vitro.
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F4JBX1
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RGF10_ARATH
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Root meristem growth factor 10 (AtRGF10) (CLAVATA3/ESR (CLE)-related protein CLELn) (AtCLELn) (Nuclear CLE-Like protein) [Cleaved into: CLELn]
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MDMLRSACFYFLLIVFVILSWSLLCDSRHLGHMEKKLSVNLDLLNKDNEEITKLEAPSTNKTNTLLSQSHAVVNHGDNGQINGKKTKEIHRVKRASDKKVSSKRVSRTWKIPKYPKKQPKSDQEHPGFNLDYMQPTTHPPHHN
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[CLELn]: Maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT), mainly at the post-transcriptional level (By similarity). Promotes root elongation.
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F4JCB2
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CPL5_ARATH
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RNA polymerase II C-terminal domain phosphatase-like 5 (FCP-like 5) (EC 3.1.3.16) (Carboxyl-terminal phosphatase-like 5) (AtCPL5) (CTD phosphatase-like 5)
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MFVAKNLSPERESKRQKKEPEIMEPSFPLLSPNNCGHWYIRYGFCIVCKSTVDKTIEGRVFDGLHLSSEALALTKRLITKFSCLNMKKLHLVLDLDLTLIHSVRVPCLSEAEKYLIEEAGSTTREDLWKMKVRGDPISITIEHLVKLRPFLCEFLKEANEMFTMYVYTKGTRPYAEAILKLIDPKKLYFGHRVITRNESPHTKTLDMVLADERGVVIVDDTRKAWPNNKSNLVLIGRYNYFRSQSRVLKPHSEEKTDESENNGGLANVLKLLKGIHHKFFKVEEEVESQDVRLTMSVVENFSSEPKAKRRKIEPTINESSSSLSSSSSCGHWYICHGICIGCKSTVKKSQGRAFDYIFDGLQLSHEAVALTKCFTTKLSCLNEKKLHLVLDLDHTLLHTVMVPSLSQAEKYLIEEAGSATRDDLWKIKAVGDPMEFLTKLRPFLRDFLKEANEFFTMYVYTKGSRVYAKQVLELIDPKKLYFGDRVITKTESPHMKTLDFVLAEERGVVIVDDTRNVWPDHKSNLVDISKYSYFRLKGQDSMPYSEEKTDESESEGGLANVLKLLKEVHQRFFRVEEELESKDVRSLLQEIDFELNVESVE
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Mediates the dephosphorylation of 'Ser-2' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II. Regulates positively abscisic acid (ABA) and drought responses, including the regulation of specific genes expression.
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F4JCC1
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PR40B_ARATH
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Pre-mRNA-processing protein 40B (AtPRP40b)
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MANNHQYPGIQPFQHPNASSIDLPRGFAPPMNFQFLPTIQAPQSEQVARLSSQNFQCVGRGGTVLSIGYPPQSYAPQLLQSMHHSHERPSQLNQVQVQHVPLGPPTLISQPNVSIASGTSLHQPYVQTPDIGMPGFGGPRALFSYPSATSYEGSRVPPQVTGPSIHSQAQQRASIIHTSAESSIMNPTFEQPKAAFLKPLPSQKALTDWVEHTSADGRKYFFNKRTKKSTWEKPVELMTLFERADARTDWKEHSSPDGRKYYYNKITKQSTWTMPEEMKIVREQAEIASVQGPHAEGIIDASEVLTRSDTASTAAPTGLPSQTSTSEGVEKLTLTSDLKQPASVPGSSSPVENVDRVQMSADETSQLCDTSETDGLSVPVTETSAATLVEKDEISVGNSGDSDDMSTKNANQGSGSGPKESQKPMVESEKVESQTEEKQIHQESFSFNNKLEAVDVFKSLLKSAKVGSDWTWEQAMREIINDKRYGALRTLGERKQAFNEFLLQTKRAAEEERLARQKKLYEDFKRMLEECVELTPSTRWSKTVTMFEDDERFKALEREKDRRNIFEDHVSELKEKGRVKALEDRKRNIIEYKRFLESCNFIKPNSQWRKVQDRLEVDERCSRLEKIDQLEIFQEYLRDLEREEEEKKKIQKEELKKVERKHRDEFHGLLDEHIATGELTAKTIWRDYLMKVKDLPVYSAIASNSSGATPKDLFEDAVEDLKKRDHELKSQIKDVLKLRKVNLSAGSTFDEFKVSISEDIGFPLIPDVRLKLVFDDLLERAKEKEEKEARKQTRQTEKLVDMLRSFKDITASSSWEELKHLVEGSEKCSTIGDESFRKRCFEDYVSLLKEQSNRIKQNKKVPEDVREEHDKGRDKYGREKDRVRERDSDDHHKKGAAGKYNHDMNEPHGKERRRSGRDSHNRHRERHTSVKENDTDHFKESHKAGGGHKKSRHQRGWVSEAEVEGKEKRRRKEEAREHTKEEELEDGECGRY
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Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries. May be involved in pre-mRNA splicing (Probable).
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F4JCN9
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PRE4_ARATH
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Transcription factor PRE4 (Basic helix-loop-helix protein 161) (AtbHLH161) (bHLH 161) (Protein BANQUO 3) (Protein PACLOBUTRAZOL RESISTANCE 4) (bHLH transcription factor bHLH161)
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MSSRKSRSRQTGASMITDEQINDLVLQLHRLLPELANNRRSGKVSASRVLQETCSYIRNLSKEVDDLSERLSQLLESTDSAQAALIRSLLMQ
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Atypical and probable non DNA-binding bHLH transcription factor that integrates multiple signaling pathways to regulate cell elongation and plant development. Regulates light responses by binding and inhibiting the activity of the bHLH transcription factor HFR1, a critical regulator of light signaling and shade avoidance. May have a regulatory role in various aspects of gibberellin-dependent growth and development.
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F4JCU0
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SUA_ARATH
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SUPPRESSOR OF ABI3-5 (REQUIRED FOR SNC4-1D protein 1) (Splicing factor SUA)
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MDPSRYGRQQEWDNNSAPEGYGTQHDPNHRFGVSYDDGYPDERLMRDDVYNYPPGHNTLGDLPQSRKRNYEENYPSELRRQEKPYIDSNYAADYYHDSEAGSRNGHYRDHEHERSSRYDGCDDYSCNDNNYRSKNYHHSRDDGREKDYDYTRRSYDSEYERASVRDGSRKSRDPQDRERNSRDREWDSRDREWDKRCYSRERDESPHKRYEKSRSRSTGRGEFSRSRSPRGRSHGRSYREDSYEGDHWNESERRREYEDRHNQDHFSATPSATVVVKGLSMKSTEEDLYQILAEWGPLHHVRVIREQNSGISRGFAFIDFPTVDAARTMMDRIEHDGIVLDGRKLMFHYSQPTGRAGVSRRQEHASRRSYGGSRNMIVPTDWICTICGCINFARRTSCFQCNEPKTKDSPSADVGLSNSAAGKRISETGPTHVLVVRGLDEDADEEMLRYEFSKHAPIKDLRLVRDKFTHVSRGFAFVHFYSVEDATKALEATNRTALERNGKILRVAYAKSVHGSGTGISAPSHSNNLAAAAIEAATFSQQYDGVGWAPKEYNTGEKQNTGGQAQGVGEIESQKGTSAPQSGYVWDEASGYYYDAASGYYYDGNSGLYYDSNSGLWYSYDQQTQQYVPCPDQNNESKVTENQPDSAKKEKSSQQKVIISAATTPNVEKVLSLPDAVQAAAAAAIASEKREKERVKEIKLASKTSLLASKKKMSNVLTMWKQRSHETQIQRPSPSLGDNPPTVSAEARSSFSTGQSMGKLKSDVIIAKERSTSNHGVSALTTAESSSSSTTGGTLMGVMRGSFGGTLGGASSSASVQMPPILPSASPASVSVSGSGRRRFSETPTAGPTHREQPQTSYRDRAAERRNLYGSSTSSGNDVIDSSEDLMGLRKGSSDPTPFPPGVGGRGITTSTEVSSFDVITEERAIDESNVGNRMLRNMGWHEGSGLGKDGSGMKEPVQAQGVDRRAGLGSQQKKVDAEFEVQPGDTYRTLLHKKALARFRDMSDNN
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Splicing factor that controls alternative splicing of the developmental regulator ABI3. Reduces splicing of a cryptic intron in ABI3, leading to a decreased in ABI3-beta transcript. Regulates the splicing of the receptor-like kinase SNC4/LRKL-2.6.
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F4JCX9
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LNK2_ARATH
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Protein LNK2 (Night light-inducible and clock-regulated 2)
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MFDWEEEELTNMIWGDDAETGDHIVPFKVRSEQLNKKEQIEESKTAEQKITGTKIDLHDKNLGSSSSHNVDEGLPQPDFCMSSWPDTSLTNATKVDQDLSATELSKCLAEPVRYDSTRGGAFLLKQSCFTWVRSFQSNHFKSCVLTLFLPEKTSELGKGPDIFHSSDESKEQGDFDDYSWANIGSFDDLDRMFSDGFAAMMSLYLVMAVSAVVMSYGHLLKITEFEQQENQQFPLTGKANGLSSQSVPSVRVTLKADQYREHKGQPSVEDQPYQQNKMMKFSKMPGTSEARPFQELYGQRIPFSNSAGKCVNQLAPPQSSLMAVNLLSESEGSGTSHYSHMPNQYMANSAFGNLANPYSSVPVISAVQHPDVRNQLMHPSYNPATATSVNMATDASARPSTMTPQEKLEKLRRRQQMQAMLAIQRQQQQFSHQVPVADQSITQNCLQDIPLQLVDKTNLQGLTAMPSFDPSSSLEQDDSGKFAAAVDNSAEFAVLYRLQDVVAKLDMGTRTCIRDSLFRLAGSAAQRHYTSDTSHSNKTSQDDQEVIPREESRYRYAGMPDTEAVTNPTDRTVAHLLFHRPFDMLAAKRMEGPESPASSKMGTEEKGNFPKCSIRETHLTKQKAQKEEGPADSLALGNAPNSGSSSTVGERVVEASQGNKRKL
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Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1. Antagonizes REV8 function in the regulation of anthocyanin accumulation. Involved in red light input to the clock. Activates clock-controlled genes with afternoon peak. Mediates light inhibition of hypocotyl elongation. Unable to bind to DNA, but recruited to the evening element (EE)-containing region of the PRR5 and TOC1 promoters through its interaction with the DNA binding proteins REV8 and REV4.
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F4JEI8
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NAP1D_ARATH
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Nucleosome assembly protein 1;4 (AtNAP1;4) (Nucleosome/chromatin assembly factor group A4)
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MSNEENIKSDNKSGDSSDLPTIPALDIGAEECDLLAELKNLTLKRPFDVKKLSPKVTKRVLFLKDIQVTHDELEEKFLAEKSALEATYDNLYKPLFAKRYEIVNGVVEAEAEKEGVPNFWLIAMKTNEMLANEITERDEAALKYLKDIRSCRVEDTSRNFKLEFLFDSNLYFKNSVLSKTYHVNDEDGPVLEKVIGTDIEWFPGKCLTHKVVVKKKTKKGPKKVNNIPMTKTENCESFFNFFKPPEIPEIDEVDDYDDFDTIMTEELQNLMDQDYDIAVTIRDKLIPHAVSWFTGEALVDEDDSDDNDDDDNDEKSD
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May modulate chromatin structure by regulation of nucleosome assembly/disassembly.
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F4JEP5
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MSH5_ARATH
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DNA mismatch repair protein MSH5 (AtMSH5) (MutS protein homolog 5)
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MEEMEDTETEPQVYMACIQHGRRVGVSYYDCSVRQLHVLEFWEEDCSDFTLINMVKYQAKPSIIYASTKSEESFVAALQQNDGTDETTMVKLVKSSTFSYEQAWHRLVYLRVTGMDDGLNIKERICYLSSMMDVGSEVQVRVSGGLLAILESERIVETLEQNESGSASIAIDSVMEVPLNKFLKLDAAAHEALQIFQTDKHPSHMGIGRAKEGFSVFGMMNKCATPMGRRLLRSWFMRPILDLEVLDRRLNAISFFISSVELMASLRETLKSVKDISHLLKKFNSPTSLCTSNDWTAFLKSISALLHVNKIFEVGVSESLREHMRRFNLDIIEKAGLCISTELDYVYELVIGVIDVTRSKERGYQTLVKEGFCAELDELRQIYEELPEFLQEVSAMELEHFPHLHKEKLPPCIVYIQQIGYLMCIFGEKLDETALNRLTEFEFAFSDMDGETQRFFYHTSKTRELDNLLGDIYHKILDMERAIIRDLLSHTLLFSAHLLKAVNFVAELDCILSLACVAHQNNYVRPVLTVESLLDIRNGRHVLQEMAVDTFIPNDTEINDNGRIHIITGPNYSGKSIYVKQVALIVFLSHIGSFVPADAATVGLTDRIFCAMGSKFMTAEQSTFMIDLHQVGMMLRQATSRSLCLLDEFGKGTLTEDGIGLLGGTISHFATCAEPPRVVVCTHLTELLNESCLPVSEKIKFYTMSVLRPDTESANMEEIVFLYRLIPGQTLLSYGLHCALLAGVPEEVVKRAAIVLDAFESNNNVDKLSLDKISSQDQAFKDAVDKFAELDISKGDIHAFFQDIFTS
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Involved in meiotic recombination in association with MSH4. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation.
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F4JF14
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ENOL1_ARATH
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Protein ENHANCER OF LHP1 1
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MKSRSLKLREAHKVGGSAAFCSILWDHKAEHFVTSSSSDPSISVHDGLSTSTLPPTILRHHQDGVTSLALSNDSTLLASGSIDHCVKLYKFPSGEFQTNITRFTLPIRVLAFNGSGSLLAAAGDDEGIKLINTFDGSIVRVLKGHKGPVTGLDFHPNGELLASIDTTGTVLCWELQNGVVSFTLKGVAPDTGFNTSIVNIPRWSPDGRTLAVPGLRNDVVMYDRFTGEKLFALRGDHLEAICYLTWAPNGKYIATSGLDKQVLLWDVDKKQDIDRHKFEERICCMSWKPNGNALSVIDAKGRYGVWESLVPSSMLSPTVGVPDIVPKKRNEILDFDDEVEEEIYRASESLDDAMGDSDDGESHHTSRKRLRKKTLIDEDVDDAYEELNDGSSLPSASEYRKKSHRGHREKQGARSGAFKGISASTKYKMQSSFQPGATPPEPGKRTFLCYNMLGCITTIEHEGNSRIETDFHDTGRGPRVSSMIDIYGFTMASINETGCVFANPCKGEKNMSVLMYRPFRSWASNSEWTMRFEGEEVKVVANGSGWVAAVTSLNLLRVFSEGGLQKHILSLDGPVVTAVGCKDHLAVVTHVSDCLPSNEQVMEFRVFNISKMTQELKGRVALTPGSRLTWIGFSEEGSLSSYDSEGVLRVFTSQYGGSWIPVFSTSKEKKQEENYWVVGLNTSSLYCIACKYAEMFPQVTPKPILTILDLSLPLASSDLGAASLENELILKQLRLYETQRKVDDMALVGVDTTALEDEAFDLEVSQDKCILRLISSCCSSDSFARASELMELLTLEKSMRAAITLVTKLKLPFLAEKFSSILEERLLEEASEAAVTNPALNPNGEVVTRVESKVQNPPASIQTSENTEAVMKSSATKLSAPTLLKKSKVSEGLKLGKEQTKKDKSDDAKIKEIKKLNLKNPVNNVNKEDKGQEKEVNQGEARRSSNPFLKSTV
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Participates in maintaining the H3K27me3 mark at target genes by interacting with LHP1-PRC2 complexes during replication, thus contributing to H3K27me3 inheritance.
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F4JFN3
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HS906_ARATH
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Heat shock protein 90-6, mitochondrial (AtHSP90.6) (AtHsp90-6) (Heat shock protein 89-1) (Hsp89-1)
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MIRLSKRSVSTLLRSGNQSFRIAAAASTSRSSPSATDVKRSDTESRWYSSLTNGQSKNSGSFAQLNMKTNWFMGYRNESSAAASDSSSQAPPPAEKFEYQAEVSRLMDLIVNSLYSNKEVFLRELISNASDALDKLRYLSVTNPELSKDAPDLDIRIYADKENGIITLTDSGIGMTRQELVDCLGTIAQSGTAKFMKALKDSKDAGGDNNLIGQFGVGFYSAFLVADRVIVSTKSPKSDKQYVWEGEANSSSFTIQEDTDPQSLIPRGTRITLHLKQEAKNFADPERIQKLVKNYSQFVSFPIYTWQEKGYTKEVEVEDDPTETKKDDQDDQTEKKKKTKKVVERYWDWELTNETQPIWLRNPKEVTTAEYNEFYRKAFNEYLDPLASSHFTTEGEVEFRSILYVPPVSPSGKDDIVNQKTKNIRLYVKRVFISDDFDGELFPRYLSFVKGVVDSHDLPLNVSREILQESRIVRIMKKRLVRKAFDMILGISLSENREDYEKFWDNFGKHLKLGCIEDRENHKRIAPLLRFFSSQSENDMISLDEYVENMKPEQKAIYFIASDSITSAKNAPFLEKMLEKGLEVLYLVEPIDEVAVQSLKAYKEKDFVDISKEDLDLGDKNEEKEAAVKKEFGQTCDWIKKRLGDKVASVQISNRLSSSPCVLVSGKFGWSANMERLMKAQSTGDTISLDYMKGRRVFEINPDHSIIKNINAAYNSNPNDEDAMRAIDLMYDAALVSSGFTPDNPAELGGKIYEMMDVALSGKWSSPEVQPQQQQMAHSHDAETFEAEVVEPVEVDGKK
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Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner.
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F4JFU8
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OBL1_ARATH
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Triacylglycerol lipase OBL1 (EC 3.1.1.-) (Oil body lipase 1) (AtOBL1)
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MHKDNDSGSGSNPGQVSNYLIVRPHRGGYIDLFRYGVRDDQTSKAKFLEMPDNREWSTITIDEEAEDHRWVIVVSILVRKIIRLLRTPMEFTGFVVDFFLNLFSANGGFFGLLLRLIQAKVVIPERGSVTFVSTIGQLDGRISLYKEWNFVEHLEGIDSVDSGRVKIELGSRGLMDLCVMASKLAYENAKVVENVVDLHWKMNLVEFLDCWNDYQKQMSTQVFVFTDKQKDANLIVISFRGTEPFDADDWGTDFDYSWYEVPNVGKLHMGFLEAMGLGNRDDTTTFHYNLFEQTSSEEENSKKNLLDMVERSAYYAVRVILKRLLSEHENARFVVTGHSLGGALAILFPTLLVLNEETEIMKRLLGVYTFGQPRIGNREVGLFMKAQLNQPVDRYFRVVYCNDIVPRLPYDDKTFLYKHFGLCLFYDSFYNETKAEDEPDPNPYGLRYKILGHVIAVWELVRGLTMGYTHGPDYKEGWFRILFRLMGLVIPGLSDHCMTDYVNSVRLGPDNELQMSSL
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Acid lipase that can hydrolyze a range of triacylglycerols without a clear preference for acyl-chains. Can also cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol, but not phosphatidylcholine, phosphatidylethanolamine, or sterol esters. Required for pollen tube growth. Triacylglycerol hydrolysis by OBL1 may provide acyl groups for the synthesis of membrane lipids in growing pollen tubes (Probable).
