ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
G5EFT4 | MAPPHPRDPSTAANYEQVTVSHYALKWKVDFEKKHIAGDVSITLDVKQDTERIVLDTRDLSVQSVALNLNGEPKKAGFTLEDNQALGQKLVITTESLKSGDRPVLEIKYESSNNAAALQFLTAEQTTDRVAPYLFSQCQAINARSIVPCMDTPSVKSTYEAEVCVPIGLTCLMSAIGQGSTPSECGKRTIFSFKQPVSIPSYLLAIVVGHLERKEISERCAVWAEPSQAEASFYEFAETEKILKVAEDVAGPYVWGRYDLVVLPATFPFGGMENPCLTFITPTLLAGDRSLVNVIAHEISHSWTGNLVTNFSWEHFWLNE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase which preferentially removes N-terminal Arg and Lys residues from peptides and proteins.
Catalytic Activity: Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
Sequence Mass (Da): 68249
Sequen... |
Q5HAP2 | MINVSFLGLMSGISVLLKTTVIVVGIFEGSNHLEDNGALEGYNDKIMEIVNGYQSFDGKFAEVLPIIGLEKDFPVVVVIGLGKSEDFDENKALKVGGVIYSELNRMKIPDASIVINTDSNVSANIGYGALLRSFKFDKYFVEKKDKNSVYLNKLVLFSKSEPQEVTALFNDLKAEGESIFLARSFVSEPPNILYPETYAQMIYEELSKVGVTVEVFDEDYMKANQMMALLGVGQGSAKKSRLVVMKWNGGDESESPIAFVGKGVTFDTGGISLKPSKGMWDMKYDMAGSASVVGIMRTLAARKAKVNAVGVVGLVENSVD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q8RHT8 | MSFQCVKKYEDSYDKYVLAATSEKVVLPDYLDKESKKIAETIIKKNKFTAKASEKISMTLVNKKKVIEFIIIGLGEKKKLDAKNTRQYLFDGLKNIIGKVLFSFDNKDLDNIDILAEVVEHINYKFDKYFSKKKEEFLEVSYLTDKKVPKLIEGYELAKISNIVKDLVNEQAEVLNPKELADRATKLGKKFGFDVEILDEKKAQKLGMNAYLSVARAAHHRPYVIVMRYKGNAKSKYTFGLVGKGLTYDTGGLSLKPTDSMLTMRCDMGGAATMIGAMCSVAKMKLKKNVTCVVAACENSIGPNAYRPGDILTAMNGKTI... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q74GB4 | MVISVEAADYTAFPCAALLVGCREDNPLEDSLLARIDQLLQGAIASLVQSREITGELNRVTILHTLGRLPAERIVLVGLGNSGALTSDRLRQVGGSAVKALKGAGVTRAASVVHRAAGVPPTSVADIAQGLSLGDYSFDIYKTKPGTTVPVTELVNLFEPGTDTADAERLLAADATICEAVSFARDLVSQPGNVATPLFLAEKALEFSARLGIACTVLDRDEMERQGMEGILSVAKGSHQLPRFIVLEYRGGSADKRPTVLVGKGITFDSGGISLKPREGMERMKDDMAGAAAVMGAVMAVAGLRLPVNVIGLIPAAENL... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferab... |
Q01433 | MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSF... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 94890
Sequence Length: 825
Pathway: Puri... |
Q9DBT5 | MASYPGPGKSKAKYPFKKRAGLQASAAAPEARSGLGASPLQSARSLPGNAPCLKHFPLDLRTSMDGKCKEIAEELFSRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRGLWERDVVLEREFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYEHCEPSAMPGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSF... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 94696
Sequence Length: 824
Pathway: Puri... |
Q01432 | MPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTPVVTGATSLPTPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYHRFPRITSQYLGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFVYDNKKMLEHQEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHA... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 88812
Sequence Length: 767
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
EC: 3.5.4.6
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O80452 | MEPNIYQLALAALFGASFVAVSGFFMHFKALNLVLERGKERKENPDGDEPQNPTLVRRRSQVRRKVNDQYGRSPASLPDATPFTDGGGGGGGDTGRSNGHVYVDEIPPGLPRLHTPSEGRASVHGASSIRKTGSFVRPISPKSPVASASAFESVEESDDDDNLTNSEGLDASYLQANGDNEMPADANEEQISMAASSMIRSHSVSGDLHGVQPDPIAADILRKEPEQETFVRLNVPLEVPTSDEVEAYKCLQECLELRKRYVFQETVAPWEKEVISDPSTPKPNTEPFAHYPQGKSDHCFEMQDGVVHVFANKDAKEDLF... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism. Essential for the transition from zygote to embryo.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 95130
Sequence Length: 839
Pathway: Puri... |
P82974 | MLLDEGWLAEARRVPSPHYDCRPDDENPSLLVVHNISLPPGEFGGPWIDALFTGTIDPNAHPYFAGIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSSYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTNALITRYPAIANNMTGHCNIAPERKTDPGPSFDWARFRALVTPSSHKEMT | Cofactor: Zn(2+) is required for amidase activity.
