ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P21918 | MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVLVCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFDIMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNWHRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVP... | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52951
Sequence Length: 477
Subcellular Location: Cell membrane
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Q95195 | SILISFPVQLNWHRDQAGSWGGLDLTNNLANWTPWEEDVWEPDVRAENCDSSLNRTYAISSSLVSFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFIL | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16627
Sequence Length: 147
Subcellular Location: Cell membrane
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Q2RBJ4 | MRIASSSGILMDANGKANGSAPSALVAYFLGMGFSREMVFRAIKEIGDTDSEQILELLLTYQAIGSDPSVGNSSHSACDPQILEEEDEEEDVNWDEDDTVDNFDRATYSDGSGDEDFLQEMSEKDEKIKSLVSMGFPEDEDTEFSSFGGRKKTKLIDGSKKKRERYRSRPQWNQVPFDGSHEEPMPLPNSMVGFSLPNDGLRSVHRNLPDQALGPPFFYYENVALAPKGVWTTISRFLYDIYPEFVYSKYFCAAARKRGYIHNLPIKNRNYTRGVSRTARYRALGNSFQVDTVAYHLSVLRDIFPNGMNVLSLFSGIGGA... | Function: Involved in de novo DNA methylation. Involved in RNA-directed DNA methylation (RdDM).
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53163
Sequence Length: 473
Subcellular Location: Nucleus
EC:... |
Q9LXE5 | MVMSHIFLISQIQEVEHGDSDDVNWNTDDDELAIDNFQFSPSPVHISATSPNSIQNRISDETVASFVEMGFSTQMIARAIEETAGANMEPMMILETLFNYSASTEASSSKSKVINHFIAMGFPEEHVIKAMQEHGDEDVGEITNALLTYAEVDKLRESEDMNININDDDDDNLYSLSSDDEEDELNNSSNEDRILQALIKMGYLREDAAIAIERCGEDASMEEVVDFICAAQMARQFDEIYAEPDKKELMNNNKKRRTYTETPRKPNTDQLISLPKEMIGFGVPNHPGLMMHRPVPIPDIARGPPFFYYENVAMTPKGVW... | Function: Involved in de novo DNA methylation. Controls asymmetric and CpNpG methylation. Required for FWA gene silencing but not for the maintenance of SUP gene silencing. Functionally redundant to CMT3 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation.
Catalytic Activity: a 2'-deoxycytidine in... |
Q9M548 | MVIWNNDDDDFLEIDNFQSSPRSSPIHAMQCRVENLAGVAVTTSSLSSPTETTDLVQMGFSDEVFATLFDMGFPVEMISRAIKETGPNVETSVIIDTISKYSSDCEAGSSKSKAIDHFLAMGFDEEKVVKAIQEHGEDNMEAIANALLSCPEAKKLPAAVEEEDGIDWSSSDDDTNYTDMLNSDDEKDPNSNENGSKIRSLVKMGFSELEASLAVERCGENVDIAELTDFLCAAQMAREFSEFYTEHEEQKPRHNIKKRRFESKGEPRSSVDDEPIRLPNPMIGFGVPNEPGLITHRSLPELARGPPFFYYENVALTPKG... | Function: Involved in de novo DNA methylation. Controls asymmetric and CpNpG methylation. Required for FWA gene silencing but not for the maintenance of SUP gene silencing. Functionally redundant to CMT3 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation (RdDM) . Acts as major DNA methyltransfera... |
A0A0U5GNT1 | MVRALILDLGDVLFNWDAPASTPISRKTLGQMLHSEIWGEYERGHLTEDEAYNALAKRYSCEAKDVAHTFVLARESLRLDTKFKTFLQTLKQNANGSLRVYGMSNISKPDFEVLLGKADDWTLFDKIFPSGHVGMRKPDLAFFRYVLKDISTPVEDVVFVDDNLDNVTSARSLGMRSVLFHKKDEVQRQLTNIFGSPAERGLEYLSANKTNLQSATTTDIPIQDNFGQLLILEATEDPSLVRMEPGKRTWNFFIGSPSLTTDTFPDDLDTTSLALSIVPTSPDVVNSVIDEIISRRDKDGIVPTYFDNTRPRVDPIVCVN... | Function: Drimenol cyclase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes . The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase drtB using f... |
A0A0U5GQ05 | MLFAKAFQSATVAGAVILAALVDVAHSTPLDDPGQCGLEAVAQCCTSLRESAVGDKVFAYGDIEYFRAKRSYYSVTTSLNSACIVLPESAEDVSTVLTTLTQPDLAETCPFAIRSGGHSMVVGFSDIAAGVTLDLSKLNHTIYHPETETVSLGPGGRWVNVYEELRPDNVMVSGGRFSSVGVGGFLTGGGITIYSAQRGLACDDVVSFDVVLANGTLIQATNATNPDLFHTLKGGSGNLGVVTNFEVRAFPQTQIWGGYTSYNVSKTPELARTLQNFTSNIEQDPKALLVTFWTYDTLTDVNRAANAMYYTDPVEYPEAF... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes . The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase d... |
A0A0U5GRB4 | MSDTYLVAASGLAVCFFVLYLLRPKTALPPGPPKLPLIGNLHQLGKKPMYERCQEWHRQFGKLISLKLGFDNVVVIGSSQIARDLLDKKGAMYSSRPKFVMAHENVTKGFHTATLPYGPRWRLHNRMQLSVLNKRIVTRCRQVQEFESLQLIHELLFTNDFHPRFQRWANSLQTGLGYGQRLAKGDECNIHEMEHISRVFREIFATGTWLVDLFPALNHLPPLLAPWKGVAEQHYNRTIELFQLNTAAALSKTSWNWTKKIRSLTESQGLPPDEVNFLVGVMAEAGGDTTGVVLDMFTLAAALHPEKMAIAQKEIDTVVG... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes . The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase... |
A0A0U5CNN8 | MSFAFSKVEFEEVEFQTLDKLTLKARLYSAAKRGPALVMNPGYNCTKEISAPSAAAYFQSKGITCLIYDPRNCGQSDGTPRREIDPHRQVDDYLDAMTYMSGLDIVDPDQIGFWGVSFSASIALAAACYDPRAKCIITVSPWTFDFGITAAEAKDNFSRLVAEREAQALGNEPFYTAMVDEEGNNPIHVNVDWGDEVRAAVNEFVSLSADGFVPTVTFQSYYKLFTFSPYLSLKFLGDTPLMMVVPEHDTVCPVEQQVKLYDAVEGPKEIYHAEGKRHLNMLAEDKFFEPMMKPQVEFFFKVMRGEAI | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes . The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase drtB using fa... |
A0A0U5CNP2 | MAPALPFALPSLAGKVYLVTGGNTGVGFHTVDELAKHGARVYMGARSPGKAEAAIKTIRAETPTADVHFLQMDLMDLHSVVAAAKSFKEKETKLHGLVNNAGIMATPYALSGDGFEAQWQTNYLSHWVLTWHLLDVLVRTLQAEGGAAGSVRVVDVTSDGHNFAPKVGIDFKDINLEKAGVFARYGQSKVGNILHAKQLNKLYGPSGSETAKKGIWTAAVHPGHLDTNLNKQTAFPKFVNTLLRAVGAYSPPRDGAFNSVFAVASPEFKVADSGEYFVPGQKKKQPSKVARDMELAGRLWKWTEEELRKRELLD | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes . The pathway begins with the synthesis of the backbone drimenol by the terpene c... |
A1KV57 | MTPLFRKAVWLLFAVSVCAFAGSLAAQYVLGMEPCVLCISQRLCVLATALCTAIVLMCRPRRRAGGLFGAVFISIPAVTGISVAAYQLWLQSLPPGTAPSCGAPWTFRLKGWSLFDWFEPVVRGFGNCAEPDYLLGVALPVWSAAYFLAVVLTVWWAWARAK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17649
Sequence Length: 162
Subcellular Location: Cell inner membrane
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Q82VB9 | MRIIFLLIALICAGLVSYALYLQLADGLLPCPLCIFQRMAYWLVGITALFAFIHHPQRLGRRIYCGLIILFSLAGAIVAGRQAWLVRFPEAFECGISPEEAFLNELPLARWWPDMFEANGDCTDGTWQFLSLTIPDWSLLIFLAFSLIAGLLWRSRSISSSNLK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18514
Sequence Length: 164
Subcellular Location: Cell inner membrane