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F4JGP4
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KN14D_ARATH
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Kinesin-like protein KIN-14D (AtKIN14b)
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MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTIAIESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNACEIGIPRRQTSAKLLDSRLSYG
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Kinesin that supports microtubule movement in an ATP-dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis, is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating force to coalign microtubules.
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F4JGR5
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PFPB2_ARATH
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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP 2) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent 2) (PPi-PFK 2) (Protein MATERNAL EFFECT EMBRYO ARREST 51) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 2)
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MASQLDLIGGDYIAGISINPPTNSRVTSVYSEVQASRIDHTLPLPSVFKTPFKIIDGPPSSSAGHPEEIEKLFPNLFGQPSALLVPNQSNEVSSDQKLKIGVVLSGGQAPGGHNVICGIFDYLQEYARGSSLFGFRGGPAGIMKGKYIELTSEFVYPYRNQGGFDMICSGRDKIETPEQFKQAEETVTKMDLDGLVVIGGDDSNTNACLLAEHFRAKNMKTLVIGCPKTIDGDLKSKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVFEKKLTLKNVTDNIVDVIYKRAENGYNYGVILVPEGLIDFIPEVQQLISELNEVLAEGNVDEEGQWKKNLKKETLEIFEFLPQTIQEQLMLERDPHGNVQVAKIETEKMLIQMVETELEKKKTEGTYEREFMGKSHFFGYEGRCGLPTNFDATYCYALGYGAGSLLQSGKTGLISSVGNLAAPVEEWTVGGTALTSLMDVERRHGKFKPVIKKAMVELEGAPFKKFASQREEWALKNRYISPGPIQFKGPGSDARNHTLMLELGAQA
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Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_03185}.
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F4JGZ1
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MED16_ARATH
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Mediator of RNA polymerase II transcription subunit 16 (Protein SENSITIVE TO FREEZING 6)
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MNQQNPEEEVSLVNNSGGGGIIEAPAIVEEKEEEGLQQKQEETIESTDPILVVVEEKLLEKSVDGEKEDDNSSSSNMEIDPVSPATVFCVKLKQPNSNLLHKMSVPELCRNFSAVAWCGKLNAIACASETCARIPSSKANTPFWIPIHILIPERPTECAVFNVVADSPRDSVQFIEWSPTSCPRALLIANFHGRITIWTQPTQGSANLVHDATSWQCEHEWRQDIAVVTKWLTGASPYRWLSSKPSSGTNAKSTFEEKFLSQSSESSARWPNFLCVCSVFSSGSVQIHWSQWPSNQGSTAPKWFSTKKGLLGAGPSGIMAADAIITDSGAMHVAGVPIVNPSTIVVWEVTPGPGNGLQATPKISTGSRVPPSLSSSSWTGFAPLAAYLFSWQEYLISEIKQGKKPSDQDSSDAISLSCSPVSNFSAYVSPEAAAQSAATTTWGSGVTAVAFDPTRGGSVIAVVIVEGQYMSPYDPDEGPSITGWRVQRWESSVQPVVLHQIFGNPTSNFGGQVPTQTVWVSRVDMSIPPTKDFKNHQVAAAGPSVDAPKEPDSGDEKANKVVFDPFDLPSDIRTLARIVYSAHGGEIAIAFLRGGVHIFSGPTFSPVENYQINVGSAIAAPAFSPTSCCSASVWHDAAKDCAMLKIIRVLPPALPRNQSKVDQSTWERAIAERFWWSLLVGVDWWDAVGCTQSAAEDGIVSLNSVIAVMDADFHSLPSTQHRQQYGPNLDRIKCRLLEGTNAQEVRAMVLDMQARLLLDMLGKGIESALVNPSALVFEPWRVDGETITGINPEAMAVDPALVSSIQAYVDAVLDLASHFITRLRRYASFCRTLASHAASAGTGSNRNNVTSPTQNASSPATPQVFPDKSLYLAVGQPTTTTTTTATTNSSGSSHVQAWMQGAIAKISSSNDGSNSTASPISGSPTFMPISINTGTFPGTPAVRLIGDCHFLHRLCQLLLFCFLQRSSRFPQRNADVSSQKLQTGATSKLEEVNSAKPTPALNRIEDAQGFRGAQLGTGVKGIDENSARTTKMGSGNAGQGYTYEEVRVLFHILMDLCKRTSGLAHPLPGSQVGSGNIQVRLHYIDGNYTVLPEVVEAALGPHMQNMPRPRGADAAGLLLRELELHPPSEEWHRRNLFGGPGSEPEDMILTDDVSKLSNSLDLPDTNFSGICDGYNRVHSLWPRKRRMSERDAAFGSNTSVGLGAYLGIMGSRRDVVTATWKTGLEGVWYKCIRCLRQTSAFASPGATKQPNPNERETWWTSRWVYCCPMCGGTWVRVV
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Involved in the regulation of the circadian clock, in the control of flowering time, in freezing- and osmotic-stress tolerance and in both salicylic acid- and jasmonate-mediated defense gene expression.
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F4JHA2
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RSH1C_ARATH
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Putative GTP diphosphokinase RSH1, chloroplastic (EC 2.7.6.5) (RelA/SpoT homolog 1) (AtRSH1) (ppGpp synthetase RSH1)
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MTSASSMSVSVECVNICNLTKGDGNARSDCSALSCAWKAPRALTGFLASTAHPPVCSVYSCGRNGRKSRMKACAWQRYEYEVGFSEAPYFVNVRNILKSRLSCGGHKRWELYCVSAESSSGASSDVTVETLWEDLFPSISYLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNFITFEKIEEEFGATVRHIVEGETKVSKLGKLKCKTESETIQDVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQFLDLVTVNTDVRSVCKETYSIYKAALKSKGSINDYNQIAQQLRIVVKPKPSVGVGPLCSPQQICYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQSLHTTVIPFLYESMFRLEVQIRTEEMDLIAERGIAVYYNGKSLSTGLVGNAVPLGRNSRGKTGCLNNADFALRVGWLNAIREWQEEFVGNMSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSKSAFQRHKQWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDFVADSDSDVEDLTEDSRKSLQWWEKILVNVKQFQSQDKSRDTTPAPQNGSVWAPKVNGKHNKAIKNSSSDEPEFLLPGDGIARILPANIPAYKEVLPGLDSWRDSKIATWHHLEGQSIEWLCVVSMDRKGIIAEVTTVLAAEGIALCSCVAEIDRGRGLAVMLFQIEANIESLVSVCAKVDLVLGVLGWSSGCSWPRSTENAQVLEC
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May be involved in a rapid plant ppGpp (guanosine 3'-diphosphate 5'-diphosphate)-mediated response to pathogens and other stresses (By similarity). Unable to functionally complement E.coli relA mutants. {ECO:0000250, ECO:0000269|PubMed:18535838}.
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F4JHH5
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SC15B_ARATH
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Exocyst complex component SEC15B (AtSec15b)
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MQSSKGRRKVGSTTAGAGIDSAEKLDELLISSAICNGEDLGPFVRKTFGTGKPETLLHHLKFFARSKESEIEEVCKAHYQDFIHAVDDLKSLLSDVESLKSALSDSNSKLQSVAAPLLSSLDSLVEAQTVSKNVDLAIGAVTHCVRVMELVSRANQHLQSGNFYMALKCVDSIESDFMEKTPSSTLKRMLENRIPAIRSYVERKVNKEFGDWLVEIRVVSRNLGQLAIGEASAARQREEELRIKQRQAEEQSRLSLRDCVYALNEEEDDEFGSGHEGSDGGSSGGGLLGFDLTPLYRAYHIHQTLSLGDTFKQYYYNNRDLQLTSDFQIAGFFIVEDRVLRTGGGLISKLEVETLWDTAVTKMCAVLEDQFSRMQTANHLLLIKDYVSLLGVSLRRYGYAVDSLLEVLSKHRDKYHELLLSDCRKQITEALSADKFEQMLMKKEYEYSMNVLSFQLQTSEIVPAFPFIAPFSTTVPDCCRIVRSFIEDSVSFMSHGGQLDFYDVVKKYLDRLLGEVLDEALLKLISTSVHGVSQAMQVAANMAVFERACDFFFRHAAHLSGVPLRMAERGRRHFPLTKSQNTAEDTLSGMLKKKIDGFMTLLENVNWTSDDIPQGGNEYMNEVLIYLETLVSTAQQILPAKVLKRVLRDVLAHISEKIVGTLCGDLVKRLSMAAIKGLDVDIQLLDSFTENLTPLLTDKEAREMKKAFVEIRQMINLLLSSHPENFVNPVIRERSYNALDYRKVATVSEKFRDPSDSIFGTFGTRGSRQNPKNKSLDALIKRLKDVS
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Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
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F4JI44
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NDX_ARATH
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Nodulin homeobox (NDX1 homeobox protein homolog) (AtNDX1)
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MVRLLQPKHMVQAVNALHWRNSVEFHKLLKDNGDFSICFNSEQVLPQKISVEKMVKMLPRHLIAVVMTPNKDGKSRYILCGIRLLQTLCDLTPRNAKLEQVLLDDVKLSAQMIDLVILVIIALGRNRKESCNSNKESLLEATLVASCLHLFHGFISPNSQDLVLVLLAHPRVDVFIDSAFGAVLNVVISLKAKLLYRQTDSPKKLGASSVEEVNFHCQQAEAALQFLHSLCQHKPFRERVAKNKELCGKGGVLRLAQSILSLTITPEFVGATVTIASTSRMKAKVLSILQHLFEAESVSFLDEVANAGNLHLAKTVASEVLKLLRLGLSKASMATASPDYPMGFVLLNAMRLADVLTDDSNFRSFFTEHFSMVLSAVFCLSHGDFLSMLCSSDLSSREDDANVDYDLFKSAGWILSVFSSSGQSVTPQFKLSLQNNLTMSSYAHQRTSLFIKMIANLHCFVPNVCQEQDRNRFIQNVMSGLRKDPSSILIKMLPGSSYTPVAQRGTGVCRNLGSLLRHAESLIPSSLNEEDFLLLRVFCDQLQPLIHSEFEESQVQVKVKKLFALLYIGFTILWLICLVTLIQDIEGRGGNLSGKLKELLNLNNEEASEDCDVRVEGVMTKQGVNEEIDTVERLKESDADASNLETSGSDTSSNRGKGLVEEGELVQNMSKRFKGSASGEVKEDEKSETFLVFEKQKKKRKRSIMNADQMGMIEKALAEEPDLQRNSASRQLWADKISQKGSEVITSSQLKNWLNNRKAKLARANKQTGPAHDNNSSGDLPESPGDENTWQQKPSTPIKDQTVTETPKTGENLMRTSSSSEEGIKQGQQVRLMDERGDEIGKGTVLRTDGEWNGLSLETRQICVVDVMELSESYDGSKKMIPYGSDDVGRTFTEANSRFGVMRVAWDVNKLQY
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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.
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F4JIN3
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DNJ29_ARATH
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DnaJ protein ERDJ2B (Chaperone protein dnaJ 29) (AtDjC29) (AtJ29) (Endoplasmic reticulum dnaJ domain-containing protein 2B) (AtERdj2B) (Translocation protein SEC63 homolog ERDJ2B)
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MAESEENSVLFPIFILTMMAIPLVPYTFVKLSRAFSKKQRSIHCQCLECDRSGKYKRSISQSISSFTSCSNLTVVLLWIVMIFLIYHTKNMSRESQLFEPFGILGLEPGASDSEIKKAYRRLSIQYHPDKNPDPEANKYFVESIAKAYQALTDPLSRENFEKYGHPDGRQGYTMGIALPQFILNMNGESGGILLLCTVGLCILLPLVIASIYLWRSSKYTGNHVKLQTRQAYFELLQPSLTPSKVMDIFIRAAEYAEISVRKSDDESLQKLFMSVKSELNLDPKKLKQEEAKFWKKHPATIKTELLIQKQLTRESSVLSPTLQRDFRHVLEFAPRLLEDLIKMAVIPRNEQGRGWLRPALGVMELSQCIVQAVPLSARKSSSEDIAPFLQLPHFNESIAKSIALQVKSFQKFQELSLAERSKLLREVVSLSETDVQDIEKVLEMIPSLKINVTCKTEGEEGIQEGDIMTVQAWITLKRPNGLIGAIPHSPYFPFHKEENFWVLLADSNHVWFFQKVKFMDEAGAIAAASNTITETMEPLGASVKETNDAVKEAVEKVKSGSRLVMGRLLAPGEGTYNLTCFCLSDTWIGCDQKTSLKVEVLKRTRDVEGENAEEGLEEEDDEIEEEDYESEYSEDEEDKKRGSKKKVNKESSSEESGSDEE
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Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
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F4JJL0
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ENDO4_ARATH
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Endonuclease 4 (AtENDO4) (EC 3.1.30.1) (Deoxyribonuclease ENDO4) (Single-stranded-nucleate endonuclease ENDO4)
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MSSSLRQWFARVLVLTQLINGALCWGKEGHYTVCKIAESYFEEETVAAVKKLLPKSADGDLASVCSWPDEIKHHWQWRWTSPLHYVDTPDYRCNYEYCRDCHDTHKNQDRCVTGAIFNYTMQLMSASENSDTIVHYNLTEALMFLSHFIGDIHQPLHVGFLGDEGGNTITVRWYRRKTNLHHVWDNMIIESALKTYYNKSLPLMIEALQANLTNDWSNDVPLWESCQLNQTACPNPYASESINLACKYAYRNATPGTTLGDDYFLSRLPIVEKRLAQGGIRLAATLNRIFSSKPKHAGS
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Endonuclease that can use single-stranded RNA and DNA as substrates. In contradiction with PubMed:23620482, cannot hydrolyze single-stranded DNA and does not cleave mismatches.
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F4JJL3
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ENDO5_ARATH
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Endonuclease 5 (AtENDO5) (EC 3.1.30.1) (Deoxyribonuclease ENDO5) (Single-stranded-nucleate endonuclease ENDO5)
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MRLWIVSVLVLTHLVHGALCWGKDGHYTVCKLAEGFFEDDTIAAVKKLLPESVDGGGLADFCSWPDEIKKLSQWQWTSTLHYVNTPEYRCNYEYCRDCHDTHKHKDWCVTGAIFNYTNQLMSASENSQNIVHYNLTEALLFLSHYMGDVHQPLHTGFLGDLGGNTIIVNWYHNKSNLHHVWDNMIIDSALETYYNSSLPHMIQALQAKLKNGWSNDVPSWKSCHFHQKACPNLYASESIDLACKYAYRNATPGTTLGDEYFLSRLPVVEKRLAQGGIRLAATLNRIFSAKPKLAGL
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Hydrolyzes, with low efficiency, only single-stranded DNA and RNA without apparent specificity for bases. 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.
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F4JKB6
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PRRP3_ARATH
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Proteinaceous RNase P 3 (EC 3.1.26.5)
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MKLKKPSLPSSLLCAVPPCLSQIRLLIPRRVRVSSSTFANAKLVTLRNHTVNLHIYYCSMAGTDNRRSRHDDESPKNPNKKKKGNRNPEKSLLINLHSCSKRKDLSAALALYDAAITSSDIRLNQQHFQSLLYLCSAFISDPSLQTVAIDRGFQIFDRMVSSGISPNESSVTAVARLAAAKGDGDYAFKLVKDLVAVGGVSVPRLRTYAPALLCFCDTLEAEKGYEVEDHMDASGIVLEEAEISALLKVSAATGRENKVYRYLQKLRECVGCVSEETSKAIEEWFYGVKASEVSDNGIGSDIELLRAAVLKNGGGWHGLGWVGEGKWIVKKGNVSSAGKCLSCDEHLACVDTNEVETEDFVNSLVTLAMERKAKMNSCEPMADFSEFQEWLEKHGDYEAILDGANIGLYQQNFADGGFSLPQLEAVVKELYNKSGSKKQPLILLHKKRVNALLENPNHRNLVEEWINNNVLYATPPGSNDDWYWLYAAAKLKCLLVTNDEMRDHIFELLSNSFFQKWKERHQVRFTFVKGCLKLEMPPPFSVVIQESEKGSWHVPITSQDKEESLRSWMCITRQSS
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Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA).
