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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|---|---|---|---|---|
O22901
|
BH151_ARATH
|
Transcription factor UPBEAT1 (Basic helix-loop-helix protein 151) (AtbHLH151) (bHLH 151) (Transcription factor EN 146) (Transcription factor bHLH151) (bHLH transcription factor bHLH151)
|
MGVTLEGQRKESIWVLMRRQRARRALVKKIMIRPRKSVEASRRPCRAIHRRVKTLKELVPNTKTSEGLDGLFRQTADYILALEMKVKVMQTMVQVLTETNCV
|
Transcription factor that modulates the balance between cellular proliferation and differentiation in root growth. Does not act through cytokinin and auxin signaling, but by repressing peroxidase expression in the elongation zone.
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O22914
|
CP121_ARATH
|
Calvin cycle protein CP12-1, chloroplastic (CP12 domain-containing protein 1) (Chloroplast protein 12-1)
|
MTTIAAAGLNVATPRVVVRPVARVLGPVRLNYPWKFGSMKRMVVVKATSEGEISEKVEKSIQEAKETCADDPVSGECVAAWDEVEELSAAASHARDKKKAGGSDPLEEYCNDNPETDECRTYDN
|
Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
|
O22921
|
WRK25_ARATH
|
Probable WRKY transcription factor 25 (WRKY DNA-binding protein 25)
|
MSSTSFTDLLGSSGVDCYEDDEDLRVSGSSFGGYYPERTGSGLPKFKTAQPPPLPISQSSHNFTFSDYLDSPLLLSSSHSLISPTTGTFPLQGFNGTTNNHSDFPWQLQSQPSNASSALQETYGVQDHEKKQEMIPNEIATQNNNQSFGTERQIKIPAYMVSRNSNDGYGWRKYGQKQVKKSENPRSYFKCTYPDCVSKKIVETASDGQITEIIYKGGHNHPKPEFTKRPSQSSLPSSVNGRRLFNPASVVSEPHDQSENSSISFDYSDLEQKSFKSEYGEIDEEEEQPEMKRMKREGEDEGMSIEVSKGVKEPRVVVQTISDIDVLIDGFRWRKYGQKVVKGNTNPRSYYKCTFQGCGVKKQVERSAADERAVLTTYEGRHNHDIPTALRRS
|
Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Functions with WRKY33 as positive regulator of salt stress response and abscisic acid (ABA) signaling. Plays a partial role in heat stress tolerance. Functions with WRKY26 and WRKY33 as positive regulator of plant thermotolerance by partially participating in ethylene-response signal transduction pathway.
|
O22932
|
CIPKB_ARATH
|
CBL-interacting serine/threonine-protein kinase 11 (EC 2.7.11.1) (SNF1-related kinase 3.22) (SOS2-like protein kinase PKS5) (SOS3-interacting protein 4)
|
MPEIEIAAGSGDNNDALFGKYELGKLLGCGAFAKVFHARDRRTGQSVAVKILNKKKLLTNPALANNIKREISIMRRLSHPNIVKLHEVMATKSKIFFAMEFVKGGELFNKISKHGRLSEDLSRRYFQQLISAVGYCHARGVYHRDLKPENLLIDENGNLKVSDFGLSALTDQIRPDGLLHTLCGTPAYVAPEILSKKGYEGAKVDVWSCGIVLFVLVAGYLPFNDPNVMNMYKKIYKGEYRFPRWMSPDLKRFVSRLLDINPETRITIDEILKDPWFVRGGFKQIKFHDDEIEDQKVESSLEAVKSLNAFDLISYSSGLDLSGLFAGCSNSSGESERFLSEKSPEMLAEEVEGFAREENLRMKKKKEEEYGFEMEGQNGKFGIGICISRLNDLLVVVEARRRGGDGDCYKEMWNGKLRVQLIRVCDQTSSTNAAI
|
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Acts as a negative regulator of the plasma membrane proton pump AHA2 by preventing its interaction with 14-3-3 protein.
|
O22943
|
STL1_ARATH
|
Probable glycosyltransferase STELLO1 (EC 2.4.-.-)
|
MLVQDRAAPSPAKPPKSQIRELPTHQQIRRRFSEPKNLDFSTWFSENLSRIAVFSLLIVTIVAFFFLYNTTDTASLLCFQSQSTQFLQSLSRPQIKWNSIPVVPDKTSPYANFQTEKWIVVSVTKYPTEELKSLVKIRGWQVLAIGNSATPKDWSLKGSIFLSLDAQAELGYRVLDHLPYDSFVRKSVGYLFAIQHGAKKIYDADDRGEVIDGDLGKHFDVELVGLDSKQEPILQYSHENPNRTVVNPYIHFGQRSVWPRGLPLENVGEINHEEYYTEVFGGKQFIQQGISNGLPDVDSVFYFTRKTTLEAFDIRFDEHSPKVALPQGVMVPVNSFNTLYHSSAFWGLMLPVSVSSMASDVLRGYWGQRLLWELGGYVAVYPPTAHRFDRIEAYPFVEEKDLHVNVGRLIKFLLAWRSEKHSFFETVLDLSFAMAEEGFWTEQDLKFTAAWLQDLIAVGYQQPRLMSLELDRPRASIGHGDRKEFVPRKLPSVHLGVEETGTVSTEIGNLIRWRKNFGNVVLVMFCNGPVERTALEWRLLYGRIFKTVVILSSQKNSDLYVEEAKLDHIYKHLPKIFDRYSSAEGFLFVEDDTVLNYWNLLQADKSKIWTTDKVSKSWTSVKPTGNSDWFSVQAELVKKTVSTMPAHFQVNYKDATKNNHETLTVCSSEVFYVPKRLVTDFIDLVDLVGDMDLHYKVAVPMFFLSMDSPQNFDPVLGSMVYKRKSASFNTSSSLYSAKAPAVHPWSISSEQDFIKLVQQMAEGDPLLMELV
|
Probable glycosyltransferase regulating the assembly and trafficking of cellulose synthase complexes.
|
O22975
|
LPAAT_ARATH
|
1-acylglycerol-3-phosphate O-acyltransferase (EC 2.3.1.51) (Lipid droplet-binding protein CGI-58 homolog)
|
MNLSRFASRLRMAEEISKTKVGSSSTASVADSSAAASAATNAAKSRWKILWPNSLRWIPTSTDYIIAAEKRLLSILKTPYVQEQVSIGSGPPGSKIRWFRSTSNESRYINTVTFDAKEGAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCRSTEETEAWFIDSFEEWRKAQNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGSAGFSAEADAKSEWLTKFRATWKGAVLNHLWESNFTPQKLVRGLGPWGPGLVNRYTTARFGAHSEGTGLTEEEAKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLQSASEWKVPTTFIYGMNDWMNYQGAVEARKSMKVPCEIIRVPQGGHFVFIDNPIGFHSAVLYACRKFISQDSSHDQQLLDGLRLV
|
Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. Is highly specific for lysophosphatidic acid and able to use different acyl-CoA donors. May regulate neutral lipid accumulation and participate in the regulation of lipid turnover in vegetative cells. Possesses additional triacylglycerol lipase and phospholipase A2 activities in vitro. Is not active as esterase or lysophospholipase.
|
O22993
|
FTSI1_ARATH
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Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic (AtFTSHI1) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 1) (Protein ARC1) (Protein FTSH INACTIVE PROTEASE 1)
|
MASIDNVFSLGTRFSIPENPKRSILKHATTSSFSARTQTRWRAPILRRSFTVLCELKTGSSSSGETNNSPAADDFVTRVLKENPSQVEPRYRVGDKLYNLKEREDLSKGTNAATGAFEFIKRKFDSKKKTETDKSEESVYLSDILREYKGKLYVPEQVFGPELSEEEEFEKNVKDLPKMSLEDFRKAMENDKVKLLTSKEVSGVSYTSGYRGFIVDLKEIPGVKSLQRTKWSMKLEVGEAQALLKEYTGPQYEIERHMTSWVGKVADFPNPVASSISSRVMVELGMVTAVIAAAAVVVGGFLASAVFAVTSFAFVTTVYVVWPIAKPFLKLFVGVFLGVLEKSWDYIVDVLADGGIFSRISDFYTFGGVASSLEMLKPILLVVMTMVLLVRFTLSRRPKNFRKWDLWQGIAFSQSKAEARVDGSTGVKFADVAGIDEAVDELQELVKYLKNPDLFDKMGIKPPHGVLLEGPPGCGKTLVAKAIAGEAGVPFYQMAGSEFVEVLVGVGSARIRDLFKRAKVNKPSVIFIDEIDALATRRQGIFKENSDQLYNAATQERETTLNQLLIELDGFDTGKGVIFLGATNRRDLLDPALLRPGRFDRKIRVRPPNAKGRLDILKIHASKVKMSDSVDLSSYASNLPGWSGAKLAQLVQEAALVAVRKTHNSILQSDMDDAVDRLTVGPTRIGLELGHQGQCRRATTEVGVAITSHLLLRYENAKIERCDRVSIIPRGQTLSQVVFHRLDDESYMFGRLPQLLHRLQVLLGGRAAEEVIYGSDTSKASVDYLSDASWLARKILTIWNLENPMVIHGEPPPWRKRPQFVGPRLDFEGSLYDDYDLVEPPVNFNMDDEVAHRSEELISQMYNKTVSLLRQNQTALLKTVKVLLNQKEISGEAIDFILDHYPPQTPLNSLLQEQNPGSLPFVPEHLRRESGDFVLVNHSTDVNAQV
|
Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
|
O23044
|
PER3_ARATH
|
Peroxidase 3 (Atperox P3) (EC 1.11.1.7) (ATPRC) (RCI3A) (Rare cold-inducible protein)
|
MNCLIAIALSVSFFLVGIVGPIQAQLQMNFYANSCPNAEKIVQDFVSNHVSNAPSLAAALIRMHFHDCFVRGCDGSVLINSTSGNAERDATPNLTVRGFGFIDAIKSVLEAQCPGIVSCADIIALASRDAVVFTGGPNWSVPTGRRDGRISNAAEALANIPPPTSNITNLQTLFANQGLDLKDLVLLSGAHTIGVSHCSSFTNRLYNFTGRGGQDPALDSEYAANLKSRKCPSLNDNKTIVEMDPGSRKTFDLSYYQLVLKRRGLFQSDSALTTNPTTLSNINRILTGSVGSFFSEFAKSMEKMGRINVKTGSAGVVRRQCSVANS
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Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
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O23066
|
C86A2_ARATH
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Cytochrome P450 86A2 (EC 1.14.14.1) (Protein ABERRANT INDUCTION OF TYPE THREE 1)
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MDVSNTMLLVAVVAAYWLWFQRISRWLKGPRVWPVLGSLPGLIEQRDRMHDWITENLRACGGTYQTCICAVPFLAKKQGLVTVTCDPKNIEHMLKTRFDNYPKGPTWQAVFHDFLGQGIFNSDGDTWLFQRKTAALEFTTRTLRQAMGRWVNRGIKLRFCPILETAQNNYEPVDLQDLILRLTFDNICGLAFGKDTRTCAPGLPENGFASAFDRATEASLQRFILPEFLWRLKKWLGLGLEVSLSRSLGEIDGYLDAVINTRKQELLSQRESGVQRHDDLLSRFMKKKDQSYSETFLRHVALNFILAGRDTSSVALSWFFWLITTHPTVEDKIVREICSVLIETRGTDVSSWTAEPLEFDEVDRLVYLKAALSETLRLYPSVPEDSKHVVNDDILPDGTFVPAGSSVTYSIYAAGRMKSTWGEDCLEFKPERWISPDDGKFVNHDQYRFVAFNAGPRICLGKDLAYLQMKTIAAAVLLRHRLTVAPGHKVEQKMSLTLFMKNGLLVNVHKRDLEVMMKSLVPKERNDVVVLNGKCNGGIGEGVAVNAAVAVAV
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Catalyzes the omega-hydroxylation of various fatty acids (FA). Acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18. Plays a major role in the biosynthesis of extracellular lipids. Involved in the biosynthesis of hydroxylated fatty acids required for cutin biosynthesis, cuticle development and repression of bacterial type III gene expression.
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O23078
|
PLDB2_ARATH
|
Phospholipase D beta 2 (AtPLDbeta2) (PLD beta 2) (EC 3.1.4.4) (PLDdelta1)
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MENYGWNYPYYPYRPPRPNPPYPAPPHHHGSMSHSGPLDHHHPPMSYYASFDYQHQPPPPYPPVSYYASFSSHSDLSYSGRLDSSGHGFTSTASPHSPGMHIVPFGKASLKVLLLHGNLDIWVSCANNLPNLDLFHKTLGVVFGGMTNMIEGQLSKKITSDPYVSISVAGAVIGRTYVISNSENPVWQQHFYVPVAHHAAEVHFVVKDSDAVGSQLIGIVTIPVEQIYSGARIEGTYSIRDSNGKPCKPGATLSLSIQYTSMNKLSVYHSGVGAGPYYQGVPGTYFPLREGGSVTLYQDAHVPEGMLPGIKLGNGMCYEHGKCWHDMFHAICQARRLIYITGWSVWHNVRLVRDKEDPSSECRLGELLRSKSQEGVRVLLLVWDDPTSQNILGYMTDGVMGTHDEETRRFFKDSSVQVLLCPRNAGKRHSWVKQREVGTIYTHHQKNLIVDADAGGNRRKIVAFVGGLDLCDGRYDTPQHPLFRTLQTDHNGDYHNPTFTGNVSGCPREPWHDLHSKIDGPAAYDVLTNFEERWLKAAKPHRINKLKTSYDDALLRIDRIPDILRVLDAPTVSANDPEAWHVQIFRSIDSNSVKGFPKDPKYATSKNLVCGKNVLIDMSIHTAYVKAIRAAQHFIYIENQYFIGSSYDWNAHKDIGANNLIPMEIALKIADKIRAKERFAAYIVIPMWPEGVPTGAATQRILYWQHKTMQMMYGTIYNALVEAGLEDEYSPQDYLNFFCLGNREMVNGNNESGTGSASNENTPQGLCRKSRRFMIYVHSKGMVVDDEYVVIGSANINQRSMEGTRDTEIAMGAYQPQHTWARRQSGPRGQIYGYRMSLWAEHMALLDDCFVEPESLGCVRKVRTVAEENWEQFRSEEVSEMRGHLMKYPVEVDRKGKVRPLPGSEEFPDVGGNVVGSFLAIQENLTI
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Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine or N-acylphosphatidylethanolamine as substrates.
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O23141
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SPE2_ARATH
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Arginine decarboxylase 2 (ADC 2) (ARGDC 2) (AtADC2) (EC 4.1.1.19) (ADC-N)
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MPALACVDTSFVPPAYAFSDTAGDVFIPASSPTSAAVVVDRWSPSLSSSLYRIDGWGAPYFIANSSGNISVRPHGSETLPHQDIDLLKIVKKVTGPKSSGGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIKSQGYDSHYQGVYPVKCNQDRFVVEDIVKFGSSFRFGLEAGSKPEILLAMSCLCKGSPDAFLVCNGFKDAEYISLALLGRKLALNTVIVLEQEEELDLVIELSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVRKLRQSGMLDCLQLLHFHIGSQIPSTSLLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAEAVVASVRVVCDRSSVKHPVICSESGRAIVSHHSVLIFEAVSADKPMVHQATPGDIQFLLEGNEEARANYEDLYAAVMRGDHESCLLYVDQLKQRCVEGFKEGVLSIEQLASVDGLCEWVLKAIGASDPVHTYNINLSVFTSIPDLWGIDQLFPIVPIHKLDQRPGARGILSDLTCDSDGKINKFIGGESSLPLHELDKNGSGGRYFLGMFLGGAYEEALGGVHNLFGGPSVVRVSQSDGPHSFAVTRAVPGQSSADVLRAMQHEPELMFQTLKHRAEEMMHTKGGSEGENEEEEEDDEFNNVAASLDRSFHNMPYLATEQASPSNSLSAAISNLGFYYCDEDVYDYISA
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Required for the biosynthesis of putrescine. Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine. Is a major contributor to basal arginine decarboxylase (ADC) activity and putrescine biosynthesis. Accumulation of putrescine plays a positive role in salt stress tolerance. Accumulation of putrescine plays a positive role in freezing tolerance. Production of PA is essential for normal seed development. Controls PA homeostasis which is crucial for normal plant growth and development.
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O23144
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PPI1_ARATH
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Proton pump-interactor 1
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MGVEVVNSGGFEVAPAPFEGKPEKNGKLDQGKGDDAPINFGSVGELPKNAEENNNKVVNSDAPKNAAEEWPVAKQIHSFYLVKYRSYADPKIKAKLDLADKELEKLNKARTGVLDKLRAKRAERSELFDLLDPLKSERKGFNTMFDEKRKEMEPLQQALGKLRSNDGGSARGPAICSSEEELNSMIYSYQYRIQHESIPLTEEKQILKEIRLLEGTRDKVIANAAMRAKIKESMGQKDDIQGQVKLMGAGLDGVKKERQAISARINELSEKLKATKDEITVLENELKTVSEKRDKAYSNIHDLRRQRDETNSEYYQNRTVLNKARDLAAQKNISELEALANAEVEKFISLWCSKKNFREDYEKRILQSLDSRQLSRDGRMRNPDEKPLIAPEAAPSKATPSETEVVPKAKAKPQPKEEPVSAPKPDATVAQNTEKAKDAVKVKNVADDDDDEVYGLGKPQKEEKPVDAATAKEMRKQEEIAKAKQAMERKKKLAEKAAAKAAIRAQKEAEKKEKKEQEKKAKKKTGGNTETETEEVPEASEEEIEAPVQEEKPQKEKVFKEKPIRNRTRGRGPETIPRAILKRKKSTNYWVYAAPAALVVLLLLVLGYYYVL
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Promotes AHA1 plasma membrane ATPase activity by binding to a site different from the 14-3-3 binding site.