Function: Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also invo... |
Q54DD0 | MSTPLRGSSPQVSFYESELDQEGGSDASHFTYRNYMEDDKINSFTFNMARKDQTQLFQRIILTNESESEIEEYAEVAEQLLDAINLREKYVFHPKIWKADAPVGEKPPYSPFESDESTNCATEHMFKEVNGVYFVYSNETDMKSNKALFSVPHTLASYYKDINNLMMLSSYGPAKTFTFKRLQLLESKFNMHTLLNDSLELFQQKTAPHRDFYNVRKVDTHVHHSSSMNQKHLLKFIKRKLKENPNEIVIFRDDKYLTLAEVFKSLNLDVDELSVDTLDVHADNNTFHRFDKFNLKYNPCGQSRLREIFLKTDNLIKGKY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia (NH4(+)) . Participates in the regulation of the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation .
Cataly... |
P13016 | MLLEQGWLVGARRVPSPHYDCRPDDETPTLLVVHNISLPPGEFGGPWIDALFTGTIDPQAHPFFAEIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSQYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTRALIDCYPDIAKNMTGHCDIAPDRKTDPGPAFDWARFRVLVSKETT | Cofactor: Zn(2+) is required for amidase activity.
Function: Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also invo... |
P82973 | MLLENGWLVDARHVPSPHHDCRPEDEKPTLLVVHNISLPPGEFGGPWIDALFTGTIDPDAHPFFAEIAHLALSADCLIRRDGEVVQYVPFDKRAWHAGVSMYQGRERCNDFSIGIELEGTDTTPYTDAQYEKLVAVTQTLIGRYPAIADNITGHSDIAPERKTDPGPAFDWSRFHAMLTTSSDKEIT | Cofactor: Zn(2+) is required for amidase activity.
Function: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety.
Catalytic Acti... |
Q84NP7 | MDSTYALHLAVATLLGASFAAASAYYMHRKTLDQLLRFARSLDRDHRRRNRHLLDADDDDDDDPPRDHDRRTTLPIPPGLPPLHTGREGKPIISPASTKRVGPLVRPTTPRSPVPTVSAFETIEDSDDDDENIAPDAKNNAVSLLTNGTIGSDPLPGKASQNGDTKPVPSTNMIRSQSATGSLHGAQHNPVAADILRKEPEHETFSRINITAVETPSPDEIEAYKVLQKCLELREKYMFREEVAPWEKEIITDPSTPKPNPNPFYYEQQTKTEHHFEMVDGVIHVYPNKDAKERIYPVADATTFFTDMHYILRVLAAGDI... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 93854
Sequence Length: 815
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway;... |
P0CL03 | MLPDKGWLVEARRVPSPHYDCRPDDEKPSLLVVHNISLPPGEFGGPWIDALFTGTIDPDAHPFFAEIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSNYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTRTLIASYPAIADNMTGHCNITPDRKTDPGPAFDWPRFRALVALSSHKEMT | Cofactor: Zn(2+) is required for amidase activity.
Function: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety.