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F4JKH6
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REC2_ARATH
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Protein REDUCED CHLOROPLAST COVERAGE 2 (Protein TPR-domain suppressor of STIMPY)
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MAPKAGKTKPHKSKGEKKKKEEKVLPTVIEISVETPDESQVTLKGISTDRILDVRKLLAVHVQTCHFTNFSLSHQVRGTKLKDSVDIVSLKPCHLTIVEEDYTEEQATAHIRRLLDIVACTTAFGPSKPPVSRTLPKDSEKKESGSTDGDSPTEKDAGDSNSGLSPKPKESEKKSVGACEAQSAEGAAKSDIDMCPPTRLGQFYEFFSFSYLTPPIQYIRRSVRPSKEDKGLDDLFQIDIKVSSGKPFTVVASRTGFYPPGKQQLLCHSLVELLQQISRPFDAAYDALMKAFIEHNKFGNLPYGFRANTWVVPPVVADSPSTFPSLPVEDETWGGDGGGVGRSGKYDKRKWAKEFAILAAMPCKTPEERQVRDRKAFLLHSLFVDVSVFKAVEIIKKIVENNQCSLKDPAALGFHEERIGDLIVRVARDDPDASAKLDRKSDGTQVLEISQEELAQRNLLKGITADESATVHDTSTLGVVVVRHCGCTAIVKVASEFKLNDGHILQDIDIEDQSEGGANALNVNSLRTLLHKSSTPSSLAQRSPNADSEQIRVAKSLVRKVIEDSLKKLEIEPSRYSKPIRWELGACWVQHLQNQASSKSESKKTEDPKPEPAVKGLGKQGALLKEIKRKIDVKANKTEQGKEAPANDTDNTSETEDQKELEKQNEEIEKMWKELVTETAYQRLKESETGFHLKSPKELIEMARKYYTDTALPKLVADFGSLELSPVDGRTLTDFMHTRGLQMHSLGRVVELAEKLPHVQSLCVHEMIVRAYKHILQAVVAAVENTADVATSIATCLNVLLGTPSDTESVYDEKIKWTWVETFISKRFGWDWKHEGCQELRKFSILRGLSHKVGLELVPKDYEMDTSYPFKKFDIISMVPVYKHVACSSADGRTLLESSKTSLDKGKLEDAVNYGTKALAKLVAVCGPYHRMTAGAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLAVFYYRLQHTELALKYVNRALYLLHLTCGPSHPNTAATYINVAMMEEGMKNAHVALRYLHEALKCNQRLLGADHIQTAASYHAIAIALSLMDAYSLSVQHEQTTLQILQAKLGPEDLRTQDAAAWLEYFESKALEQQEAARNGTPKPDASISSKGHLSVSDLLDYITPDSGIKARDAQRKARPKVKGKPGQSPGPVSEENQKDDEILSPAHLTGESSSDKENKSETKSEEKKVENFDLEQSKPQDQLKLVKPEATVHEDDDSDEGWQEAVPKNRFSSGRRTRPSLAKLNTNFMNVTQQPSRSRGKSTNFTSPRTSSNELSISVAGSTSSPASKMFVKSPLNKKQNNSSVVGERPVNDKSALASSACTEQINKPTPMLSPVSVKAGKLFSYKEVALAPPGTIVKIVAEQLPEETKAPQNLDAAKIAVDGPEKVNAQDAESENKHVATETEAENTDCNEQGRVVVGGSELTSSPKEIKNVEVEKAAEKAFPIETAVSNARPGKSKSAQMAEDSDTCLLNKSPTANDSNGSESVIGVKLQKDLCDAELKTVDGETENLPNGDSSPKSSVAADGEKQDACEAQKEMSKKLSASAPPYTPTTIPIFGSIAVPGFKDHGGILPSPLNMPPMLPINHVRRSTPHQSVTARVPYGPRLSGGGYNRSGNRVPRNKPSFPNSTESNGEANQFNGPRIMNPHAAEFIPSQPWVSNGYPVSPNGYLASPNGAEITQNGYPLSPVAGGYPCNMSVTQPQDGLVSEELPGAGSSEEKSGSEEESNNDKNAGEDDEAVGQETTDTPENGHSTVGEVETTSHETCDEKNGERQGGKCWGDYSDNEIEQIEVTS
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Negatively regulates meristematic tissue proliferation by integrating developmental signals with carbon source availability. 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. Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment.
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F4JKK0
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SUD1_ARATH
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Probable E3 ubiquitin ligase SUD1 (EC 2.3.2.27) (Protein ECERIFERUM 9) (Protein SUPPRESSOR OF DRY2 DEFFECTS 1) (AtSUD1) (RING-type E3 ubiquitin transferase SUD1) (RING/U-box domain-containing protein)
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MEISPADSLSISGAAASEVVSEPSVSSSSSSSSPNQASPNPFSNMDPAVSTATGSRYVDDDEDEEDVCRICRNPGDADNPLRYPCACSGSIKFVHQDCLLQWLNHSNARQCEVCKHPFSFSPVYADNAPSRLPFQEFVVGIAMKACHVLQFFLRLSFVLSVWLLTIPFITFWIWRLAFVRTFGEAQRLFLSHISTTVILTDCLHGFLLSASIVFIFLGATSLRDYFRHLRELGGQEERDDDVDRNGARAARRPAGQANRNLAGEGNGEDAGDQGAAVGQIARRNPENVLARLDIQAARLEAQVEQMFDGLDDADGAEDVPFDELVGMQGPVFHLVENAFTVLASNMIFLGVVIFVPFTLGRIILYHVSWLFAAARGPAVAASLHLTDTGLSLENITLKSALTAVSNLTSEGQGNGLLGQLTEMMKVNGSELNGANNTLSVATDLLKGSTVGASKLSDITTLAVGYMFIVFLVFLYLGIIALIRYAKGEPLTVGRFYGIASIVEAVPSLLRQFLAAMRHLMTMIKVAFLLVIELGVFPLMCGWWLDVCTVRMFGKTMSHRVQFLSISPLASSLVHWVVGIMYMLQISIFVSLLRGVLRPGVLYFLRDPADPNYNPFRDLIDDPVHKHARRVLLSVAVYGSLIVMLVFLPVKLAIRMAPSIFPLDISVSDPFTEIPADMLLFQICIPFIIEHFRLRTTIKSLLRCWFTGVGWALGLTDFLLPRPEDNIGQDNGNGEPGRQNRAQVLQVGGPDRAMAALPVADDPNRSRLRAGNVNTGEEYEDDDEQSDSDRYNFVVRIILLLLVAWVTLLLFNSALIVVPVSLGRALFSAIPILPITHGIKCNDLYAFVIGTYAFWTTISGARYAIEHVKSKRTSVLLNQIWKWCGIVFKSSVLLAIWVFIIPVLIGLLFELLVIVPMRVPVDESPVFLLYQDWALGLIFLKIWTRLVMLDHMLPIVDDSWRAKFERVREDGFSRLQGLWVLREIVFPIVMKLLTALCVPYVLARGVFPMLGYPLVVNSAVYRFAWIGCLSVSLFCFCAKRCHVWFRNLHNSIRDDRYLIGRRLHNFGEAALANQNQNQSSEDAGDGVLIGREGDVDNGLRLRRAIQQEA
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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}.
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F4JL11
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IMPA2_ARATH
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Importin subunit alpha-2 (IMPa-2)
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MSLRPNAKTEVRRNRYKVAVDAEEGRRRREDNMVEIRKSKREESLQKKRREGLQANQLPQFAPSPVPASSTVEKKLESLPAMVGGVWSDDRSLQLEATTQFRKLLSIERSPPIEEVIDAGVVPRFVEFLTREDYPQLQFEAAWALTNIASGTSENTKVVIEHGAVPIFVQLLASQSDDVREQAVWALGNVAGDSPRCRDLVLGQGALIPLLSQLNEHAKLSMLRNATWTLSNFCRGKPQPPFDQVRPALPALERLIHSTDEEVLTDACWALSYLSDGTNDKIQSVIEAGVVPRLVELLQHQSPSVLIPALRSIGNIVTGDDLQTQCVISHGALLSLLSLLTHNHKKSIKKEACWTISNITAGNRDQIQAVCEAGLICPLVNLLQNAEFDIKKEAAWAISNATSGGSPDQIKYMVEQGVVKPLCDLLVCPDPRIITVCLEGLENILKVGEAEKVTGNTGDVNFYAQLIDDAEGLEKIENLQSHDNSEIYEKAVKILETYWLEEEDETLPPGDPSAQGFQFGGGNDAAVPPGGFNFQ
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Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation.
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F4JL28
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EBS_ARATH
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Chromatin remodeling protein EBS (Protein EARLY BOLTING IN SHORT DAYS)
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MAKTRPGVASKIKTGRKELDSYTIKGTNKVVRAGDCVLMRPSDAGKPPYVARVEKIEADARNNVKVHCRWYYRPEESLGGRRQFHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENVGAEDYYCRFEYKAATGAFTPDRVAVYCKCEMPYNPDDLMVQCEGCKDWYHPACVGMTIEEAKKLDHFVCAECSSDDDVKKSQNGFTSSPADDVKVRLSLFSHLLYRCSITYL
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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. 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. Involved in the chromatin-mediated repression of floral initiation and controls genes regulating flowering. 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.
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F4JLC1
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MRL7_ARATH
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Thioredoxin-like fold domain-containing protein MRL7, chloroplastic (Protein EARLY CHLOROPLAST BIOGENESIS 1) (AtECB1) (Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7) (AtMRL7) (Protein REGULATOR OF CHLOROPLAST BIOGENESIS) (Protein SUPPRESSOR OF VARIEGATION 4)
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MSFFAVACSAPRSSMLLTGLNSSFSDMHRSPLFVFPVTISSRSVKRFAAVSSDSVLDPESKNQTRSRRKNKEAVTPIAETENNEKFPTKVPRKSKRGRRSEADAVEDYVRSSLERTFSTIKEQNPEVFENKEKANFIKDRGVDEEEEEEEEMVVEEEDPDWPVDTDVGWGIKASEYFDTHPIKNVVGDDGSEIDWEGEIDDSWVKEINCLEWESFAFHPSPLVVLVFERYKRASDNWKTLKELEKAIKVYWDAKDRLPPRAVKIDLNIETDLAYALKAKECPQILFLRGNRILYREKDFRTADELVHMIAHFYYKAKRPSCVDKANVTPYC
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Plays an essential role in early steps of chloroplast development. Involved in the regulation of plastid gene expression. May positively regulate plastid-encoded RNA polymerase (PEP) activity through binding to FSD3 and CITRX/TRXZ. Involved in redox-mediated regulation of chloroplast development. Possesses disulfide reductase activity in vitro. 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. May mediate some aspect of thylakoid structure or function that controls non-photochemical quenching (NPQ). Participates in the early light signaling events of photobody biogenesis in chloroplasts. May mediate the degradation of two repressors of chloroplast biogenesis, PIF1 and PIF3 in nucleus.
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F4JLE5
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SFH1_ARATH
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Phosphatidylinositol/phosphatidylcholine transfer protein SFH1 (Phosphatidylinositol transfer protein 1) (AtPITP1) (Protein CAN OF WORMS1) (Protein SEC FOURTEEN HOMOLOGS 1) (AtSFH1) (Protein SHORT ROOT HAIR 1)
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MAETKPEIEMSEEERKIVKISSLKKKAINASNRFKNSFKKKGRRSSSRVMSVPIEDDIDAEDLQALDAFRQALILDELLPSKLDDLHMMLRFLRARKFDIEKAKQMWSDMIQWRKDFGADTIIEDFDFEEIDEVMKHYPQGYHGVDKEGRPVYIERLGQIDANKLLQVTTMDRYVKYHVKEFEKTFKVKFPSCSVAANKHIDQSTTILDVQGVGLKNFSKSARELLQRLCKIDNENYPETLNRMFIINAGSGFRLLWSTVKSFLDPKTTAKIHVLGNKYHSKLLEVIDASELPEFFGGACTCEDKGGCMRSDKGPWNDPEVLKIAINREAKCSPISEDEHKHVDQGRSTSGFESLERIKKKTDEDNVYEKQIATIDKSMDMAWLAKTQKAENFPISKGLECYVRKGAPKKGDGLLVGGVMAFVMGIVAMVRLSKDVPRKLTEAALYGNSVCYEESTKSKQNQGQFAAPVSSSEYMLMVKRMAELEDKCMFLDLKPAHVESEKEEKLQAALNRVQVLEQELTETKKALEEALVSQKEILAYIEKKKKKKKLFFGF
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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}.
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F4JLP5
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PLPD2_ARATH
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Dihydrolipoyl dehydrogenase 2, chloroplastic (ptLPD2) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 2) (Protein LIPOAMIDE DEHYDROGENASE 2) (Pyruvate dehydrogenase complex E3 subunit 2) (E3-2) (PDC-E3 2)
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MQSVLSLSFSQASLPLANRTLCSSNAAPSTPRNLRFCGLRREAFCFSPSKQLTSCRFHIQSRRIEVSAAASSSAGNGAPSKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKAFGLQVSAAGYDRQGVADHASNLATKIRNNLTNSMKALGVDILTGFGAVLGPQKVKYGDNIITGKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINTRKIDYHTGVFASKITPAKDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENINVTTQRGFIPVDERMRVIDGNGKLVPHLYCIGDANGKLMLAHAASAQGISVVEQVTGRDHVLNHLSIPAACFTHPEISMVGLTEPQAREKAEKEGFKVSIAKTSFKANTKALAENEGEGLAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVVDELFKAAKVDSPASVTAQSVKVTV
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Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC).
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F4JLZ6
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SMO13_ARATH
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Methylsterol monooxygenase 1-3 (EC 1.14.18.11) (EC 1.14.18.9) (Sterol 4-alpha-methyl-oxidase 1-3) (AtSMO1-3)
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MIPYPTVEDASVALGRNLTWFETVWFDYSATKSNFHVYCHTILVLFLVFSLAPFPLVIVEWTGWFDQFKIQKKVKYSLSDMFQCYKEVMKLFLLVVGTLQIVSYPSIQMVGIRSGLPLPSLMEIVAQLVVYFLIEDYTNYWIHRWMHCKWGYEKIHRIHHEYTSPIGYASPYAHWAEILILGIPTFLGPAIAPGHIMTFWLWISLRQFEAIETHSGYDFPWSVTKLIPFYGGPEYHDYHHYVGGQSQSNFASVFTYCDYIYGTDKGYRIHKKLLHHQIKEEAEEKRVRKHD
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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).
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F4JN35
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NTL9_ARATH
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Protein NTM1-like 9 (Calmodulin-binding NAC protein)
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MGAVSMESLPLGFRFRPTDEELVNHYLRLKINGRHSDVRVIPDIDVCKWEPWDLPALSVIKTDDPEWFFFCPRDRKYPNGHRSNRATDSGYWKATGKDRSIKSKKTLIGMKKTLVFYRGRAPKGERTNWIMHEYRPTLKDLDGTSPGQSPYVLCRLFHKPDDRVNGVKSDEAAFTASNKYSPDDTSSDLVQETPSSDAAVEKPSDYSGGCGYAHSNSTADGTMIEAPEENLWLSCDLEDQKAPLPCMDSIYAGDFSYDEIGFQFQDGTSEPDVSLTELLEEVFNNPDDFSCEESISRENPAVSPNGIFSSAKMLQSAAPEDAFFNDFMAFTDTDAEMAQLQYGSEGGASGWPSDTNSYYSDLVQQEQMINHNTENNLTEGRGIKIRARQPQNRQSTGLINQGIAPRRIRLQLQSNSEVKEREEVNEGHTVIPEAKEAAAKYSEKSGSLVKPQIKLRARGTIGQVKGERFADDEVQVQSRKRRGGKRWKVVATVMVAVMVGVGMGIWRTLVSS
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Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Calmodulin-regulated transcriptional repressor. Binds several synthetic promoters with randomly selected binding sites. 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. Acts as positive regulator of innate immunity. Involved in the effector-triggered immunity (ETI) induction of immunity-related gene expression. Mediates osmotic stress signaling in leaf senescence by up-regulating senescence-associated genes.
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F4JNX3
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CMKMT_ARATH
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Calmodulin-lysine N-methyltransferase (CLNMT) (CaM KMT) (EC 2.1.1.60)
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MDPTSSSSSALRWKILRQALLRRSDSQSQTETKRISRKATQGFNLIPCQVVDSSPQSDKSREASVCYTLPITGSPKLYLTQRVDNCSDLNDFEISNRYNIDNTGLVCQWPSEEVLAYFCKSQPERFRGKRVIELGSGYGLAGLVIAAATEASEVVISDGNPQVVNYIKRNIETNSMAFGGTSVKAMELHWNQHQLSELTNTFDIIVASDCTFFKEFHKDLARTIKMLLKAKKASEALFFSPKRGDSLEKFMKEIKDIGLHYILTENYDAQVWKRHETLVKGDEAWPNYDKNHCYPLLIQITNQI
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Catalyzes the trimethylation of calmodulin. 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.
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F4JNY0
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APE2_ARATH
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DNA-(apurinic or apyrimidinic site) endonuclease 2 (EC 3.1.-.-) (Apurinic-apyrimidinic endonuclease 2)
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MKIVTYNVNGLRQRVSQFDSLLKLLDSFDADIICFQETKLRRQELTADLAIADGYESFFSCTRTSEKGRTGYSGVATFCRVKSASSSCETALPVTAEEGITGLVNSNSRGGKSETSTVAEGLEEYEKEELLMIDQEGRCVITDHGHFVVFNVYGPRAVADDADRIEFKHRFYGVLERRWECLLRQGRRVFVVGDLNIAPFAMDRCEAGPDFEKNEFRKWFRSLLVERGGSFSDVFRSKHPERKDAFTCWSSSSGAEQFNYGSRIDHILVAGSCLHQDEDKQGHSFLACHVKECDILTEYKRFKNENMPTRWKGGLVTKFKGSDHVPVFISFDDLPDIPEHSTPPLASRYLPMIYGFQQTLVSVFKKRRANEEAKAIEVSCSSSTQSNTSSICGDISTGPLRNCGSMGISLEKSCSFENKSTSGVTEAETVAATGSIDNLSDGIRASSVRALNISRDGDRKKARKIQSSQLSLKSFFTTNSKVNNVEDSSSSYVSSSPSSQVESITEPNVSGKEDSEPTTSTQEQDQTGSSAKQKNDAALMEWQRIQNLMQNSIPLCKGHKEACVARVVKKPGPTFGRRFYVCSRAEKQTVVISNGLHQNSETSKRVMRSK
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Exhibits apurinic/apyrimidinic (AP) endonuclease activity in vitro. By contrast, another report show that APE2 has no biochemical activity. Unable to catalyze the conversion of 3'-phosphor-alpha,beta-unsaturated aldehyde (3'-PUA) to 3'-OH. Has no in vitro 3'-phosphatase activity. Redundant with APE1L and at least one functional allele is required for seed viability. Has a strong non-specific affinity to DNA.
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F4JP36
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HAP2_ARATH
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Protein HAPLESS 2 (GENERATIVE CELL SPECIFIC 1)
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MVNAILMACILAGIFVGMFNEVDGIQILSKSKLEKCEKTSDSGNLNCSTKIVLNLAVPSGSSGGEASIVAEIVEVEDNSSSNMQTVRIPPVITVNKSAAYALYDLTYIRDVPYKPQEYHVTTRKCEHDAGPDIVQICERLRDEKGNVLEQTQPICCPCGPQRRMPSSCGDIFDKMIKGKANTAHCLRFPGDWFHVFGIGQRSLGFSVRVELKTGTRVSEVIIGPENRTATANDNFLKVNLIGDFGGYTSIPSFEDFYLVIPREAAEAGQPGSLGANYSMWMLLERVRFTLDGLECNKIGVGYEAFNTQPNFCSSPYWSCLHNQLWNFRESDINRIDRHQLPLYGLEGRFERINQHPNAGPHSFSIGVTETLNTNLMIELRADDIEYVFQRSPGKIINIAIPTFEALTQFGVAAVIIKNTGEVEASYSLTFDCSKGVAFVEEQFFIIKPKAVTTRSFKLYPTKDQAAKYICTAILKDSQFSEVDRAECQFSTTATVLDNGTQVTNPFQIPETQPKGFFDSIRILWTKIINGLVDFITGDTCRNKCSSFFDFSCHIQYVCLSWMVMFGLLLALFPITCLLLWLLHQKGLFDPCYDWWEDHFDLDHHRRLLPSRADVVNRHHHHHKHRHHHNHHRRTHQRHKHHHGQDDDVLQKMMLERDHSDSHYYHQLHRVHKDSKQKQRRRAKHGIVLPRDVHVERQRKQRLRES
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Required for male fertility. Plays a role in pollen tube guidance and successful gamete attachment. 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. Mediates the fusion of cell membranes. Not required for pollen tube outgrowth.