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O23147
|
ADPG1_ARATH
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Polygalacturonase ADPG1 (AtADPG1) (PG ADPG1) (EC 3.2.1.15) (Pectinase ADPG1) (Protein ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 1)
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MARCCRHLAVFLCVLLMLSLCKALSSNVDDGYGHEDGSFESDSLLKLNNDDVLSLISSDETTLEASTVSVSNFGAKGDGKTDDTQAFKKAWKKACSTNGVTTFLVPKGKTYLLKSTRFRGPCKSLRNFQILGTLSASTKRSDYKDKNHWLILEDVNNLSIDGGSTGIINGNGKTWWQNSCKIDKSKPCTKAPTALTLYNLKNLNVKNLRVKNAQQIQISIEKCNKVEVSNVEITAPGDSPNTDGIHITNTQNIRVSNSDIGTGDDCISIEDGTQNLQIFDLTCGPGHGISIGSLGDDNSKAYVSGINVDGAKFSESDNGVRIKTYQGGSGTAKNIKFQNIRMENVKNPIIIDQDYCDKDKCEDQESAVQVKNVVYKNISGTSATDVAITLNCSEKYPCQGIVLENVKIKGGTASCKNANVKNQGTVSPKCS
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Polygalacturonase involved in cell separation in the final stages of pod shatter and in anther dehiscence. Not involved in floral organ abscission.
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O23160
|
MYB73_ARATH
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Transcription factor MYB73 (Myb-related protein 73) (AtMYB73)
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MSNPTRKNMERIKGPWSPEEDDLLQRLVQKHGPRNWSLISKSIPGRSGKSCRLRWCNQLSPEVEHRAFSQEEDETIIRAHARFGNKWATISRLLNGRTDNAIKNHWNSTLKRKCSVEGQSCDFGGNGGYDGNLGEEQPLKRTASGGGGVSTGLYMSPGSPSGSDVSEQSSGGAHVFKPTVRSEVTASSSGEDPPTYLSLSLPWTDETVRVNEPVQLNQNTVMDGGYTAELFPVRKEEQVEVEEEEAKGISGGFGGEFMTVVQEMIRTEVRSYMADLQRGNVGGSSSGGGGGGSCMPQSVNSRRVGFREFIVNQIGIGKME
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Transcription factor that functions in salt stress response. Acts as negative regulator of NHX7/SOS1 and CBL4/SOS3 induction in response to salt stress. In response to auxin, activates the transcription of the auxin-responsive gene IAA19. The IAA19 transcription activation by MYB73 is enhanced by direct interaction between MYB73 and PYL8.
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O23166
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TR164_ARATH
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Thioredoxin-like protein HCF164, chloroplastic (Protein HIGH CHLOROPHYLL FLUORESCENCE 164)
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MARLVFSLNLPSSHGFNLSPRNLQSFFVTQTGAPRFRAVRCKPNPESSETKQEKLVIDNGETSSASKEVESSSSVADSSSSSSSGFPESPNKDINRRVAAVTVIAALSLFVSTRLDFGISLKDLTASALPYEEALSNGKPTVVEFYADWCEVCRELAPDVYKIEQQYKDKVNFVMLNVDNTKWEQELDEFGVEGIPHFAFLDREGNEEGNVVGRLPRQYLVENVNALAAGKQSIPYARAVGQYSSSESRKVHQVTDPLSHG
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Thiol-disulfide oxidoreductase that participates in various redox reactions in the chloroplast. Mediates the reduction of PSI-N in the thylakoid lumen. May interact and probably reduce other target proteins of the thylakoid membrane, such as FTSH2, FTSH8, LHCB5, atpA, atpB, atpE, petA and petC. Involved in the biogenesis of the plastid cytochrome b6f complex. Reducing equivalents are provided by stromal M-type thioredoxins and probably transduced through the thylakoid membrane by CCDA. Possesses low insulin disulfide bonds reducing activity.
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O23171
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MES9_ARATH
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Methylesterase 9 (AtMES9) (EC 3.1.1.-)
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MKHYVLVHGGCHGAWCWYKVKPMLEHSGHRVTVFDLTAHGVNMSRVEDIQTLEDFAKPLLEVLESFGSDDKVVLVAHSLGGIPAALAADMFPSKISVAVFVTSFMPDTTNPPSYVFEKFLGSITEEERMDFELGSYGTDDHPLKTAFLGPNYLKNMYLLSPIEDYELAKMLMRVTPAITSNLTGTKSLTAQGYGSISRVYIVCGEDKGIRVDFQRWMIENSPVKEVMEIKDADHMPMFSKPHELCDRLLKIADKYP
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Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro. Required to convert methyl salicylate (MeSA) to salicylic acid (SA) as part of the signal transduction pathways that activate systemic acquired resistance in systemic tissue. MeSA is believed to be an inactive form that needs to be demethylated to exert a biological effect.
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O23179
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PLP1_ARATH
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Patatin-like protein 1 (AtPLP1) (EC 3.1.1.-) (Patatin-related phospholipase A IIgamma) (pPLAIIg) (Phospholipase A IVA) (AtPLAIVA)
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MENKSPSKKNKPPSCGSLVTILSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAMTAVSKQIVKNNPDMGKLKPLGFDRFLVISIGTGSTKREEKYSAKKAAKWGIISWLYDDGSTPILDITMESSRDMIHYHSSVVFKALQSEDKYLRIDDDTLEGDVSTMDLATKSNLENLQKIGEKMLTNRVMQMNIDTGVYEPVAENITNDEQLKRYAKILSDERKLRRLRSDTMIKDSSNESQEIK
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Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
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O23180
|
PLP5_ARATH
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Patatin-like protein 5 (AtPLP5) (EC 3.1.1.-) (Patatin-related phospholipase A IIdelta) (pPLAIId) (Phospholipase A IVB) (AtPLAIVB)
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MENESPSKKNMPPSCGTLVTILSLDGGGVRGIIAGVILAYLEKQLQELDGEHVRVADYFDVIAGTSTGGLVTAMLTAPDENGRPRFAAKEIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGNYLRTTLGKLLGETKLRQTLTNVVIPTFDIKTLQPTIFSSYQALTDPSLDVKVSDICIGTSAAPTYFPPYYFSNEDSQGKTRHFNLVDGGVTANNPTLVAMTAVTKQIVNNNPDMGTLNPLGYDQFLVISIGTGSAKKEERYSAKKAAKWGIISWLYEDGTTPILDITFESSRDIVHYHSSVVFKALQSEDKYLRIDDDTLEGDASTLDLSTKSNLENLIKLGEKMLTNRVMQMNIDTGTYEPAAENINNDEQLKRFAKILSEERKLRRKRSDKMTKDSSIGSQEIK
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Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
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O23181
|
PLP3_ARATH
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Patatin-like protein 3 (AtPLP3) (EC 3.1.1.-) (Patatin-related phospholipase A IIbeta) (pPLAIIb) (Phospholipase A IVC) (AtPLAIVC)
|
MDTERGSISSSEISRTAHLQDRTVACLPPSYGQLVTILSIDGGGIRGIIPGTILAYLESQLQELDGEEARLVDYFDVISGTSTGGLIVAMLTAQDQSGGHSRNSNRPLFEAKEIVPFYLKHSPKIFPQPRGIFCGWGETIVRLVGGPKFNGKYLHDLVEGFLGDTKLTQSLTNVVIPCFDIKKLQPVIFSSYQAVNNQAMNAKLSDICISTSAAPTFFPAHRFTNEDSEGIKHEFNLIDGGIAANNPTLCAIAEVTKQIIKKNPVMGDISPLDFTRFLVISIGTGSIRNQEKYNAKMASKWGLMCWVFESGSTPILDCYSEAIHDMVDYQSSVVFQALRSEKNYLRIDDDSLKGDLGSVDISTEKNMEGLVEVGEALLKKRVSRVNLESGHYQPISENVTNEEALKRFAKVLSEERKLRESRSPKLKI
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Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
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O23212
|
U2A2A_ARATH
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Splicing factor U2af large subunit A (U2 auxiliary factor 65 kDa subunit A) (U2 small nuclear ribonucleoprotein auxiliary factor large subunit A) (U2 snRNP auxiliary factor large subunit A)
|
MSEFEDHEGNGTVADAIYDEENGGRDGEIEDQLDSKPKRESRDHERETSRSKDREREKGRDKDRERDSEVSRRSRDRDGEKSKERSRDKDRDHRERHHRSSRHRDHSRERGERRERGGRDDDDYRRSRDRDHDRRRDDRGGRRSRRSRSRSKDRSERRTRSRSPSKSKQRVSGFDMAPPASAMLAAGAAVTGQVPPAPPTLPGAGMFPNMFPLPTGQSFGGLSMMPIQAMTQQATRHARRVYVGGLSPTANEQSVATFFSQVMAAVGGNTAGPGDAVVNVYINHEKKFAFVEMRSVEEASNAMSLDGIIFEGAPVKVRRPSDYNPSLAATLGPSQPSPHLNLAAVGLTPGASGGLEGPDRIFVGGLPYYFTESQVRELLESFGGLKGFDLVKDRETGNSKGYAFCVYQDLSVTDIACAALNGIKMGDKTLTVRRANQGTMLQKPEQENVLLHAQQQIAFQRVMLQPGAVATTVVCLTQVVTEDELRDDEEYGDIMEDMRQEGGKFGALTNVVIPRPSPNGEPVAGLGKVFLKYADTDGSTRARFGMNGRKFGGNEVVAVYYPEDKFEQGDYGA
|
Necessary for the splicing of pre-mRNA.
|
O23240
|
D2HDH_ARATH
|
D-2-hydroxyglutarate dehydrogenase, mitochondrial (AtD-2HGDH) (EC 1.1.99.39)
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MMMQKLRRSGEFIRFGCKSLISSRPNKDSVSRSVSGFVNHYKSKGKLFELSDGNYKTELHHPCISRNVGMLLQQYKCFGSSAASLIQRNPLFSSLDSKDVSYFKEILGEKNVVEDKERLETANTDWMHKYKGSSKLMLLPKNTQEVSQILEYCDSRRLAVVPQGGNTGLVGGSVPVFDEVIVNVGLMNKILSFDEVSGVLVCEAGCILENLATFLDTKGFIMPLDLGAKGSCHIGGNVSTNAGGLRLIRYGSLHGTVLGLEAVTANGNVLDMLGTLRKDNTGYDLKHLFIGSEGSLGIVTKVSILTQPKLSSVNLAFIACKDYLSCQKLLVEAKRNLGEILSAFEFLDNNSMDLVLNHLDGVRNPVSSSENFYILIETTGSDETNDREKLEAFLLKSLEKGLVSDGVIAQDINQASSFWRIREGITEALQKAGAVYKYDLSLPVEEIYNIVNDLRGRLGDLANVMGYGHLGDGNLHLNISAAEYNDKLLGLIEPYVYEWTSKHRGSISAEHGLGVMKANEIFYSKSPETVALMASIKKLLDPKGILNPYKVLPHSLFSN
|
Catalyzes the oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate. May be involved in the catabolism of propionyl-CoA derived from beta-oxidation. Involved in degradation of lysine for the supply of carbon and electrons to the ETF/ETFQO complex during dark-induced sugar starvation.
|
O23249
|
CKS1_ARATH
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Cyclin-dependent kinases regulatory subunit 1 (CKS1-At)
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MGQIQYSEKYFDDTFEYRHVVLPPEVAKLLPKNRLLSENEWRAIGVQQSRGWVHYAVHRPEPHIMLFRRPLNYQQQQENQAQNMLVK
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Associates with cyclin-dependent kinases (CDKs) and plays an essential role in the regulation of the cell cycle that affects plant growth rate. May inhibit both the G1/S and G2/M phases.
|
O23252
|
IF4E1_ARATH
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Eukaryotic translation initiation factor 4E-1 (eIF-4E-1) (eIF4E-1) (Protein cucumovirus multiplication 1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
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MAVEDTPKSVVTEEAKPNSIENPIDRYHEEGDDAEEGEIAGGEGDGNVDESSKSGVPESHPLEHSWTFWFDNPAVKSKQTSWGSSLRPVFTFSTVEEFWSLYNNMKHPSKLAHGADFYCFKHIIEPKWEDPICANGGKWTMTFPKEKSDKSWLYTLLALIGEQFDHGDEICGAVVNIRGKQERISIWTKNASNEAAQVSIGKQWKEFLDYNNSIGFIIHEDAKKLDRNAKNAYTA
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Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.
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O23254
|
GLYC4_ARATH
|
Serine hydroxymethyltransferase 4 (AtSHMT4) (EC 2.1.2.1) (Glycine hydroxymethyltransferase 4) (Serine methylase 4)
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MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKGPKPPKKGQPEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGFLMSEMKYKD
|
Catalyzes the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF.
|
O23255
|
SAHH1_ARATH
|
Adenosylhomocysteinase 1 (AdoHcyase 1) (EC 3.13.2.1) (Protein EMBRYO DEFECTIVE 1395) (Protein HOMOLOGY-DEPENDENT GENE SILENCING 1) (S-adenosyl-L-homocysteine hydrolase 1) (SAH hydrolase 1)
|
MALLVEKTSSGREYKVKDMSQADFGRLELELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEIFEKTGQVPDPTSTDNPEFQIVLSIIKEGLQVDPKKYHKMKERLVGVSEETTTGVKRLYQMQQNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKTAGARVIVTEIDPICALQALMEGLQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPETKAGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKASGKYEKKVYVLPKHLDEKVALLHLGKLGARLTKLSKDQSDYVSIPIEGPYKPPHYRY
|
Essential protein during embryogenesis. Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. Required for DNA methylation-dependent gene silencing.
|
O23273
|
DNMT4_ARATH
|
DNA (cytosine-5)-methyltransferase 4 (EC 2.1.1.37) (DNA methyltransferase 4) (DNA methyltransferase IIa) (DMT02) (MET02)
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MEMETKAGKQKKRSVDSDDDVSKERRPKRAAACTNFKEKSLRISDKSETVEAKKEQILAEEIVAIQLTSSLESNDDPRPNRRLTDFVLHDSEGVPQPVEMLELGDIFIEGVVLPLGDEKKEEKGVRFQSFGRVENWNISGYEDGSPVIWISTALADYDCRKPSKKYKKLYDYFFEKACACVEVFKSLSKNPDTSLDELLAAVSRSMSGSKIFSSGGAIQEFVISQGEFIYNQLAGLDETAKNHETCFVENRVLVSLRDHESNKIHKALSNVALRIDESKVVTSDHLVDGAEDEDVKYAKLIQEEEYRKSMERSRNKRSSTTSGGSSRFYIKISEDEIADDYPLPSYYKNTKEETDELVLFEAGYEVDTRDLPCRTLHNWTLYNSDSRMISLEVLPMRPCAEIDVTVFGSGVVAEDDGSGFCLDDSESSTSTQSNDHDGMNIFLSQIKEWMIEFGAEMIFVTLRTDMAWYRLGKPSKQYAPWFGTVMKTVRVGISIFNMLMRESRVAKLSYANVIKRLCGLEENDKAYISSKLLDVERYVVVHGQIILQLFEEYPDKDIKRCPFVTSLASKMQDIHHTKWIIKKKKKILQKGKNLNPRAGIAPVVSRMKAMQATTTRLVNRIWGEFYSIYSPEVPSEAINAENVEEEELEEVEEEDENEEDDPEENELEAVEIQNSPTPKKIKGISEDMEIKWDGEILGKTSAGEPLYGRAFVGGDVVVVGSAVILEVDDQDDTQLICFVEFMFESSNHSKMLHGKLLQRGSETVLGMAANERELFLTNECLTVQLKDIKGTVSLEIRSRLWGHQYRKENIDVDKLDRARAEERKTNGLPTDYYCKSLYSPERGGFFSLPRNDMGLGSGFCSSCKIRENEEERSKTKLNDSKTGFLSNGIEYHNGDFVYVLPNYITKDGLKKGSRRTTLKCGRNVGLKAFVVCQLLDVIVLEESRKASKASFQVKLTRFYRPEDISEEKAYASDIQELYYSQDTYILPPEAIQGKCEVRKKSDMPLCREYPILDHIFFCEVFYDSSTGYLKQFPANMKLKFSTIKDETLLREKKGKGVETGTSSGMLMKPDEVPKEKPLATLDIFAGCGGLSHGLENAGVSTTKWAIEYEEPAGHAFKQNHPEATVFVDNCNVILRAIMEKCGDVDDCVSTVEAAELAAKLDENQKSTLPLPGQVDFINGGPPCQGFSGMNRFSHGSWSKVQCEMILAFLSFADYFRPKYFLLENVKKFVTYNKGRTFQLTMASLLEMGYQVRFGILEAGTYGVSQPRKRVIIWAASPEEVLPEWPEPMHVFDNPGSKISLPRGLRYDAGCNTKFGAPFRSITVRDTIGDLPPVENGESKINKEYGTTPASWFQKKIRGNMSVLTDHICKGLNELNLIRCKKIPKRPGADWRDLPDENVTLSNGLVEKLRPLALSKTAKNHNEWKGLYGRLDWQGNLPISITDPQPMGKVGMCFHPEQDRIITVRECARSQGFPDSYEFSGTTKHKHRQIGNAVPPPLAFALGRKLKEALYLKSSLQHQS
|
Maintains chromatin CpG methylation that plays a role in genomic imprinting, regulation of embryogenesis and seed viability. Required for proper patterns of CG DNA methylation in dividing cells (By similarity).