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Q3J7Z4 | MRLSVRWVFFLGFFLCALMLAIAGYFQFVENLEPCPLCILSRVAVLAIGGVFLVAALHNPKSWGIKVYALLGFVVTLIGIGITGRHVWLQSLPADQVPACGPGLNFMLDNFPLTETLELVFRGSGECAEVQWSFLGLTIPGWTLVAFLFLGVISLWQMGRTGGGAGKLT | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18351
Sequence Length: 169
Subcellular Location: Cell inner membrane
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Q6D4M8 | MLRFLNRCSRGRGAWLLLAFTALALELTALYFQHVMLLKPCVLCIYQRSALWGVFAAGIVGAIAPSSLLRYPAIALWIYSSYEGIRLAWKHTDILLNPSPFTTCDFFVSFPSWLPLDKWLPAIFNATGDCSERQWSFLSMEMPQWLLGIFAAYLLIAVLVLIAQPFRSKRRDLFSR | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20114
Sequence Length: 176
Subcellular Location: Cell inner membrane
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Q7N3Z3 | MMRFLNHCSQGRSAWLLMILTALILESSALYFQHVMKLQPCVMCIYERVALFGVLSAGILGVIAPKTPLRWLAIILWIYSAWGGLQLAWQHTMMQLHPSPFNTCDFFVNFPSWLALNQWLPSVFEATGDCSVRQWQFLTLEMPQWLVGIFAAYLVVAALVLISQFFSRK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19375
Sequence Length: 169
Subcellular Location: Cell inner membrane
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Q12AY6 | MFLTYFDAMPRRVLALVSLACVALLAFGLYLQHVVGLEPCPMCIVQRYALVLVAVVAGITAVAKSRGLLITGSGLLVLLSGFGAFVAARQSFLQWYPPEVASCGRDFYGMIETFPLKRAIPMIFKGSGDCTKIDWTFLGLSIANWSFLCFVAIALVGLVLITRLARQR | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18327
Sequence Length: 168
Subcellular Location: Cell inner membrane
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Q15S31 | MTFISNLADTRLAWGLLFLSALVLVAYALFSQHAMGLQPCIMCIYQRTAIFGIMFACVPVLAANNMLTRLFAFTVWGISAIWGGLIAWEHYDIQNAANPFFATCEIVPNFPSWLPLHEWLPNLFAATGDCGNIDWVFMDMSMPQWMMVVFAIYSSIWFVVLASRLIGNRAI | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19270
Sequence Length: 171
Subcellular Location: Cell inner membrane
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Q887H2 | MSNDTFYLKREKRFLVLLGIICLSLIGGALYMQIALGEAPCPLCILQRYALLFIAIFAFIGAAMNGRRGVTVFEALVTLSALCGIAAAGRHAWILAHPSDSCGIDILQPIVDGLPLATLFPTGFQVSGFCTTPYPPVLGLSLAQWALTAFVLTAILVPACIIRNRRKPY | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18213
Sequence Length: 169
Subcellular Location: Cell inner membrane
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Q3IE23 | MNWLAQLPTQRTPWLLFSGIVFLLEITALFFQYKMGLAPCIMCIYQRTAVLGLLIAGIIGTSNPEHRGVRLLAYSVWAVSSVWGFIIAREHIEMQTTTDPFAFSCEFEPNFPAFMPLHEWIPSFFAATGDCGNIDWQFAGLSMPAWMEVIFALFAATLFLLVTSRLMTKRSL | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19467
Sequence Length: 172
Subcellular Location: Cell inner membrane
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A0A8V1ABE9 | MWLGALLDTLPTPALTIDRTTAHRNAERMRERCRALGVRLRPHVKTHKTLEGGLLATGGTRRGIAVSTLAEARFFADGGFDDILLAYPVPTARLEECAGLARRLDAFHVLLDRPEALASLRQRPLGHGKRWLVWLKLDCGNGRAGVRPTDPAALELAQAIANDAPEEVTLVGVYAHCGNTYGCSGADTIQAIARTTTNAVLSFVAALRQAGVPCPQASIGSTPSCSHPIPEMSQLTELHPGNYIFYDLQQTQLGSCQPQDVAIRVLTRVIGHYAHRGQLLVDCGWAALSLHGAGAGQGPQGCAAIDGHPELRLVGLTQEH... | Function: Catalyzes the conversion of D-serine, an allosteric activator of the N-methyl-D-aspartate (NMDA) receptor for L-glutamate, to pyruvate and ammonia.
Catalytic Activity: D-serine = NH4(+) + pyruvate
Sequence Mass (Da): 40379
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 4.3.1.18
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Q9US35 | MASNVDKFSSRFYLNVNKEELKKEYVGKTIQQVPTPGFVIDEAIFEKNCNRMLDRASDIGVTFRAHVKTHKTIEGTLLQLGDGRTKAVVVSTLMEGFSLIPLILEGKIDDLLYGLPVAKSRLPELYELSKIVPHLRLMIDNPKQLDILREFTSTLPDDAKPWSIFVKIDMGTHRAGVTNDSQVVKDLISTILSDKSLFDLFGFYCHAGHSYASRSIDAASEFLCAEIDAANTAAKFATSIDPSLKLTLSVGATPTAHSVSPKVKELLPTLSGKLEVHAGNYPMNDVQQMITKCISQADVADYVFAEVISNYPGRNGEPGE... | Function: Catalyzes the conversion of D-serine to pyruvate and ammonia. May play a role in D-serine detoxification.
Catalytic Activity: D-serine = NH4(+) + pyruvate
Sequence Mass (Da): 45647
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 4.3.1.18
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P53095 | MSDVLSQYKGCSVRDLPTPNFVINEEKFDKNCTTMLNNVEKLSQECGVPIKFRAHVKTHKTAKGTLKQLGHGLPLAKRTTRAILVSTLKEAEELLNYQDRQCSDYIDDITYSLPCCVPEFIPLLSNLSRRVNNFQVFVDNIEHLENLKNFGRPASGKKWSVFIKVDMGTKRAGLAFDSPEFLSLLKKLTSSEIKEVIEPYGFYAHAGHSYSSTSINDTQNLLMEEVKAVNSAAKVLCSVDPQFDPSKLTLSVGATPTSNSLKLDNKSTLVKFITTQLVSTLEIHCGNYCMYDLQQVATGCVQDHELSGFVLGTVLSSYPS... | Function: Catalyzes the conversion of D-serine to pyruvate and ammonia . May play a role in D-serine detoxification .
Catalytic Activity: D-serine = NH4(+) + pyruvate
Sequence Mass (Da): 47828
Sequence Length: 428
EC: 4.3.1.18
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A0A0H2VAP9 | MHSQIWVVSTLLISIVLIVLTIVKFKFHPFLALLLASFFVGTMMGMGPLDMVNAIESGIGGTLGFLAAVIGLGTILGKMMEVSGAAERIGLTLQRCRWLSADVIMVLVGLICGITLFVEVGVVLLIPLAFSIAKKTNTSLLKLAIPLCTALMAVHCVVPPHPAALYVANKLGADIGSVIVYGLLVGLMASLIGGPLFLKFLGQRLPFKPVPTEFADLKVRDEKTLPSLGATLFTVLLPIALMLVKTIAELNMARESGLYTLLEFIGNPITATFIAVFVAYYVLGIRQHMSMGTMLTHTENGFGSIANILLIIGAGGAFNA... | Function: Protein that allows transport of D-serine across the inner membrane, does not transport D-alanine nor probably glycine. Is probably a H(+) symporter, as CCCP inhibits transport. Transports D-serine more efficiently than CycA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47107
Sequence Le... |
Q88JU3 | MQRSIATVSLSGTLPEKLEAIAAAGFDGVEIFENDLLYYAGSPRQVRQMCADLGIAITLFQPFRDFEGCRRDRLQKNLDRAERKFDLMQELGTDLVLVCSNVQADALGDEQLLVDDLRLLGEHAGKRGLRIGYEALAWGRHVNTYQQVWNLVRQADHPALGVILDSFHTLSLKGDPSAIRDIPGDKIFFVQMADAPILAMDVLEWSRHFRCFPGQGEMDMAGFLAPILATGYRGPLSLEIFNDGFRAAPTRQNAADGLRSLLYLEEQTRLRLEQENTPIEPGVLFSPPPASAYDGVEFLEFAVDEAVGARLGNWLKRLGF... | Cofactor: Requires a divalent metal cation for DSD activity, with a preference for Co(2+) but can also use Ni(2+), Mn(2+) and Mg(2+).