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F4JP48
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MSH4_ARATH
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DNA mismatch repair protein MSH4 (AtMSH4) (MutS protein homolog 4)
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MEDDGGERSSFVAGLIENRAKEVGMAAFDLRSASLHLSQYIETSSSYQNTKTLLRFYDPSVIIVPPNKLAADGMVGVSELVDRCYSTVRKVVFARGCFDDTKGAVLIQNLAAEEPLALGLDTYYKQHYLSLAAAAATIKWIEAEKGVIVTNHSLTVTFNGSFDHMNIDATSVENLELIDPFHNALLGTSNKKRSLFQMFKTTKTAGGTRLLRANLLQPLKDIETINTRLDCLDELMSNEQLFFGLSQVLRKFPKETDRVLCHFCFKPKKVTEAVIGFENTRKSQNMISSIILLKTALDALPILAKVLKDAKCFLLANVYKSVCENDRYASIRKKIGEVIDDDVLHARVPFVARTQQCFALKAGIDGFLDIARRTFCDTSEAIHNLASKYREEFNLPNLKLPFNNRQGFFFRIPQKEVQGKLPNKFTQVVKHGKNIHCSSLELASLNVRNKSAAGECFIRTETCLEALMDAIREDISALTLLAEVLCLLDMIVNSFAHTISTKPVDRYSRPELTDSGPLAIDAGRHPILESIHNDFVSNSIFMSEATNMLVVMGPNMSGKSTYLQQVCLVVILAQIGCYVPARFATIRVVDRIFTRMGTMDNLESNSSTFMTEMRETAFIMQNVTNRSLIVMDELGRATSSSDGLAMAWSCCEYLLSLKAYTVFATHMDSLAELATIYPNVKVLHFYVDIRDNRLDFKFQLRDGTLHVPHYGLLLAEVAGLPSTVIDTARIITKRITDKENKRIELNCGKHHEIHRIYRVAQRLICLKYSRQTEDSIRQALQNLNESFTEERL
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Involved in meiotic recombination in association with MSH5. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation.
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F4JP52
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PQT3_ARATH
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E3 ubiquitin ligase PARAQUAT TOLERANCE 3 (EC 2.3.2.27)
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MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA
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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.
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F4JPW1
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BASS5_ARATH
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Probable sodium/metabolite cotransporter BASS5, chloroplastic (Bile acid transporter 5) (Bile acid-sodium symporter family protein 5)
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MGVISPTETLFLKSQHRLLQPRNYSYALAFHSTRRVANFPRNSFSSLGSCSVDFPLRSNPISQNSKSIHPWRRYVSESDSNELYHKKVSSIMETLKQAYSFIPHGILLSTILALVYPPSFTWFKPRYFVPGLGFMMFAVGINSNERDFLEALKRPDAIFAGYIGQYLIKPLLGYIFGVIAVSLFNLPTSIGAGIMLVSCVSGAQLSNYTTFLTDPSLAALSIVMTSISTATAVLVTPMLSLLLIGKKLPVDVFGMISSILQVVITPIAAGLLLNRLFPRLSNAIKPFLPALTVIDMSCCIGAPLALNIDSILSPFGATILFLVITFHLLAFVAGYFFTGFFFSKAPDVKALQRTISYETGMQSSLLALALATKFFQDPLVGVPPAISTVVMSLMGVSLVTIWKNRKE
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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.
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F4JQH3
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AMPP1_ARATH
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Aminopeptidase P1 (AtAPP1) (EC 3.4.11.9)
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MSEILSSLRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKKEARLWTDGRYFLQALQQLSDEWTLMRMGEDPLVEVWMSDNLPEEANIGVDSWCVSVDTANRWGKSFAKKNQKLITTTTDLVDEVWKSRPPSEMSPVVVHPLEFAGRSVSHKFEDLRAKLKQEGARGLVIAALDEVAWLYNIRGTDVAYCPVVHAFAILTTDSAFLYVDKKKVSDEANSYFNGLGVEVREYTDVISDVALLASDRLISSFASKTVQHEAAKDMEIDSDQPDRLWVDPASCCYALYSKLDAEKVLLQPSPISLSKALKNPVELEGIKNAHVRDGAAVVQYLVWLDNQMQELYGASGYFLEAEASKKKPSETSKLTEVTVSDKLESLRASKEHFRGLSFPTISSVGSNAAVIHYSPEPEACAEMDPDKIYLCDSGAQYLDGTTDITRTVHFGKPSAHEKECYTAVFKGHVALGNARFPKGTNGYTLDILARAPLWKYGLDYRHGTGHGVGSYLCVHEGPHQVSFRPSARNVPLQATMTVTDEPGYYEDGNFGIRLENVLVVNDAETEFNFGDKGYLQFEHITWAPYQVKLIDLDELTREEIDWLNTYHSKCKDILAPFMNQTEMEWLKKATEPVSVSA
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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.
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F4JQZ3
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REN1_ARATH
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Rho GTPase-activating protein REN1 (Protein ROP1 ENHANCER 1) (Rho-type GTPase-activating protein REN1)
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MANKNAESSSQPPPHVQPNQQQQQQPPIANEQEQEPHGDTCSIPPAQSGNTDSRSRGGNTVFKSGPLSISSKGIGWTSWKKRWFILTRTSLVFFRSDPSAVQQKGSEVNLTLGGIDLNNSGSVVVKADKKLLTVLFPDGRDGRAFTLKADTMEDLHEWKAALENALTQAPSASHVMGQNGIFRNDHADPAVGVDEKKDETPTKSTVLGRPVLLALEDVDGAPSFLEKALRFVENHGVRIEGILRQAADVDDVEHRIREYEKGKNEFSPEEDAHIIADCLKYFLRELPSSPVPASCCNALLEACRTDRGNRVNAMRAAICESFPEPNRRLLQRILMMMQTVASNKTVNRMNTNAVAACMAPLLLRPLLAGDCEIENDFDVGGDGSMQLLQAAAAANHAQAIVITLLEEYESIFGEGSLSPGLYSDSEESGSGTEEGSDDEEYDDDDDGSQGSEDYTDEEEDLENESNGSYSESAASEDKYADSIDPDDHKINDNLSTESKSPKRSKEPKKLLSGSRRSSLPRHDDGKKDEDIVVKGVNNTEVKAVVEVSTSEDKNSSTSDVASDTQKPSKLSDAPGGSKRHWGRTPGKKNLSMESIDFSVEVDEDNADIERLESTKLELQSRITEEVKSNAVLQASLERRKKALYGRRQALEQDVGRLQEQLQQERDRKLALETGLNMSKGNQPIPETIDENLKKDLQEVAQAEADIAKLEHKVDDLENRLGHHDGKASGSTHSASKESRKLPEHNAKMKEKQKDTEAASTHISERSTSKDGQGAARENETEKQQDSRSKSSQQETSRGSSKLVGLSKRSGTKGEGSTTTTSALSKLTMRLNFLKERRSQIANELQNMDKGKTLGQPSPTSGQNRVSEETEKGSGSNQDPDSSKLQSPHILDRGRSENGGDRGRGSSGGNHPNTTPRTFSR
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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.
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F4JRB0
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HHO5_ARATH
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Transcription factor HHO5 (MYB-domain transcription factor HHO5) (Protein HRS1 HOMOLOG 5) (Protein ULT1 INTERACTING FACTOR 1)
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MVQTETDQRMGLNLNLSIYSLPKPLSQFLDEVSRIKDNHSKLSEIDGYVGKLEEERNKIDVFKRELPLCMLLLNEEIVFLCVAIGALKDEARKGLSLMASNGKFDDVERAKPETDKKSWMSSAQLWISNPNSQFRSTNEEEEDRCVSQNPFQTCNYPNQGGVFMPFNRPPPPPPPAPLSLMTPTSEMMMDYSRIEQSHHHHQFNKPSSQSHHIQKKEQRRRWSQELHRKFVDALHRLGGPQVATPKQIRDLMKVDGLTNDEVKSHLQKYRMHIRKHPLHPTKTLSSSDQPGVLERESQSLISLSRSDSPQSPLVARGLFSSNVGHSSEEDEEEEDEEEEKSDGRSSCRNDETKKKRQVLDLEL
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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.
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F4JRS4
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MORC7_ARATH
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Protein MICRORCHIDIA 7 (AtMORC7) (EC 3.6.-.-) (Protein CRT1-homolog 3) (CRT1-h3)
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MDNSIHVKREIQLPSTSPAGFPGRESVTVVDLCSSDDDSDIGEVAGGLEKVGNNFVGLKRGRDTFGGSSEVDRNNVKKVTTLAELGVGLPEGFGQSNPPESLTHPIPANPCNVFRPVPPPPPPPYAGTSGKIGGCKQFWKAGDYEGAAGDNWDLSSGGFDHVRVHPKFLHSNATSHKWALGAFAELLDNALDEVASGATYVKVDMLENNKGGNRMLLIEDNGGGMDPEKMRQCMSLGYSAKSKLANTIGQYGNGFKTSTMRLGADVIVFSRCPGKDGKSSTQSIGLLSYTFLRSTGKEDIVVPMLDYERRDPEWSKIIRSSTRDWDKNVETIIQWSPFSSEEDLLHQFDLMKDRGTRIIIYNLWEDDQGMLELDFDADPYDIQLRGVNREERNIKMASQFPNSRHFLTYKHSLRSYVSILYLRIPPGFRIILRGIDVEHHSVVNDMMQTEQITYRPQSESYGVVTNMSAIVIIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNATGSDGRGVIGVLEANFVEPAHDKQGFERTTVLARLESRLVQMQKTYWSTNCHKIGYAPRRREKSAYGYDNRDSSPENDREGPSSIKTPTPASDKFYSSSYPNHNGDNGVSGKDGARLQEELRREKERRKALEVEVQLSRQKIEEMKKEQENLIEIFSEERDRRDGEEEVLRNKLEEASNTIDDLLNKIKKMEGSKVPSWRH
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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).
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F4JS25
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SRFR1_ARATH
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Suppressor of RPS4-RLD 1 (Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 5) (AtSNC5)
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MATATATSERFELAKHCSSRNWSKAIRVLDSLLAKESSILDICNRAFCYNQLELHKHVIKDCDKALLLEPFAIQAFILKGRALLALGRKQEAVLVLEQGYKSALQQTADVKQLLELEELLKDARREIDGILKSHATESPQETPAYHSEKSDEKSDKLDNHESGASSNGNSHESSSELGEQSKIVSFSKVASKASKQSDGNSDLCNGSVYKEKENGKCGSQINGYYESCKPCNGSDLHDNLAESSDRFGELSINGNKISIKSSKMSHKAEARCGISDESRKNKKYTIARISGTHSISVDFRLSRGIAQVNEGNYTKAISIFDKVLKEEPTYPEALIGRGTAYAFQRELESAIADFTKAIQSNPAASEAWKRRGQARAALGEYVEAVEDLTKALVFEPNSPDVLHERGIVNFKSKDFTAAVKDLSICLKQEKDNKSAYTYLGLAFASLGEYKKAEEAHLKSIQLDSNYLEAWLHLAQFYQELADHCKALECIEQVLQVDNRVWKAYHLRGLVFHGLGEHRKAIQELSIGLSIENTIECLYLRGSCYHAVGEYRDAVKDYDATVDVELDAVEKFVLQCLAFYQKELALYTASKVSSEFLCFDIDGDIDPMFKEYWCKRLHPKNVCEKVYRQPPLRESLKKGKLKKQDLAITKQKANILRFADLIGKRIQYDCPGFLPNKRQHRMAGLAVIEIAQKVSKAWRIEWRNSTKGTTKNGKKNRRRERTNILSQNRGGAGCSSSSFSETSTGYASLEDRSSGRSILSWQDVYSPAVRWRQISEPCDPVVWVNKLSEEFNSGFGSHTPMVLGQAKVVRYFPNYERTLTLAKSIIKDKLSVRSKKDKVIDLSKDEKIEKIMRAETCDELHNIVGEDFWVATWCDSTGSEGKRLEGTRITCIQKPGRLGYDFSIRTPCTPARWSDFDEEMTSAWEALCTAYCGENYGSTELDALETVRDAILRMTYYWYNFMPLARGTAVTGFVVLLGLLLAANMEFTETIPKGLQIDWEAILNVEPGSFVDSVKSWLYPSLKINTSWRDHTEISSAFSTTGAVVAALSTYND
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Negative regulator of effector-triggered immunity associated with the EDS1 resistance pathway. May localize its interactors to a microsomal membrane. May therefore negatively regulate RPS4 and SNC1 translocation to the nucleus. Contributes to the regulation of RPS2 and RPS4 protein levels and negatively regulates SNC1 stability.
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F4JSE7
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EDR2_ARATH
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Protein ENHANCED DISEASE RESISTANCE 2
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MSKVVYEGWMVRYGRRKIGRSYIHMRYFVLEPRLLAYYKKKPQDYQVPIKTMLIDGNCRVEDRGLKTHHGHMVYVLSVYNKKEKSHRITMAAFNIQEALMWKEKIESVIDQHQESQVPNGQQYVSFEYKSGMDTGRTASSSDHESQFSAAEDEEDSRRSLMRRTTIGNGPPESVLDWTKEFDAELANQNSDNQAFSRKHWRLLQCQNGLRIFEELLEVDYLPRSCSRAMKAVGVVEATCEEIFELLMSMDGTRYEWDCSFQFGSLVEEVDGHTAVLYHRLLLDWFPMIVWPRDLCYVRYWRRNDDGSYVVLFRSREHENCGPQPGCVRAHLESGGYNISPLKPRNGRPRTQVQHLIQIDLKGWGAGYLPAFQQHCLLQMLNSVAGLREWFSQTDERGVHTRIPVMVNMASSSLSLTKSGKSLHKSAFSLDQTNSVNRNSLLMDEDSDDDDEFQIAESEQEPETSKPETDVKRPEEEPAHNIDLSCFSGNLKRNENENARNCWRISDGNNFKVRGKNFGQEKRKIPAGKHLMDLVAVDWFKDSKRIDHVARRKGCAAQVAAEKGLFSMVVNVQVPGSTHYSMVFYFVMKELVPGSLLQRFVDGDDEFRNSRLKLIPLVPKGSWIVRQSVGSTPCLLGKAVDCNYIRGPTYLEIDVDIGSSTVANGVLGLVIGVITSLVVEMAFLVQANTAEEQPERLIGAVRVSHIELSSAIVPNLESE
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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.
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F4JSH1
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APY7_ARATH
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Probable apyrase 7 (AtAPY7) (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (NTPDase) (Nucleoside triphosphate diphosphohydrolase 7)
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MVFGRITELFTAASSRLPAGSQSSVPYMPTGSSPDVGTSVSDSISIGNGGRKNCLRHSASLQDFSSYHGFDPEESILPREAISWGQNGSSFSKEKGSVPNGTNPSTRRKLIRAVMIVMCLFLFAFLVYIVSMYIYTNWSRGASRYYVVFDCGSTGTRAYVYQASINYKKDSSLPIVMKSLTEGISRKSRGRAYDRMETEPGFDKLVNNRTGLKTAIKPLIQWAEKQIPKNAHRTTSLFVYATAGVRRLRPADSSWILGNVWSILAKSPFTCRREWVKIISGTEEAYFGWTALNYQTSMLGALPKKATFGALDLGGSSLQVTFENEERTHNETNLNLRIGSVNHHLSAYSLAGYGLNDAFDRSVVHLLKKLPNVNKSDLIEGKLEMKHPCLNSGYNGQYICSQCASSVQGGKKGKSGVSIKLVGAPNWGECSALAKNAVNSSEWSNAKHGVDCDLQPCALPDGYPRPHGQFYAVSGFFVVYRFFNLSAEASLDDVLEKGREFCDKAWQVARTSVSPQPFIEQYCFRAPYIVSLLREGLYITDKQIIIGSGSITWTLGVALLESGKALSSTLGLKSYETLSMKINPIALISILILSLLLLLCALSRVSNCLPRFFRKSYLPLFRHNSTSASSVLNIPSPFRFQRWSPMSTGVKTPLSPTVRGSPRRPFSFGSSIQLMESSLYSSSSCVMHSCSSDSLGDIQYDSTGSFWSSPRRSQMRLQSRRSQSREDLSSSLADSHMLKM
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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}.
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F4JT76
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VPS54_ARATH
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Vacuolar protein sorting-associated protein 54, chloroplastic (AtVPS54)
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MDSHPSLMGRSITNSNRSSLDLGRPSSSSSSSPSPLTKSISDASSQSLSSILNNPHGGKSGVYGSDASWVGWWSSSTFVAPAEFAPVASTKLPGSELTRSDFHGYVSSISESHGRFEDIRKHTREESCGFDQESHVSGLAACLREVPSLYFKEDFALEDGATFRSACPFSSLNENLALQEKLSQYLDVVELHLVKEISVRSDSFFEAQGQLQDLNVKIVEGCSRIRELKETIRLLDRNLVDSARQIQELSSTRINMLELQRKLRLILYVNQALSALKLLVASADCAGALDITDDLQNLLAGDELTGLYCFRHLRDHVTSSIDSINSILTSEFMRISIHDTGEIDVLILSAANIRGSISSNGNTGEEVKLEEEDTSTLCDRLLPLVIGLLRTAKFPSILRMYRDTLTSEMKNAIKKAVADLLPILVARSLESDFSHGERSVDDGGGLSLASKLRTLSSEAFVNLLTAIFKIVQAHLVRASEVKKAIEWILCNIDGHYAADSVAAAIAVGAVAAETAQEIGFQGGSLVSSPLGKATSKAPPLQGKSSDASSLMNMSRNFRADVLRENTEAVFAACEVTHGRWAKLLGVRALLHPKLKLQEFMSIYDLTQEFITSTEKIGGRLGSSIRGTLQSQAKAFVDSQHESRMTKLKAVLDQETWDEIDVPEEFQSIISSLFASQRLISGKVDDADLNSYHSNRLPLNGSLTSGSGDQNSELRNEKSESSEGSVVSDAQVKPTVSPESLERSKAGVSSATNNQSNQKAHGKSNLFYQGVGYHMVNCGLILLKMLSEYIDMNNSLPALSSEIVLRVVEVLRFFNTRTCQLVLGAGAMQVSGLKSIKAKHLALASQVIDFTYTIIPETRRILFSKVPETRKPLLSVEIDKVAQDFRIHRDEIYTKLVQIMRERLLAHLHGLPKVVEGWNRPPDTNKQTKEFAWPLTREVGYLHRVLSETLHEADVQAIFRQVISIIHTQTSQTLTNLEISSTEAKKRLKLHVELILKCIRSLPSDNANQSDIPNWGQLDEFFAEHFREEEAGEAE
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Acts as 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}.