|
O23299
|
ECI2_ARATH
|
Enoyl-CoA delta isomerase 2, peroxisomal (EC 5.3.3.8) (Delta(3),Delta(2)-enoyl CoA isomerase 2) (AtECI2) (Indole-3-butyric acid response 10)
|
MCTLEKRGDLFLLTLTGDGEHRFHPDTIATILSLLEQAKSQSTRGSILITTANGKFFSNGFDLAWAQTAGSKTGAANRLHQMVESFKPVVAALLDLPMPTIAALNGHAAAAGLILALSHDYVFMRKDRGVLYMSEVDIGLSMPDYFSALVRAKIGTSAARRELLLSGKKIRGEEAVGLGIVDSAAYDSEEGVVVASVRLGEKLAAKKWSGEVYASIRKSLYPELCGILGLETRVFATPKL
|
Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Essential for the beta oxidation of unsaturated fatty acids. Involved with IBR1 and IBR3 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin.
|
O23304
|
BLUS1_ARATH
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Serine/threonine-protein kinase BLUS1 (EC 2.7.11.1) (Protein BLUE LIGHT SIGNALING 1)
|
MARNKLEFPLDAEAYEIICKIGVGVSASVYKAICIPMNSMVVAIKAIDLDQSRADFDSLRRETKTMSLLSHPNILNAYCSFTVDRCLWVVMPFMSCGSLHSIVSSSFPSGLPENCISVFLKETLNAISYLHDQGHLHRDIKAGNILVDSDGSVKLADFGVSASIYEPVTSSSGTTSSSLRLTDIAGTPYWMAPEVVHSHTGYGFKADIWSFGITALELAHGRPPLSHLPPLKSLLMKITKRFHFSDYEINTSGSSKKGNKKFSKAFREMVGLCLEQDPTKRPSAEKLLKHPFFKNCKGLDFVVKNVLHSLSNAEQMFMESQILIKSVGDDDEEEEEEDEEIVKNRRISGWNFREDDLQLSPVFPATESDSSESSPREEDQSKDKKEDDNVTITGYELGLGLSNEEAKNQEGEVVGFDKDLVLEKLKVLKKSLEHQRARVSIIIEALSGDKEEKSREEELLEMVEKLKIELETEKLKTLRADKDSVLG
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Ser/Thr protein kinase mediating a primary step for phototropin signaling in guard cells. Essential for stomatal opening.
|
O23310
|
NFYB3_ARATH
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Nuclear transcription factor Y subunit B-3 (AtNF-YB-3) (AtNF-YB3) (Transcriptional activator HAP3C)
|
MADSDNDSGGHKDGGNASTREQDRFLPIANVSRIMKKALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYVEPLKVYLQKYREVEGEKTTTAGRQGDKEGGGGGGGAGSGSGGAPMYGGGMVTTMGHQFSHHFS
|
Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity). Promotes the expression of heat stress-inducible genes by contributing to the formation of a heat stress-specific transcriptional complex with NF-Y subunits (e.g. DPB3-1, NF-YA2 and NF-YB3) and DREB2A at the promoter of target genes, thus promoting heat tolerance.
|
O23349
|
AO1_ARATH
|
Primary amine oxidase 1 (AtAO1) (EC 1.4.3.21)
|
MNTSILAILFLIQCVFTLGLHFHPLDPLTPQEINKTSFIVKKSHLGNLKDLTFHYLDLEEPNKSHVLQWLSPNPSKKPPPPRRRSFVVVRAGGQTYELIIDLTTSKIASSRIYTGHGFPSFTFIELFKASKLPLTYPPFKKSILDRSLNISEVSCIPFTVGWYGETTTRRELKASCFYRDGSVNVFTRPIEGITVTIDVDSMQVIKYSDRFRKPIPDKEGNDFRTKHRPFPFFCNVSDTGFKILGNRVKWANWKFHVGFTARAGVTISTASVLDPRTKRFRRVMYRGHVSETFVPYMDPTYEWYYRTFMDIGEFGFGRSAVNLQPLIDCPQNAAFLDGHVAGPDGTAQKMTNVMCVFEKNGYGASFRHTEINVPGQVITSGEAEISLVVRMVATLGNYDYIVDWEFKKNGAIRVGVDLTGVLEVKATSYTSNDQITENVYGTLVAKNTIAVNHDHYLTYYLDLDVDGNGNSLVKAKLKTVRVTEVNKTSSRRKSYWTVVKETAKTEADGRVRLGSDPVELLIVNPNKKTKIGNTVGYRLIPEHLQATSLLTDDDYPELRAGYTKYPVWVTAYDRSERWAGGFYSDRSRGDDGLAVWSSRNREIENKDIVMWYNVGFHHIPYQEDFPVMPTLHGGFTLRPSNFFDNDPLIG
|
Oxidizes preferentially the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide. May be involved in the regulation of developmental programmed cell death (PCD) in both vascular tissue and the root cap. Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H(2)O(2) accumulation in roots.
|
O23372
|
ATXR3_ARATH
|
Histone-lysine N-methyltransferase ATXR3 (EC 2.1.1.354) (Protein SET DOMAIN GROUP 2) (Trithorax-related protein 3) (TRX-related protein 3)
|
MSDGGVACMPLLNIMEKLPIVEKTTLCGGNESKTAATTENGHTSIATKVPESQPANKPSASSQPVKKKRIVKVIRKVVKRRPKQPQKQADEQLKDQPPSQVVQLPAESQLQIKEQDKKSEFKGGTSGVKEVENGGDSGFKDEVEEGELGTLKLHEDLENGEISPVKSLQKSEIEKGEIVGESWKKDEPTKGEFSHLKYHKGYVERRDFSADKNWKGGKEEREFRSWRDPSDEIEKGEFIPDRWQKMDTGKDDHSYIRSRRNGVDREKTWKYEYEYERTPPGGRFVNEDIYHQREFRSGLDRTTRISSKIVIEENLHKNEYNNSSNFVKEYSSTGNRLKRHGAEPDSIERKHSYADYGDYGSSKCRKLSDDCSRSLHSDHYSQHSAERLYRDSYPSKNSSLEKYPRKHQDASFPAKAFSDKHGHSPSRSDWSPHDRSRYHENRDRSPYARERSPYIFEKSSHARKRSPRDRRHHDYRRSPSYSEWSPHDRSRPSDRRDYIPNFMEDTQSDRNRRNGHREISRKSGVRERRDCQTGTELEIKHKYKESNGKESTSSSKELQGKNILYNNSLLVEKNSVCDSSKIPVPCATGKEPVQVGEAPTEELPSMEVDMDICDTPPHEPMASDSSLGKWFYLDYYGTEHGPARLSDLKALMEQGILFSDHMIKHSDNNRWLVNPPEAPGNLLEDIADTTEAVCIEQGAGDSLPELVSVRTLPDGKEIFVENREDFQIDMRVENLLDGRTITPGREFETLGEALKVNVEFEETRRCVTSEGVVGMFRPMKRAIEEFKSDDAYGSESDEIGSWFSGRWSCKGGDWIRQDEASQDRYYKKKIVLNDGFPLCLMQKSGHEDPRWHHKDDLYYPLSSSRLELPLWAFSVVDERNQTRGVKASLLSVVRLNSLVVNDQVPPIPDPRAKVRSKERCPSRPARPSPASSDSKRESVESHSQSTASTGQDSQGLWKTDTSVNTPRDRLCTVDDLQLHIGDWFYTDGAGQEQGPLSFSELQKLVEKGFIKSHSSVFRKSDKIWVPVTSITKSPETIAMLRGKTPALPSACQGLVVSETQDFKYSEMDTSLNSFHGVHPQFLGYFRGKLHQLVMKTFKSRDFSAAINDVVDSWIHARQPKKESEKYMYQSSELNSCYTKRARLMAGESGEDSEMEDTQMFQKDELTFEDLCGDLTFNIEGNRSAGTVGIYWGLLDGHALARVFHMLRYDVKSLAFASMTCRHWKATINSYKDISRQVDLSSLGPSCTDSRLRSIMNTYNKEKIDSIILVGCTNVTASMLEEILRLHPRISSVDITGCSQFGDLTVNYKNVSWLRCQNTRSGELHSRIRSLKQTTDVAKSKGLGGDTDDFGNLKDYFDRVEKRDSANQLFRRSLYKRSKLYDARRSSAILSRDARIRRWAIKKSEHGYKRVEEFLASSLRGIMKQNTFDFFALKVSQIEEKMKNGYYVSHGLRSVKEDISRMCREAIKDELMKSWQDGSGLSSATKYNKKLSKTVAEKKYMSRTSDTFGVNGASDYGEYASDREIKRRLSKLNRKSFSSESDTSSELSDNGKSDNYSSASASESESDIRSEGRSQDLRIEKYFTADDSFDSVTEEREWGARMTKASLVPPVTRKYEVIEKYAIVADEEEVQRKMRVSLPEDYGEKLNAQRNGIEELDMELPEVKEYKPRKLLGDEVLEQEVYGIDPYTHNLLLDSMPGELDWSLQDKHSFIEDVVLRTLNRQVRLFTGSGSTPMVFPLRPVIEELKESAREECDIRTMKMCQGVLKEIESRSDDKYVSYRKGLGVVCNKEGGFGEEDFVVEFLGEVYPVWKWFEKQDGIRSLQENKTDPAPEFYNIYLERPKGDADGYDLVVVDAMHMANYASRICHSCRPNCEAKVTAVDGHYQIGIYSVRAIEYGEEITFDYNSVTESKEEYEASVCLCGSQVCRGSYLNLTGEGAFQKVLKDWHGLLERHRLMLEACVLNSVSEEDYLELGRAGLGSCLLGGLPDWMIAYSARLVRFINFERTKLPEEILKHNLEEKRKYFSDIHLDVEKSDAEVQAEGVYNQRLQNLAVTLDKVRYVMRHVFGDPKNAPPPLERLTPEETVSFVWNGDGSLVDELLQSLSPHLEEGPLNELRSKIHGHDPSGSADVLKELQRSLLWLRDEIRDLPCTYKCRNDAAADLIHIYAYTKCFFKVREYQSFISSPVHISPLDLGAKYADKLGESIKEYRKTYGENYCLGQLIYWYNQTNTDPDLTLVKATRGCLSLPDVASFYAKAQKPSKHRVYGPKTVKTMVSQMSKQPQRPWPKDKIWTFKSTPRVFGSPMFDAVLNNSSSLDRELLQWLRNRRHVFQATWDS
|
Histone methyltransferase specifically required for trimethylation of 'Lys-4' of histone H3 (H3K4me3) and is crucial for both sporophyte and gametophyte development. Function as a diurnal 'writer' to counteract the nocturne 'eraser' demethylase activity of JMJ14 thus orchestrating the circadian rythm of histone modifications (e.g. H3K4me3) and modulating the rythmic expression of diurnal target genes this mechanism relies also on the circadian clock oscillators CCA1 and LHY.
|
O23393
|
BIA1_ARATH
|
BAHD acyltransferase BIA1 (EC 2.3.1.-) (Protein ABNORMAL SHOOT 1) (Protein BRASSINOSTEROID INACTIVATOR 1)
|
MEAKLEVTGKEVIKPASPSPRDRLQLSILDLYCPGIYVSTIFFYDLITESSEVFSENLKLSLSETLSRFYPLAGRIEGLSISCNDEGAVFTEARTDLLLPDFLRNLNTDSLSGFLPTLAAGESPAAWPLLSVKVTFFGSGSGVAVSVSVSHKICDIASLVTFVKDWATTTAKGKSNSTIEFAETTIYPPPPSHMYEQFPSTDSDSNITSKYVLKRFVFEPSKIAELKHKAASESVPVPTRVEAIMSLIWRCARNSSRSNLLIPRQAVMWQAMDIRLRIPSSVAPKDVIGNLQSGFSLKKDAESEFEIPEIVATFRKNKERVNEMIKESLQGNTIGQSLLSLMAETVSESTEIDRYIMSSWCRKPFYEVDFGSGSPVWVGYASHTIYDNMVGVVLIDSKEGDGVEAWISLPEEDMSVFVDDQELLAYAVLNPPVVA
|
Monitors brassinosteroids (BR) responses and homeostasis, particularly in the root and hypocotyl in darkness. Promotes flavonoid biosynthesis.
|
O23403
|
PPD1_ARATH
|
PsbP domain-containing protein 1, chloroplastic (OEC23-like protein 3) (PsbP-related thylakoid lumenal protein 1)
|
MASSAFAFPSYIITKGASTDSFKSTSLSSSRSLVTDFHLLFSRPISSGPKYQSAKSAKPESPVAINCLTDAKQVCAVGRRKSMMMGLLMSGLIVSQANLPTAFASTPVFREYIDTFDGYSFKYPQNWIQVRGAGADIFFRDPVVLDENLSVEFSSPSSSNYTSLEDLGSPEEVGKRVLRQYLTEFMSTRLGVKRQANILSTSSRVADDGKLYYQVEVNIKSYANNNELAVMPQDRVARLEWNRRYLAVLGVENDRLYSIRLQTPEKVFLEEEKDLRRVMDSFRVEKI
|
Photosystem I assembly factor that assists the proper folding and integration of PsaB and PsaA into the thylakoid membrane.
|
O23404
|
PPDK1_ARATH
|
Pyruvate, phosphate dikinase 1, chloroplastic (EC 2.7.9.1) (Pyruvate, orthophosphate dikinase 1)
|
MLYIRKKMTSMIVKTTPELFKGNGVFRTDHLGENRMVSRSNRLGDGSNRFPRTGTIHCQRLSIAKTGLHRETKARAILSPVSDPAASIAQKRVFTFGKGRSEGNKGMKSLLGGKGANLAEMASIGLSVPPGLTISTEACQQYQIAGKKLPEGLWEEILEGLSFIERDIGASLADPSKPLLLSVRSGAAISMPGMMDTVLNLGLNDQVVVGLAAKSGERFAYDSFRRFLDMFGDVVMGIPHAKFEEKLERMKERKGVKNDTDLSAADLKELVEQYKSVYLEAKGQEFPSDPKKQLELAIEAVFDSWDSPRANKYRSINQITGLKGTAVNIQCMVFGNMGDTSGTGVLFTRNPSTGEKKLYGEFLVNAQGEDVVAGIRTPEDLDTMKRFMPEAYAELVENCNILERHYKDMMDIEFTVQEERLWMLQCRAGKRTGKGAVKIAVDMVGEGLVEKSSAIKMVEPQHLDQLLHPQFHDPSGYREKVVAKGLPASPGAAVGQVVFTAEEAEAWHSQGKTVILVRTETSPDDVGGMHAAEGILTARGGMTSHAAVVARGWGKCCIAGCSEIRVDENHKVLLIGDLTINEGEWISMNGSTGEVILGKQALAPPALSPDLETFMSWADAIRRLKVMANADTPEDAIAARKNGAQGIGLCRTEHMFFGADRIKAVRKMIMAVTTEQRKASLDILLPYQRSDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGDLDNIVHELAEETGVKEDEVLSRIEKLSEVNPMLGFRGCRLGISYPELTEMQARAIFEAAASMQDQGVTVIPEIMVPLVGTPQELGHQVDVIRKVAKKVFAEKGHTVSYKVGTMIEIPRAALIADEIAKEAEFFSFGTNDLTQMTFGYSRDDVGKFLPIYLAKGILQHDPFEVLDQQGVGQLIKMATEKGRAARPSLKVGICGEHGGDPSSVGFFAEAGLDYVSCSPFRVPIARLAAAQVVVA
|
Formation of phosphoenolpyruvate. May be involved in regulating the flux of carbon into starch and fatty acids of seeds and in the remobilization of nitrogen reserves in senescing leaves.