Catalytic Acti... |
P50998 | MNMEQEDDQVPAVAAETVPLKRYVTNPGANRDEEVAAAPSSQDTPYFDYAYERSLRHQDAKFLAMNGTQNGRDGLPSKSPRRPSVSASTVRNSDDVNHSKAGPGSGKLLNDTLQSKISSIHMPHVQQGDNAVVSSVGGPETDPGNMETTDPLFSDELAEIYLSIHKCMDMRHKYIRVSLQGELDNPIDDDSWIIYPDCKEGEDDTGLFNFADCKIPGIENEMEYHMDHQGIFQVYENDSAYIAGTPSFHIPTIRDYYIDLEFLLSASSDGPSKSFSFRRLQYLEGRWNMYMLLNEYQELADTKKVPHRDFYNVRKVDTHV... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 95887
Sequence Length: 831
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
Subcellular Location: C... |
P15274 | MDNQATQRLNDLSLEPAPSHDEQDGSGLVIDIDQRKIGDEQAGVVVDDETPPLEQQDSHESLAADSRNANFSYHENQQLLENGTKQLALDEHDSHSAILEQPSHSTNCSSSNIAAMNKGHDSADHASQNSGGKPRTLSASAQHILPETLKSFAGAPVVNKQVRTSASYKMGMLADDASQQFLDDPSSELIDLYSKVAECRNLRAKYQTISVQNDDQNPKNKPGWVVYPPPPKPSYNSDTKTVVPVTNKPDAEVFDFTKCEIPGEDPDWEFTLNDDDSYVVHRSGKTDELIAQIPTLRDYYLDLEKMISISSDGPAKSFAY... | Cofactor: Binds 1 zinc ion per subunit.
Function: AMP deaminase plays a critical role in energy metabolism.
Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+)
Sequence Mass (Da): 93302
Sequence Length: 810
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.
EC: 3.5.4.6
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O25681 | MKGLERESHFTLNENAMFFECAYSCDNALFLQLDDRSFFITDSRYTQEAKESVQPKNGVLAEVVESSDLVQSAIDLIVKSSVKKLFFDPNQVNLQTYKRLNSALGDKVALEGVPSYHRQKRIIKNEHEIQLLKKSQALNVEAFENFAEYVKKIFDEKESLSERYLQHKVKDFLTREGVYDLSFEPILALNANASKPHALPSAKDFLKAEHSILLDMGIKYERYCSDRTRTAFFDPKDFVFKREQSFKDKERQKIYDIVKEAQEKAISGIRAGMTGKEADSLARGVISDYGYGQYFTHSTGHGIGLDIHELPYISSRSETI... | Cofactor: Binds 2 cobalt ions per subunit.
Function: Hydrolyzes the N-terminal amino acid residue from a polypeptide chain, with a preference for substrates containing multiple alanine residues.
Sequence Mass (Da): 40796
Sequence Length: 357
EC: 3.4.11.-
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B6Q8T5 | MTSTDGILAGKYPAKAHARRVVEYLRQNGFQGDGVLYLEAQKTRMIEDNDSEQPFRQRRFFFYLSGCLLPDAHLTYHISTDKLTLFIPPLDPESVIWSGLPLSPAQAKELYDVDEVLYTTDVNPTLAHLASKVGFVFAIDGQISDDVSLKSFPDTDKVALKTAIEECRAVKDAYEVAMIRKANDVTSQAHVAVLKAAKSATNERELEAAFIGTCIAQGCREMAYHPIVASGTSSATLHYVNNDEPLIDSSTNKKKLNLLLDAAGEYKAYCADVTRTFPLSGKFSPESREIYDIVLEMQTESLAMLKEGVLWEDVHITAHR... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Sequence Mass (Da): 51734
Sequence Le... |
C9SEV5 | MASGDNVDYEAVMVDEFDALNIEVRVSAGPSSSVPGAALSAPRCPGMRALPLKAPVMSTPVPAAAPLPTPPAVDDGPSAVGVGNVPPAVDDVPSAVDDVVIQKETTKYSAKLHAAKVADELKASAGLVFLPGEPSRTYEYSDMGPAFSSNAATSSTSPASTSLTPRKVLYNGRVPSIKDVLAASDVDEVRHMQDLPAFLHAYAHQHDKATVYLLDASQSHPALVDNARVHIDTAALRPAMDEARVTKTAHEIALIREANAVSSAAHRAVMRHIRRFASERQVAALFTAECTVRGAPTQAYAPIAGSGPNAATLHYGANDE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Sequence Mass (Da): 60027
Sequence Le... |