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F4JTE7
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GPP1_ARATH
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(DL)-glycerol-3-phosphatase 1, mitochondrial (EC 3.1.3.21) (5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase) (AtGpp1/PyrP3) (EC 3.1.3.104) (5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase) (ARPP phosphatase) (Glycerol-1-phosphatase 1) (AtGPP1) (Haloacid dehalogenase-like hydrolase domain-containing protein GPP1)
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MLTTPTRFVALRIPFRSSNKIPISIAPSPKVFPRKPVIRVPASLRFVATMSTPAAAVNATVTVTDAGRGSITHVIFDMDGLLLDTEKFYTEVQEKILARYNKTFDWSLKAKMMGRKAIEAARLFVDESGISDSLSAEDFIVERESMLQDLFPTSDLMPGASRLLRHLHGKGIPICIATGTHTRHFDLKTQRHRELFSLMHHVVRGDDPEVKEGKPAPDGFLAASRRFEDGPVDPRKVLVFEDAPSGVQAAKNAGMNVIMVPDSRLDKSYCNVADQVLASLLDFKPEEWGLPSFQDSHN
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Acts as a glycerol-3-phosphatase with higher stereospecificity for L-glycerol-3-phosphate than DL-glycerol-3-phosphate. Can also dephosphorylate in vitro 5-amino-6-(5-phospho-D-ribitylamino)uracil, also known as ARPP.
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F4JTN2
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LAZ1_ARATH
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Protein LAZ1 (Lazarus1)
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MDILKSYHLLAAAYSAPAWASFMAGAFLVLTLSLSLFLVFDHLSTYKNPEEQKFLIGVILMVPCYSIESFASLVKPSISVDCGILRDCYESFAMYCFGRYLVACIGGEERTIEFMERQGRKSFKTPLLDHKDEKGIIKHPFPMNLFLKPWRLSPWFYQVVKFGIVQYMIIKSLTALTALILEAFGVYCEGEFKWGCGYPYLAVVLNFSQSWALYCLVQFYGATKDELAHIQPLAKFLTFKSIVFLTWWQGVAIALLSSLGLFKSSIAQSLQLKTSVQDFIICIEMGIASVVHLYVFPAKPYGLMGDRFTGSVSVLGDYASVDCPIDPDEIRDSERPTKVRLPHPDVDIRSGMTIKESMRDVFVGGGEYIVKDVRFTVTQAVEPMEKSITKFNEKLHKISQNIKKHDKEKRRVKDDSCMSSSPSRRVIRGIDDPLLNGSFSDSGVTRTKKHRRKSGYTSAESGGESSSDQAYGGFEVRGRRWITKD
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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.
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F4JTP5
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STY46_ARATH
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Serine/threonine-protein kinase STY46 (EC 2.7.11.1) (Serine/threonine/tyrosine-protein kinase 46)
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MVMEDNESCASRVIFDALPTSQATMDRRERIKMEVFDEVLRRLRQSDIEDAHLPGFEDDLWNHFNRLPARYALDVNVERAEDVLMHKRLLHSAYDPQNRPAIEVHLVQVQPAGISADLDSTSNDAGHSSPTRKSIHPPPAFGSSPNLEALALAASLSQDEDADNSVHNNSLYSRPLHEITFSTEDKPKLLFQLTALLAELGLNIQEAHAFSTTDGYSLDVFVVDGWPYEETERLRISLEKEAAKIELQSQSWPMQQSFSPEKENGQTGARTHVPIPNDGTDVWEINLKHLKFGHKIASGSYGDLYKGTYCSQEVAIKVLKPERLDSDLEKEFAQEVFIMRKVRHKNVVQFIGACTKPPHLCIVTEFMPGGSVYDYLHKQKGVFKLPTLFKVAIDICKGMSYLHQNNIIHRDLKAANLLMDENEVVKVADFGVARVKAQTGVMTAETGTYRWMAPEVIEHKPYDHKADVFSYGIVLWELLTGKLPYEYMTPLQAAVGVVQKGLRPTIPKNTHPKLAELLERLWEHDSTQRPDFSEIIEQLQEIAKEVGEEGEEKKKSSTGLGGGIFAALRRSTTHH
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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. Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins.
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F4JTS8
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NOV_ARATH
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Protein NO VEIN (Protein EMBRYO DEFECTIVE 2597)
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MQGNHDGSWSLHPSTNNGSGRANGNININTVPGGGYLPQANPVFPNFNQPIRYPIPQFPANFYRPNFPDFSLGNPNFQPHQNLNFLHQQIPHQYGSAANHFLQNHNQNSFSFPPQSIPNNDISISQNHGAFENSSLKRRRQEEVVQVTDVVPKSNFASGESANNSFSVSLPIPIATDDSGVSRVHGEKSSGKPKRKVDVLRIDKAVNKTRKLFVAAGESVSSTRVSRAVLEELQADSWRSLGVQMQDVPSLRQLMAIEGKINAFIHCFVGARRIVTLHDLEVAICRNEFVDSFDDLELGPLLQHPLVLLYFPSISSSTGPVKITSEEIISFLDSYLHTYMTEDVKLDEFLNFVASQKSVTSKEKLGVRIQSLRMYVSFILDAKRQEGETLKVLLTELHQKYHIPSSKKQQRDKSLTVSERADSFALHHKDYCGKHIRFDSSSSDENDNVYEVRNLNSSDHINSCPYPSVAEEMKRLGGSNKKRKGERRNHEKSDSSKLLRKSPSKLQGHAKQEIPKLADDSEAKKVFSVDEADFTLSEGDLRLFISTWKDTCKELSISTFVEKMLSFYNLGGSEGRAQIKRAKAMSSFPFVGLLNVAVTSLRRGMWDSIYDNFQMTSLSDTTNTGSGNQVGEINPIENSELSKTQHVMPPTHCNTVEEIIRRLSLYFEHDLSGAKHIGIFRKLQTCENLLAEQFQVQDFESLGWGGFFAFLEKHMLLLPTQLQRFLSRELQEEFPLEVHVNENLLTLLLSQASEFSSDKVLSRQTLARLVAEQFPSISFKVVGRDSEENFSEIIGKKKSSSKCVLFSATLLGAENSLTSKYLEESLTVGNDTEARSTTLNAVASKEVLDVLLRVPLLSDLNSWCHWDLRYAPQFGPLMGCLNEINSTDLLCLVTRDGKIIRADPSATADSFLEAALQGSAYRTAAQLLSLISLNGRTHLPFSLLKCYAKRAFEVFFYNYSEEMELNDRNSLVQMHGPEKLSTSFDKVIVVGEKAKVAKRDYAASKFLLDCLGYLPGEFRSLVVDILLPGLRSVVKDAPTRVLSACEQTEQRIMLHDAGLLLGIVEWISDYHKFCSSCSPNSSIVENASSNLDSGAGFVQNELEDPVQTKQRCMIVSEKSCEYKEEPHESCHTFGGSGILCDSVGEAFTQTAPEFYDNRASVIDSIRRDEFGLDLTSSGSEMSMLQKQHARLGRALQCLSQELYSQDSHFILELVQNADDNKYPEHVEPTLTFILQKTGIVVLNNECGFMPENIRALCDVGQSTKKGSGGYIGKKGIGFKSVFRVSDAPEIHSNGFHFKFDISEGQIGYILPTVVPPHDIESLSSMLSGRALHLKDAGWNTCITLPFRAIDSERTTVNHIEPMFSDLHPSLLLFLHRLQCIVYRNVLDDSLLVMRKEVVSKNIVKVSCGENSMTWFVASEKLKATNLRDDVQTTEISIGFTLDMLEDGTYRSCMIQEPVFAFLPLRTYGLKFIIQGDFILTSSREDVDEDSPWNQWLLSEFPGLFVDALRSFCSLPSFTQNLGKGVSSYMQLVPLVGEVHGFFSSLPRSIISRLRTTNCLLLEGDGEEWVPPCKVLRNWNEKIRVLLKDGLLQEHLALGFLDKDIVLSDSLSRALGIEDYGPKTLVQILSSLSHKNGCLQSMGFTWLSSILTELYLLFRSSGHGNVELGIDKSLIDDLHKIPFIPLSNGKFTSLDEGAVWLHHDTTGLDLGDVFEAFPVLYGNLRTIDHSLLLASSVDEKSSVDDLVNMLCAIGVQKLSAHEIVKAHILPAFEARSTGAVDGLMVDYLCFVMTHLRSGCHICLKERKYIISELRSKALVLSNYGLKQLGEGSIHFGEEYGNQVNMKKLTKNLDISWHVVDGTYLKHPASKFYACGLKEWREFFQEIGIADFVQVVQVEKSIAEFYSVSHCEKYDINLLSPDLTVKDWESPELVDLLSLLHKSNGRKGCKYLLEVLDRLWDDCYYDKTTVNYNSGTHGIIRSSESSFMRVICDSLWIVSSMDSKLHLSKDLYHDCDDVQSILGMNAPYAVPTVTSVKLLSDIGFKTKVSLDDALEVLESWVHCGDSFKSSISQITRFYKYLWNEMADSKQKITEKLHTLPSVFVPHGIASRQNDMISGIFLSLDDVYWNDSAGVLDEIKEISSQISSVVEPLRRKTLGNIYPGLHDFFVNGCGVPETPSFQEYLKILGQFAHNVSPSSAAKAVFKIFLKWSDDLNSGKSSEDVIHFKERLSELEYTVLPTENDKWVSLHSSFGLVCWCDNEKLKKRFKNKDKIEFISFGENDDEGQEVLQTKVSGLMHSLGIPSISEVVKREAKYEGLQDNTVTVSLVNWALPYAQRYIFTLHHEKYTQTKKTVHSQVKRLQVFVVDKLSYRNVIPQYGISSKKEFKCSSLLQDKALYTTPSLDSHSLFMELSRLFFNGVPDLHLANFLHLIKTMAESGLSEEQMESFILNSQKVHQVPDGEEIWSLKSAVKAKKKAGISLSWLPSSSKTRHGSSKTNTDDSKQELDTSSSKEDVTEALEEKIPIEMTNTNLVSGYDNCAGTSSRASEPNPLHSMHMISGSTSGNQAAMHLNPNLPHEWNNSFTANFSDRDQLHTGTPWAAQAQQTGRKGEEIAYRYFVAKYGNEALVKWVNDQSETGLPYDLMIENRGGKKEYVEVKATVSTRKDYFNLTVREWQFANEKGESYIIAHVLLGNSNAILTQHRNPVKLCQEGHLRLLVLMPNQRNEVNVTF
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Essential protein required for cell fate determination during embryogenesis. 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). 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.
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F4JUI3
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BPC5_ARATH
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Protein BASIC PENTACYSTEINE5 (AtBPC5) (GAGA-motif binding transcriptional activator BBR/BPC5)
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MESGGQYENGRYKPDYYKGTQSVNVMPKKEQHNALVMNKKIISILAERDAAVKERNEAVAATKEALASRDEALEQRDKALSERDNAIMETESALNALRYRENNLNYILSCAKRGGSQRFITEESHLPNPSPISTIPPEAANTRPTKRKKESKQGKKMGEDLNRPVASPGKKSRKDWDSNDVLVTFDEMTMPVPMCTCTGTARQCYKWGNGGWQSSCCTTTLSEYPLPQMPNKRHSRVGGRKMSGSVFSRLLSRLAGEGHELSSPVDLKNYWARHGTNRYITIK
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Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes.
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F4JUU5
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S2P_ARATH
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Membrane-bound transcription factor site-2 protease homolog (EC 3.4.24.-) (Endopeptidase S2P)
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MEISGRRMRRFRMRFRRDHLTGGENIENEASCCYCDLKISNFNEPIFRLGRRFSGVLKVWFSIGLGFGVASLILVTVFLLLQFHSNPLFSNRLTSAVFGFSPSTRVSLSGIAYVLVSTVITVSVHELGHALAAASEGIQMEYIAVFIAAIFPGGLVAFDNDVLQSLPSFNALRIYCAGIWHNAVFCALCVFALFLLPVMLSPFYKHGESLTVVDVPSVSPLFGYLSPGDVIVSLDGIQVHKPSEWLELAAILDKENSKTSNGSLYLGGSRRFHHGKGYCVPISLIEEGYKGKMVENQFVCPGDLTAFRTMPCSNAAIREVSVCLDAKDIVKLQKCGDGWVTTSDTDNQSDCVCPQGDLCLQAMQSPGVLWTEITYKRTSSQDCSRLGLDFNTSNCLGTFVFVGDLIAMSHSVHLTAYQPRWLFNFFGKSFPNILERSLTCTFHVSLALVLLNSLPVYYLDGESILESSLQSFTWLSPRKKKKALQVCLVGGSLLSFLAFFRIFLLGLPLSRRW
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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 functions 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.
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F4JUY5
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GAMT1_ARATH
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Gibberellic acid methyltransferase 1 (Gibberellin A(9) O-methyltransferase) (EC 2.1.1.275)
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MESSRSLEHVLSMQGGEDDASYVKNCYGPAARLALSKPMLTTAINSIKLTEGCSSHLKIADLGCAIGDNTFSTVETVVEVLGKKLAVIDGGTEPEMEFEVFFSDLSSNDFNALFRSLDEKVNGSSRKYFAAGVPGSFYKRLFPKGELHVVVTMSALQWLSQVPEKVMEKGSKSWNKGGVWIEGAEKEVVEAYAEQADKDLVEFLKCRKEEIVVGGVLFMLMGGRPSGSVNQIGDPDSSLKHPFTTLMDQAWQDLVDEGLIEEEKRDGFNIPVYFRTTEEIAAAIDRCGGFKIEKTENLIIADHMNGKQEELMKDPDSYGRDRANYAQAGLKPIVQAYLGPDLTHKLFKRYAVRAAADKEILNNCFYHMIAVSAVRV
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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.
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F4JVH1
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CFM3B_ARATH
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CRM-domain containing factor CFM3B, chloroplastic (Protein CRM FAMILY MEMBER 3B) (AtCFM3b) (Protein SUPPRESSOR OF RFC THREE 2)
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MAINSSHHFCPMTTTTTTSAKFVDSLGSSFCKFHGTSSSISLRSYRFGFSFMKNVKRLSCEGSSSSSSSRNENWNRTQKQNQFRPSKVVLNRRKDERFSDLGVISGENSSRSGDVGGGSGSSSTMEKIVEKLKKYGFVDEDQFQDKEVEQERRIEKSSVEERFYVEERRGGFSEESPFGVYGGNDEVKFPWEKVSSMEKKELVNGEWTAKKESRYSLAEMTLSEFELNRLRNVMFRTKSKMRVTGAGVTQAVVDAIQEKWKGSEIVRLKIEGSSALNMRRMHEILERKTGGLVIWRSGTSIALYNYKGGSNRDGSGNMNKQVYRRAERLPSSLPTSTVDQSVQLVNLPQLEKEPTVVGNKDRTSPQEVEYEDEINELLEGLGPRYTDWQGGYPLPVDADLLPGIVPGYEPPFRALPYGVRSTLGTKEATSLRRIATVLPPHFALGRSRQLQGLATAMVKLWQKSLIAKVALKRGVQLTTSERMAEDIKRLTGGMLLSRNKDFLVFYRGKSFLSLEVGEALMEKEMLVRTLQDEEEQARLRASSALVVPSIKANQQLARTLQDKEEQARPSALVLPSTKANQNLVSAGTLGETLDATGKWGKNLDNDDHVEEMKQEVEKVRSAKLVRKLERKLAFAEKKLLKAERALAKVEESLKPAEQRTDLEGITEEERFMFQKLGLKMKAFLLLGRRGVFDGTVENMHLHWKYRELIKILVKAKTLEGAQKVAMALEAESGGILVSVDKISKGYAVIVYRGKDYKRPTTLRPKNLLTKRKALARSLELQKREALIKHIEAIQTRSEQLRAEIEQVELVKDKGDETLYDKLDMAYSSDEETEETDGEEDDVYLDTYEDEGEDDEEGGIQANGSLSETDVEFGSDESDTDFGDNSASSTTPETTFVELQNEELDVQP
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Binds specific group II introns in chloroplasts and facilitates their splicing. Exhibits non-specific action during plastid rRNA biogenesis RFC3 prevents unaccurate splicing to improve the accuracy of plastid rRNA processing. Acts on subgroup IIB introns. 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. Required for seed development.
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F4JVI3
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MTEF5_ARATH
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Transcription termination factor MTERF5, chloroplastic (Mitochondrial transcription termination factor 5) (mTERF5) (Protein MTERF DEFECTIVE IN ARABIDOPSIS 1)
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MQSLSQLGPSEIFLVARREKPSTRAQLWFTGRLSFRQETNGIRLKNRVEFSPRPVPPNLIAAEKEEAKAVLTLFFKKQGLSNSLSSRLINKSDLFIDHLVSRLHSVHKARYLVGRELTTLEIRDSLIPYLEQLHEEHGDLLAELVVSFPDPPAEPRLVASSPVSVLPPRGDTDSAADTRKLRAVSRVSELDTEGALRPQTLYLLDLGLNLEQIKTITRKFAAFPYYSLDGKIKPVVEFLLDLGIPKSDIPTILCKRPQICGISLTDNLKPTMAFLETLGIDKNQWAKIISRFPAILTYSRQKLTSTVEFLSQTGLTEEQIGRILTRCPNIMSYSVEDKLRPTMEYFRSLNVDVAVLLHRCPQTFGLSIESNLKPVTEFFLEKGFGLDEIGIMISRYGALYTFSLKENVMPKWDYFQTMDYPKSELVKFPQFFGYSLQERIKPRYELVQRSGVRLLLNQVLSLSGIEFEKVVKKKMMKLVSNNVIAEQSSGGLL
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Transcription termination factor required for processing and steady-state levels of plastid transcripts. Involved also in chloroplast transcriptional pausing, a general feature of chloroplast genes. 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. May play a role in response to abiotic stresses.