|
O23463
|
CMTA5_ARATH
|
Calmodulin-binding transcription activator 5 (AtCAMTA5) (Ethylene-induced calmodulin-binding protein f) (EICBP.f) (Signal-responsive protein 6) (AtSR6)
|
MAGVDSGKLIGSEIHGFHTLQDLDIQTMLDEAYSRWLRPNEIHALLCNHKFFTINVKPVNLPKSGTIVLFDRKMLRNFRKDGHNWKKKKDGKTIKEAHEHLKVGNEERIHVYYAHGEDTPTFVRRCYWLLDKSQEHIVLVHYRETHEVHAAPATPGNSYSSSITDHLSPKIVAEDTSSGVHNTCNTGFEVRSNSLGSRNHEIRLHEINTLDWDELLVPADISNQSHPTEEDMLYFTEQLQTAPRGSVKQGNHLAGYNGSVDIPSFPGLEDPVYQNNNSCGAGEFSSQHSHCGVDPNLQRRDFSATVTDQPGDALLNNGYGSQDSFGRWVNNFISDSPGSVDDPSLEAVYTPGQDSSTPPTVFHSHSDIPEQVFNITDVSPAWAYSTEKTKILVTGFFHDSFQHLGRSNLICICGELRVPAEFLQMGVYRCFLPPQSPGVVNLYLSVDGNKPISQLFSFEHRSVQFIEKAIPQDDQLYKWEEFEFQVRLAHLLFTSSNKISVLTSKISPENLLEAKKLASRTSHLLNSWAYLMKSIQANEVPFDQARDHLFELTLKNRLKEWLLEKVIENRNTKEYDSKGLGVIHLCAVLGYTWSILLFSWANISLDFRDKQGWTALHWAAYYGREKMVAALLSAGARPNLVTDPTKEFLGGCTAADLAQQKGYDGLAAFLAEKCLVAQFKDMQTAGNISGNLETIKAEKSSNPGNANEEEQSLKDTLAAYRTAAEAAARIQGAFREHELKVRSSAVRFASKEEEAKNIIAAMKIQHAFRNFEVRRKIAAAARIQYRFQTWKMRREFLNMRKKAIRIQAAFRGFQVRRQYQKITWSVGVLEKAILRWRLKRKGFRGLQVSQPDEKEGSEAVEDFYKTSQKQAEERLERSVVKVQAMFRSKKAQQDYRRMKLAHEEAQLEYDGMQELDQMATEES
|
Transcription activator. Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2.
|
O23507
|
1MMP_ARATH
|
Metalloendoproteinase 1-MMP (At1-MMP) (EC 3.4.24.-)
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MSRNLIYRRNRALCFVLILFCFPYRFGARNTPEAEQSTAKATQIIHVSNSTWHDFSRLVDVQIGSHVSGVSELKRYLHRFGYVNDGSEIFSDVFDGPLESAISLYQENLGLPITGRLDTSTVTLMSLPRCGVSDTHMTINNDFLHTTAHYTYFNGKPKWNRDTLTYAISKTHKLDYLTSEDVKTVFRRAFSQWSSVIPVSFEEVDDFTTADLKIGFYAGDHGDGLPFDGVLGTLAHAFAPENGRLHLDAAETWIVDDDLKGSSEVAVDLESVATHEIGHLLGLGHSSQESAVMYPSLRPRTKKVDLTVDDVAGVLKLYGPNPKLRLDSLTQSEDSIKNGTVSHRFLSGNFIGYVLLVVGLILFL
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Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses. Can cleave myelin basic protein as well as fluorigenic peptide substrates, McaPLANvaDpaAR-NH(2) and McaPChaGNvaHADpa-NH(2) 4-fold more efficiently than McaPLGLDpaAR-NH(2) (QF24). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24) and beta-casein.
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O23512
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MES16_ARATH
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pFDCC methylesterase MES16 (EC 3.1.1.-) (Methylesterase 16) (AtMES16) (Pheophorbidase) (AtPPD)
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MGGEGGAEPVIHFVFVHGASHGAWCWYKLTTLLDAAGFKSTSVDLTGAGISLIDSNIVFDSDQYNRPLFSLLSDLPPHHKVILVGHSIGGGSVTEALCKFTDKISMAIYLAASMVQPGSIPSPHLSNIHVGEEDIWEYTYGEGTDKPPTGVLMKPEFIRHYYYSQSPLEDVTLSSKLLRPAPMRAFQDLDKLPPNPEAEKVPRVYIKTAKDNLFDSVRQDLLVENWPPSQLYVLEDSDHSAFFSVPTTLFAYLLRAVSFLQR
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Involved in the chlorophyll breakdown by its action in fluorescent chlorophyll catabolites (FCCs) demethylation. Demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll. Uses primary fluorescent dioxobilin-type chlorophyll catabolite (pFDCC) as substrate to produce O13(4)-desmethyl pFDCC. Also able to catalyze pheophorbides in vitro. Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro.
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O23523
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RGGA_ARATH
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RGG repeats nuclear RNA binding protein A (AtRGGA)
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MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLPPAQAVREARSDAPRGGGGRGGFNRGRGGYNRDDGNNGYSGGYTKPSGEGDVSKSSYERRGGGGAPRGSFRGEGGGPGGGRRGGFSNEGGDGERPRRAFERRSGTGRGSDFKRDGSGRGNWGTPGEEIAAETEAVAGVETEKDVGEKPAVDDVAADANKEDTVVEEKEPEDKEMTLDEYEKILEEKKKALQSLTTSERKVDTKVFESMQQLSNKKSNDEIFIKLGSDKDKRKDDKEEKAKKAVSINEFLKPAEGGNYYRGGRGGRGRGGRGRGGVSSGESGGYRNEAAPAIGDAAQFPSLGGK
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Ribosome-binding protein that acts as a regulator of mRNA translation by promoting ribosome inactivation (By similarity). Binds RNA. Regulates responses to abscisic acid (ABA). Promotes stomata closure in drought conditions. Involved in resistance to salt and drought stresses via the accumulation of Pro.
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O23530
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SNC1_ARATH
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Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 (AtSNC1) (Disease resistance RPP5-like protein) (Probable NAD(+) hydrolase SNC1) (EC 3.2.2.6)
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MMDTSKDDDMEIASSSGSRRYDVFPSFRGEDVRDSFLSHLLKELRGKAITFIDDEIERSRSIGPELLSAIKESRIAIVIFSKNYASSTWCLNELVEIHKCYTNLNQMVIPIFFHVDASEVKKQTGEFGKVFEETCKAKSEDEKQSWKQALAAVAVMAGYDLRKWPSEAAMIEELAEDVLRKTMTPSDDFGDLVGIENHIEAIKSVLCLESKEARIMVGIWGQSGIGKSTIGRALYSKLSIQFHHRAFITYKSTSGSDVSGMKLRWEKELLSEILGQKDIKIEHFGVVEQRLKQQKVLILLDDVDSLEFLKTLVGKAEWFGSGSRIIVITQDRQLLKAHEIDLIYEVEFPSEHLALTMLCRSAFGKDSPPDDFKELAFEVAKLAGNLPLGLSVLGSSLKGRTKEWWMEMMPRLRNGLNGDIMKTLRVSYDRLHQKDQDMFLYIACLFNGFEVSYVKDLLKDNVGFTMLTEKSLIRITPDGYIEMHNLLEKLGREIDRAKSKGNPGKRRFLTNFEDIHEVVTEKTGTETLLGIRLPFEEYFSTRPLLIDKESFKGMRNLQYLEIGYYGDLPQSLVYLPLKLRLLDWDDCPLKSLPSTFKAEYLVNLIMKYSKLEKLWEGTLPLGSLKEMNLRYSNNLKEIPDLSLAINLEELDLVGCKSLVTLPSSIQNATKLIYLDMSDCKKLESFPTDLNLESLEYLNLTGCPNLRNFPAIKMGCSDVDFPEGRNEIVVEDCFWNKNLPAGLDYLDCLTRCMPCEFRPEQLAFLNVRGYKHEKLWEGIQSLGSLEGMDLSESENLTEIPDLSKATKLESLILNNCKSLVTLPSTIGNLHRLVRLEMKECTGLEVLPTDVNLSSLETLDLSGCSSLRSFPLISTNIVWLYLENTAIEEIPSTIGNLHRLVRLEMKKCTGLEVLPTDVNLSSLETLDLSGCSSLRSFPLISESIKWLYLENTAIEEIPDLSKATNLKNLKLNNCKSLVTLPTTIGNLQKLVSFEMKECTGLEVLPIDVNLSSLMILDLSGCSSLRTFPLISTNIVWLYLENTAIEEIPSTIGNLHRLVKLEMKECTGLEVLPTDVNLSSLMILDLSGCSSLRTFPLISTRIECLYLQNTAIEEVPCCIEDFTRLTVLMMYCCQRLKTISPNIFRLTRLELADFTDCRGVIKALSDATVVATMEDHVSCVPLSENIEYIWDKLYRVAYLQEHFSFRNCFKLDRDARELILRSCFKPVALPGEEIPKYFTYRAYGDSLTVIVPQSSLSQNFLRFKACVVVEPLSKGKGFYPFLKVNVGFNGKQYQKSFSKDAELELCKTDHLFFCSFKFRSEDLPSKLNFNDVEFKFCCSNRIKECGVRLMYVSQEENNQQTTRSEKRMRMTSGTSEEDINLPYGLIVADTGLAALNMELSLGQGEPSSSTSLEGEALCVDYMITEEQDKGIPILFPVSGN
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Disease resistance protein of the TIR-NB-LRR-type. Part of the RPP5 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. 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. Expression regulated by MOS1 at chromatin level. Nuclear localization of SNC1 is essential for its activity. ABA deficiency can rescue high-temperature inhibition of SNC1-mediated defense responses.
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O23553
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BAM3_ARATH
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Beta-amylase 3, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 8) (Chloroplast beta-amylase) (CT-BMY)
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MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMKPPTYQFQAKNSVKEMKFTHEKTFTPEGETLEKWEKLHVLSYPHSKNDASVPVFVMLPLDTVTMSGHLNKPRAMNASLMALKGAGVEGVMVDAWWGLVEKDGPMNYNWEGYAELIQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEISKNPDLVYTDKSGRRNPEYISLGCDSVPVLRGRTPIQVYSDFMRSFRERFEGYIGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEFQCYDKYMKSSLQAYAESIGKTNWGTSGPHDAGEYKNLPEDTEFFRRDGTWNSEYGKFFMEWYSGKLLEHGDQLLSSAKGIFQGSGAKLSGKVAGIHWHYNTRSHAAELTAGYYNTRNHDGYLPIAKMFNKHGVVLNFTCMEMKDGEQPEHANCSPEGLVKQVQNATRQAGTELAGENALERYDSSAFGQVVATNRSDSGNGLTAFTYLRMNKRLFEGQNWQQLVEFVKNMKEGGHGRRLSKEDTTGSDLYVGFVKGKIAENVEEAALV
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Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.
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O23627
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SYGM1_ARATH
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Glycine--tRNA ligase, mitochondrial 1 (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase 1) (GlyRS-1)
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MRIFSTFVFHRRQQIFNLRQFQTTTILRNPISIAPIQIPMDATEQSLRQSLSEKSSSVEAQGNAVRALKASRAAKPEIDAAIEQLNKLKLEKSTVEKELQSIISSSGNGSLNREAFRKAVVNTLERRLFYIPSFKIYSGVAGLFDYGPPGCAIKSNVLSFWRQHFILEENMLEVDCPCVTPEVVLKASGHVDKFTDLMVKDEKTGTCYRADHLLKDYCTEKLEKDLTISAEKAAELKDVLAVMEDFSPEQLGAKIREYGITAPDTKNPLSDPYPFNLMFQTSIGPSGLIPGYMRPETAQGIFVNFKDLYYYNGKKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDPENKSHPKFSDVAKLEFLMFPREEQMSGQSAKKLCLGEAVAKGTVNNETLGYFIGRVYLFLTRLGIDKERLRFRQHLANEMAHYAADCWDAEIESSYGWIECVGIADRSAYDLRAHSDKSGTPLVAEEKFAEPKEVEKLVITPVKKELGLAFKGNQKNVVESLEAMNEEEAMEMKATLESKGEVEFYVCTLKKSVNIKKNMVSISKEKKKEHQRVFTPSVIEPSFGIGRIIYCLYEHCFSTRPSKAGDEQLNLFRFPPLVAPIKCTVFPLVQNQQFEEVAKVISKELASVGISHKIDITGTSIGKRYARTDELGVPFAITVDSDTSVTIRERDSKDQVRVTLKEAASVVSSVSEGKMTWQDVWATFPHHSSAAADE
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Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
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O23628
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H2AV1_ARATH
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Histone H2A variant 1 (H2A.F/Z 1) (H2AvAt) (HTA11)
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MAGKGGKGLVAAKTMAANKDKDKDKKKPISRSARAGIQFPVGRIHRQLKTRVSAHGRVGATAAVYTASILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDTLIKGTIAGGGVIPHIHKSLINKTTKE
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Variant histone H2A which may replace conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity).
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O23629
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H2B6_ARATH
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Histone H2B.6 (H2BAt) (HTB9)
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MAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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O23647
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GLGB1_ARATH
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1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic (AtSBE II-1) (EC 2.4.1.18) (Branching enzyme 3) (AtBE3) (Starch-branching enzyme 2-1)
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MVYTISGVRFPHLPSIKKKNSSLHSFNEDLRRSNAVSFSLRKDSRSSGKVFARKPSYDSDSSSLATTASEKLRGHQSDSSSSASDQVQSRDTVSDDTQVLGNVDVQKTEEAQETETLDQTSALSTSGSISYKEDFAKMSHSVDQEVGQRKIPPPGDGKRIYDIDPMLNSHRNHLDYRYGQYRKLREEIDKNEGGLEAFSRGYEIFGFTRSATGITYREWAPGAKAASLIGDFNNWNAKSDVMARNDFGVWEIFLPNNADGSPAIPHGSRVKIRMDTPSGIKDSIPAWIKYSVQPPGEIPYNGVYYDPPEEDKYAFKHPRPKKPTSLRIYESHVGMSSTEPKINTYANFRDDVLPRIKKLGYNAVQIMAIQEHAYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGLVVLMDIVHSHASKNTLDGLDMFDGTDGQYFHSGSRGYHWMWDSRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVEFTGNYNEYFGYSTDVDAVVYLMLVNDLIHGLYPEAIVVGEDVSGMPAFCVPVEDGGVGFDYRLHMAVADKWIELLKKRDEDWQVGDITFTLTNRRWGEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRQATPRVDRGIALHKMIRLITMGLGGEGYLNFMGNEFGHPEWIDFPRTDQHLPDGRVIAGNNGSYDKCRRRFDLGDAEYLRYHGLQEFDRAMQNLEETYGFMTSEHQYISRKDEGDRVIVFERGNLLFVFNFHWTNSYSDYRIGCSVPGKYKIVLDSDNSLFGGFNRLDDSAEFFTSDGRHDDRPCSFMVYAPCRTAVVYAAVDDDDDDERSSLVPIGLLPEDV
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Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
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O23653
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AK2_ARATH
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Aspartokinase 2, chloroplastic (EC 2.7.2.4) (Aspartate kinase 2)
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MASLQLYGVKTPGLALSSKRLEFASKGACFSVTLPSSSAVFRDVEHSCRNIGLRVSCEALRVDLLQRKEPETCDSSGTGKELTCVMKFGGSSVESAERMKEVANLILSFPDERPVIVLSAMGKTTNKLLKAGEKAVTCGVTNVESIEELSFIKELHLRTAHELGVETTVIEKHLEGLHQLLKGISMMKELTLRTRDYLVSFGECMSTRLFSAYLNKIGHKARQYDAFEIGFITTDDFTNADILEATYPAVSKTLVGDWSKENAVPVVTGYLGKGWRSCAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNIYPGAQSVPYLTFDEAAELAYFGAQVLHPLSMRPARDGDIPVRVKNSYNPTAPGTVITRSRDMSKAVLTSIVLKRNVTMLDIASTRMLGQYGFLAKVFTTFEDLGISVDVVATSEVSISLTLDPAKLWGRELIQRVNELDNLVEELEKIAVVKLLQRRSIISLIGNVQKSSLILEKVFQVFRSNGVNVQMISQGASKVNISLIVNDEEAEQCVRALHSAFFETDP
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Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
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O23654
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VATA_ARATH
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V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar H(+)-ATPase subunit A) (Vacuolar proton pump subunit alpha)
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MPAFYGGKLTTFEDDEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGMDGQKITYTLIKHRLGDLFYRLVSQKFEDPAEGEDTLVEKFKKLYDDLNAGFRALEDETR
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Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
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O23661
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ARFC_ARATH
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Auxin response factor 3 (Protein ETTIN)
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MGGLIDLNVMETEEDETQTQTPSSASGSVSPTSSSSASVSVVSSNSAGGGVCLELWHACAGPLISLPKRGSLVLYFPQGHLEQAPDFSAAIYGLPPHVFCRILDVKLHAETTTDEVYAQVSLLPESEDIERKVREGIIDVDGGEEDYEVLKRSNTPHMFCKTLTASDTSTHGGFSVPRRAAEDCFPPLDYSQPRPSQELLARDLHGLEWRFRHIYRGQPRRHLLTTGWSAFVNKKKLVSGDAVLFLRGDDGKLRLGVRRASQIEGTAALSAQYNQNMNHNNFSEVAHAISTHSVFSISYNPKASWSNFIIPAPKFLKVVDYPFCIGMRFKARVESEDASERRSPGIISGISDLDPIRWPGSKWRCLLVRWDDIVANGHQQRVSPWEIEPSGSISNSGSFVTTGPKRSRIGFSSGKPDIPVSEGIRATDFEESLRFQRVLQGQEIFPGFINTCSDGGAGARRGRFKGTEFGDSYGFHKVLQGQETVPAYSITDHRQQHGLSQRNIWCGPFQNFSTRILPPSVSSSPSSVLLTNSNSPNGRLEDHHGGSGRCRLFGFPLTDETTAVASATAVPCVEGNSMKGASAVQSNHHHSQGRDIYAMRDMLLDIAL
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Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Involved in the establishment or elaboration of tissue patterning during gynoecial development.