Function: Catalyzes the conversion of 3-dehydroshikimate to protocatechuate (3,4-dihydroxybenzoate), a common intermediate of quinate and shikimate degradation pathways.
Catalytic Activi... |
Q6LYK1 | MDYLLISSETDPASQNLKKHVENYGYSVFNIEKKSTQTNYSEFPQSEMYIFLSKHASESKKPTLTVHTPGNLTDDNSHGGNPEEISPCNPVFNTLMLQNMNKYNEMEEYKELGFDVSFEVLHHGPTDLKAPSAFVEIGSSEEQWQIDDAAEIITNSLIDTLNSIQNSEYDEKEKIIGIGGGHYSPKFTKLALREEYYVGYLTPKHAKLSENILNQLTSKQEFDFIGIDWKGLYGEDKRKYVEFFDENDISWQRV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
B8GIX8 | MKITLVNSRLDPAGVTIREQIQVLLADPEYQREGIDWEFLEIDGRLIHQERIDTGLNSDLLIFLSRHTSRRPVPVLTVHPTGNPGEALLGGEAGSFAPAAPGWMQAVLQNLVRLVPDGYQASYEVTHHGPTTLSTPSFFVEIGSTDHEWSDPVAGAAVAEAVLTAAPVDPISLIGFGGTHYAPRETAVALETRGAFGHILHSREIGGLTGSLLAKIATAAEAEAVYIDRKAIDRPALDHLYALLEETDLPVLGEKELHQIGSLSWQEYRSLRQIAGDAAPGAHLVIGTLPGGGTPVTATVPADLLAQAISADQGRVMTAI... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A4YEU7 | MDVSVIISSKDPVGQTVKRLGYSFEEIDEDVTEFSYSKGDSIVMICRHESSTRTPAFTIHHPGNPGKSAMGGKPESLAIANARLLTSIFRSMTRIDANIEKIIEATHHGPTEIPKPITFVEIGSDPEMWNNEKLVGKLVEAVLKGIERMEETDCQNTTLIYGGPHYSKLASTVAQSDCISHIISKHYISELSSNVIVQSIERNITRPRTAVLDSIPRSKRETLTSILSSNNISIELR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A0B5C3 | MSEVVIICSSSDPASSNIASRLLELAEWDEEGTLRFHRSYCMLCIEGELVGLRNLEDMLDRIGLSPRLIIFASRHISKEAVPWLGGHFTGVVREGSFELSRPAPYALKKLLMALQRHAPSTFRLSAEATHHGPVDLRTPSLFAEIGSCEQHWIDPAAGAAVARAILELESYEAHADETVLLGIGGGHYVQRQTELILSRPVAFGHMFSKYQASMLNVEAIKKAADLSGASGVYLDGKSFRSDERRRLEEIAASLDLNVMGIKEVRSL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q6L1F5 | MDLIIASRMDEASMLMAEKIIDLYDFNRLNENEYQKDGFKLMFIDDLHIYHNMEKLDFDTLIFLSRHSSSAGVKSLTVHSIGNYRKAELGGYDNKTVLSAPYEMSSSLRSIKELYNDDGYNITFEATHHGPYTKNRSYFIEIGTSGEDWHNDKILEIMARSVIEKNVKRFRSGIGIGGGHYAPKISDYFFNNDINIGHIIPKYVSETIKDNQIIESIENTENCSFILIDWKGSPSRLRSLALDAADKCSLELIKI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q9V2R8 | MKVIMTTKVDKASMNIMQKLIENFGFKETELKFDGNPVYKKDDMVILTTNDEMIYYDYLDREIEKQLSFKPEIIAFASRHSSKQKLPALTTHVTGNWGEAMYGGKDESFAIAIPSAMKLALLKMNELNDLGWTVCYEATHHGPSELEVPSFFIEIGSSEEEWVNDRAGEIIAETIVYVLDNYENSKFKVALGIGGGHYAPKQTKRALNSDLAFGHILPKYAQPVSRDVILKAINRFHEKVEAIYVDWKGSKGETRQLAKSLAQELGLEFIKD | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D... |
A1RS86 | MYVIVASLNDPVSRIFLDVIAPTPLVKTEGNIEIRKFVDFPVVVYRGEPTDFSREDILASFGKYAIFISRHEMANPRPLFTVHTPGSWPDVSISNPPLTSSIFRTLCKLAYEPYTCAFEATHHTPNTSYISATFVEVGSTENEWKDRKAVETLAQAVEEVLNSQIKPNTPAMAIGDLHYVTVTDPVLKGELDLGHVIPKYVDISLQVVQNAYLKHTTPIERAILFKKNVKNPARSEIIEFLKSRGVEIITKG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q97WI2 | MDIKLVYSTLDPVGVTIKKLGYRFEEINEDVTDFHYENGEAIVIFSRHESKAGIPSLTVHYPGNPSEEIMGGEPKKLGIAYPRLLTSILREIKKIDLNIEKTMEATHHGPTYQNVPVIFVEVGSNETYWTNDTIVKALVDSTIRSIDKVDEIDCEYYISGFGGPHYSRLFTKLADESCIGHVISKHYIDKLDDKVIIQTITNSVNTINKVVIDSLNSKQKERIIASLKKLNNINIEFR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D... |
A3DLP6 | MEIYGIVYSVKDPAGFGMAEYIIKYYGLEKSNVCKNAITCYVGNNFVLAGFSEDVIYFDFLDGRLPDKVSRYIVLSRHSSAKKVCSYTVHHTGNFGPEAPYGGRPRTLSIANPIVSHKLLINLSILAEEYGRIDEYEVSYEATHHGPTDVRKPLNFIEIGSTIDEWKDPVNHEIVALAVIKFLENPNHECIPVTGVGGGHYPRKHTKMAFEKNYCYGHIMAKYALQYLSPEILEEMIVKSDPVPQRIIVEKKGTRREHRRIIEQYVLNRGIVLEYI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
B9ML29 | MRAVVQRVKEAFVIVDGKEVGRIQRGLCLLVGVAQDDTEEDADYLCEKVANLRIFEDETSKFNLSLMDVGGEVLVISNFTVMGDARKGRRPNFMFAAEKEKAERLYNYFVEKLKQKVRKVECGVFQAHMEVSILNDGPVTVLLDSKKIF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8RAL7 | MRAVVQRVTRGEVRVDGEVVGAIGKGFVVLVGIAEDDTEEDIAYMADKLVNLRVFEDEEGKMNLSLLDVGGEMLLVSQFTLMGDVRKGRRPSFTSAKKPEEALPYFNKLVEEVRKKGVKVETGKFQAMMKVLIENDGPVTILIDSKKLF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q93RD9 | MRVLLQRCYEASVSMEDEVISEIAGGLCLLVGFTHTDTPETVDYMAKKIVGLRIFEDESEKMNISLAERGGAILSVSQFTLYADVSRGKRPSFTKSAPGEKAEALYDLFNQKLAEAGFIVETGVFGAMMDVKIVNHGPVTIMLDSEEMRK | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0AIX1 | MRVLLQRCYEASVSVEEEVISEIAGGLCLLVGFTHDDTPETVEYMAKKVVGLRIFEDESEKMNISLAERGGAILSVSQFTLYADVSKGKRPSFTKSAPGEKAERLYDLFNTKLSEAGFIVETGVFGAFMDVKIINHGPITMMLDSAEMRK | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0L7S8 | MRALVQRVSEASVVVEGQVVGAVERGLLVLLAVERGDGEKQLEEMVRKVARLRIFPDEAGKMNLSVKDIEGEVLVVSQFTLAADMRKGYRPSFSLAEEPKRAEALYLDYCQRLNQHEGVVVAQGLFGADMQVKLINDGPVTIWLDLPPQEG | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A1TYQ0 | MKGLIQRVSEASVAVDGETIARIGPGLLLLLGVERNDTLNEAKELCRKVLSYRVFPDEQGRMNVNVQAAGGSLLVVPQFTLAADTSSGTRPGFSLAAAPELANRLYGDFVAEASGLLGAGRVGTGEFGADMKVALINDGPVTFMLESGQRGSCTKM | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B3DVT5 | MIGLVQRVKQAAVEIDQLPVCAIGRGILLFLAIEKGDNEKNGDLLIEKVLNCRIFSDQSGKMNLSLLDIRGELLIVPEFTLAGKIAKGKRPSFDMAAPAEVAKKLFDYVSGQIENKYKAVKKGYFGADMSVYLINDGPVTFWLKC | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q2NG79 | MKLVVQRVTSAKVEVNNNIVGKIGKGYLVLLGIKKTDTKKEADYMINKLMKLRVFEDEENKMNLSIQDIDGEILLIPQFTLYGDVTHNNRPSFSNAMKPTDAKKLFEYCCNECEKKVHTQKGEFGAFMDVNLVNNGPVTIIIEKEYNS | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