A2BJU0 | MPVKGLKVEAASIDPGHDAVILNPRDAEHLGVVAGLRASVVCRGRGVGAVVIVDPRVPERVAQLTKGLVERLGDCDTVDVHPIDVPPSFDAFKKRLSGARLSAAEYKMLIADIVAGYYDDAQIASFLVSQLYSKLADEELEHLIRAMVETGEVVKFGEPVYDVHSIGGVPGNSKVALLVVPIVASRGLLIPKTSSRAITSPAGTADTMEVLAKVAFKPQELHDMALRARGLIVWGGALNLAPADDIFVRVERRIGVDPPTQMVASILAKKLAMSVSRLVIDLPTGRGAKVQDESEAELLASMFLAQAGRLNIAMRVAITF... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
Q12Z64 | MQLKVQPIDVKVGKYKVILNTIDAKELGVHEGDRVRIKNHVTLTAIVDFTEDMISPGMIGLYHEVKEALSKEWTETVEVFPAEKPKSTYIIRKTMDGQKLTKEEIDILVKDIVEENLAEIEIAAFLTATYINDMTDDETEWLTRAMIDSGDKLEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEILAPVEFDAAEIKRMTEEVGGVLVWGGATNIAPADDKLIKVEYPLSIDPHCQMLASIMAKKGAIGADHVVMDIPTGPGTKIKNVQEGRKLARDLINLGDRLGMDVDCALTYG... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
Q2FTS5 | MRLTVRLVDIAARGILLHHNDAKSLGVLAGDRIVISSPVTGKATVDYVETTGTLIDQGRIGVYHHTNEQLTLTENEVVEVRVADRPVSLDYIKKKMEGEKLTREDIRAIVADIVQDTLSPSEITAFVVSSYINQLDMDEIESLTRAMVETGDQLSFHAGPIVDKHSIGGVPGNKISLIVVPIIAASGLLIPKTSSRAITGAGGTADLMEVLAPVEFSASEVQEMTIKTGGVIVWGGATNIAPADDKIIIQEYPFKIDQIGQMIASVMAKKFAVGADVVAIDIPVGKYCKVHTIEEGKKLARQFIDLGERLNMRVECALTY... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
Q6M0E4 | MLFLNAKFIDLDLGENAVIVNEDDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEIGEMTKRIAETGDMISWEKNLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEDEIKRIVKTTNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYSVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLT... | Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic Activity: AMP + phosphate = adenine + alpha-... |
Q9BLG4 | MVAGEIIKGVAAEITNGSSSSVVQKYLDCANQVAPDPGNTTWVLLSTILVLGMMPALAFFEAGLLRSKNTLSIITQIMSGIVVLTVMWQAFGYSLTFGPDQKGIIGNLDHAFLINVSYDDCSPNAPNIPAAAYAFFMMMFANITPLLMTGAFAERVKFKAFIALTVAWEIIVFYPVAHWIWGGGWLHKYFGVLDFAGGIVIHTSAGVSALVIALYVGRRKDFEKYGGEFPPSNLPLATIGAALLWMGWFGFNAGSALAAGNIATSAVASTQIGGSFSAIVWIILSAAKGKPNTVSVINGVIAGLAGITPASGYINSQYSI... | Function: Ammonium transporter that mediates the excretion of ammonium. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49051
Sequence Length: 463
... |
I3R0S7 | MIPLQVDPNVVAQGVNYVWILVVSFLIFFMQPGFALLEAGQVRAKNVGNVLMKNMTDWALGVLVYFVVGAGVATIVGGLTSPGGFDVAAAFSYIGDSGAWIDWLFGAVFAMTAATIVSGAVAERMDFRAYVVFAATITGFIYPVVQGLTWSGGLLSGSGYLGAALGVGYLDFAGATVVHMCGGVAGLVGAKMVGPRKGRFGASGESQPIPGHSMLLAVLGTLILAFGWYGFNVGTQATVLATTESGGLEFMGAALGRVALVTTLGMGAGAVAAMVVSTNYQGKPDPLWMANGLLAGLVAVTGAVPHVTWWGGLVLGALGG... | Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52311
Sequence Length: 516
Subcellular Location: Cell membrane
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Q60366 | MFEVKHMDGIDVFFFMWAASLIFFMKAGFIALEIGQFRAKNVSYHCVLKLLDLAAVFIAYLFIGYGISYGFENIMPLITGTFDADLGAWWMKMVMFAAAAVTIITGGVAERIKILPYFIGALIVGGILYPIVEHLVWGGGFANLGINFHDYAGSGAVHLFGGLVGLMAAYVLGPRIDKYINGKPQAIPGHNIPIAVLGAFILAFGWYGFNIGSASGIANGVELASVAMATTMALAGGIIGGALSSRNDPLYTANGMCAGLVAVCSGVDLFTPIGAFIVGLLAGIQQPFTYKFIEEKLKIDDVCAIGPVHAMSGLIGVICA... | Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41153