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O23674
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PKSA_ARATH
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Type III polyketide synthase A (PKS-A) (EC 2.3.1.-) (Hydroxyalkyl alpha-pyrone synthase PKS-A) (Protein LESS ADHESIVE POLLEN 6)
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MSNSRMNGVEKLSSKSTRRVANAGKATLLALGKAFPSQVVPQENLVEGFLRDTKCDDAFIKEKLEHLCKTTTVKTRYTVLTREILAKYPELTTEGSPTIKQRLEIANEAVVEMALEASLGCIKEWGRPVEDITHIVYVSSSEIRLPGGDLYLSAKLGLRNDVNRVMLYFLGCYGGVTGLRVAKDIAENNPGSRVLLTTSETTILGFRPPNKARPYDLVGAALFGDGAAAVIIGADPRECEAPFMELHYAVQQFLPGTQNVIEGRLTEEGINFKLGRDLPQKIEENIEEFCKKLMGKAGDESMEFNDMFWAVHPGGPAILNRLETKLKLEKEKLESSRRALVDYGNVSSNTILYVMEYMRDELKKKGDAAQEWGLGLAFGPGITFEGLLIRSLTSS
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Plant type III polyketide synthases (PKSs) that catalyzes the condensation of malonyl-CoA units with various CoA ester starter molecules to generate a diverse array of natural products including long-chain alkyl alpha-pyrones. Accepts up to C(20) chain-length fatty acyl CoAs as starter substrates, and carries out sequential condensations with malonyl-CoA to produce triketide and tetraketide alpha-pyrones, potential sporopollenin precursors. Favorite substrates for are midchain- and v-hydroxylated fatty acyl-CoAs (e.g. 12-hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA). Required for pollen development and sporopollenin biosynthesis, the major constituent of exine in the outer pollen wall. In vitro, can use 4-coumaroyl-coenzyme A as substrate to produce bis-noryangonin and fatty acyl-coenzyme A as substrate to produce medium-chain alkyl pyrones. May play a role in both the synthesis of pollen fatty acids and phenolics found in exine.
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O23676
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MGN_ARATH
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Protein mago nashi homolog (AtMAGO)
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MAAEEATEFYLRYYVGHKGKFGHEFLEFEFREDGKLRYANNSNYKNDTIIRKEVFLTPAVLKECKRIVSESEILKEDDNNWPEPDRVGKQELEIVLGNEHISFATSKIGSLVDCQSSNDPEGLRIFYYLVQDLKCLVFSLISLHFKIKPI
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Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). Can increase in vitro the expression from reporter constructs that contain leader introns required for the expression of different genes. In association with MAGO and PYM, participates in intron-mediated enhancement of gene expression. The MAGO-Y14 heterodimer works synergistically with the NMD pathway to regulate male gametophyte development.
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O23680
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TOC33_ARATH
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Translocase of chloroplast 33, chloroplastic (AtToc33) (EC 3.6.5.-) (33 kDa chloroplast outer envelope protein) (Plastid protein import 1)
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MGSLVREWVGFQQFPAATQEKLIEFFGKLKQKDMNSMTVLVLGKGGVGKSSTVNSLIGEQVVRVSPFQAEGLRPVMVSRTMGGFTINIIDTPGLVEAGYVNHQALELIKGFLVNRTIDVLLYVDRLDVYRVDELDKQVVIAITQTFGKEIWCKTLLVLTHAQFSPPDELSYETFSSKRSDSLLKTIRAGSKMRKQEFEDSAIAVVYAENSGRCSKNDKDEKALPNGEAWIPNLVKAITDVATNQRKAIHVDKKMVDGSYSDDKGKKLIPLIIGAQYLIVKMIQGAIRNDIKTSGKPL
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GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Binds GTP, GDP, XTP, but not ATP. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast, especially during early development stages.
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O23702
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CTBP_ARATH
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C-terminal binding protein AN (CtBP) (Protein ANGUSTIFOLIA) (Protein DETORQUEO)
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MSKIRSSATMPHRDQPSPASPHVVTLNCIEDCALEQDSLAGVAGVEYVPLSRIADGKIESATAVLLHSLAYLPRAAQRRLRPHQLILCLGSADRAVDSTLAADLGLRLVHVDTSRAEEIADTVMALILGLLRRTHLLSRHALSASGWLGSLQPLCRGMRRCRGMVLGIVGRSVSARYLASRSLAFKMSVLYFDVPEGDEERIRPSRFPRAARRMDTLNDLLAASDVISLHCALTNDTVQILNAECLQHIKPGAFLVNTGSCQLLDDCAVKQLLIDGTIAGCALDGAEGPQWMEAWVKEMPNVLILPRSADYSEEVWMEIREKAISILHSFFLDGVIPSNTVSDEEVEESEASEEEEQSPSKHEKLAIVESTSRQQGESTLTSTEIVRREASELKESLSPGQQHVSQNTAVKPEGRRSRSGKKAKKRHSQQKYMQKTDGSSGLNEESTSRRDDIAMSDTEEVLSSSSRCASPEDSRSRKTPLEVMQESSPNQLVMSSKKFIGKSSELLKDGYVVALYAKDLSGLHVSRQRTKNGGWFLDTLSNVSKRDPAAQFIIAYRNKDTVGLRSFAAGGKLLQINRRMEFVFASHSFDVWESWSLEGSLDECRLVNCRNSSAVLDVRVEILAMVGDDGITRWID
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Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Required for cortical microtubules (MTs) arrangement that confers cell shape. Cooperatively with IPGA1, regulates negatively cortical microtubules (CMTs) organization in response to mechanical stress and modulates pavement cells morphogenesis leading to puzzle shape, probably in an AAA1/KTN1-dependent manner. Regulates the width of leaves by controlling the polar elongation of leaf cells. Involved in the regulation of trichome branching. Seems to not be able to regulate gene transcription. Regulates epidermal cell divisions and elongation in a non-cell-autonomous manner (regulated by subepidermal cells), but regulates epidermal cell polarity, shape, trichome branching and elongation in a cell-autonomous manner. Negatively regulates growth in the petiole elongation. Prevents lipid peroxidation as a result of abiotic stress response. Is involved in the SUB-dependent signaling mechanism and may act in a membrane trafficking event around the trans-Golgi network. {ECO:0000250, ECO:0000269|PubMed:10572032, ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:12079678, ECO:0000269|PubMed:17972097, ECO:0000269|PubMed:19843316, ECO:0000269|PubMed:23368817, ECO:0000269|PubMed:23672620, ECO:0000269|PubMed:35975703, ECO:0000269|PubMed:8625845, ECO:0000269|PubMed:9736998}.
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O23710
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PSB7A_ARATH
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Proteasome subunit beta type-7-A (EC 3.4.25.1) (20S proteasome beta subunit B-1) (Proteasome component FA) (Proteasome component FB) (Proteasome subunit beta type-2)
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MSQSTVDVPPKGGFSFDLCKRNDMLTQKGLKAPSFLKTGTTIVGLIFKDGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVITALTLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAESICSGIFNDLGSGSNVDICVITKGNKEYLRNYMEPNPRTYVSSKGYSFTKKTEVLLTKITPLLERVEITEVGEAMEE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
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O23712
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PSA1B_ARATH
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Proteasome subunit alpha type-1-B (20S proteasome alpha subunit F-2) (Proteasome component 2B) (Proteasome subunit alpha type-6)
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MFRNQYDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESFQESSKEDLIKDAIMAIRETLQGETLKSSLCTVSVLGVDEPFHFLDQESIQKVIDTFEKVPEEEEDAGEGEAEPEAAPGAAGTGEQGGSGDQDVAPMEI
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. May play a role in thiol biosynthesis and arsenic tolerance in association with PAF1/ARS5.
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O23715
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PSA3_ARATH
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Proteasome subunit alpha type-3 (20S proteasome alpha subunit G-1) (DiDi 17A-2a) (Proteasome component 8) (Proteasome subunit alpha type-7)
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MSSIGTGYDLSVTTFSPDGRVFQIEYAAKAVDNSGTVVGIKCKDGIVMGVEKLIASKMMLPGSNRRIHSVHRHAGMAVAGLAADGRQIVARAKSEARSYESVYGDAVPVKELSERVASYVHLCTLYWWLRPFGCGVILGGYDRDGPQLYMIEPSGISYRYFGAAIGKGKQAAKTEIEKLNLSEMTCKEGVIEVAKIIYKLHDEAKDKAFELEMSWICEESKREHQKVPDDLLEEAKTAAKTALEEMDAD
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
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O23722
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MVD1_ARATH
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Diphosphomevalonate decarboxylase MVD1, peroxisomal (EC 4.1.1.33) (Mevalonate 5-diphosphate decarboxylase 1) (AtMDD1) (AtMVD1)
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MAEEKWVVMVTAQTPTNIAVIKYWGKRDEVRILPINDSISVTLDPDHLCTLTTVAVSPSFDRDRMWLNGKEISLSGSRYQNCLREIRSRADDVEDKEKGIKIAKKDWEKLHLHIASHNNFPTAAGLASSAAGFACLVFALAKLMNVNEDPSQLSAIARQGSGSACRSLFGGFVKWNMGNKEDGSDSVAVQLVDDKHWDDLVIIIAVVSSRQKETSSTSGMRESVETSLLLQHRAKEVVPVRILQMEEAIKNRDFTSFTKLTCSDSNQFHAVCMDTSPPIFYMNDTSHRIISLVEKWNRSAGTPEIAYTFDAGPNAVMIARNRKVAVELLQGLLYCFPPKPDTDMKSYVLGDTSIVKEAGLEGELPQGIKDKIGSQDQKGEVSYFICSRPGRGPVVLQDQTQALLHPQTGLPK
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Performs the first committed step in the biosynthesis of isoprene-containing compounds such as sterols and terpenoids. Is specific for (R)-5-diphosphomevalonate (MVAPP). The catalytic efficiency with (R)-5-phosphomevalonate (MVAP) as substrate is 10000-fold lower than for MVAPP. Can complement a yeast mutant defective in MVD activity.
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O23736
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GSH1_BRAJU
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Glutamate--cysteine ligase, chloroplastic (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase)
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MALLSQAGGAYTVPSGHVSSRTGTKTVSGCVNVLRMKETYVSSYSRTLSTKSMLKRSKRGHQLIVAASPPTEEAVVATEPLTREDLIAYLASGCKSKEKWRIGTEHEKFGFEVNTLRPMKYDQIAELLNSIAERFEWEKVMEGDKIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGMGFQPKWRREDIPTMPKGRYDIMRNYMPKVGSLGLDMMLRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGFLSMRSHIWTDTDKDRTGMLPFVFDDSFGFEQYVDYALDVPMYFAYRNGKYVDCTGMTFRQFLAGKLPCLPGELPTYNDWENHLTTIFPEVRLKRYMEMRGADGGPWRRLCALPAFWVGLLYDEDVLQSVLDLTADWTPAEREMLRNKVPVTGLKTPFRDGLLKHVAEDVLKLAKDGLERRGYKEVGFLNAVTEVVRTGVTPAENLLEMYNGEWGQSVDPVFQELLY
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Participates in the detoxification process.
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O23813
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SIR_MAIZE
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Sulfite reductase [ferredoxin], chloroplastic (ZmSiR) (EC 1.8.7.1)
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MSGAIGGAEVHGFRGAAAQLPRSRVLGRPIRVAPPAAARPGGASAGSIRAVSAPAKKDASEVKRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRDVRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPYVKKDILFAQQTAENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYMIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVNKWAESPSAA
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Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth.
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O23887
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ALDO1_MAIZE
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Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase) (ZmAO-1)
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MGKEAGAAESSTVVLAVNGKRYEAAGVAPSTSLLEFLRTQTPVRGPKLGCGEGGCGACVVLVSKYDPATDEVTEFSASSCLTLLHSVDRCSVTTSEGIGNTRDGYHPVQQRLSGFHASQCGFCTPGMCMSIFSALVKADNKSDRPDPPAGFSKITTSEAEKAVSGNLCRCTGYRPIVDTCKSFASDVDLEDLGLNCFWKKGEEPAEVSRLPGYNSGAVCTFPEFLKSEIKSTMKQVNDVPIAASGDGWYHPKSIEELHRLFDSSWFDDSSVKIVASNTGSGVYKDQDLYDKYIDIKGIPELSVINKNDKAIELGSVVSISKAIEVLSDGNLVFRKIADHLNKVASPFVRNTATIGGNIMMAQRLPFESDVATVLLAAGSTVTVQVASKRLCFTLEEFLEQPPCDSRTLLLSIFIPEWGSDYVTFETFRAAPRPFGNAVSYVNSAFLARTSGSLLIEDICLAFGAYGVDHAIRAKKVEDFLKGKSLSSFVILEAIKLLKDTVSPSEGTTHHEYRVSLAVSFLFSFLSSLANSSSAPSNIDTPNGSYTHETGSNVDSPERHIKVDSNDLPIRSRQEMVFSDEYKPVGKPIKKVGAEIQASGEAVYVDDIPAPKDCLYGAFIYSTHPHAHVRSINFKSSLASQKVITVITAKDIPSGGENIGSSFLMQGEALFADPIAEFAGQNIGVVIAETQRYANMAAKQAVVEYSTENLQPPILTIEDAIQRNSYIQIPPFLAPKPVGDYNKGMAEADHKILSAEVKLESQYYFYMETQAALAIPDEDNCITIYSSTQMPELTQNLIARCLGIPFHNVRVISRRVGGGFGGKAMKATHTACACALAAFKLRRPVRMYLDRKTDMIMAGGRHPMKAKYSVGFKSDGKITALHLDLGINAGISPDVSPLMPRAIIGALKKYNWGTLEFDTKVCKTNVSSKSAMRAPGDVQGSFIAEAIIEHVASALALDTNTVRRKNLHDFESLEVFYGESAGEASTYSLVSMFDKLALSPEYQHRAAMIEQFNSSNKWKKRGISCVPATYEVNLRPTPGKVSIMNDGSIAVEVGGIEIGQGLWTKVKQMTAFGLGQLCPDGGECLLDKVRVIQADTLSLIQGGMTAGSTTSETSCETVRQSCVALVEKLNPIKESLEAKSNTVEWSALIAQASMASVNLSAQPYWTPDPSFKSYLNYGAGTSEVEVDILTGATTILRSDLVYDCGQSLNPAVDLGQIEGCFVQGIGFFTNEDYKTNSDGLVIHDGTWTYKIPTVDNIPKEFNVEMFNSAPDKKRVLSSKASGEPPLVLATSVHCAMREAIRAARKEFSVSTSPAKSAVTFQMDVPATMPVVKELCGLDVVERYLENVSAASAGPNTAKA
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In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. Involved in the biosynthesis of auxin from (indol-3-yl)acetaldehyde. Can also use indole-3-aldehyde and benzaldehyde as substrate.
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O24006
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AMP_IMPBA
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Antimicrobial peptides (IB-AMP) [Cleaved into: Basic peptide AMP3 (IB-AMP3); Basic peptide AMP1-1 (IB-AMP1-1); Basic peptide AMP1-2 (IB-AMP1-2); Basic peptide AMP1-3 (IB-AMP1-3); Basic peptide AMP2 (IB-AMP2); Basic peptide AMP4 (IB-AMP4)]
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MVQKGVVFGVLLILFICSTLTSADSKPNPTKEEEPAKKPDEVSVKSGGPEVSEDQYRHRCCAWGPGRKYCKRWCANAEEAAAAIPEASEELAQEEAPVYSEDQWGRRCCGWGPGRRYCVRWCQNAEEAAAAIPEATEKAQEAPVYSEDQWGRRCCGWGPGRRYCVRWCQNAEEAAAAVAIPEASEKAQEGPVYSEDQWGRRCCGWGPGRRYCVRWCSNAADEVATPEDVEPGQYGRRCCNWGPGRRYCKRWCHNAAEEATLKAFEEEAAREQPVYSEDQWGRRCCGWGPGRRYCRRWCQSAEEAAAFQAGEVTASLMLIMFKACPCMGPVPSV
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Plays a role in the defense of the germinating seed against microorganisms, by inhibiting the growth of a range of filamentous fungi and bacteria, especially Gram-positive bacteria. Not cytotoxic for cultured human cells and are the smallest known plant-derived antimicrobial peptides. Peptide IB-AMP4 has a higher antifungal activity than IB-AMP1.
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O24023
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NCED1_SOLLC
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9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic (LeNCED1) (SlNCED1) (EC 1.13.11.51) (Nine-cis-epoxycarotenoid dioxygenase 1)
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MATTTSHATNTWIKTKLSMPSSKEFGFASNSISLLKNQHNRQSLNINSSLQAPPILHFPKQSSNYQTPKNNTISHPKQENNNSSSSSTSKWNLVQKAAAMALDAVESALTKHELEHPLPKTADPRVQISGNFAPVPENPVCQSLPVTGKIPKCVQGVYVRNGANPLFEPTAGHHFFDGDGMVHAVQFKNGSASYACRFTETERLVQEKALGRPVFPKAIGELHGHSGIARLMLFYARGLFGLVDHSKGTGVANAGLVYFNNRLLAMSEDDLPYHVKVTPTGDLKTEGRFDFDGQLKSTMIAHPKLDPVSGELFALSYDVIQKPYLKYFRFSKNGEKSNDVEIPVEDPTMMHDFAITENFVVIPDQQVVFKMSEMIRGGSPVVYDKNKVSRFGILDKYAKDGSDLKWVEVPDCFCFHLWNAWEEAETDEIVVIGSCMTPPDSIFNECDEGLKSVLSEIRLNLKTGKSTRKSIIENPDEQVNLEAGMVNRNKLGRKTEYAYLAIAEPWPKVSGFAKVNLFTGEVEKFIYGDNKYGGEPLFLPRDPNSKEEDDGYILAFVHDEKEWKSELQIVNAMSLKLEATVKLPSRVPYGFHGTFINANDLANQA
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Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid (ABA) biosynthesis from carotenoids. Required for ABA accumulation upon drought (Ref.2). Required for ABA-mediated regulation of anther/pollen development, including metabolism, cell wall modification and transcription level. Positive regulator of fruit ripening involved in the biosynthesis of abscisic acid (ABA) initiates ABA biosynthesis at the onset of fruit ripening. Modulates the degree of pigmentation and carotenoid composition as well as pectin catabolism during ripening and may regulate the ethylene production and action in climacteric tomato fruit.