P63996 | MRVLVQRVSSAAVRVDGRVVGAIRPDGQGLVAFVGVTHGDDLDKARRLAEKLWNLRVLADEKSASDMHAPILVISQFTLYADTAKGRRPSWNAAAPGAVAQPLIAAFAAALRQLGAHVEAGVFGAHMQVELVNDGPVTVMLEG | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8TDB6 | MASHLRPPSPLLVRVYKSGPRVRRKLESYFQSSKSSGGGECTVSTQEHEAPGTFRVEFSERAAKERVLKKGEHQILVDEKPVPIFLVPTENSIKKNTRPQISSLTQSQAETPSGDMHQHEGHIPNAVDSCLQKIFLTVTADLNCNLFSKEQRAYITTLCPSIRKMEGHDGIEKVCGDFQDIERIHQFLSEQFLESEQKQQFSPSMTERKPLSQQERDSCISPSEPETKAEQKSNYFEVPLPYFEYFKYICPDKINSIEKRFGVNIEIQESSPNMVCLDFTSSRSGDLEAARESFASEFQKNTEPLKQECVSLADSKQANK... | Function: E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses . Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4 . In response to DNA damage, mediates monoubiquitination of 'Lys-91'... |
Q3UIR3 | MASSPDPPSPLLVRLRESIPKAHRKLEIYFQSRASGGGECSVQPVGPSAPDTYEVKFLKKADKEKVLKKSEHEMLVHNKPVTIVLETTKKPVEDLRPRLPSLTQPVETPSSRPPSLTGSLDEALCDDIHPQDGLVSNSVDSVVQKIFLAVTAELNCDLLSKEQRASITTVCPHIIKSMEGSDGIKKVCGNFKDIEKIHHFLSEQLLEREQKRKGSEQKRKCAPQKHTPPDVEREPPDQSSIQVPVLLLEYFKHVNPGRLEFIEYKFGVNIEIQASSPNMVTVGFTSSPFGNVEEASQSFVRDFQKCSQSLKQDCISLEEH... | Function: E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses. Monoubiquitinates several histones, including histone H2A, H2B, H3 and H4. In response to DNA damage, mediates monoubiquitination of 'Lys-91' o... |
Q8N9I9 | MSFVLSRMAACGGTCKNKVTVSKPVWDFLSKETPARLARLREEHRVSILIDGETSDIYVLQLSPQGPPPAPPNGLYLARKALKGLLKEAEKELKKAQRQGELMGCLALGGGGEHPEMHRAGPPPLRAAPLLPPGARGLPPPPPPLPPPLPPRLREEAEEQESTCPICLGEIQNAKTLEKCRHSFCEGCITRALQVKKACPMCGRFYGQLVGNQPQNGRMLVSKDATLLLPSYEKYGTIVIQYVFPPGVQGAEHPNPGVRYPGTTRVAYLPDCPEGNKVLTLFRKAFDQRLTFTIGTSMTTGRPNVITWNDIHHKTSCTGG... | Function: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context (By similarity). Functions as an ubiquitin ligas... |
Q9LYT3 | MSSTETYEPLLTRLHSDSQITERSSPEIEEFLRRRGSTVTPRWWLKLAVWESKLLWTLSGASIVVSVLNYMLSFVTVMFTGHLGSLQLAGASIATVGIQGLAYGIMLGMASAVQTVCGQAYGARQYSSMGIICQRAMVLHLAAAVFLTFLYWYSGPILKTMGQSVAIAHEGQIFARGMIPQIYAFALACPMQRFLQAQNIVNPLAYMSLGVFLLHTLLTWLVTNVLDFGLLGAALILSFSWWLLVAVNGMYILMSPNCKETWTGFSTRAFRGIWPYFKLTVASAVMLCLEIWYNQGLVIISGLLSNPTISLDAISICMYY... | Function: Acts as a flavonoid/H(+)-antiporter that control the vacuolar sequestration of flavonoids in the seed coat endothelium . Could transport the anthocyanin cyanidin-3-O-glucoside and epicatechin 3'-O-glucoside in vitro.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55147
Sequence Length: 5... |
Q9SYD6 | MMSEDGYNTDFPRNPLYIFFSDFRSVLKFDELGLEIARIALPAALALTADPIASLVDTAFIGQIGPVELAAVGVSIALFNQVSRIAIFPLVSITTSFVAEEDACSSQQDTVRDHKECIEIGINNPTEETIELIPEKHKDSLSDEFKTSSSIFSISKPPAKKRNIPSASSALIIGGVLGLFQAVFLISAAKPLLSFMGVKHDSPMMRPSQRYLSLRSLGAPAVLLSLAAQGVFRGFKDTTTPLFATVIGDVTNIILDPIFIFVFRLGVTGAATAHVISQYLMCGILLWKLMGQVDIFNMSTKHLQFCRFMKNGFLLLMRVI... | Function: Citrate transporter critical for aluminum tolerance. Responsible for citrate exudation into the rhizosphere to protect roots from aluminum toxicity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55374
Sequence Length: 515
Subcellular Location: Cell membrane
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Q9SFB0 | MTETGDDLATVKKPIPFLVIFKDLRHVFSRDTTGREILGIAFPAALALAADPIASLIDTAFVGRLGAVQLAAVGVSIAIFNQASRITIFPLVSLTTSFVAEEDTMEKMKEEANKANLVHAETILVQDSLEKGISSPTSNDTNQPQQPPAPDTKSNSGNKSNKKEKRTIRTASTAMILGLILGLVQAIFLIFSSKLLLGVMGVKPNSPMLSPAHKYLSIRALGAPALLLSLAMQGIFRGFKDTKTPLFATVVADVINIVLDPIFIFVLRLGIIGAAIAHVISQYFMTLILFVFLAKKVNLIPPNFGDLQFGRFLKNGLLLL... | Function: Citrate transporter responsible for loading citrate into xylem tissues, which helps facilitate iron transport to shoots . Mediates the citrate release in the apoplastic spaces during plant development allowing iron nutrition between symplastically disconnected tissues .