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F4JVN6
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TPPII_ARATH
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Tripeptidyl-peptidase 2 (EC 3.4.14.10) (Tripeptidyl-peptidase II) (TPPII)
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MDLSLQLQIHGALINKGPSCTSYWASSSSLSLPRDFISSSTFLLHRRLRRRSCSRSRGIRLRRSGFSAMPCSSSDTLTASRVGCGGGGGGGAVGGGAENASVANFKLNESTFIASLMPKKEIRADCFIEAHPEYDGRGVVIAIFDSGFDPSAAGLHVTSDGKPKVLDVIDCTGSGDIDTSTVVKANEDGHIRGASGATLVVNSSWKNPTGEWRVGSKLVYQLFTDDLTSRVKKERRKSWDEKNQEEIAKAVNNLYDFDQKHSKVEDAKLKKTREDLQSKVDFLKKQADKYEDKGPVIDAVVWHDGEVWRVALDTQSLEEDPDSGKLADFSPLTNYRIERKYGVFSRLDACSFVANVYDEGKVLSIVTDSSPHGTHVAGIATAHHPEEHLLNGVAPGAQIISCKIGDSRLGSMETGTGLTRALIAALEHNCDLVNMSYGEPALLPDYGRFVDLVTEAVNKRRLIFVSSAGNSGPALTTVGAPGGTTSSIIGVGAYVSPAMAAGAHSVVEPPSEGLEYTWSSRGPTSDGDLGVCISAPGGAVAPVPTWTLQRRMLMNGTSMASPSACGAIALLLSAMKAEGIPVSPYSVRRALENTSTPVGDLPEDKLTTGQGLMQVDKAYEYLKQFQDYPCVFYQIKVNLSGKTIPTSRGIYLREGTACRQSTEWTIQVDPKFHEGASNLKELVPFEECLELHSTDEGVVRVPDYLLLTNNGRGFNVVVDPTNLGDGVHYFEVYGIDCKAPERGPLFRIPVTIIIPKTVANQPPVISFQQMSFISGHIERRYIEVPHGATWAEATMRTSGFDTTRRFYIDTLQVCPLRRPIKWESAPTFASPSAKSFVFPVVSGQTMELAIAQFWSSGLGSREPTIVDFEIEFHGVGVDKEELLLDGSEAPIKVEAEALLASEKLVPIAVLNKIRVPYQPIDAQLKTLSTGRDRLLSGKQILALTLTYKFKLEDSAEVKPYIPLLNNRIYDTKFESQFFMISDTNKRVYAMGDVYPESSKLPKGEYKLQLYLRHENVELLEKLKQLTVFIERNMGEIRLNLHSEPDGPFTGNGAFKSSVLMPGVKEAFYLGPPTKDKLPKNTPQGSMLVGEISYGKLSFDEKEGKNPKDNPVSYPISYVVPPNKPEEDKKAASAPTCSKSVSERLEQEVRDTKIKFLGNLKQETEEERSEWRKLCTCLKSEYPDYTPLLAKILEGLLSRSDAGDKISHHEEIIEAANEVVRSVDVDELARFLLDKTEPEDDEAEKLKKKMEVTRDQLADALYQKGLAMARIENLKGEKEGEGEEESSQKDKFEENFKELTKWVDVKSSKYGTLTVLREKRLSRLGTALKVLDDLIQNENETANKKLYELKLDLLEEIGWSHLVTYEKQWMQVRFPKSLPLF
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Serine protease of the proteasome pathway that may function with the 20S proteasome to degrade oxidized proteins generated by environmental stress.
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F4JW79
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RDM3_ARATH
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Protein RNA-directed DNA methylation 3 (KOW domain-containing transcription factor 1) (Protein SPT5-like)
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MDRKGKGKQVAGSDSYSGGQKRKNSVEFRDEGLRIKKRKNPEVLQFFEESAEVGYYGGSSDEDDDGLGFLNDMEDEPEVEESSKAGKGEKGKSSFVFPKEEDLNEEEFDRIMEERYKPGSGFLRYADDDIKDAIEMDALAPTSKDPPIWKVKCAIGRERRSVFCLMHKFVELRKIGTKLEIISVFSVDHVKGFIFIEADKEHDVLEACKSLVGIYATRMVLLPKAETPNLLTVQKKTKKVSEGTWARVKNGKYKGDLAQIVAVSDTRNKALIKLIPRIDIQALTQKYGGGVTVQKGQTPAPRLISSSELEEFRPLIQVRRDRDTGITFEHLDSLMLKDGYLYKKVSLDSISSWGVIPTKDELLKFTPVDRKETGDVEWISEIYGEERKKKILPTCREGGKGEGSGGGKGEGSGGGKGEGSRGGKGEGSSDFKSESSYELYNLVCFSRKDFGLIVGVDDKGDGYKVLKEGIDGPVVVTVGKKEMQNGPFDSKFTALDLNKKQISVNDVVKISKGPSEGKQGVVRQVYRGIIFLYDESEEENGGYFCCKSQSCEKVKLFTEESNEKTGGFDGTAFEDFVSSPKSPLSPEKEWQPRERYNSSNQGDIGSTYSIGQKLRIRVGPLKGYLCRVIALRYSDVTVKLDSQHKIFTVKSEHLAEVRDRNTVLSTSGDAGTGSFQPFGMLGTESSTGDWAIGAGTSSEGGNWNIGGPSTDSHESLNIERNMVQLCREKNPWGGSKPTSDVSPTVADDNTSAWANAAAENKPASASDQPGGWNPWGKTPASEAGTVSGWGDTSASNVEASSWEKQGASTSNVADLGSWGTHGGSSGGNKQDEDSVWGKLCEASESSQKKEESSWGKKGGSDGESSWGNKDGNSSASKKDGVSWGQQDKGSDESKGGSAWSNQCGDFGSGKKKDGSSGWNKSAEDSNANSKGVPDWGQPNDGSSWGKKGDGAASWGKKDDGGSWGKKDDGNKDDGGSSWGKKDDGQKDDGGSSWEKKFDGGSSWGKKDDGGSSWGKKDDGGSLWGKKDDGGSSWGKEDDGGSLWGKKDDGESSWGKKDDGESSWGKKDDGGSSWGKKDEGGYSEQTFDRGGRGFGGRRGGGRRGGRDQFGRGSSFGNSEDPAPWSKPSGGSSWGKQDGDGGGSSWGKENDAGGGSSWGKQDNGVGSSWGKQNDGSGGGSSWGKQNDAGGGSSWGKQDSGGDGSSWGKQDGGGDSGSAWGKQNNTSGGSSWGKQSDAGGGSSWGKQDGGGGGSSWGKQDGGGGSGSAWGKQNETSNGSSWGKQNDSGGGSSWGKQDGGGGGSSWGKQNDGGGGSSWGKQGDGGSKPWNEHSGGGRGFGERRGGGGFRGGRNQSGRGGRSFDGGRSSSWKTDNQENTWKSDQSGGSDWKKGWGEDSNNSKPSGSSAGGCAGNWPSWDTNSKKETNDKPGDDSKSAWGTSNDQVNTDNNNDSWNKKPNNDVGTSGEADNAWGGKTNAVAPSPSGSAAWGTGDKKTGW
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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. Promotes the expression of 24-nt RNAs. Required for the initial establishment of DNA methylation. Together with AGO4, required for transcriptional gene silencing (TGS) by DNA methylation and repressive histone modifications (H3K9me2) of several chromatin loci.
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F4JWB3
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MYTM2_ARATH
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Phosphatidylinositol-3-phosphatase myotubularin-2 (AtMTM2) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
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MTALRPLSGRSRSLRCSSEKMEGTGSWDVLEWTKLDSASWSGSYSNLDCLLESERIIFEACGVILINTDEAGTLLLSNFRILFLSEGTRKLVPLGTIPFVAIEKFNKLAPKVQSNKYHNNENAPTRLLQVTGKDMRIVVYGFRPGTKQRHTVVDTLLRCNKPERVWDLYAFTCGPSQFGNTNPKERLLNEYFRLLGKSSQRASMNMIEDGSFTLSNDLWRITNLNSNYDLCQSYPFALMVPKSISDEELLQTSTFRARCRLPVISWCHPGSGAVIARSSQPLVGLMMNMRSNSDEKLVASFCTQLAGHKGARRKLYIVDARPRKNALANGAKGGGSESSSNYLQSEIVFLGIDNIHAMRESFSRLRDYLDMHGTTSSDGTSSFLRHGGWTWGGGNLSSMSASVSVLGDSGWLSHIQSILAGVAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFSGFQALVEKDWLSFGHPFSDRVGMPNVSESGNFELPIQSSSARSFPSSPVRQSPGSAAAQSSSSSYGLNNYSPIFLQWLDCISQLMRMYPSAFEFSPTFLVDFIDCLLSCRFGNFLCNSEKERQQCGISETCGCIWAYLADLRSSSGTSHVHCNPFYDPSRYDGPLLPPAAALAPTLWPQFHLRWACPVEPNVTETEDQCRAMTVKYSEMKKEKEEAERKVDELSSAMESLNEELLNERDISRAARESAKRATKERAVISRAVQSLGCKVKFTRNGDCTVEVEDGPQKCSHSIPQKQSEDNTTDVSESISSVTEQNVCEAVCPLRTREGTCRWPDAGCARIGNQFLGLKTNFEAFDNLCVYDSYFTAE
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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.
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F4JXF1
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GAF1_ARATH
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Protein GAMETOPHYTE DEFECTIVE 1 (Probable ribonuclease P protein subunit p30) (AtRPP30) (RNaseP protein p30) (EC 3.1.26.-)
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MGFFDLSIPYNEPPRSGGKEIAGGKTLRLKLATKAMELGYVGIAHNRSIKGVMSDKDSCTIPLLTLGSLIKVAPRLASSVGFHRDLLGVPRTTPFRQYTRLTVHVESNAQCQSLNSGNPILKSYDIIAVRPMNQNAFDYACEKAEVDLISIDFTDKMLFRLKHPMVKAAIQRGIYFEIKYSDILMDAQTRRQVISNAKLLVDWTRGKNLIISSGAPSVTELRGPNDVINLMFLLGLSAERARAAISKNCRNMIAKVLKKKRFHKEAVRVELLSAGDTFSLEQPLSEDCMKWDRLSSGEGDMLLDDLAKAFDATNVVAHKSSKAIDFTSVLDGLPKHGFRVKDIVGTESVTQPSAAKVIDTQVHSSNQVSELRMATASSDDNLREIETISQIDMLMSEDDNKVEPTTNVLKEEAFALRKCSASHGQGILVQNQTATPFTLTRCTKSEAASDVSMNIESTSEGGSMSPSKSDHGIPQSPVEVNNMGNAAFEEEASVDENSKERATTGHASNDEMHITESGHHASIDDEKHIPEPEHLTSIADEMKIDCSSEANHDEYMEVTMEDQMHETVQMRLCKTMTKHQD
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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.
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F4JY12
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GFS12_ARATH
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Protein GFS12 (EC 2.7.10.-) (BEACH domain-containing protein D) (BEACH-domain homolog D) (GREEN FLUORESCENT SEED 12)
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MRGEDSDLCFDCLDQRINSDFSDQIVFSYGVSDSPLPFGSSAVVKVSDSSEEFSASCSSCESTSSQFILEYLRKDEHGCLAKYVDKFVVKDREGNSNDAVESDECLDCSTSGSQATEDDDTENITCGSVTCEHSGSFSCWRTVAALLPIAQIRKCSASELQKLASSFHYECPEDQILASLHRLIDGKSSGQATHSFLCLLLGLPLLEEKSKLRCLRHPNLSPVLGLLTSSDCLVSVLPKAPYTLENILYYSPSAIKSEWHRNFIIYQLLSALAHLHGLKVSHGDIRPSNILLSDSLWSWLTIYSKPDLGSVDANSSASRRRWCVEGCYSYGLYADLKISSHLDWQTHFDKWWKGELSNFEYLLVLNKLAGRRWGDHTFHPVMPWVIDFSKKPENDSDSGWRDLRKSKWRLAKGDEQLDFTYSTFEFPHHVSDECLSELAVCSYKARRLPLSVLRKAVRSVYEPNEYPSDMQRLYDWTPDECIPEFYCDPRIFCSLHPSMSDLAVPPWASSPDEFIRLHRDALESPHVSSLIHHWIDITFGYKMSGHAAITAKNVMLSSSEPTVPRSVGRRQLFFRPHPVRLGFSREKEQSRNELEMHTFHGFGVDNKRSVILLADEYLEETEEASAFSDHATHLCPKYHLRENLVESPLHVSYSENTKKVNTSLPGTSKNKGLSSRISLNYLLEHMEVRDEASTELQELLQWRQDFCTGNISKDIAGDIFSIGCVLAELYLMKPLFNSVSLATYLEGGDLPELIKELPPPTQVIVEACIEQDWRRRPSAKSLLDSPYFSATVRSAHLFAAPLQLLAKGQTRLCYAASFAKQGVLKVMGTFVAEMCAVYCLPLVTTPLSEDECELAYVLLKEFTKSLTPMAVQRLVLPSIQKILLTTGYSHLKVSLLQDSFVRELWNQIGKRVYLEMIHPLVISNLYNSPDKISASAASVLLIGSSEELGAPVTVHQTILPLISYFGKGICTDGIDVLVRIGRLLGVNFIVKQMLPLLEHVVCFCIDLSSMKKPEPVHSWCSLALSDCLITLDGLVALISDELLIHELTKGRLCLHVRVLMQKNLELRVLQFAATSLMSICQRIGQEMTALHVLPQLKELFDEFAFSEKSTDASDSLSWKIRTAEQKFHPESPIKSRMDLVLLLYPSFASLLGMEKLRQGCPTWLLLEQYLLKHHNWKWEYTGRSSRYNMEARPVLKQGPASKHTPKVLLNGSGRSVPQSQGLRNSNHLKLHIHVPVEGQEAVLNPLVHEPWSWFPSPVTCWDGLDIGRFGNPKDENRWKIRASVLSSARAHHGALRSLVVSEDECTVFTSGIDPGFKGSVQKWELASLSCVSSYHAHEEVVNDIGILSSTGKVASCDGTIHVWNSQTGKLISLFSESPSDQDQASSDPSSKNNSNPCNRHASHGLSSGIFDENLYTCMHYLEYMDQLIVGTGFGALRFIDLARGQKLELWGGEAIESGFTSLVSALCSGGSQTKHGDGASVSPSWIAAGFSSGQCRLFDLRENGFISSWRAHDGYVTKLVAPESHLLVSSSLDKTLRIWDLRKSWTPQPFVVKGHNDGVSGFSIWGKDVISISRNNIGIFSLAKSQDEEEQQQQRIIPQKLYMAEKGGRVKSDLSTICVLPFSRLFIVGAHDGHLRICC
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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.
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F4JY24
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CHR17_ARATH
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ISWI chromatin-remodeling complex ATPase CHR17 (EC 3.6.4.-) (Protein CHROMATIN REMODELING 17)
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MARASKREVSSDEAYSSEEEEQVNDQANVEEDDDELEAVARSAGSDEEDVAPDEAPVSDDEVVPVEDDAEEDEEDEEKAEISKREKARLKEMQKMKKQKIQQILDSQNASIDADMNNKGKGRIKYLLQQTELFAHFAKSDPSPSQKKGKGRGRHSSKLTEEEEDEECLKEEEGGIVGSGGTRLLTQPACIQGKLRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPEERRHIREELLVAGKFDICVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLEVVNGGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLVTNAGKMVLLDKLLPKLKDRDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTENAIEAKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDSADFYDFDDDNKDESKVDFKKIVSENWNDPPKRERKRNYSEVEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQAHQKTQMKDTIEVDEPEEVGDPLTAEEVEEKELLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAQVFQVRYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGNWDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLIEKENQEFDERERQARKEKKLSKSATPSKRPSGRQANESPSSLLKKRKQLSMDDYGKRRK
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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. 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. Necessary to acquire heat stress (HS) memory.
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F4JY37
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RUK_ARATH
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Serine/threonine-protein kinase RUNKEL (Protein EMBRYO DEFECTIVE 3013) (Protein RUNKEL) (EC 2.7.11.1)
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MNQYHIYEAIGHGKCSTVYKGRKKKTIEYFACKSVDKSRKNKVLQEVRILHSLNHPNVLKFYAWYETSAHMWLVLEYCVGGDLRTLLQQDCKLPEESIYGLAYDLVIALQYLHSKGIIYCDLKPSNILLDENGHIKLCDFGLSRKLDDISKSPSTGKRGTPYYMAPELYEDGGIHSFASDLWALGCVLYECYTGRPPFVAREFTQLVKSIHSDPTPPLPGNASRSFVNLIESLLIKDPAQRIQWADLCGHAFWKSKINLVQLPTQPAFDDMIGINTKPCLSERNGDRPNKTPPKYREKDRKGGSKQNENSIQGSKGHETPIKGTPGGSKAQAKLPSRATEEKHGGRPAANRQVNILRLSRIAKANLQKENEKENYRRPLPNSNENCAEVKIDNTDMELDFDENNDDEGPDESEGTENTSCAQEERVMSHNENHRRQRVVSSNVPDENSSANETPTLGEARDCHEDQSEPMDMSAAPPSASPQLKTHRGRETSGVAVNHDSSKAPTSLTDVFWHISDLSVRPVMPSRKSDKEAVHSLSFETPQPSDFSKKGKQELEPLNNRIITVLSGSSSGLSEKQNLIRYLETLSTNADAANILTNGPIMLVLVKVLRLSKTPAFRVQIASLIGLLIRHSTSIEDDLANSGILDSLTNGLRDKHEKVRRFSMAALGELLFYISTQNEHKDFKPPESPSKETRSASGWQVSNALISLVSSVLRKGEDDLTQVYALRTIENICSQGAYWATRFSSQDLISNLCYIYKATGKQESMRQTAGSCLVRLARFNPPCIQTVVEKLSLKEIASSFVKGSAREQQVCLNLLNMAMIGSHTFTSFGRHLVTLTEEKNLFPSLLSIIEQGTEVLRGKALLFVAFLCKNSRRWLTNFFCNARFLPVVDRLAKEKDSYLQQCLEAFVNVIASIIPGMLDTITNDIQQLMTGRRHGPVSPLNSRAPVKTNAHLFPVVLHLLGSSSFKNKMVTPQVLRQLANLTKLVEASFQGRDDFRVTLLQVLECITGDAPLVTQNGEIIIREILPSLAAIYNGNKDGDARFLCLKIWFDSLTILLTECTEIEQQISEDLKSISNSHFLPLYPALIQDEDPIPAYAQKLLVMLVEFDYIKISNLLRHNTVSQCFEFLLGDLSSANVNNVKLCLALASAPEMESKLLSQLKVVRRIGNLLEFVNAKDMEDFLEPTLSLCRAFLLRSLGNKKGLSSNYTKEPTLLSEASFTFEVDPQECIRDIADFGSNIGLFLHFAGLDDDTSIAVADIASECVVLLLKAASREATTGFLTNLPKITPILDSWRRRKSTELHLLVLKRVLHCLGYACKQYLSQAMILSISGHDVSKINAIVSEMKNSDAAGLNSIASLVAMELQRLPR
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Essential protein that regulates phragmoplast microtubule organization during cell plate expansion in cytokinesis during cell division, both somatic and syncytial. Required for endosperm cellularisation. In pollen development, involved in cellularisation during microsporogenesis by regulating radial microtubules (MT) organization in microspore mother cells. Seems to not have kinase activity.