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O24144
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CAMT1_TOBAC
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Caffeoyl-CoA O-methyltransferase 1 (EC 2.1.1.104) (Trans-caffeoyl-CoA 3-O-methyltransferase 1) (CCoAMT-1) (CCoAOMT-1)
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MATNGRHQEVGHKSLLQSDALYQYILETSVYPREPEPMKELREITAKHPWNLMTTSADEGQFLSMLIKLINAKNTMEIGVFTGYSLLATAMALPDDGKILAMDINRENYEIGLPVIEKAGLAHKIEFKEGPALPVLDQMIEDGKYHGSYDFIFVDADKDNYLNYHKRLIDLVKIGGLIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADSRIEICQLPVGDGITLCRRIS
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Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.
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O24146
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4CL2_TOBAC
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4-coumarate--CoA ligase 2 (4CL 2) (Nt4CL-19) (Nt4CL-2) (EC 6.2.1.12) (4-coumaroyl-CoA synthase 2) (Caffeate--CoA ligase) (EC 6.2.1.-) (Cinnamate--CoA ligase) (EC 6.2.1.-) (Ferulate--CoA ligase) (EC 6.2.1.34)
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MEKDTKQVDIIFRSKLPDIYIPNHLPLHSYCFENISEFSSRPCLINGANKQIYTYADVELNSRKVAAGLHKQGIQPKDTIMILLPNSPEFVFAFIGASYLGAISTMANPLFTPAEVVKQAKASSAKIIVTQACHVNKVKDYAFENDVKIICIDSAPEGCLHFSVLTQANEHDIPEVEIQPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYIHSEDVMLCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVSFLELIQRYKVTIGPFVPPIVLAIAKSPMVDDYDLSSVRTVMSGAAPLGKELEDTVRAKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFEIKSGACGTVVRNAEMKIVDPKTGNSLPRNQSGEICIRGDQIMKGYLNDPEATARTIDKEGWLYTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSTITEDEVKDFISKQVIFYKRIKRVFFVDAIPKSPSGKILRKDLRAKLAAGLPN
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Major enzyme of the phenylpropanoid pathway that mediates the production of several precursors for numerous metabolites and regulates carbon flow. Catalyzes the formation of CoA thioesters using 4-coumarate, ferulate, caffeate, and cinnamate as substrates. Follows a two-step reaction mechanism, wherein a (hydroxy)cinnamate substrate first undergoes adenylation by ATP leading to an acyl-AMP, followed by a thioesterification in the presence of CoA to yield the final (hydroxy)cinnamoyl-CoA product. Almost inactive toward sinapate.
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O24164
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PPOM_TOBAC
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Protoporphyrinogen oxidase, mitochondrial (EC 1.3.3.4) (PX-2) (Protoporphyrinogen IX oxidase isozyme II) (PPO II) (PPX II)
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MAPSAGEDKHSSAKRVAVIGAGVSGLAAAYKLKIHGLNVTVFEAEGKAGGKLRSVSQDGLIWDEGANTMTESEGDVTFLIDSLGLREKQQFPLSQNKRYIARNGTPVLLPSNPIDLIKSNFLSTGSKLQMLLEPILWKNKKLSQVSDSHESVSGFFQRHFGKEVVDYLIDPFVAGTCGGDPDSLSMHHSFPELWNLEKRFGSVILGAIRSKLSPKNEKKQGPPKTSANKKRQRGSFSFLGGMQTLTDAICKDLREDELRLNSRVLELSCSCTEDSAIDSWSIISASPHKRQSEEESFDAVIMTAPLCDVKSMKIAKRGNPFLLNFIPEVDYVPLSVVITTFKRENVKYPLEGFGVLVPSKEQQHGLKTLGTLFSSMMFPDRAPNNVYLYTTFVGGSRNRELAKASRTELKEIVTSDLKQLLGAEGEPTYVNHLYWSKAFPLYGHNYDSVLDAIDKMEKNLPGLFYAGNHRGGLSVGKALSSGCNAADLVISYLESVSTDSKRHC
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Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
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O24174
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BADH1_ORYSJ
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Betaine aldehyde dehydrogenase 1 (OsBADH1) (EC 1.2.1.8)
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MAAPSAIPRRGLFIGGGWREPSLGRRLPVVNPATEATIGDIPAATAEDVELAVSAARDAFGRDGGRHWSRAPGAVRAKYLKAIAAKIKDKKSYLALLETLDSGKPLDEAAGDMEDVAACFEYYADLAEALDGKQRAPISLPMENFESYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASLTCLELGGICAEIGLPPGVLNIITGLGTEAGAPLASHPHVDKIAFTGSTETGKRIMITASQMVKPVSLELGGKSPLIVFDDVDIDKAVEWAMFGCFANAGQVCSATSRLLLHEKIAKRFLDRLVAWAKSIKISDPLEEGCRLGSVVSEGQYQKIMKFISTARCEGATILYGGARPQHLKRGFFIEPTIITNVSTSMQIWREEVFGPVICVKEFRTEREAVELANDTHYGLAGAVISNDLERCERISKAIQSGIVWINCSQPCFVQAPWGGNKRSGFGRELGQWGLDNYLSVKQVTKYCSDEPYGWYRPPSKL
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Dehydrogenase that can use N-acetyl-gamma-aminobutyraldehyde (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4-aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N-trimethylaminobutyraldehyde (TMAB-ald) and 3-N-trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the oxidation of GAB-ald more efficiently than Bet-ald. May convert acetaldehyde into acetate, thus facilitating the production of acetyl-CoA in peroxisomes under anaerobic conditions.
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O24370
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LOX21_SOLTU
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Linoleate 13S-lipoxygenase 2-1, chloroplastic (EC 1.13.11.12) (Lipoxygenase 2-1)
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MLKPQLQQSSQSTKALIPSWNTNPLFLASFPINILNKNFRLKKKNNFRVHHNYNGASTTKAVLSSTEKATGVKAVVTVQKQVNLNLSRGLDDIGDLLGKSLLLWIVAAELDHKTGIEKPGIRAYAHRGRDVDGDTHYEADFVIPQDFGEVGAILIENEHHKEMYVKNIVIDGFVHGKVEITCNSWVHSKFDNPDKRIFFTNKSYLPSQTPSGVSRLREEELVTLRGDGIGERKVFERIYDYDVYNDLGEADSNNDDAKRPVLGGKELPYPRRCKTGRPRSKKDPLSETRSTFVYVPRDEAFSEVKSVAFSGNTVYSVLHAVVPALESVVTDPNLGFPHFPAIDSLFNVGVDLPGLGDKKSGLFNVVPRLIKAISDTRKDVLLFESPQLVQRDKFSWFRDVEFARQTLAGLNPYSIRLVTEWPLRSKLDPKVYGPPESEITKELIEKEIGNYMTVEQAVQQKKLFILDYHDLLLPYVNKVNELKGSMLYGSRTIFFLTPQGTLKPLAIELTRPPVDDKPQWKEVYSPNDWNATGAWLWKLAKAHVLSHDSGYHQLVSHWLRTHCCTEPYIIASNRQLSAMHPIYRLLHPHFRYTMEINALAREALINANGVIESSFFPGKYAIELSSIAYGAEWRFDQEALPQNLISRGLAVEDPNEPHGLKLAIEDYPFANDGLVLWDILKQWVTNYVNHYYPQTNLIESDKELQAWWSEIKNVGHGDKRDEPWWPELKTPNDLIGIITTIVWVTSGHHAAVNFGQYSYAGYFPNRPTVARSKMPTEDPTAEEWEWFMNKPEEALLRCFPSQIQATKVMAILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEVFSGKLKELEGIIDARNNDSKLSNRNGAGVMPYELLKPYSEPGVTGKGVPYSISI
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Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids.
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O24371
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LOX31_SOLTU
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Linoleate 13S-lipoxygenase 3-1, chloroplastic (EC 1.13.11.12)
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MALAKEIMGISLLEKSSSFMNSSSMALFNPNNYHKENHLWFNQQFQGRRNLSRRKAFRQSTMAAISENLIKVVPEKAVRFKVRAVVTVRNKNKEDLKETIVKHLDAFTDKIGRNVTLELISTDMDPNTKGPKKSNQAVLKDWSKKSNLKTERVNYTAEFIVDSNFGNPGAITVTNKHQQEFFLESITIEGFACGPVHFPCNSWVQPKKDHPGKRIFFSNQPYLPDETPAGLKSLRERELRDLRGDGKGVRKLSDRIYDYDIYNDLGNPDKGIDFARPKLGGDDNVPYPRRCRSGRVPTDTDISAESRVEKPNPTYVPRDEQFEESKMNTFSTSRLKAVLHNLIPSLMASISSNNHDFKGFSDIDNLYSKGLLLKLGLQDEVLKKLPLPKVVSSIKEGDLLKYDTPKILSKDKFAWLRDDEFARQAIAGVNPVSIEKLQFFPPVSKLDPEIYGPQESALKEEHILGHLNGMTVQEALDANKLFIVDHHDVYLPFLDRINALDGRKAYATRTIFFLSDVGTLKPIAIELSLPQTGPSSRSKRVVTPPVCATGNWTWQIAKAHVCANDAGVHQLVNHWLRTHASLEPFILAAHRQLSAMHPIYKLLDPHMRYTLEINGLARQSLINADGVIEACFTPGRYCMEISAAAYKNWRFDLEGLPADLIRRGMAVPDSTQPHGLKLLIEDYPYAADGLMIWGAIESWVRDYVNHYYPSSAQVCSDRELQAWYAETINVGHVDLRNEEWWPTLATPEDLISILTTLIWLASAQHAALNFGQYPYGGYVPNRPPLMRRLIPDENDPEYAVFLADPQKYFFSALPSLLQATKFMAVVDTLSTHSPDEEYLGERHQPSTWTGDAEIVEAFYKFSAEIGRIEKEIDERNANTKLKNRCGAGVLPYELLAPSSGPGVTCRGVPNSVSI
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Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids.
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O24379
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LOX12_SOLTU
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Linoleate 9S-lipoxygenase 2 (EC 1.13.11.58) (Lipoxygenase 1-2)
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MIGQITSGLFGGPDDSKKLKGTVVMMNKNALDFTDLAGSLTDKAFEFLGQTVSFQLISSVQGDPTNGLQGKHSNPAYLENSLFTLTPLTAGSETAFGVTFDWNEEFGVPGAFIIKNTHINEFFLKSLTLEDVPNHGKVHFVCNSWVYPSFRYKSDRIFFVNQPYLPSKTPELLRKYRENELLTLRGDGTGKREAWDRIYDYDIYNDLGNPDEGKENVRTTLGGSAEYPYPRRGRTGRPPTRTDPKSESRIPLILSLDIYVPRDERFGHLKMSDFLTYALKSIVQFILPELHALFDGTPNEFDSFEDVLRLYEGGIKLPQGPLFKALTAAIPLEMIRELLRTDGEGILRFPTPLVIKDSKTAWRTDEEFAREMLAGVNPVIISRLQEFPPKSKLDPEAYGNQNSTITAEHIEDKLDGLTVDEAMNNNKLFILNHHDVLIPYLRRINTTTTKTYASRTLLFLQDNGSLKPLAIELSLPHPDGDQFGVTSKVYTPSDQGVESSIWQLAKAYVAVNDSGVHQLISHWLNTHAVIEPFVIATNRQLSVLHPIHKLLYPHFRDTMNINAMARQILINAGGVLESTVFQSKFAMEMSAVVYKDWVFPDQALPADLVKRGVAVEDSSSPHGVRLLIEDYPYAVDGLEIWSAIKSWVSDYCSFYYGSDEEILKDNELQAWWKELREVGHGDKKNEPWWPEMERPQELIDSCTTIIWIASALHAAVNFGQYPYAGYLPNRPTVSRRFMPEPGTPEYEELKKNPDKAFLKTITAQLQTLLGVSLIEILSRHTTDEIYLGQRESPEWTKDKEPLAAFDKFGKKLTDIEKQIIQRNGDNILTNRSGPVNAPYTLLFPTSEGGLTGKGIPNSVSI
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Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linoleic acid is the preferred substrate, but is also active with linolenic and arachidonic acids. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8702864}.
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O24407
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IAA16_ARATH
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Auxin-responsive protein IAA16 (Indoleacetic acid-induced protein 16)
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MINFEATELRLGLPGGNHGGEMAGKNNGKRGFSETVDLKLNLSSTAMDSVSKVDLENMKEKVVKPPAKAQVVGWPPVRSFRKNVMSGQKPTTGDATEGNDKTSGSSGATSSASACATVAYVKVSMDGAPYLRKIDLKLYKTYQDLSNALSKMFSSFTIGNYGPQGMKDFMNESKLIDLLNGSDYVPTYEDKDGDWMLVGDVPWEMFVDSCKRIRIMKGSEAIGLAPRALEKCKNRS
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Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
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O24408
|
IAA18_ARATH
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Auxin-responsive protein IAA18 (Indoleacetic acid-induced protein 18)
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MEGYSRNGEISPKLLDLMIPQERRNWFHDEKNSVFKTEEKKLELKLGPPGEEDDDESMIRHMKKEPKDKSILSLAGKYFSPSSTKTTSHKRTAPGPVVGWPPVRSFRKNLASGSSSKLGNDSTTSNGVTLKNQKCDAAAKTTEPKRQGGMFVKINMYGVPIGRKVDLSAHNSYEQLSFTVDKLFRGLLAAQRDFPSSIEDEKPITGLLDGNGEYTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKTSEISSALTYGNGKQEKMRR
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Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
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O24409
|
IAA19_ARATH
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Auxin-responsive protein IAA19 (Indoleacetic acid-induced protein 19) (Protein MASSUGU 2)
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MEKEGLGLEITELRLGLPGRDVAEKMMKKRAFTEMNMTSSGSNSDQCESGVVSSGGDAEKVNDSPAAKSQVVGWPPVCSYRKKNSCKEASTTKVGLGYVKVSMDGVPYLRKMDLGSSQGYDDLAFALDKLFGFRGIGVALKDGDNCEYVTIYEDKDGDWMLAGDVPWGMFLESCKRLRIMKRSDATGFGLQPRGVDE
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Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
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O24410
|
IAA20_ARATH
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Auxin-responsive protein IAA20 (Indoleacetic acid-induced protein 20)
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MGRGRSSSSSSIESSSKSNPFGASSSTRNLSTDLRLGLSFGTSSGTQYFNGGYGYSVAAPAVEDAEYVAAVEEEEENECNSVGSFYVKVNMEGVPIGRKIDLMSLNGYRDLIRTLDFMFNASILWAEEEDMCNEKSHVLTYADKEGDWMMVGDVPWEMFLSTVRRLKISRANYHY
|
Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
|
O24412
|
PSD7A_ARATH
|
26S proteasome non-ATPase regulatory subunit 7 homolog A (26S proteasome regulatory subunit RPN8a) (AtRPN8a) (Protein ASYMMETRIC LEAVES ENHANCER 3) (Protein MOV34) (AtMOV34)
|
MDVIKTQQISARTIEKVVVHPLVLLSIVDHYNRVAKDSSKRVVGVLLGSSSRGVVDVTNSYAVPFEEDDKDPSIWFLDHNYHESMFHMFKRINAKEHVVGWYSTGPKLRENDLDVHALFNGYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVSTEIAAHEVEEIGVEHLLRDVKDTTISTLATEVTAKLTALKGLDARLREIRSYLDLVIEGKLPLNHEILYHLQDVFNLLPNLNVNELVKAFSVKTNDMMLVIYLSSLIRSVIALHNLINNKLLNKEHEKAEDSKPVAIPATS
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Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Required for innate immunity. {ECO:0000250, ECO:0000269|PubMed:22577987}.
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O24454
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UBP3_ARATH
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Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.4.19.12) (Deubiquitinating enzyme 3) (AtUBP3) (Ubiquitin thioesterase 3) (Ubiquitin-specific-processing protease 3)
|
MGAAGSKLEKALGDQFPEGERYFGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEENLMTCLADLFSQISSQKKKTGVIAPKRFVQRLKKQNELFRSYMHQDAHEFLNYLLNEVVDILEKEAKATKTEHETSSSSSPEKIANGLKVPQANGVVHKEPIVTWVHNIFQGILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPYADVEYSLFAVVVHVGSGPNHGHYVSLVKSHNHWLFFDDENVEMIEESAVQTFFGSSQEYSSNTDHGYILFYESLGPTK
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Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Required for the correct development of pollen.