Location Topology: Multi-pass membrane ... |
Q945F0 | MLIKSQRLTLFSPLLSKTRRIPVNSHQTLVAESVITRRTLGAITATPSFHKNPVVIRRRIKLERVTRNCVRIDREIDEEEEEEEKERGDLVKQSIWEQMKEIVKFTGPAMGMWICGPLMSLIDTVVIGQGSSIELAALGPGTVLCDHMSYVFMFLSVATSNMVATSLAKQDKKEAQHQISVLLFIGLVCGLMMLLLTRLFGPWAVTAFTRGKNIEIVPAANKYIQIRGLAWPFILVGLVAQSASLGMKNSWGPLKALAAATIINGLGDTILCLFLGQGIAGAAWATTASQIVSAYMMMDSLNKEGYNAYSFAIPSPQELW... | Function: Functions as a multidrug and toxin extrusion transporter in the export of salicylic acid (SA) from the chloroplast to the cytoplasm . Plays an essential function in plant defense via the pathogen-induced salicylic acid (SA) accumulation . Acts also as a key component of the Age-related resistance (ARR) pathwa... |
Q9SLV0 | MCNSKPSSASSSLLSCKDKTHISKLETCDTDNPHYSEFRDTDSLDLKRWPSFLEGLEEVKAIGKISGPTAMTGLLMYSRAMISMLFLGYLGELELAGGSLSIGFANITGYSVISGLSMGMEPICGQAYGAKQMKLLGLTLQRTVLLLLSCSVPISFSWLNMRRILLWCGQDEEISSVAQQFLLFAIPDLFLLSLLHPLRIYLRTQNITLPVTYSTAVSVLLHVPLNYLLVVKLEMGVAGVAIAMVLTNLNLVVLLSSFVYFTSVHSDTWVPITIDSLKGWSALLSLAIPTCVSVCLEWWWYEFMIILCGLLANPRATVAS... | Function: Functions as a multidrug and toxin extrusion transporter. Contributes to iron homeostasis during stress responses and senescence . Could be involved in specifying the lateral organ initiation rate . May act as a negative regulator of hypocotyl cell elongation in the light .
Location Topology: Multi-pass membr... |
Q9Y2E6 | MLLASAVVVWEWLNEHGRWRPYSPAVSHHIEAVVRAGPRAGGSVVLGQVDSRLAPYIIDLQSMNQFRQDTGTLRPVRRNYYDPSSAPGKGVVWEWENDNGSWTPYDMEVGITIQHAYEKQHPWIDLTSIGFSYVIDFNTMGQINRQTQRQRRVRRRLDLIYPMVTGTLPKAQSWPVSPGPATSPPMSPCSCPQCVLVMSVKAAVVNGSTGPLQLPVTRKNMPPPGVVKLPPLPGSGAKPLDSTGTIRGPLKTAPSQVIRRQASSMPTGTTMGSPASPPGPNSKTGRVALATLNRTNLQRLAIAQSRVLIASGVPTVPVKN... | Function: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations (By similarity). Functions as a ubiquitin ligase protein in vivo, mediating 'Lys48'-linked polyubiquitination and promoting degradation of TBK1, targeting to TBK1 ... |
P44965 | MRIGSYQLRNRVLLAPMAGITDQPFRRLCAYYGAGLTFSEMMSTNPQVWHTEKSKLRLAHSEDLGLNAVQIAGSDPLEMAQAAAINVEYGAQIIDINMGCPAKKVNRKLAGSALLQFPDLVEKILREVVSAVNVPVTLKIRTGWDKSNRNCVQIGKIAEQCGIQALTVHGRTRACLFEGEAEYDNIKAVKQAIAIPVIANGDIDSARKAKFVLNYTGADAIMIGRAALGNPWLFQAVENLIEHNSISQMPSLKEKCGQILRHIQELHQFYGEQKGYRIARKHVAWYLQGIQPDSVFKQTFNAISDPKEQLIVLEDFFNLI... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Mass (Da): 36765
Sequence Length: 330
EC: 1.... |
Q9HUW1 | MSVVRIGPYTLPNRLILAPMAGVTDRPFRQLCRRLGAGMVVSEMVTSDVRLWNSRKSRLRLIHDGEDEPRSVQIAGGDPAMLAEAAQRNVELGAQIIDINMGCPAKKVCNKAAGSALLRDEALVAEILDAVVRAVDVPVTLKIRTGWDRDNRNGVTVAKLAEQAGIQALAVHGRTRADLYTGEAEYETIAAIKQAVSIPVFANGDIDSPEKARKVIEQTGVDALLIGRAAQGRPWIFREIDHYLRTGEHLPAAPLPEVQSILLEHLAELHLFYGEEMGVRIARKHVGWYLATLPGAREFRAQFNRLQDTDAQCASVRQFF... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Mass (Da): 36411
Sequence Length: 332
EC: 1.... |
Q88BD3 | MHALQAKILDPRIGNEFPLPAYATVGSAGLDLRAMLKEDTLLEPGQTLLIPTGLSIYIGDPGLAALILPRSGLGHKHGIVLGNLVGLIDSDYQGELMVSCWNRGQTAFTIAVGERIAQLVLVPVVQARFELVEEFDESQRGTGGFGHSGSH | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16084
Seq... |
Q6UDM0 | MEATTKKMAMIEIGKGWAASCLEARTCVISNEEDIYAEPRADTPVLKLDSTVRTALPPGYGIVISGTARNHKTAWEIVPGLVDSGYTGLLGLLLVPTDETPATGSAGGGIVSFSRGGVHARLTVIKLVPDDIMGACGAGAQRLPLKTAITSFKGDEDLLGNGFDHCMESLASIYPDILHVQLDCPVYFGCTGCKAFYRRLGSCLETRPLNELGSDHIYLRRGSAYESVNRFAAPDDVMFVAMYGKWLLIGMAETPNEKLTVELRDDDSSPAALIPFHDTFGQKEAEDAGYDIRAPENCTLPPGGSVRVILRQKLHMGKGR... | Function: Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP to avoid uracil incorporation into viral DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 44834
Sequence Length: 414
EC: 3... |
Q9SAF8 | MKMGGSKRRVSSKGLGAVLKEQRAKLYIIRRCVVMLLCWHD | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coor... |
Q6X5T8 | MKTTGSSVGGTKRKMWSRGVGGVVREQKAKLYIIRRCVVMLLCWHD | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coor... |
Q6IM94 | MREKYTKEEAVKNWEKKKNKPSSPKGVGEFLKKKKGRFYIIGKCITMLLCSHK | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Sin... |
Q6IM93 | MSRLRNSAQLQLSKKESLGDNGGALNTTRSSRQKQGKYGFTRKCGRLVKEQRARFYIMRRCVVMLICWTDHNNNNSDHS | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Sin... |
Q6IM92 | MDEKWRLSKKDALAASCSSSSTSSKSKFSRSFSTSASSSKAPAFVRSSSTKCSVPSSSSSSISRSSSKKEKGSITQKYSSLAKEQKGRFYIMRRCVAMLVCWHKHDS | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Sin... |
K9NVA6 | MAAMKKAMKVKKSAKKSAKKSGKKGGMKKKAKRVSKVARGKRAKSSVFRGTKERTSGGLTKNSLVKNKQGRVVSKKQSEHGKKIFKKHGLQKWIDAVTKARKALGIKGFQAVGGSSAKGKILLAKSRSFYKK | Function: DNA-binding protein, which similarly to histones, may compact DNA into chromatin.
PTM: Phosphorylated.
Sequence Mass (Da): 14359
Sequence Length: 132
Subcellular Location: Nucleus
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Q6NPN9 | MQGGSSGIGYGLKYQARCISDVKADRDHTSFLTGTLSLKEENEVHLLRLSSGGSELLCEGLFSHPNEIWDLASSPFDQRIFSTVFSTGDSYGAAIWQIPEPYGQSNSSTLECVASLDAHVGKINCVLWCPSGNSDKLISMDEQNLVFWSLDSSKKSAEVLSKESAGMRHSLSGGAWNPHDVNSVAATSESSIQFWDLRTMKKNNSIERAHVRNVDYNLKREHILVSADDESGIHLWDLRKTKFPVQELPGHTHWTWAVRCNPEYEELILSVGTDSAVNLWFASASSEHKTSESPVEASRQRVNPLLNSYTDYEDSVYGLA... | Function: Component of the CUL4-RBX1-DDB1-DWA1/DWA2 E3 ubiquitin-protein ligase complex that acts as negative regulator in abscisic acid (ABA) signaling. May function as the substrate recognition module within this complex leading to ABI5 degradation. Functionally redundant with DWA1.