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F4JYC8
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PTM_ARATH
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DDT domain-containing protein PTM (DDT domain-containing protein 1) (Membrane-bound transcription factor PTM) (PHD type transcription factor with transmembrane domains)
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MEAKVPRPRGRPRKRQRLEDDNRKLNNRGKKQVLEVEPAVPISLLGCYMLKDFDDNEVFLGKIVSYDTGLYRVIYEDGDCEELESGDLRRLIISDSYLDDELRVRRKKLDKLILKKEEKKKRNSPENKAVELPNQVNGVQARAVTNSEDGDSYSDSESSESGDKRGSDLEIEAPLVPPVDLPPSSGTIGIPEEAVAHLLSVYGFLRSFSFQLYICPFELNDFVGALYFSGPNSLLDAVHVALLRALKGHLERLSSSKSVLASKCLRCIDWSLLDVLTWPVYLVQYFTAMGHASGPQWNIFNKFVVEIEYYSLPIGMKLKILQILCDDIFDVADLRDEIDAREESEIGFDPDRVATGLLENVPRRVHPRFAKTSAYKEKEVTDSSTNESKDLDSRCTNGGSNEVSSDLDGNSDECRICGMDGTLLCCDGCPLAYHSRCIGVVKMYIPDGPWFCPECTINKKGPKIAHGTSLRGAVQFGMDPHGRLFLGTCNHLLVLNISVNGDAVVKYYNVNDISKVVLVLISASSHTLEYVEICKAITQYWDLPEGISLREGEIGLTQAKDREDGKVSEITKSDSANISNRSHTQTVFDLPTSTLGNTNSAVTGGSCGIQGKKLAARVTYLGLSFKPNTYNNHYTNGELAVSAAASLAVLSSEETHEPDLRKYNSAKKAASSNILEQMKAFSLVAPRFFWPSPDKKEITRERCGWCHSCRLTSASRRGCMLNAAVAGATKGAMKIFSGLFPLKNGEGVLSSIAAYILYLEESLRGLIAGPFLSESPRKQWRKQVEEASTCKALKAPLLELEENICSIALSCDWFKQMDDWLIEHSIFQSAPVTLGVPQRRGPGRTKQNTQAEVTAEGSDADSFTWWRGGKLSKVILLKAVLSQPATKKAAWQGGSKKIPGLNYGDASYIPRRSRRSFWKAAVESSKNISQLALQVRYLDMSLRWRELVRPDQNLQNVKGPETDVAIFRNARICDKKLSDNKVSYGVFFGNQKHLPSRVMKNIMEVEKTQDRNEKYWLQEAHVPLYLIKEFEESLHRVQMPSSTKKPSKKLSKLQRKQLKASLMDIFSYIASRRDKMEKCSCASCDHDVLLRDTTTCSSCHGFCHKDCTSMSQHTNGNVEVLVTCKRCYLSKTRVPTNINHRQSTAPQFTINVRHQNAVIPVIKVKPPSQQLSSQKPRENTSGVKQVTPDSSVSKSKQKTLSCGVIWRKKNVEDTGVDFRNQNILLAGRSDKPSLEPVCGICLLPYNPGLTYIHCTKCEKWFHTEAVKLKDSQIPEVVGFKCCKCRRIRSPDCPYMDPKLKEQKQIKRIVFTNQKQRQGNSGLDSDSERMSEQKDSKPSTPLPATPLYPPDDVFIPEDDPLLVSVSKVKQITPSSFDLEWSTTAFAPGPQKLPVRRQVKREDSDAAYPELHPIVKPEAEEQALPVLTEWDLSGELLFDYEDMEFEPQTYFSLTELLTADDSGGGQYQENGDMVVSGNPQFEPTEKEECEDDMGPCQRCLQMDPAPDLLCTVCGLLIHSHCSPWSALPGSSWSCGQCRIRALGSITLGSFGAITQFKSILPDRSTKVDISLAGPFAGAALSVSMFAVGLFLSTEPDAANDLVQVPSMLFQGSLLLGLISRATLGYAALHAATVSIHPLVIAGWCGLTTTAFNMLPVGCLDGGRAVQGAFGKNALVTFGLSTYVMLGLRVLGGPLALPWGLYVLICRNT
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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.
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F4JYE9
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DHFS_ARATH
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Dihydrofolate synthetase (AtDFA) (EC 6.3.2.12) (Protein GLOBULAR ARREST 1)
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MRTLWNHFSTISYIKISPRMRRISAANLISNRNLSTISSTEDPELRDFVGFLESLKNYEKSGVPKGAGTDSDDGFDLGRMKRLMLRLRNPHYKYKVVHVAGTKGKGSTSAFLSNILRAGGYSVGCYSSPHILSIKERISCNGEPVSASTLNDLFYSVKPILEQSIQEENGSLSHFEILTGIAFSLFEKENVDIAVIEAGLGGARDATNVIESSNLAASVITTIGEEHMAALGGSLESIAEAKSGIIKHGRPVVLGGPFLPHIEGILRSKAASVSSSVILASNIGSSSSIKGIINKNGIGLCQSCDIVIQNEKDDQPIVELSDVNLRMLGHHQLQNAVTATCVSLCLRDQGCGRVTDEAIRIGLENTRLLGRSQFLTPKEAETLLLPGATVLLDGAHTKESARALKEMIKKDFPEKRLVFVVAMASDKDHVSFAKELLSGLKPEAVILTEADIGGGKIRSTESSVLKESWIKAADELGSRSMEASENKTVLGSLKLAYKILSDDTTSSDSGMVIVTGSLHIVSSVLASLQH
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Conversion of folates to polyglutamate derivatives, including tetrahydrofolate. Required during embryogenesis from maternal tissues until the globular stage, and from the embryo after the globular stage.
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F4JYG0
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PIAL2_ARATH
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E4 SUMO-protein ligase PIAL2 (EC 2.3.2.-) (Protein INHIBITOR OF ACTIVATED STAT-LIKE 2)
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MSTAAAARPVAGTGLREKTAASLVNSFRLASVTQRLRYHIQDGAKVDPKEFQICCISFAKGIDFAIANNDIPKKVEEFPWLLKQLCRHGTDVYTKTALMVLMISVKHACHLGWFSDSESQELIALADEIRTCFGSSGSTSPGIKSPGSTFSQIMERFYPFVKLGHVLVSFEVKAGYTMLAHDFYISKNMPHSLQEKIRLFVAQTDNIDTSACISNPPEVSFLLNGKGVEKRVNIAMDTGPQLPTNVTAQLKYGTNLLQVMGNFKGNYIIIIAFTGLVVPPEKPVLKDYLQSGVIEASPDSDIIEGPSRVSLSCPISRKRIKLPVKGQLCKHLQCFDFSNYVHINMRNPTWRCPHCNQPVCYPDIRLDQNMAKILKDVEHNAADVIIDAGGTWKVTKNTGETPEPVREIIHDLEDPMSLLNSGPVVFDLTGDDDAELEVFGDNKVEDRKPCMSDAQGQSNNNNTNKHPSNDDYSSIFDISDVIALDPEILSALGNTAPQPHQASNTGTGQQYSNLSQIPMSIDPMPVPVPFSQTPSPRDRPATTSTVFTIPNPSPQYSQVHASPVTPTGTYLGRTTSPRWNQTYQSQAPPMTTPYTSRKVSVPVTSQSPANVSSFVQSQHVPRVLSQPNNYGVRGLTSSHASTSRQHPSGPTVQSVSRLSDLVDVDLTVPDTSNWRPRMRGSLVPGSHSTALDHMIIRPSQQSQTSTRLNSSQPVQTPSVQTSQAQSPFTTAAYRTETVLGNRNHPVPAPPGIVRPTGPTS
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Together with MOM1 and PIAL1, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation. 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. Involved in stress responses and sulfur metabolism.
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F4JZC2
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ENAS1_ARATH
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Cytosolic endo-beta-N-acetylglucosaminidase 1 (ENGase 1) (EC 3.2.1.96) (Endo-beta-N-acetyglucosaminidase 85A) (AtENGase85A)
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MSVAPPAPSPPPFDPTKPSTPISFPIKTLQDLKSRSYFDSFHYPFNRSSVPLRRNIGALSDRPRLLVCHDMKGGYVDDKWVQGCGNNAGYAIWDWYLMDVFVYFSHSLVTLPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKELLATKESAQMYAERLAELAAALGFDGWLINIENVIDEVQIPNLMVFVSHLTKVMHSSVPGGLVIWYDSVTIDGHLAWQDQLTENNKPFFDICDGIFMNYTWKENYPKASAEIAGDRKYDVYMGIDVFGRGTYGGGQWTANVALDLLKSSNVSAAIFAPGWVYETEQPPDFYTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGLGSHTSLGGRKLSEAPWYNISCQSLQPFLEFNEGRNSETIQVTVDGREASYNGGGNVSFRGKLKRNAHFTARLFKPQLQLSAAPISIFFSVKSDKRSELSILLHFSSPSQEKKSMLMVPNESINRFGDMFLPCLLTSKQTTSGWTVHETNLVLDGHTLTEISAFCSRPDDLTEETNTLEYFALLGHISIKSQQKAKVYPLASSWVIEAHHVKFVPGDSGSKTLSCKLEWRLKHPEEDSVFPKYNVYAENLSSSEYRPRKVMEEPRSEKVFLGTAHVDAYYVSEMVVGSDVKGVRFVVQTCGEDGSWQELDASPNLVVEVERVSSKLCCCGLI
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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.
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F4JZG9
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TERC_ARATH
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Thylakoid membrane protein TERC, chloroplastic (Protein PIGMENT DEFECTIVE 149) (Protein TELLURITE RESISTANCE C) (AtTerC)
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MSLASVIHHGILPPAKSDRIFLTIPVFPPDFRARGWTKSPFSLLINPSLASAANRRLSHLPPIACSRGIDQEDEEKESRELLPHKNDENATTSRSSSSVDSGGLKDYQQEETYKTSFKTVALCVGTAVAFGIGIGLKEGVGKASEFFAGYILEQSLSVDNLFVFVLVFKYFKVPLMYQNKVLTYGIAGAIVFRFTLILLGTATLQKFEAVNLLLAAVLLYSSFKLFASEEDDTDLSDNFIVKTCQRFIPVTSSYDGNRFFTKHDGILKATPLLLTVAVIELSDIAFAVDSIPAVFGVTRDPFIVLTSNLFAILGLRSLYTLISEGMDELEYLQPSIAVVLGFIGVKMILDFFGFHISTEASLGVVALSLSTGVLLSLTNKSSDS
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Integral thylakoid membrane protein that plays a crucial role in thylakoid membrane biogenesis and thylakoid formation in early chloroplast development. 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.
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F4JZW1
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PBL13_ARATH
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Serine/threonine-protein kinase PBL13 (EC 2.7.11.1) (PBS1-like protein 13) (Ser/Thr protein kinase ACIK1b)
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MVLCFQDPDNIYSPKKTKKDDGERVITKQKSFLGLSILDISNPSSTTLSEDLSISLAGSDLHVFTQAELRVITQSFSSSNFLGEGGFGPVHKGFIDDKLRPGLKAQPVAVKLLDLDGLQGHREFMTEVMCLGKLKHPNLVKLIGYCCEEAHRLLVYEFMPRGSLESQLFRRCSLPLPWTTRLNIAYEAAKGLQFLHEAEKPIIYRDFKASNILLDSDYTAKLSDFGLAKDGPQGDDTHVSTRVMGTQGYAAPEYIMTGHLTAKSDVYSFGVVLLELLTGRKSVDIARSSRKETLVEWARPMLNDARKLGRIMDPRLEDQYSETGARKAATLAYQCLRYRPKTRPDISTVVSVLQDIKDYKDDIPIGIFTYTVPTKPRREVKETSLQNFDKPRRETKVTSLQNFDKTRREVKDTSLQNFDKTRREVKETSLQNFDKTRREVKETSLQNFDKPRNVSTTDNHQKFRSPAHTARNHRITLRNGYNSPMRNEAGGERY
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Involved in defense responses. Acts as negative regulator of plant immune responses.
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F4JZY1
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CIP1_ARATH
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COP1-interactive protein 1
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MKKHKFRETLKSFFEPHFDHEKGEMLKGTKTEIDEKVNKILGMVESGDVNEDESNRQVVADLVKEFYSEYQSLYRQYDDLTGEIRKKVNGKGESSSSSSSDSDSDHSSKRKVKRNGNGKVEKDVELVTGALKQQIEAANLEIADLKGKLTTTVEEKEAVDSELELALMKLKESEEISSKLKLETEKLEDEKSIALSDNRELHQKLEVAGKTETDLNQKLEDIKKERDELQTERDNGIKRFQEAEKVAEDWKTTSDQLKDETSNLKQQLEASEQRVSELTSGMNSAEEENKSLSLKVSEISDVIQQGQTTIQELISELGEMKEKYKEKESEHSSLVELHKTHERESSSQVKELEAHIESSEKLVADFTQSLNNAEEEKKLLSQKIAELSNEIQEAQNTMQELMSESGQLKESHSVKERELFSLRDIHEIHQRDSSTRASELEAQLESSKQQVSDLSASLKAAEEENKAISSKNVETMNKLEQTQNTIQELMAELGKLKDSHREKESELSSLVEVHETHQRDSSIHVKELEEQVESSKKLVAELNQTLNNAEEEKKVLSQKIAELSNEIKEAQNTIQELVSESGQLKESHSVKDRDLFSLRDIHETHQRESSTRVSELEAQLESSEQRISDLTVDLKDAEEENKAISSKNLEIMDKLEQAQNTIKELMDELGELKDRHKEKESELSSLVKSADQQVADMKQSLDNAEEEKKMLSQRILDISNEIQEAQKTIQEHMSESEQLKESHGVKERELTGLRDIHETHQRESSTRLSELETQLKLLEQRVVDLSASLNAAEEEKKSLSSMILEITDELKQAQSKVQELVTELAESKDTLTQKENELSSFVEVHEAHKRDSSSQVKELEARVESAEEQVKELNQNLNSSEEEKKILSQQISEMSIKIKRAESTIQELSSESERLKGSHAEKDNELFSLRDIHETHQRELSTQLRGLEAQLESSEHRVLELSESLKAAEEESRTMSTKISETSDELERTQIMVQELTADSSKLKEQLAEKESKLFLLTEKDSKSQVQIKELEATVATLELELESVRARIIDLETEIASKTTVVEQLEAQNREMVARISELEKTMEERGTELSALTQKLEDNDKQSSSSIETLTAEIDGLRAELDSMSVQKEEVEKQMVCKSEEASVKIKRLDDEVNGLRQQVASLDSQRAELEIQLEKKSEEISEYLSQITNLKEEIINKVKVHESILEEINGLSEKIKGRELELETLGKQRSELDEELRTKKEENVQMHDKINVASSEIMALTELINNLKNELDSLQVQKSETEAELEREKQEKSELSNQITDVQKALVEQEAAYNTLEEEHKQINELFKETEATLNKVTVDYKEAQRLLEERGKEVTSRDSTIGVHEETMESLRNELEMKGDEIETLMEKISNIEVKLRLSNQKLRVTEQVLTEKEEAFRKEEAKHLEEQALLEKNLTMTHETYRGMIKEIADKVNITVDGFQSMSEKLTEKQGRYEKTVMEASKILWTATNWVIERNHEKEKMNKEIEKKDEEIKKLGGKVREDEKEKEMMKETLMGLGEEKREAIRQLCVWIDHHRSRCEYLEEVLSKTVVARGQRRVSQRT
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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).
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F4K0A6
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MYO2_ARATH
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Myosin-2 (AtATM2) (AtMYOS1)
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MMLSASPNTLAKSSLEEMLESLRQKDECDRPKDMPPALPSRPNSRARLPSARRSLPANFNVSSVMEDQNGSVVSVTPAVEAESERKEEGVKRKEKDLGVKRNSFGSKKMRTGLRSESPYAAEKEEEGVKISIAKVSLVENTEEHNKPESEWNNNVEYFIKKKLRVWCRVSNGQWQLGKIQSTSADTSLVMLSTANVVKVSTEELFPANPDILEGVEDLIQLSYLNEPSVLYNLRVRYLQDVIYSKAGPVLIAVNPFKNVEIYGNDVISAYQKKVMDAPHVYAVADAAYDEMMREEKNQSLIISGESGAGKTETAKFAMQYLAALGGGSCGVEYEILKTTCILEAFGNAKTSRNANSSRFGKLIEIHFSAMGKICGAKLETFLLEKSRVVQLFNGERSYHIFYELCAGASPILKERLKLKTASEYTYLSQSDCLTIAGVDDAQKFHKLLEAFDIVQIPKEHQERAFALLAAVLWLGNVSFRVTDNENHVEVVADEAVANAAMLMGCNTEELMVVLSTRKLQAGTDCIAKKLTLRQATDMRDGIAKFIYANLFDWLVEQINIALEVGKSRTGRSISILDIYGFESFKNNSFEQFCINYANERLQQHFNRHLFKLEQEEYEEDGIDWTKVEFVDNQECLDLIEKKPIGLLSLLDEESNFPKATDLTFANKLKQHLKTNSCFKGERGRAFRVNHYAGEVLYDTNGFLEKNRDPLPADLINLLSSCDCQLLKLFSTKMRGKSQKPLMLSDSTNQTVGTKFKGQLFKLMNKLENTSPHFIRCIKPNSKQLPRVYEEDLVLQQLRCCGVLEVVRISRSGYPTRLTHQEFAGRYGFLLSDKKVAQDPLSVSIAVLKQYDVHPEMYQVGYTKLYLRTGQIGIFEDRRKKVLQGIVGLQKHFRGHLSRAYFQNMRKVTLVLQSYIRGENARRLFDTEAKFHADSVSEASTDELSAVIHLQSAVRGWLARKHFNSMQRQKELRNVATKSKRKAGRRISEDKDIPLEQPQVQPTSMSDLQKRILKSEAALSQKEEENTALREQLRQFEERWSEYDIKMKSMEETWQKQMSSLQMSLAAARKSLAAESITGQAGGRQDTSISPFGYDSEDTMSTGTPGVRTPTNKFTNGNTPELRIRELNGSLNAVNHLAREFDQRRLNFDEDARAIVEVKLGPQATPNGQQQQHPEDEFRRLKLRFETWKKDYKARLRDTKARLHRVDGDKGRHRKWWGKRG
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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}.