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O24456
|
GBLPA_ARATH
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Small ribosomal subunit protein RACK1z (Guanine nucleotide-binding protein subunit beta-like protein A) (Receptor for activated C kinase 1A) (WD-40 repeat auxin-dependent protein ARCA)
|
MAEGLVLKGTMRAHTDMVTAIATPIDNADIIVSASRDKSIILWKLTKDDKAYGVAQRRLTGHSHFVEDVVLSSDGQFALSGSWDGELRLWDLAAGVSTRRFVGHTKDVLSVAFSLDNRQIVSASRDRTIKLWNTLGECKYTISEGGEGHRDWVSCVRFSPNTLQPTIVSASWDKTVKVWNLSNCKLRSTLAGHTGYVSTVAVSPDGSLCASGGKDGVVLLWDLAEGKKLYSLEANSVIHALCFSPNRYWLCAATEHGIKIWDLESKSIVEDLKVDLKAEAEKADNSGPAATKRKVIYCTSLNWSADGSTLFSGYTDGVIRVWGIGRY
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Major component of the RACK1 regulatory proteins that play a role in multiple signal transduction pathways. Involved in multiple hormone responses and developmental processes. MAPK cascade scaffolding protein involved in the protease IV and ArgC signaling pathway but not the flg22 pathway.
|
O24495
|
GLO2M_ARATH
|
Hydroxyacylglutathione hydrolase 1, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II)
|
MPVISKASSTTTNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKIELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEALRRIQRARDRF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
O24496
|
GLO2C_ARATH
|
Hydroxyacylglutathione hydrolase cytoplasmic (EC 3.1.2.6) (Glyoxalase II) (Glx II)
|
MKIFHVPCLQDNYSYLIIDESTGDAAVVDPVDPEKVIASAEKHQAKIKFVLTTHHHWDHAGGNEKIKQLVPDIKVYGGSLDKVKGCTDAVDNGDKLTLGQDINILALHTPCHTKGHISYYVNGKEGENPAVFTGDTLFVAGCGKFFEGTAEQMYQSLCVTLAALPKPTQVYCGHEYTVKNLEFALTVEPNNGKIQQKLAWARQQRQADLPTIPSTLEEELETNPFMRVDKPEIQEKLGCKSPIDTMREVRNKKDQWRG
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
O24527
|
SIK1_ARATH
|
Serine/threonine-protein kinase 1 (EC 2.7.11.1)
|
MDHNSPKSRRSRKPEPKPDIYSTFVVHSDSDSDQGRDRDKRKAKPEEDENVDLYATMVYKGDSDGEGEEDDDDDSMLPPLLKRLPKDFGGGASLDYDDDDGDESGDFGTMIVKTDRSSHSKKNSPYSSKPRMGVSPRRRARGGDEESSDEEDEEEDDDDDDGDYGTFVVKSKDKKGKKKDKEIDMTTMGRAVASMQKSNFGGKTRKLDPSSSSSKLHGEDNRKMQQQNSKMSTTSLPDSITREDPTTKYEFLNELGKGSYGSVYKARDLKTSEIVAVKVISLTEGEEGYEEIRGEIEMLQQCNHPNVVRYLGSYQGEDYLWIVMEYCGGGSVADLMNVTEEALEEYQIAYICREALKGLAYLHSIYKVHRDIKGGNILLTEQGEVKLGDFGVAAQLTRTMSKRNTFIGTPHWMAPEVIQENRYDGKVDVWALGVSAIEMAEGLPPRSSVHPMRVLFMISIEPAPMLEDKEKWSLVFHDFVAKCLTKEPRLRPTAAEMLKHKFVERCKTGASAMSPKIEKSRQIRATMALQAQSVVAPSLEDTSTLGPKSSEELGITVPSKPPQNSTEAPLTSTLNRQHITGNTVLAGEGGDFGTMIVHGEDETEESDSRSQLVREKESSSSQFEGVPREFPGEELPDSWIHDKKKPPAIDLPVEASISQSMQASSSHEHRTKLHNIAGTQMEGGSDASGSTLKNETVGRKAFALQDKLWSIYAAGNTVPIPFLRATDISPIALLSENMIGGMQQDGNGTVAVEALQELFTSSDPQSKKGRRGQNEMPLPPSVYQRLTTSSSLMNLAQVLAYHRACYEEMPLQELQATQEQQTIQNLCDTLRTILRL
|
Serine/threonine-protein kinase. Regulates organ size in coordination with MOB1A by modulating cell proliferation and cell expansion, possibly by facilitating cell cycle exit. Positive regulator of the pathogen-associated molecular pattern (PAMP, e.g. flg22)-triggered immunity (PTI) signaling by stabilizing BIK1 and activating RBOHD by phosphorylation to promote the extracellular reactive oxygen species (ROS) burst involved in defense responses to bacterial infection.
|
O24585
|
CRI4_MAIZE
|
Putative receptor protein kinase CRINKLY4 (EC 2.7.11.1)
|
MDHVPALVLAGCCFLALLPGWACGLGSMSSIAVSYGEDGPVFCGLNSDGSHLVACFGADASVLYGAPPNIPFLGLTAGDGFVCGLLLDTRQPYCWGSNSYVKSGVPQPMVEGARYSELSAGDNHLCALRAAQDGGRGSSAATSLIDCWGYNMTATHAVDEAVSTVSAGSVFNCGLFARNRTVFCWGDETVSGVVGLAPRDLHFQSIGAGGYHVCGVLENAQVFCWGRSLEMQQVVPSSAIGDGDVNIVPMDAMSTVVGGRFHACGIRSLDHQVACWGFTLHNSTSPPKGLKMYALVAGDYFTCGVPAETSLMPRCWGNSGPLALPMAVPPGICVPTACSHGYYEYVNHGEVGSIKVCKPANSRLCLPCSTGCPEGLYESSPCNATADRVCQFDCLKCVTDECLSFCLSQKRTKSRKLMAFQMRIFVAEIVFAVVLVLSVSVTTCLYVRHKLRHCQCSNRELRLAKSTAYSFRKDNMKIQPDMEDLKIRRAQEFSYEELEQATGGFSEDSQVGKGSFSCVFKGILRDGTVVAVKRAIKASDVKKSSKEFHNELDLLSRLNHAHLLNLLGYCEDGSERLLVYEFMAHGSLYQHLHGKDPNLKKRLNWARRVTIAVQAARGIEYLHGYACPPVIHRDIKSSNILIDEDHNARVADFGLSILGPADSGTPLSELPAGTLGYLDPEYYRLHYLTTKSDVYSFGVVLLEILSGRKAIDMQFEEGNIVEWAVPLIKAGDIFAILDPVLSPPSDLEALKKIASVACKCVRMRGKDRPSMDKVTTALEHALALLMGSPCIEQPILPTEVVLGSSRMHKVSQMSSNHSCSENELADGEDQGIGYRAPSWITFPSVTSSQRRKSSASEADIVGRRATDGRNVGSSIGDGLRSLEEEIAPASPQENLYLQHNF
|
Putative receptor protein kinase. Could play a role in a differentiation signal. The CRINKLY4 (CR4) mutation affects leaf epidermis differentiation such that cell size and morphology are altered, and surface functions are compromised, allowing graft-like fusions between organs.
|
O24591
|
HDT1_MAIZE
|
Histone deacetylase HDT1 (Histone deacetylase 2a) (HD2a) (Nucleolar histone deacetylase HD2-p39) (Zm-HD2a)
|
MEFWGLEVKPGSTVKCEPGYGFVLHLSQAALGESKKSDNALMYVKIDDQKLAIGTLSVDKNPHIQFDLIFDKEFELSHTSKTTSVFFTGYKVEQPFEEDEMDLDSEDEDEELNVPVVKENGKADEKKQKSQEKAVAAPSKSSPDSKKSKDDDDSDEDETDDSDEDETDDSDEGLSSEEGDDDSSDEDDTSDDEEEDTPTPKKPEVGKKRPAESSVLKTPLSDKKAKVATPSSQKTGGKKGAAVHVATPHPAKGKTIVNNDKSVKSPKSAPKSGGSVPCKPCSKSFISETALQAHSRAKMGASESQVQ
|
Mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Able to deacetylate all 4 core histones.
|
O24592
|
NCED1_MAIZE
|
9-cis-epoxycarotenoid dioxygenase 1, chloroplastic (EC 1.13.11.51) (Protein VIVIPAROUS14) (VP-14) (VP14)
|
MQGLAPPTSVSIHRHLPARSRARASNSVRFSPRAVSSVPPAECLQAPFHKPVADLPAPSRKPAAIAVPGHAAAPRKAEGGKKQLNLFQRAAAAALDAFEEGFVANVLERPHGLPSTADPAVQIAGNFAPVGERPPVHELPVSGRIPPFIDGVYARNGANPCFDPVAGHHLFDGDGMVHALRIRNGAAESYACRFTETARLRQERAIGRPVFPKAIGELHGHSGIARLALFYARAACGLVDPSAGTGVANAGLVYFNGRLLAMSEDDLPYHVRVADDGDLETVGRYDFDGQLGCAMIAHPKLDPATGELHALSYDVIKRPYLKYFYFRPDGTKSDDVEIPLEQPTMIHDFAITENLVVVPDHQVVFKLQEMLRGGSPVVLDKEKTSRFGVLPKHAADASEMAWVDVPDCFCFHLWNAWEDEATGEVVVIGSCMTPADSIFNESDERLESVLTEIRLDARTGRSTRRAVLPPSQQVNLEVGMVNRNLLGRETRYAYLAVAEPWPKVSGFAKVDLSTGELTKFEYGEGRFGGEPCFVPMDPAAAHPRGEDDGYVLTFVHDERAGTSELLVVNAADMRLEATVQLPSRVPFGFHGTFITGQELEAQAA
|
Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.
|
O24606
|
EIN3_ARATH
|
Protein ETHYLENE INSENSITIVE 3
|
MMFNEMGMCGNMDFFSSGSLGEVDFCPVPQAEPDSIVEDDYTDDEIDVDELERRMWRDKMRLKRLKEQDKGKEGVDAAKQRQSQEQARRKKMSRAQDGILKYMLKMMEVCKAQGFVYGIIPENGKPVTGASDNLREWWKDKVRFDRNGPAAITKYQAENNIPGIHEGNNPIGPTPHTLQELQDTTLGSLLSALMQHCDPPQRRFPLEKGVPPPWWPNGKEDWWPQLGLPKDQGPAPYKKPHDLKKAWKVGVLTAVIKHMFPDIAKIRKLVRQSKCLQDKMTAKESATWLAIINQEESLARELYPESCPPLSLSGGSCSLLMNDCSQYDVEGFEKESHYEVEELKPEKVMNSSNFGMVAKMHDFPVKEEVPAGNSEFMRKRKPNRDLNTIMDRTVFTCENLGCAHSEISRGFLDRNSRDNHQLACPHRDSRLPYGAAPSRFHVNEVKPVVGFPQPRPVNSVAQPIDLTGIVPEDGQKMISELMSMYDRNVQSNQTSMVMENQSVSLLQPTVHNHQEHLQFPGNMVEGSFFEDLNIPNRANNNNSSNNQTFFQGNNNNNNVFKFDTADHNNFEAAHNNNNNSSGNRFQLVFDSTPFDMASFDYRDDMSMPGVVGTMDGMQQKQQDVSIWF
|
Transcription factor acting as a positive regulator in the ethylene response pathway, by promoting histone acetylation in an ENAP1-dependent manner, thus accelerating the expression of ethylene-responsive genes. Binds DNA. Is required for ethylene responsiveness in adult plant tissues. Binds a primary ethylene response element present in the ETHYLENE-RESPONSE-FACTOR1 promoter with consequence to activate the transcription of this gene.
|
O24610
|
CNDD3_ARATH
|
Condensin-2 complex subunit CAP-D3 (Protein CHROMOSOME-ASSOCIATED POLYPEPTIDE D-3) (AtCap-D3)
|
MDEELLLTRILAGIEGGDDESDYHELVTDLKSLLDTDDDEILNRFYGSLSSMASSFLRCISAAMDSPVESGRLAILASDAYLSLLLSTNCPVFTFFSPIAFLSLLGSIRRYLKRRDDSAGQGSNSQREKGNKKKRGRGKRNLGYEDGEETEEGGFDAKLMFIVLEKLGSVLSFVHLDRFPDSLKSLVQTVSEIPLLALEHSGVLNYDRLMEMCGKILGGVLNSDHGDMALTAAEISKSLTPLLLMGKHQARSFALGFVSRKLMSLAKDNPELKKVVSNLPKFLVHKAPEKAEPRGFAVEAVLEIVKAMEVEGQSEFVDFVMKMCQGKSNFRVLAVDIIPLLISSLGNPLGDISSENGLKDSWGLGCIDALVQRCSDTSALIRARALSNLAQVVEFLSGDERSRSILKQALGFNGETSEGKGAVTDLLKKRCVDEKAAVRRAALLLVTKLTSLMGGCFDGSILKTMGTSCSDPLISIRKAAVSAISEAFRICTDEIVTTEWLHSVPRMIMDNETSIQEECENVFHELVLERILRAGNVLSPDSASLPNNRNTTSKDLDRDIEALFPEGVLVLLRELCNSEVSPWVTKICGSLGKKKRLKPRVALALQCIIKESESLWLSRSMPINRWTAPAGAWFLLSEVSVYLSKSVEWEFLHHHWQLLDKNDVQGLDEQGDEQGVECNSSTWAGDRVCLLQTISNVSLQLPAEPAADLADNLLKKIENFNLHSAEVDAHVKALKTLCKKKASTSEEADMLVKKWVEQVSLKASKVTEKYIEGVSSHNHSFVTPATLGSRRSKRLDTVSKKLSKAVTAVYTIGSCVIIYPSADTTKIVPFLHTVITSGNSDSKLKNKLPQANVCLKQKAPLLYSQSWLTMAKMCLADGKLAKRYLPLFAQELEKSDCAALRNNLVVAMTDFCVHYTAMIECYIPKITKRLRDPCEVVRRQTFILLSRLLQRDYVKWRGVLFLRFLLSLVDESEKIRRLADFLFGSILKVKAPLLAYNSFVEAIYVLNDCHAHTGHSNPDSKQSRTKDQVFSIRGNDERARSKRMQIYVTLLKQMAPEHLLATFAKLCAEILAAASDGMLNIEDVTGQSVLQDAFQILACKEIRLSVSRGASSETADIEEEGGDAATAKGRAITHAVRKGLIQNTIPIFIELKRLLESKNSPLTGSLMDCLRVLLKDYKNEIEEMLVADKQLQKELVYDMQKHEAAKARSMANQGVACGTSHRNGEPEASAASEENVRDSGLESRVVSAAADVVAAKAARSVLREVNGGAATPPLSAMSVPKLRSSRGVSQSGRPSADVLESLRRRPTFMSDDES
|
Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis (By similarity). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids (By similarity). Required for plant vigor, fertility, chromatin condensation and sister chromatid cohesion both during mitosis and meiosis. Necessary to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions of gametogenesis, especially to prevent interchromosome connections at metaphase I. Seems also involved in crossover formation during meiotic prophase I. Prevents centromeric and pericentromeric heterochromatin repeats association.
|
O24617
|
MSH2_ARATH
|
DNA mismatch repair protein MSH2 (AtMSH2) (MutS protein homolog 2)
|
MEGNFEEQNKLPELKLDAKQAQGFLSFYKTLPNDTRAVRFFDRKDYYTAHGENSVFIAKTYYHTTTALRQLGSGSNALSSVSISRNMFETIARDLLLERNDHTVELYEGSGSNWRLVKTGSPGNIGSFEDVLFANNEMQDTPVVVSIFPSFHDGRCVIGMAYVDLTRRVLGLAEFLDDSRFTNLESSLIALGAKECIFPAESGKSNECKSLYDSLERCAVMITERKKHEFKGRDLDSDLKRLVKGNIEPVRDLVSGFDLATPALGALLSFSELLSNEDNYGNFTIRRYDIGGFMRLDSAAMRALNVMESKTDANKNFSLFGLMNRTCTAGMGKRLLHMWLKQPLVDLNEIKTRLDIVQCFVEEAGLRQDLRQHLKRISDVERLLRSLERRRGGLQHIIKLYQSTIRLPFIKTAMQQYTGEFASLISERYLKKLEALSDQDHLGKFIDLVECSVDLDQLENGEYMISSSYDTKLASLKDQKELLEQQIHELHKKTAIELDLQVDKALKLDKAAQFGHVFRITKKEEPKIRKKLTTQFIVLETRKDGVKFTNTKLKKLGDQYQSVVDDYRSCQKELVDRVVETVTSFSEVFEDLAGLLSEMDVLLSFADLAASCPTPYCRPEITSSDAGDIVLEGSRHPCVEAQDWVNFIPNDCRLMRGKSWFQIVTGPNMGGKSTFIRQVGVIVLMAQVGSFVPCDKASISIRDCIFARVGAGDCQLRGVSTFMQEMLETASILKGASDKSLIIIDELGRGTSTYDGFGLAWAICEHLVQVKRAPTLFATHFHELTALAQANSEVSGNTVGVANFHVSAHIDTESRKLTMLYKVEPGACDQSFGIHVAEFANFPESVVALAREKAAELEDFSPSSMIINNEESGKRKSREDDPDEVSRGAERAHKFLKEFAAIPLDKMELKDSLQRVREMKDELEKDAADCHWLRQFL
|
Component of the post-replicative DNA mismatch repair system (MMR). Forms three different heterodimers: MutS alpha (MSH2-MSH6 heterodimer), MutS beta (MSH2-MSH3 heterodimer) and MutS gamma (MSH2-MSH7 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. MutS alpha and MutS beta recognize single base mismatches and trinucleotide insertion-deletion loops (IDL) in the DNA. MutS gamma recognizes specifically the T/G single base mismatch. Plays a role in DNA homologous recombination repair and has a broad range of anti-recombination effects. Can suppress recombination between divergent direct repeats in somatic cells and possesses an anti-recombination meiotic effect. Is involved in a UV-B-induced DNA damage response pathway.