Sequence Mass (Da): 39054
Sequence... |
P0DN84 | MAEKAGSTFSHLLVPILLLIGWIVGCIIMIYVVFS | Function: Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity. Does not directly stimulate SERCA pump activity. Enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing ... |
O00148 | MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGM... | Function: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49130
Sequence Length: 427
Subcellular Location: Nucleus
EC: 3.6.4.13
|
Q8VDW0 | MAEQDVENELLDYDEDEEPQAPQESTPAPPKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVSVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEDVLKKNCPHVVVGTPGRILALVRSRSLNLRNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKEIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVVIFVKSVQRCMALAQLLVEQNFPAIAIHRGM... | Function: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49067
Sequence Length: 427
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q185R8 | MKKISILGSTGSIGKQTLDVVRDNRDKFEIVAISANSNIELLLEQIVEFKPKYVTVFEENKALKLKEMLPKNIEIEVLAGMEGLKIISSLDEVDVLLTAVVGMIGLVPTLCAIKKGIDIALANKETLVTAGELVMKEAEKYNVNILPVDSEHSAIFQCLNGENKKNIEKIILTASGGPFRGKKKGELVNITKNEALKHPNWSMGRKISIDSSTLMNKGLEVIEARWLFGVEQENIDVVVHPQSIIHSMVQYTDSSIIAQLGCPDMRLPIQYALTYPDRMESSFERMNFSKFSTLTFEEPDLETFPCLKLAYECLKMGGTY... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 43038
Sequence Length: 384
Pathw... |
Q8NP10 | MGVVTKKILILGSTGSIGTQALDVIADNSDKFEVVGIAAGGSQPDLVISQAQQLGLAADKVAVADAQAAAVISKALGGEIISGTDAAKILVETTKADTVLNALVGSLGLAATLATLESGAHLALANKESLVAGGEFVTSKAKLGQIIPVDSEHSAMAQCLRSGTRDEVARIVLTASGGPFRGWTREKMWEVTPEQAAAHPTWAMGQMNTLNSATLINKGLELIEATLLFETDADLIDVTVHPQSIIHSMITFTDGATIAQASPPSMKLPIALALDWPHRVPKAQPALDFTAAHTWAFEPVDDAAFPAVQLARHVAKQKGT... | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 40958
Sequence Length: 392
Pathw... |
Q3Z8G9 | MHTGLEISIPHNLQMSKLLDTINSPSDLKKLTLDELRELAVQIREELVNRVTLNGGHLASSLGVVELTIALHRVFESPKDKIIWDVGHQSYAHKLLTGRREQFATLRQHGGLSGFTCRDESPHDPFGAGHASTSISAGLGMAVARDLAKEDYSVISVIGDGAISGGMSFEAINNAGHLHTKFIVILNDNGMAISPSTGALSKFLNNVRFDPRFEFAKRGAKQTITNMPFGKSVWAFTKSIKRKFEKSMLPGSLWEELGFIYLGPVDGHNIRELEAALKCAKDFESQPVLIHMITKKGKGYDDAEADAVKYHGIAPKSGGL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q9RUB5 | MNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
B1I3J6 | MGLLDGISHLTDLRALTPDQLDELAAELRDLIVSTVSRTGGHLAPNLGVVELTLALHYVFRAPDDRIVWDVGHQCYVHKILTGRKSQFHTLRQFEGLSGFPNRNESEYDCFGTGHSSTSISAALGMALARDLSGEDRNVVAVIGDGALSGGMAFEALNQAGHLGCRLIVVLNDNEMSIARNVGAMARYLSRLRTDPMYSRSKDEVESLLRRIPAIGPRVLGWIERIKDSLKYLVVAGMLFEELGFTYLGPIDGHNIPAMLNVFRQAQAVEGPVLVHVLTKKGKGYAPAEKNPDKFHGVGPFDPATGNTPTDARVSFTEVF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q72U01 | MQQELTLLDRINYPAELRNIPLEKLPQICKEVRNYIIDTLSGIGGHFASNLGVVELTVALHYVFDTPKDRLVWDVGHQTYPHKILTGRKDKLNTVRKFNGLSGFPKREESPYDLYNTGHAGTSISQALGEAAARDLVKENYNVVAIIGDASIATGMALEAMNHAGHLKKDMIVILNDNYMSISKNVGSISNYLNNIITSHFYNHWKRVFYTFLKWLPIIGPATERFFKKVEKGFKDVLTPGGLFEDLGFGYIGPEDGHDVIRLVKMLEKVKKMKGPILLHIITQKGKGYDPAERDPIKYHGVTPFRKEDGAMDSGDTSKI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q2W367 | MTPPPATGKPSSSLLDRVSSPADIRDFSIEELEQLTYEVRQEMIQSVSFTGGHLGAGLGVAELTVALHHIFDTPRDRLIWDVGHQAYPHKILTGRRGRMRTMRQGGGLSGFTRRSESEYDPFGAGHSSTSISAALGMAVARDLKGATNNVIAVIGDGAMSAGQAYEAMNNAGAAGSRLIVILNDNDMSIAPPVGALSAHLSRLLSSPSYHSLRHLVKDLAHLLPPSLERAVGRAEEYARGMVSGGGTLFEELGFYYVGPIDGHNFEHLLPVLKNLRDSDDTKPVMLHVVTKKGRGYPPAEAAADKYHGVGRFDVLTGQLE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q8EWX7 | MKKNKVKIDKIPNYEDFKKMKLHELLDLAVLLRKKIIDISENKSAHLSSNLGIVELSMALLYVFDSPQDLIAYDTGHQCYVHKMITDRADKISTIRESNGLSGFQEPNESIHDFISTGHSGNILSICQGFIEKNNSKSKSVIPVIGDAAISNGLAFEALNNIAYNKTPMLIIINDNGMSISKNVGALHKIMSKFQMSKSVFLTEKILRKILFKKEWSKKIYWSIYKSFSKLSKFFKGKNFFESLGFHYFGVIDGNNLKKTINVLKRIKNIVPFGPTILHVKTIKGLGYKEAELDDKGLYHSLKLSDPNLNSNNQTYGSVA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequ... |
Q13627 | MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQ... | Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities . Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 . Plays an important role in double-strand breaks (DSBs) repair following DNA damage . Mechanistically, phosphorylates RNF169 ... |
P85051 | QPSISDQQVSALPYSDQIQQPLTNQVMPDIVMLQRRWMDRYEIDSLIGKVEQEWVAIKAFLNQAQIEVRHDTEMKYYIVHLKIVDFGSSCQLGQRIVEVLGIPPAHILDQAPKFFEKLPDGTWSLKKLHNILGVETGGPGGRFKDLILRMLDYDPKIQPYYALQHSFFKQETGIAGHPTYQFSANTGPAHYMTEGHLAMR | Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities . Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Plays an important role in double-strand breaks (DSBs) repair following DNA damage. Mechanistically, phosphorylates RNF169 an... |
Q9Y463 | MAVPPGHGPFSGFPGPQEHTQVLPDVRLLPRRLPLAFRDATSAPLRKLSVDLIKTYKHINEVYYAKKKRRAQQAPPQDSSNKKEKKVLNHGYDDDNHDYIVRSGERWLERYEIDSLIGKGSFGQVVKAYDHQTQELVAIKIIKNKKAFLNQAQIELRLLELMNQHDTEMKYYIVHLKRHFMFRNHLCLVFELLSYNLYDLLRNTHFRGVSLNLTRKLAQQLCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGTPYDLAIDMWSLGCILVEMHTGEPLFSGSNEVD... | Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Plays an essential role in ribosomal DNA (rDNA) double-strand break repair and rDNA copy number maintenance . During DNA damage, mediates transcription silencing in part via phosphorylating and enforcing DSB accumula... |