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F4K0E8
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ISPG_ARATH
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4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin), chloroplastic (EC 1.17.7.1) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase) (Protein CHLOROPLAST BIOGENESIS 4) (Protein CONSTITUTIVE SUBTILISIN 3)
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MATGVLPAPVSGIKIPDSKVGFGKSMNLVRICDVRSLRSARRRVSVIRNSNQGSDLAELQPASEGSPLLVPRQKYCESLHKTVRRKTRTVMVGNVALGSEHPIRIQTMTTSDTKDITGTVDEVMRIADKGADIVRITVQGKKEADACFEIKDKLVQLNYNIPLVADIHFAPTVALRVAECFDKIRVNPGNFADRRAQFETIDYTEDEYQKELQHIEQVFTPLVEKCKKYGRAMRIGTNHGSLSDRIMSYYGDSPRGMVESAFEFARICRKLDYHNFVFSMKASNPVIMVQAYRLLVAEMYVHGWDYPLHLGVTEAGEGEDGRMKSAIGIGTLLQDGLGDTIRVSLTEPPEEEIDPCRRLANLGTKAAKLQQGVAPFEEKHRHYFDFQRRTGDLPVQKEGEEVDYRNVLHRDGSVLMSISLDQLKAPELLYRSLATKLVVGMPFKDLATVDSILLRELPPVDDQVARLALKRLIDVSMGVIAPLSEQLTKPLPNAMVLVNLKELSGGAYKLLPEGTRLVVSLRGDEPYEELEILKNIDATMILHDVPFTEDKVSRVHAARRLFEFLSENSVNFPVIHHINFPTGIHRDELVIHAGTYAGGLLVDGLGDGVMLEAPDQDFDFLRNTSFNLLQGCRMRNTKTEYVSCPSCGRTLFDLQEISAEIREKTSHLPGVSIAIMGCIVNGPGEMADADFGYVGGSPGKIDLYVGKTVVKRGIAMTEATDALIGLIKEHGRWVDPPVADE
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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.
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F4K128
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CHR23_ARATH
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Probable ATP-dependent DNA helicase CHR23 (EC 3.6.4.12) (Protein CHROMATIN REMODELING 23) (AtCHR23) (Protein MINUSCULE 2)
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MVKQLQEQEENDPVEKTKSLISALNYLSRDLLLPSHLYASVSSIYHASVSDLSPSPPLRGNSYTPNRGDLMSEFEDALLQQRLNYESGSRLAELKETRYKNRIHNRLSQLEGLPSNRGEDLQEKCLLELYGLKLQELQCRVRGEVSAEYWLRLNCADPERQLYDWGMMRLPRRMYGVGDSFVMEADDQFRNKRDAERLLRLEEEEKNLIETTQRKFFAEVLNAVREFQLQIQASHRRCKQRNDGVQAWHGKQRQRATRAEKLRIMALKSDDQEEYMKLAKESKNEKLTLFLEETNKIFVSLGAAVQRQKDAKLSENTKLLKGSESDLSDVDAPEDVLPAQDIEIIDSDNNDDSNDLLEGERQFNLAIHSIQEKVTKQPSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVIRPFLLRRKKSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGNGKSKSLQNLTMQLRKCCNHPYLFVGADYNMCKKPEIVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLLSTRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLFNTTSTAQDRREMLEEIMSKGTSSLGEDVPSEREINRLAARTEEEFWMFEQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDKTNAKNHFGSLTGKRKRKEAVYSDSLSDLQWMKAMESEDEDASKVSQKRKRTDTKTRMSNGSKAEAVLSESDEEKEEEEEERKEESGKESEEENEKPLHSWKTNKKKRSRYPVMTSSPNSRGKGSSKGSKRN
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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. May promote seed maturation and repress initiation of germination. May repress plant growth.
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F4K1J4
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ATXR7_ARATH
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Histone-lysine N-methyltransferase ATXR7 (EC 2.1.1.354) (EC 2.1.1.357) (Protein SET DOMAIN GROUP 25) (Trithorax-related protein 7)
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MVAVDSTFPSHGSSYSSRRKKVSALEPNYFGSMCMGVYSDDVSISAREVAQDYSCDSCGDLATVSSACCNFDELCGLDSALEMGCRSNEDCRAGQEASGSGIASGLDKSVPGYTMYASGWMYGNQQGQMCGPYTQQQLYDGLSTNFLPEDLLVYPIINGYTANSVPLKYFKQFPDHVATGFAYLQNGIISVAPSVTSFPPSSSNATVHQDEIQTEHATSATHLISHQTMPPQTSSNGSVLDQLTLNHEESNMLASFLSLGNEHACWFLVDGEGRNHGPHSILELFSWQQHGYVSDAALIRDGENKLRPITLASLIGVWRVKCGDANCDEPVTGVNFISEVSEELSVHLQSGIMKIARRALLDEIISSVISDFLKAKKSDEHLKSYPPTSAVESISSRVINAEKSVVSNTESAGCKNTMNEGGHSSIAAESSKYTKSVGSIENFQTSCSAVCRTLHHHCMQIMWNAVFYDTVATHSSCWRKNKIWFRSSDISTVNYCKGSHTKYSDKPESFESFTCRVDSSSSKTAYSDEFDLATNGARVRGLSSDTYGTESVIASISEHVENELFLSLKTHLTDYTSILIKDGANNTTSSARDGKMHEGSFREQYNLEGSSKKKNGLNVVPAKLRFSNDFSDSQRLLQEGESSEQITSEDIIANIFSTALETSDIPVNDELDALAIHEPPPPGCESNINMPCLRYKYQPVRSKESIPEIKAYVSMALCRQKLHNDVMRDWKSLFLKCYLNEFLASLKGSHQVSRKETLALKKRKTVTRNKKLVQSNISNQTAEKLRKPCVGASEKVLVKRSKKLSDSHSMKEVLKVDTPSIDLSVRKPSQQKMRNTDRRDHCIIKDATKLHKEKVGKDAFSKVICDKSQDLEMEDEFDDALLITRLRRISRNKTKELRECRNAAKSCEEISVTAEESEETVDCKDHEESLSNKPSQKVKKAHTSKLKRKNLSDARDEGTKSCNGAVKSFTEISGKEGDTESLGLAISDKVSHQNLSKRRKSKIALFLFPGFENTSRKCFTKLLSPEDAAKNGQDMSNPTGNPPRLAEGKKFVEKSACSISQKGRKSSQSSILKRKHQLDEKISNVPSRRRLSLSSTDSEDAVIKEDYDVRNEEKLPCHTSDKLQKGPNKLIRRRKPLAKHTTERSPIKDLSVDDGRPKPIALKPLEKLSSKPSKKKLFLSIPKSDGCARTSINGWHWHAWSLKASAEERARVRGSSCVHMQHFGSKSSLTQNVLSARTNRAKLRNLLAAADGADVLKMSQLKARKKHLRFQQSKIHDWGLVALEPIEAEDFVIEYVGELIRSSISEIRERQYEKMGIGSSYLFRLDDGYVLDATKRGGIARFINHSCEPNCYTKIISVEGKKKIFIYAKRHIDAGEEISYNYKFPLEDDKIPCNCGAPNVYCFCEQVPWIAKLKRRTWFSRRN
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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. Required for histone H3 dimethylation on 'Lys-36' H3K36me2 at the FLC locus. Required for histone H3 trimethylation on 'Lys-4' (H3K4me3) at the FLC locus. Prevents trimethylation on 'Lys-27' (H3K27me3) at the same locus. Involved in the control of seed dormancy and germination.
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F4K2A1
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FPGS1_ARATH
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Folylpolyglutamate synthase (EC 6.3.2.17) (DHFS-FPGS homolog B) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase)
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MFAVSIVPRTTSCRLSSAFLCQLSIPLTLRLHHHYQHHQPHLPSPLSFQIHSLRKQIDMAAQGGDSYEEALAALSSLITKRSRADKSNKGDRFELVFDYLKLLDLEEDILKMNVIHVAGTKGKGSTCTFTESIIRNYGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLGYFWWCYNRLKERTNEEIPMPTYFRFLALLAFKIFAAEEVDAAILEVGLGGKFDATNAVQKPVVCGISSLGYDHMEILGDTLGKIAGEKAGIFKLGVPAFTVPQPDEAMRVLEEKASETEVNLEVVQPLTARLLSGQKLGLDGEHQYVNAGLAVSLASIWLQQIGKLEVPSRTQMSILPEKFIKGLATASLQGRAQVVPDQYTESRTSGDLVFYLDGAHSPESMEACAKWFSVAVKGDNQSGSSGHLVNGSAGSSHDKWSNETCEQILLFNCMSVRDPNLLLPHLKNMCAKYGVNFKKALFVPNMSVYHKVGTAADLPENDPQVDLSWQFTLQKVWESLVQSERDGEKDGESDGNSEVFTSLPMAIKCLRDTVHESSSATRFQVLVTGSLHLVGDVLRLIRK
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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.
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F4K2E9
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PRP16_ARATH
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Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP16) (Protein CLUMSY VEIN) (Protein EMBRYO DEFECTIVE 3011) (Protein PSR1-INTERACTING PROTEIN 1)
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MGVDPFKTTETLEADKETNGGVPVKDKLTFKAPERKSRLGLDARAIEKKDNAKTEGEFKVPKKSAISVTSSLDEEDKSDVSGLDFGTENTRPVHSSRRYREKSSRSQSAQESTVTTENAGTSDISITPRTLSCTSSYERGGSNRHREEHRRDRSETPRSRQRNTYDEMDHYRRRESYRQSDRDYHGEKRRRYNSDWRTPGRSDWDDGQDEWERSPHGDRGSSYSRRPQPSPSPMLAAASPDARLASPWLDTPRSTMSSASPWDMGAPSPIPIRASGSSIRSSSSRYGGRSNQLAYSREGDLTNEGHSDEDRSQGAEEFKHEITETMRVEMEYQSDRAWYDTDEGNSLFDADSASFFLGDDASLQKKETELAKRLVRRDGSKMSLAQSKKYSQLNADNAQWEDRQLLRSGAVRGTEVQTEFDSEEERKAILLVHDTKPPFLDGRVVYTKQAEPVMPVKDPTSDMAIISRKGSGLVKEIREKQSANKSRQRFWELAGSNLGNILGIEKSAEQIDADTAVVGDDGEVDFKGEAKFAQHMKKGEAVSEFAMSKTMAEQRQYLPIFSVRDELLQVIRENQVIVVVGETGSGKTTQLTQYLHEDGYTINGIVGCTQPRRVAAMSVAKRVSEEMETELGDKIGYAIRFEDVTGPNTVIKYMTDGVLLRETLKDSDLDKYRVVVMDEAHERSLNTDVLFGILKKVVARRRDFKLIVTSATLNAQKFSNFFGSVPIFNIPGRTFPVNILYSKTPCEDYVEAAVKQAMTIHITSPPGDILIFMTGQDEIEAACFSLKERMEQLVSSSSREITNLLILPIYSQLPADLQAKIFQKPEDGARKCIVATNIAETSLTVDGIYYVIDTGYGKMKVFNPRMGMDALQVFPISRAASDQRAGRAGRTGPGTCYRLYTESAYLNEMLPSPVPEIQRTNLGNVVLLLKSLKIDNLLDFDFMDPPPQENILNSMYQLWVLGALNNVGGLTDLGWKMVEFPLDPPLAKMLLMGERLDCIDEVLTIVSMLSVPSVFFRPKERAEESDAAREKFFVPESDHLTLLNVYQQWKEHDYRGDWCNDHYLQVKGLRKAREVRSQLLDILKQLKIELRSCGPDWDIVRKAICSAYFHNSARLKGVGEYVNCRTGMPCHLHPSSALYGLGYTPDYVVYHELILTTKEYMQCATSVEPHWLAELGPMFFSVKDSDTSMLEHKKKQKEEKSGMEEEMEKLRRDQVESELRSKERERKKRAKQQQQISGPGLKKGTTFLRPKKLGL
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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. Also involved in root-meristem maintenance and planar polarity of root-hair positioning. Acts as a component of RNA silencing that regulates distinct classes of endogenous small RNAs. Functions as a positive regulator of plant immunity.
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F4K2R6
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CB60G_ARATH
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Calmodulin-binding protein 60 G
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MKIRNSPSFHGGSGYSVFRARNLTFKKVVKKVMRDQSNNQFMIQMENMIRRIVREEIQRSLQPFLSSSCVSMERSRSETPSSRSRLKLCFINSPPSSIFTGSKIEAEDGSPLVIELVDATTNTLVSTGPFSSSRVELVPLNADFTEESWTVEGFNRNILTQREGKRPLLTGDLTVMLKNGVGVITGDIAFSDNSSWTRSRKFRLGAKLTGDGAVEARSEAFGCRDQRGESYKKHHPPCPSDEVWRLEKIAKDGVSATRLAERKILTVKDFRRLYTVNRNELHNIIGAGVSKKTWNTIVSHAMDCVLDETECYIYNANTPGVTLLFNSVYELIRVSFNGNDIQNLDQPILDQLKAEAYQNLNRITAVNDRTFVGHPQRSLQCPQDPGFVVTCSGSQHIDFQGSLDPSSSSMALCHKASSSTVHPDVLMSFDNSSTARFHIDKKFLPTFGNSFKVSELDQVHGKSQTVVTKGCIENNEEDENAFSYHHHDDMTSSWSPGTHQAVETMFLTVSETEEAGMFDVHFANVNLGSPRARWCKVKAAFKVRAAFKEVRRHTTARNPREGL
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Transcription activator that binds DNA in a sequence-specific manner, 5'-GAAATTTTGG-3', to promote the expression of target genes. 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. Mediates resistance to drought and sensitivity to abscisic acid (ABA), especially for ABA-mediated signaling process that regulates early seedling growth.
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F4K3G5
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EDM2_ARATH
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Protein ENHANCED DOWNY MILDEW 2
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MTFVDDDEEEDFSVPQSASNYYFEDDDKEPVSFARLPIQWSVEEKVDGSGLGFYLRGRSDNGLLPLHKLVKAWRYDLSNFQPEISVLTKDNIWIKLEEPRKSYGELIRTVLVTLHSIQFLRRNPQASEKALWEKLTRSLRSYDVKPSQNDLVDHIGLIAEAAKRDRNLANSKFILAFLTKKPTKRRLPDEDNAKDDFIVGDEDTYVASDEDELDDEDDDFFESVCAICDNGGEILCCEGSCLRSFHATKKDGEDSLCDSLGFNKMQVEAIQKYFCPNCEHKIHQCFICKNLGSSDNSSGAAEVFQCVSATCGYFYHPHCVTRRLRLGNKEESEALERQIIAGEYTCPLHKCSVCENGEVKTDSNLQFAVCRRCPKSYHRKCLPREISFEDIEDEDILTRAWDGLLHNRVLIYCQEHEIDEELLTPVRDHVKFPFTEEQKVFVKEQRRILESHVGRDKARLKVKDPALQDTCGKASKNSFRSSFPSSKDGFSTKKHGLVSSVPDHSRKRKDIDPSIKHKMVPQKSQKMMEDSREAGKNKLGVKEARDAGKSKISLGERLFSYTQEPNPVKPGRVIPVDSKHNKTDSIASKEPGSEIPTLDNDSQRRLLAVMKKATEEITMGTILKKFKIQSTMSTHSTRNVVDKTITMGKVEGSVQAIRTALKKLEEGGNIEDAKAVCEPEVLSQILKWKDKLKVYLAPFLHGARYTSFGRHFTNPEKLQQIVDRLHWYADDGDMIVDFCCGSNDFSCLMNAKLEETGKKCLYKNYDLFPAKNNFNFERKDWMTVSKDELEPGSKLIMGLNPPFGVNASLANKFITKALEFRPKILILIVPPETERLDKKKSSYVLIWEDKTFLSGNSFYLPGSVNEEDKQLEDWNLVPPPLSLWSRSDFAAKHKKIAEKHCHLSRDVGSSKLKIVEEEANASLHPLGASDGMCDDIPMEKDELEVAECVNKILVSEKIDTVETVARVHQSDHLSRRSQLKKEGKTKDYSGRKLGKSMDSNNVDWKSNDMEEDQGELSRAPESIKVKIPEMTSDWQSPVRSSPDDIYAVCTSISTTTPQRSHEAVEASLPAITRTKSNLGKNIREHGCKVQGTGKPEVSRDRPSSVRTSREDIYTVRPSPENTGQKPFEAFEPSYGASLSHFDDGLAAKYGGFGGGYRMPDPPFLPDQFPLRNGPNEMFDFRGYSDLDRGIGQREYPQQYGGHLDPMLAPPPPPNLMDNAFPLQQRYAPHFDQMNYQRMSSFPPQPPLQPSGHNLLNPHDFPLPPPPPSDFEMSPRGFAPGPNPNYPYMSRSGGWIND
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Cellular antisilencing factor and regulator of genome DNA methylation patterns involved in the regulation of chromatin states. 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. 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. 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. 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. 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. Regulates development processes such as the formation of leaf pavement cells, leaf expansion, fertility and flowering. Prevents FLC accumulation to control flowering. Modulates stomatal development by regulating the methylation-mediated silencing of ERECTA receptor genes (e.g. ER, ERL1 and ERL2) and preventing cell divisions.
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F4K410
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SVR3_ARATH
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Putative elongation factor TypA-like SVR3, chloroplastic (Protein HAPPY ON NORFLURAZON 23) (Protein SUPPRESSOR OF VARIEGATION 3)
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MELSLSTSSASPAVLRRQASPLLHKQQVLGVSFASALKPGGGALRFPSRRPLPRPITCSASPSTAEPASEVKKKQLDRRDNVRNIAIVAHVDHGKTTLVDSMLRQAKVFRDNQVMQERIMDSNDLERERGITILSKNTSITYKNTKVNIIDTPGHSDFGGEVERVLNMVDGVLLVVDSVEGPMPQTRFVLKKALEFGHAVVVVVNKIDRPSARPEFVVNSTFELFIELNATDEQCDFQAIYASGIKGKAGLSPDDLAEDLGPLFEAIIRCVPGPNIEKDGALQMLATNIEYDEHKGRIAIGRLHAGVLRKGMDVRVCTSEDSCRFARVSELFVYEKFYRVPTDSVEAGDICAVCGIDNIQIGETIADKVHGKPLPTIKVEEPTVKMSFSVNTSPFSGREGKYVTSRNLRDRLNRELERNLAMKVEDGETADTFIVSGRGTLHITILIENMRREGYEFMVGPPKVINKRVNDKLLEPYEIATVEVPEAHMGPVVELLGKRRGQMFDMQGVGSEGTTFLRYKIPTRGLLGLRNAILTASRGTAILNTVFDSYGPWAGDISTRDLGSLVAFEDGTSTSYALASAQERGQMFVGSGVDVYKGQIVGIHQRPGDLGLNICKKKAATNIRSNKDVTVILDTPLTYSLDDCIEYIEEDELVEVTPSSIRMCKNQKMAKKGRQ
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Putative chloroplastic elongation factor involved in response to chilling stress. Required for proper chloroplast rRNA processing and/or translation at low temperature. Involved in plastid protein homeostasis.
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