|
O24621
|
SIGC_ARATH
|
RNA polymerase sigma factor sigC (Sigma factor C) (Sigma-C) (RNA polymerase sigma factor sig3) (Atsig3) (Sigma factor 3)
|
MASFNSFPIPKQIVGSSSSSSSSTSRPRILVRSSLTSSMTSTNSMLVFVHPHPLIKHWLSLLRSDQTSFPIFVRIPMTSVVATRWSFLSSVKEESRIYQNDSLKACGCASVSPYTAQNNVYVELKDPKENIGVGSAERSYSSRSMLQYNLLAKNLLALEETFVALDSVRMERDIMLQMGKLGAAELFKTCLSRYRGSSITSCLSDTTELVDTTPNQQVFVSSRRKVKKKARRSSVTAENGDQSSLPIGLRTTWNNIDVPRVRRPPKYRKKRERISRNETEMSTGVKIVADMERIRTQLEEESGKVASLSCWAAAAGMNEKLLMRNLHYGWYCRDELVKSTRSLVLFLARNYRGLGIAHEDLIQAGYVGVLQGAERFDHTRGYKFSTYVQYWIRKSMSTMVSRHARGVHIPSSIIRTINHIQKARKTLKTSHGIKYAADEEIAKLTGHSVKKIRAANQCLKVVGSIDKKVGDCFTTKFLEFTPDTTMESPEEAVMRQSARRDIHDLLEGLEPREKQVMVLRYGLQDYRPKSLEEIGKLLKVSKEWIRKIERRAMAKLRDQPNAEDLRYYLNQ
|
Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released.
|
O24629
|
SIGA_ARATH
|
RNA polymerase sigma factor sigA (Sigma factor A) (Sigma-A) (RNA polymerase sigma factor sig1) (Atsig1) (Sigma factor 1) (RNA polymerase sigma factor sig2) (Atsig2) (Sigma factor 2) (RNA polymerase sigma factor sigB) (Sigma factor B) (Sigma-B)
|
MATAAVIGLNTGKRLLSSSFYHSDVTEKFLSVNDHCSSQYHIASTKSGITAKKASNYSPSFPSSNRHTQSAKALKESVDVASTEKPWLPNGTDKELEEECYDDDDLISHSVEAILLLQKSMLEKSWNLSFEKAVSSEYPGKGTIRKKKIPVITCSGISARQRRIGAKKKTNMTHVKAVSDVSSGKQVRGYVKGVISEDVLSHVEVVRLSKKIKSGLRLDDHKSRLKDRLGCEPSDEQLAVSLKISRAELQAWLMECHLAREKLAMSNVRLVMSIAQRYDNLGAEMSDLVQGGLIGLLRGIEKFDSSKGFRISTYVYWWIRQGVSRALVDNSRTLRLPTHLHERLGLIRNAKLRLQEKGITPSIDRIAESLNMSQKKVRNATEAVSKVFSLDRDAFPSLNGLPGETHHSYIADTRLENNPWHGYDDLALKEEVSKLISATLGEREKEIIRLYYGLDKECLTWEDISKRIGLSRERVRQVGLVALEKLKHAARKRKMEAMILKN
|
Essential protein. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Controls the transcription of the psaA gene and thus modulates photosystem stoichiometry. Thereby maintains a harmonious electron flow and photosynthetic efficiency.
|
O24646
|
HY5_ARATH
|
Transcription factor HY5 (Protein LONG HYPOCOTYL 5) (bZIP transcription factor 56) (AtbZIP56)
|
MQEQATSSLAASSLPSSSERSSSSAPHLEIKEGIESDEEIRRVPEFGGEAVGKETSGRESGSATGQERTQATVGESQRKRGRTPAEKENKRLKRLLRNRVSAQQARERKKAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKNTTGNKRGGGGGSNADASL
|
Transcription factor that promotes photomorphogenesis in light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in the blue light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevents the activation of light-induced genes (Probable). Involved in responses to cold conditions probably by modulating the expression of several genes and triggering anthocyanin biosynthesis. Acts coordinately with SPL7 to regulate the microRNA miR408 and its target genes in response to changes in light and copper conditions. Regulates the abscisic acid (ABA) signaling pathway. Also involved in root gravitropism. Involved in the repression of hypocotyl cell elongation to promote photomorphogenesis. Recruits the histone deacetylase HDA15 to the promoters of a subset of cell wall organization and auxin signaling-related genes. HDA15 represses their transcription by decreasing the levels of histone H4 acetylation in a light-dependent manner.
|
O24648
|
G3OX_PEA
|
Gibberellin 3-beta-dioxygenase 1 (EC 1.14.11.15) (GA 3-oxidase 1) (Gibberellin 3 beta-hydroxylase 1)
|
MPSLSEAYRAHPVHVNHKHPDFNSLQELPESYNWTHLDDHTLIDSNNIMKESTTTVPVIDLNDPNASKLIGLACKTWGVYQVMNHGIPLSLLEDIQWLGQTLFSLPSHQKHKATRSPDGVSGYGIARISSFFPKLMWYEGFTIVGSPLDHFRELWPQDYTRFCDIVVQYDETMKKLAGTLMCLMLDSLGITKEDIKWAGSKAQFEKACAALQLNSYPSCPDPDHAMGLAPHTDSTFLTILSQNDISGLQVNREGSGWITVPPLQGGLVVNVGDLFHILSNGLYPSVLHRVLVNRTRQRFSVAYLYGPPSNVEICPHAKLIGPTKPPLYRSVTWNEYLGTKAKHFNKALSSVRLCTPINGLFDVNDSNKNSVQVG
|
Converts the inactive gibberellin (GA) precursors GA9 and GA20 in the bioactives gibberellins GA4 and GA1. Has a small activity on GA29, producing GA8. Unable to convert GA20 to GA5, GA5 to GA3 or GA12 to GA14. Involved in the production of bioactive GA for vegetative growth and development, but not for the 3-beta-hydroxylation of GA in developing seeds.
|
O24767
|
INGK_EXIAC
|
Guanosine-inosine kinase (EC 2.7.1.73) (ATP:guanosine 5'-phosphotransferase) (Guanosine kinase) (GKase)
|
MNKIAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHLCRKMELPLFGVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGLVPEMLDALQ
|
Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively. Can also use deoxyguanosine. Shows a strong preference for guanosine. dATP, GTP and dGTP can serve as phosphate donors.
|
O24915
|
MQMTN_HELPY
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Aminodeoxyfutalosine nucleosidase (AFL nucleosidase) (Aminofutalosine nucleosidase) (EC 3.2.2.30) (5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase) (MTA/SAH nucleosidase) (MTAN) (EC 3.2.2.9) (6-amino-6-deoxyfutalosine N-ribosylhydrolase)
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MVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL
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Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2. Does not act on futalosine (FL) as substrate.
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O25001
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HCPA_HELPY
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Beta-lactamase HcpA (EC 3.5.2.6) (Cysteine-rich 28 kDa protein)
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MLGNVKKTLFGVLCLGTLCLRGLMAEPDAKELVNLGIESAKKQDFAQAKTHFEKACELKNGFGCVFLGAFYEEGKGVGKDLKKAIQFYTKGCELNDGYGCNLLGNLYYNGQGVSKDAKKASQYYSKACDLNHAEGCMVLGSLHHYGVGTPKDLRKALDLYEKACDLKDSPGCINAGYIYSVTKNFKEAIVRYSKACELKDGRGCYNLGVMQYNAQGTAKDEKQAVENFKKGCKSSVKEACDALKELKIEL
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Slowly hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives. May be involved in the synthesis of the cell wall peptidoglycan.
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O25067
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AMIE_HELPY
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Aliphatic amidase (EC 3.5.1.4) (Acylamide amidohydrolase)
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MRHGDISSSPDTVGVAVVNYKMPRLHTKNEVLENCRNIAKVIGGVKQGLPGLDLIIFPEYSTHGIMYDRQEMFDTAASVPGEETAIFAEACKKNKVWGVFSLTGEKHEQAKKNPYNTLILVNDKGEIVQKYRKILPWCPIECWYPGDKTYVVDGPKGLKVSLIICDDGNYPEIWRDCAMRGAELIVRCQGYMYPAKEQQIAIVKAMAWANQCYVAVANATGFDGVYSYFGHSSIIGFDGHTLGECGEEENGLQYAQLSVQQIRDARKYDQSQNQLFKLLHRGYSGVFASGDGDKGVAECPFEFYKTWVNDPKKAQENVEKITRPSVGVAACPVGDLPTK
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Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. Hydrolyzes propionamide, acetamide and acrylamide, but has no activity with formamide or urea. The natural substrates of AmiE in its gastric environment are not known. Probably functions to ensure nitrogen supply to the bacteria. Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. The highest level of acyl transfer activity is observed with acetamide.
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O25080
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PGDAE_HELPY
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Peptidoglycan deacetylase (PG deacetylase) (EC 3.5.1.-) (Acetylxylan esterase) (EC 3.1.1.72)
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MAKEILVAYGVDIDAVAGWLGSYGGEDSPDDISRGLFAGEVGIPRLLKLFKKYHLPATWFSPGHSIETFSEQMKMIVDAGHEVGAHGYSHENPIAMTAKQEEDVLLKSVELIKDLTGKAPTGYVAPWWEFSNITNELLLKHGFKYDHSLMHNDFTPYYVRVGDSWSKIDYSLEAKDWMKPLIRGVETDLVEIPANWYLDDLPPMMFIKKSPNSFGFVSPHDIGQMWIDQFDWVYREMDYAVFSMTIHPDVSARPQVLLMHEKIIEHINKHEGVRWVTFNEIADDFLKRNPRKK
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Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans.
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O25119
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FLIG_HELPY
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Flagellar motor switch protein FliG (Flagellar motor switch protein G)
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MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE
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One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.
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O25503
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SPEE_HELPY
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Polyamine aminopropyltransferase (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16)
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MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNRQLLFKNFLHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDTHIDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQLLDLDIKKYDLIFCLQEPDIHRIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGGVFSVAMPFVAPLRILSNKGYIYASFKTHPLKDLMTPKIEALTSVRYYNEDIHRAAFALPKNLQEVFKDNIKS
|
Involved in the cell growth and proliferation. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Spermidine cannot be used as an aminopropyl acceptor.
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O25533
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COAX_HELPY
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Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)
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MPARQSFTDLKNLVLCDIGNTRIHFAQNYQLFSSAKEDLKRLGIQKEIFYISVNEENEKALLNCYPNAKNIAGFFHLETDYVGLGIDRQMACLAVNNGVVVDAGSAITIDLIKEGKHLGGCILPGLAQYIHAYKKSAKILEQPFKALDSLEVLPKSTRDAVNYGMVLSVIACIQHLAKNQKIYLCGGDAKYLSAFLPHSVCKERLVFDGMEIALKKAGILECK
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Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can also utilize CTP or GTP instead of ATP as a phosphoryl donor, albeit to a lesser extent.
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O25560
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HYPB_HELPY
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Hydrogenase/urease maturation factor HypB (Hydrogenase/urease nickel incorporation protein HypB)
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MSEQRQESLQNNPNLSKKDVKIVEKILSKNDIKAAEMKERYLKEGLYVLNFMSSPGSGKTTMLENLADFKDFKFCVVEGDLQTNRDADRLRKKGVSAHQITTGEACHLEASMIEGAFDLLKDEGALEKSDFLIIENVGNLVCPSSYNLGAAMNIVLLSVPEGDDKVLKYPTMFMCADAVIISKADMVEVFNFRVSQVKEDMQKLKPEAPIFLMSSKDPKSLEDFKNFLLEKKRENYQSTHSF
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Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Is also required for maturation of urease. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion.
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O25830
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DHPRS_HELPY
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Bifunctional dihydropteroate synthase/dihydropteroate reductase [Includes: Dihydropteroate reductase (DHPR) (EC 1.5.8.-); Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase)]
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MIVKRLNPDALKNALQKIGPEKIAQDRMHQKGVSFVFEIQHLPLSATLILKQEAISVGGDFATPRDCILAKEPFYDGVLIASAKQLERLIVKCHSQPFGLKHLAQELKSHLKAPKPNTPQIMAVLNLTPDSFYEKSRFDSKKALEEIYQWLEKGITLIDIGAASSRPESEIIDPKIEQDRLKEILLEIKSQKLYQCAKFSIDTYHATTAQMALEHYFSILNDVSGFNSAEMLEVAKDYKPTCILMHTQKTPKDMQENVFYHNLFDEMDRFFKEKLEVLEKYVLQDIILDIGFGFAKLKEHNLALIKHLSHFLKFKKPLLVGASRKNTIGLITGREVQDRLAGTLSLHLMALQNGASVLRVHDIDEHIDLIKVFKSLEETD
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Bifunctional enzyme that catalyzes the formation of dihydropteroate, the immediate precursor of folic acid and the reduction of dihydropteroate to tetrahydropteroate.
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O26061
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THYX_HELPY
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Flavin-dependent thymidylate synthase (FDTS) (EC 2.1.1.148) (FAD-dependent thymidylate synthase) (Thymidylate synthase ThyX) (TS) (TSase)
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MEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHSSTLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFLPLNETNLERAKEFLVFVDNEKVNAMSVLALENLRILLSEHNIKNDLAKYAMPESYKTHLAYSINARSLQNFLTLRSSNKALKEMQDLAKALFDALPGEHQYLFEDCLKH
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NAD(P)H and FADH(2) as the reductant.
|
O26901
|
HELS_METTH
|
ATP-dependent DNA helicase Hel308 (EC 3.6.4.12)
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MKSLPPEMRQILGDCYPHIRELNPAQRSAIEAGYLESEDNYIIAIPTASGKTLLGIIAALKTVMEGGRVIYTVPLLSIQNEKIKEFRKLEEHGIRVGKDPRTSDIAVMVFESFDSLTRFSWNILREVDLLIVDEFHMIGEYTRGPVIESAITRARTLNPSVRIVALSATLSNMDEIAGWLDARVVEHDYRPVPLHREVLDTEMFGVREKNDVVLKVLERSLEDGSQTLAFVSTRRFTESLASHLADKISGKIPDDMVESFREVAGKVLEVPKSRGSPPTSTCLKLAECLEAGIAFHHAGLFNRQREIIEDEFRDGNILMITATPSLMYGVNLPSRTVVIRDYTRWTSQGPRRIPVFDYEQMSGRAGRPQYDDAGYSYLIARSHDEAMDLEEYYIRGEVERTTSRIIENRDALYRQIIAQVASGLSGTTEELADFFRNTFYGYQMVEGPFSDSFGMDSIQYEVENATEYLMRNRILYPGPEGFSATEFGLLIAKSNYSVETAIKLHQFASEMDEMDIYRLIYEITRTPDMPLISFKGRKSRDPVRDKLMEHGLFLMDVGNEEATAAALIEWINERTEYEIENAFHVYAASTRRSAYEASKIVKFFGKICEIMGVYRHSSQLEILSARLYYGVKEDAIPLVVGVRGLGRVRARKIIKTFGEDLRHVREDELKRIDGIGPKMAGAIRRYCERF
|
DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Helicase with 3'-to 5'- polarity able to unwind over 100 bp of DNA at 50 degrees Celsius. Unwinds forked DNA, preferentially on lagging strand forks has weaker activity on Holliday junctions. Displaces the invading strand in DNA D-loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks. Replication forks bind both this protein and RPA. RPA does not stimulate the helicase activity of this protein. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15994460, ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:19143605, ECO:0000269|PubMed:28738244}.
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O27026
|
CAPPA_METTH
|
Phosphoenolpyruvate carboxylase (PEPC) (PEPCase) (EC 4.1.1.31)
|
MKVPRCMSTQHPDNVNPPFFAEEPELGGEDEIREAYYVFSHLGCDEQMWDCEGKEVDNYVVKKLLTKYQAFFRDHVLGEDLRLTLRVPNPTVERAEAKILLETLESIPRSYDTASLFYGMDAAPVFEVILPMTSSSSCLNRIHSYYLDFVKGKERLQLADGVTVKEWIGEFRPDEINVIPLFEDHEGMLNAAKITGEYLDGKDIQEQRVFLARSDPAMNYGMISATLLNRIALSDFRDLEEESGVKLYPIIGMGSAPFRGNLRPDNVEDVTWEYRGAYTFTVQSSFKYDHEPSDVIRGIKKLRSVKPGRAAEIERESVLEIISAYCREYRRQVMDLVDIINRVARYVPGRRKRKLHIGLFGYSRSMGNVSLPRAITFTAALYSLGVPPELLGFNALSSGDLEFIEEVYPGLGRDLHDAARYANPESPFLSPEVKSSFEEYLEPEYDEGHMKTTEEIIRALRINRTANLQELILEAASQRKFLG
|
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
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