P00382 | MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFESMGALPNRKYAVVTRSSFTSDNENVLIFPSIKDALTNLKKITDHVIVSGGGEIYKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYSYQIWQKG | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 17575
Sequence Length: 157
Pathway: Cof... |
Q5V3R2 | MTMIPDTELVLVVAADENNVIGLDGGVPWHYPEDVRQYKNRIAGHPIILGRRTFESMKPIPDCYTVVLTSDDRRSADSETVEYATTPQIAVEAAARAGASGAFAGDSAGADSSPPVTYVIGGEAVYDLFLPFAGRVFLSRIHEHNEGDRYFPDLGAEWTELSREPHDGFDVIEYEQASPRPLDDL | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 20284
Sequence Length: 185
Pathway: Cof... |
P00383 | MERSSNEVSNPVAGNFVFPSNATFGMGDRVRKKSGAAWQGQIVGWYCTNLTPEGYAVESEAHPGSVQIYPVAALERIN | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 8446
Sequence Length: 78
Domain: The active site is sit... |
Q5V600 | MCMKLSLIAAVAANGVIGAGGDIPWQYPEDLTHFKETTVGHPVIMGRRTFESIRRDLDGPLPERLNIVLTTTPHQLPDSVTAVTSTTAAVAEAADSDASTTYVIGGATVYEQFLPQADELILTELAAAFDGDTVFPTVDWSNWTEMERTTHSEFAIVRYTRTSSDSA | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 18093
Sequence Length: 167
Pathway: Cof... |
P12833 | MLISLIAALAHNNLIGKDNLIPWHLPADLRHFKAVTLGKPVVMGRRTFESIGRPLPGRRNVVVSRNPQWQAEGVEVAPSLDAALALLTDCEEAMIIGGGQLYAEALPRADRLYLTYIDAQLNGDTHFPDYLSLGWQELERSTHPADDKNSYACEFVTLSRQR | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 18033
Sequence Length: 162
Pathway: Cof... |
P11731 | MKVSLMAAKAKNGVIGCGPHIPWSAKGEQLLFKALTYNQWLLVGRKTFESMGALPNRKYAVVTRSAWTADNDNVIVFPSIEEAMYGLAELTDHVIVSGGGEIYRETLPMASTLHISTIDIEPEGDVFFPNIPNTFEVVFEQHFSSNINYCYQIWQKG | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 17531
Sequence Length: 157
Pathway: Cof... |
P95524 | MKISLMAAVSENGVIGSGLDIPWHVQGEQLLFKAMTYNQWLLVGRKTFDSMGKLPNRKYAVVTRSKIISNDPDVVYFASVESALAYLNNATAHIFVSGGGEIYKALIDQADVIHLSVIHKHISGDVFFPPVPQGFKQTFEQSFSSNIDYTYQIWAKG | Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 17444
Sequence Length: 157
Pathway: Cof... |
Q65200 | MGGSTSKNSFKNTTNIISNSIFNQMQNCISMLDGKNYIGVFGDGNILNHVFQDLNLSLDTSCVQKHVNEENFITNLSNQITQNLKDQEVALTQWMDAGHHDQKTDIEENIKVNLTTTLIQNCVSSLSGMNVLVVKGNGNIVENATQKQSQQIISNCLQGSKQAIDTTTGITNTVNQYSHYTSKNFFDFIADAISAVFKNIMVAAVVIVLIIVGFIAVFYFLHSRHRHEEEEEAEPLISNKVLKNAAVS | Function: Essential for viral fusion with host endosomal membrane and core release.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27462
Sequence Length: 248
Subcellular Location: Host membrane
|
P12827 | MESVQTRLCASSNQFAPFKKRQLAVPVGSVNSLTHTITSTTVTSVIPKNYQEKRQKICHIISSLRNTHLNFNKIQSVHKKKLRHLQNLLRKKNEIIAELVRKLESAQKKTTHRNISKPAHWKYFGVVRCDNTIRTIIGNEKFVRRRLAELCTLYNAEYVFCQARADGDKDRQALASLLTAAFGSRVIVYENSRRFEFINPDEIASGKRLIIKHLQDESQSDINAY | Function: Plays a role in the sorting of ODV envelope proteins to the host inner nuclear membrane. May facilitate the fusion and release of nucleocapsids into the cytoplasm. Modulates the expression levels of IE0 and IE1.
PTM: Palmitoylated.
Sequence Mass (Da): 25910
Sequence Length: 225
Subcellular Location: Host nucl... |
E1BE02 | MEVNCLTLKDLISRPPRLDFAIEDGENAQKENIFVDLSRMAPKTPIKNEPIDLSKQKIFTPERNPITPVKLVDRQQVEPWTPTANLKILISAASPDIRDREKKKELFRPIENKDDVFTDSLQLDAVDDSAVDEFEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYSWHGRHSLPKTLRNLQRLGEKQKYEEQMAHLQQKELNPIDHKSGERRRDGCPDSQDPQLLDFPEPDCPSSSANSRKDKSLKIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQD... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-... |
Q5RIX9 | MQEVKCLTLKDLLGVRTLVNKTGSDDAASMNDHKENICMDRRKMTPLKSESLTAALNGHGKISSPEITHITPIKLTEKAHPDPWTPTANLKMLINAASPDIRDREMKKTLFKPIENKGKIAEEEEEEELDDSCQYEALDESERRPSRKQKSLGLLCQKFLALYPDYPESSESINISLDEVATCLGVERRRIYDIVNVLESLMLVSRKAKNMYVWHGRSRLPQTLQGLLQAGRDQHYDLLMDQREGNGLHAVQHVQNAHAASSRRKDKSLRIMSQKFVMLFLVSKTQTVTLDMAAKILIEEGQEESYDSKYKTKVRRLYDI... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... |
Q6S7F2 | MEVNCLTLKDLISPRQTRLDFAIEDAENAQKENIFVDRSRMTPKTPMKNEPIDLSKQRIFTPDRNPITPVKPVDRQPQVEPWTPTANLKMLISAASPDIRDREKKKELFRPIENKEDAFVNSLQLDVAGDGAVDEYEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRTLQRLGEEQKYEEQMACLQQKELDLMGYRFGERRKDGSPDPRDPHLLDFSEADYPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEES... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-... |
F6YVB9 | MEVTSCLTLKDLISTKKNKSDPVADGRSAQKENMFDRFKISPRLPLRSEPIDLSKQKSFTPERIPVTPVKVAERPQADPWTPTANLKMLISAASPEIRDREKKKELFRPIENNGIEETDTDLQLMDSVDDIDDLEKRPSRKQKSLGLLCQKFLARYPSYPISTEKMTISLDEAASSLGVERRRIYDIVNVLESLHLVSRVAKNQYCWHGQHNLNETLRNLQHIGEKQNYRAQIACFNLRDMGMEYKCDEQEKGCHIDHLNTPLIELSEADCPSVSSSSRKDKSLRIMSQKFVMLFLVSTTKIITLEIAAKILIEESQDAA... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... |
F1QZ88 | MSSTLSEGQTLIKKSLSPSKATSTNNKGHVFVEPQTPLKNSNKASTSEAALPETLKIMGPLTTPTKVLDAPSSDPWTPTSNLKMLISAASPEIRNREKERAVDSSESENSQETEQGEEVEKLHISRKDKSLGLLCYKFLARYPNYPNPALNNGISLDDVAAELHVERRRIYDIMNVLESLNMVSRLAKNRYTWHGRVKLAQTLAVLKRAGKENRYEQLMQQIRQRSQEREEREFDLDGEEKENEEMSSFEVDGDSGLADLPGADSKAASANSRKDKSLRVMSQKFVMLFLVSSPPVVSLDVAAKILIGEDHVVDQDKNKF... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... |
A0AVK6 | MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIAN... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... |
F7EA39 | MEEGSKENCGFNGSPMGSRSPPKQLTSAASVLGEIQIAAANLKTPTKPQERNNADPWTPTANLKMLISAASPEIRNREREILEEQFSGDELEKTLPSRKEKSLGLLCHKFLARYPSYPNPAVNNSICLDEVAGELSVERRRIYDIVNVLESLHMVSRLAKNKYIWHGRLNLSKTFDALKKVGEENRYGEQIQLLRKREQEECDSQNSPNAETQKPLAKQPEVGFVELPGLEFRAASVNSRKEKSLRVMSQRFVMLFLVSDPQIVSLEVAAKILIGEDQLEDLDKSKFKTKIRRLYDIANVLTSLNLIKKVHVTEEKGRKP... | Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... |
Q9FNY0 | MSGVVRSSPGSSQPPPPPPHHPPSSPVPVTSTPVIPPIRRHLAFASTKPPFHPSDDYHRFNPSSLSNNNDRSFVHGCGVVDREEDAVVVRSPSRKRKATMDMVVAPSNNGFTSSGFTNIPSSPCQTPRKGGRVNIKSKAKGNKSTPQTPISTNAGSPITLTPSGSCRYDSSLGLLTKKFVNLIKQAKDGMLDLNKAAETLEVQKRRIYDITNVLEGIDLIEKPFKNRILWKGVDACPGDEDADVSVLQLQAEIENLALEEQALDNQIRQTEERLRDLSENEKNQKWLFVTEEDIKSLPGFQNQTLIAVKAPHGTTLEVPD... | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The binding of retinoblastoma-related proteins represses transa... |
Q9FV71 | MSEEVPQQFPSSKRQLHPSLSSMKPPLVAPGEYHRFDAAETRGGGAVADQVVSDAIVIKSTLKRKTDLVNQIVEVNELNTGVLQTPVSGKGGKAKKTSRSAKSNKSGTLASGSNAGSPGNNFAQAGTCRYDSSLGLLTKKFINLIKQAEDGILDLNKAADTLEVQKRRIYDITNVLEGIGLIEKTLKNRIQWKGLDVSKPGETIESIANLQDEVQNLAAEEARLDDQIRESQERLTSLSEDENNKRLLFVTENDIKNLPCFQNKTLIAVKAPHGTTLEVPDPDEAGGYQRRYRIILRSTMGPIDVYLVSQFEESFEDIPQ... | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The binding of retinoblastoma-related proteins represses transa... |
Q9FV70 | MAATSNSGEDPTLSYHHRSPFRFELLQSISSSDPRYSSLTPSSTNRPFSVSQSLPNSQLSPLISPHWDDSYSQITQKVQKSRKNHRIQLGSIANMSGGESIDIAKVIVKQESSPQNVKRVYNKSKGGTKLLKAGKRMANGEVQNGGLNGASINCRYDSSLGLLTKKFVKLIQEAEDGTLDLNYCAVVLEVQKRRIYDITNVLEGIGLIEKTTKNHIRWKGADNLGQKDLGDQISRLKSEVESMQSEESRLDDLIRERQEALRSLEEDDYCRRYMFMTEEDITSLPRFQNQTLLAIKAPTASYIEVPDPDEMSFPQQYRMV... | Function: Involved in transcriptional repression. May act by repressing E2F-regulated genes in mature differentiated cells, but is not an antagonist of E2FA. Restricts cell division and is involved in the coordination between cell proliferation and endoreduplication during development. May play a role during the transi... |
Q9LFQ9 | MDSLALAPQVYSRKDKSLGVLVANFLTLYNRPDVDLFGLDDAAAKLGVERRRIYDVVNILESIGLVARSGKNQYSWKGFGAVPRALSELKEEGMKEKFAIVPFVAKSEMVVYEKEGEESFMLSPDDQEFSPSPRPDNRKERTLWLLAQNFVKLFLCSDDDLVTFDSATKALLNESQDMNMRKKVRRLYDIANVFSSMKLIEKTHVPETKKPAYRWLGSKTIFENRFIDGSASLCDRNVPKKRAFGTELTNVNAKRNKSGCSKEDSKRNGNQNTSIVIKQEQCDDVKPDVKNFASGSSTPAGTSESNDMGNNIRPRGRLGV... | Function: Inhibitor of E2F-dependent regulation of gene expression. Binds specifically the E2 recognition site as a monomer without interacting with DP proteins. May be up-regulating E2FA and down-regulating repressors of cell cycle progression. Promotes cell proliferation and represses cell elongation. Regulated by pr... |
Q6RUF5 | MGGVTMKNNLKKYIKYILSVILVFFVGVNGMEVYALEESRDVYLSDLDWLNATHGDDTKSKIVQKNHPFTPGNNNQSTKISLKMEDGSISEFEKGLGTIAGSPSTITYDISGAGVTKFFSYLGIDRSANPINEQYAKVDKIEVVVDGKVIYSTINQFPNGLTYETPAIKVDLNIPENAKRLQLKSYAGEKTWGDEVVYADAKFTAKGDFVNPNDWTPAEKRREISNEKPLLMIPLYANGSKYEKGDYAFWGDDTLVGKWKEVPDDLKPYTVIQLHPDDLPKRDGVAADFYEHMLNEAQSYVNPKTNKNEPIPIVLTVYTA... | Function: Endo-beta-galactosidase capable of releasing both the blood group A trisaccharide (A-Tri; GalNAcalpha1-->3(Fucalpha1-->2)Gal) and B trisaccharide (B-Tri; Galalpha1-->3(Fucalpha1-->2)Gal) glycotopes from blood group A- and B-containing glycoconjugates, respectively.
Catalytic Activity: Endohydrolysis of (1->4)... |
P82593 | MSRIRWRYGTAATALLVAAGLVPTATAHAEDVTDYSITVDPAAKGAAIDDTMYGVFFEDINRAADGGLYAELVQNRSFEYSTDDNRSYTPLTSWIVDGTGEVVNDAGRLNERNRNYLSLGAGSSVTNAGYNTGIRVEQGKRYDFSVWARAGSASTLTVALKDAAGTLATARQVAVEGGWAKYRATFTATRTSNRGRLAVAANDAAALDMVSLFPRDTYRNQQNGLRKDLAEKIAALHPGFVRFPGGCLVNTGSMEDYSAASGWQRKRSYQWKDTVGPVEERATNANFWGYNQSYGLGYYEYFRFSEDIGAMPLPVVPALV... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing poly... |
P96463 | MHRGSLSRGQHVRGTRRRGAALAALAALLVATAPAQAAGSGALRGAGSNRCLDVLGGSQDDGALLQLYDCWGGTNQQWTSTDTGRLTVYGDKCLDVPGHATAPGTRVQIWSCSGGRNQQWRVNSDGTVVGVESGLCLEAAGAGTPNGTAVQLWTCNGGGNQKWTGLTGTPPTDGTCALPSTYRWSSTGVLAQPKSGWVALKDFTTVTHNGRHLVYGSTSSGSSYGSMVFSPFTNWSDMASAGQNAMNQAAVAPTLFYFAPKNIWVLAYQWGSWPFIYRTSSDPTDPNGWSAPQPLFTGSISGSDTGPIDQTLIADGQNMY... | Function: Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from ... |
P94522 | MKKKKTWKRFLHFSSAALAAGLIFTSAAPAEAAFWGASNELLHDPTMIKEGSSWYALGTGLTEERGLRVLKSSDAKNWTVQKSIFTTPLSWWSNYVPNYGQNQWAPDIQYYNGKYWLYYSVSSFGSNTSAIGLASSTSISSGGWKDEGLVIRSTSSNNYNAIDPELTFDKDGNPWLAFGSFWSGIKLTKLDKSTMKPTGSLYSIAARPNNGGALEAPTLTYQNGYYYLMVSFDKCCDGVNSTYKIAYGRSKSITGPYLDKSGKSMLEGGGTILDSGNDQWKGPGGQDIVNGNILVRHAYDANDNGIPKLLINDLNWSSGW... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays ... |
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