Sequence Length: 391
Subcellular Location: Cell membrane
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Q9C0V1 | MSSTTDATPTPSGVNGGDSMTVNLNQFYNNGDVAWILTSTALVFIMIPGVGFFYSGLARRRSAISMLFLSMMSVAIVAFQWFFWGYSLTFSHEGGPYIGSLANFGLRQTLGRPSSGASSVPDILFCVFQGMFAAITPALAIGAAADRGRMFPCMVFMFLWTSIVYDPIAFWTWNPNGWLNKLGSYDFAGGSPVHISSGMAALAYSIVIGKRCDHGTTKYRPHNVPHVVLGTVFLWFGWFGFNGGSSAAANMRGVMAVVVTHLAASVGGIVWCVIDFAKNRHWSVVGFCEGAVAGLVAITPGSGFVPPWAAVVIGALGAVF... | Function: Transporter for ammonium to use as a nitrogen source. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53387
Sequence Length: 497
Subcellular Location: Membrane
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Q84KJ7 | MAAAGAYSASLPAVPDWLNKGDNAWQLTASTLVGIQSMPGLVVLYGSIVKKKWAVNSAFMALYAYASSLLVWVLVGFRMAFGDQLLPFWGKAGVALTQSYLVGRATLPATAHGAIPRTEPFYPEATLVLFQFEFAAITLVLLAGSVLGRMNIKAWMAFTPLWLLLSYTVGAFSLWGGGFLYRWGVIDYSGGYVIHLSSGIAGFTAAYWVGPRLKSDRERFSPNNILLMIAGGGLLWMGWAGFNGGAPYAANIAASVAVLNTNVCAATSLLMWTCLDVIFFRKPSVIGAVQGMMTGLVCITPGAGLVQTWAAVVMGIFAGS... | Function: Involved in ammonium transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51411
Sequence Length: 486
Subcellular Location: Cell membrane
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Q8S230 | MHLRMASPPQPGPYMPDLPAVPAWLNKGDTAWQLVAATFVGIQSMPGLVVIYGSIVKKKWAVNSAFMALYAYASTLIVWVLVGFRMAFGDRLLPFWAKAGPALTQDFLVQRAVFPATAHYGSDGTLETPRTEPFYAEAALVLFEFEFAAITLVLLAGSLLGRMNIKAWMAFTPLWLLFSYTVGAFSLWGGGFLYQWGVIDYSGGYVIHLSSGVAGFTAAYWVGPRLKSDRERFSPNNILLMIAGGGLLWLGWAGFNGGAPYAPNVTATVAVLNTNVSAATSLLTWTCLDVIFFGKPSVIGAVQGMMTGLVCITPGAGLVH... | Function: Involved in ammonium transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53740
Sequence Length: 501
Subcellular Location: Membrane
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G7LAA8 | MNFNSSKYISHLPESLLPNDASPEWNNKADNAWQLTAATLVGLQTVPGLVILYGSMVKKKWAVNSAFMALYAFAAVLVCWVLWAHHMAFGTKLLPFVGKPNFALSQKFLLSKASTNYYLPMADFVFYQFAFAAITLVLLGGSLLGRMNFYAWMLFVPLWLTLSYTVGAFTIWGNGFLEGKIIDYAGGFVIHLSSGVAGFTAAYWVGPRTSNDRQNFPPNNIIHMLGGAGFLWMGWTGFNGGAPFQVGEITSLAIFNTHLCTATSILVWISLDMAVYKKGSLIGSVQGMMTGLVCITPGAGLVDPWAAILMGALSGSIPWY... | Function: Involved in ammonium transport (By similarity). Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme and G.intraradices) in low nitrogen conditions .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53080
Sequence Length: 481
Subcellular Location: Cell mem... |
G7L1W7 | MELPSNLLPDEASPEWMNKGDNAWQLTAATMVGLQSIPGLVILYGSLVKKTWAINSAFMAFYAFASVLLCWVSWAYQMSFGEKMVFFLGKPNVALDEKFLLGKAFLGNFPNATMVFYQGVFAGLTLILIAGALLGRMNIRAWMLFVPLWVTFSYTVVAFSIWCPDGWLAKRGVIDFAGGYVIHLSAGVAGFTAAYWVGPRADKDRETFPAATNNMIMVLAGAGLLWMGWSGFNGGAPFVASTIASLAILNTHVCTAASITVWVMLDTFYFGKPTVFGAVQGMITGLVCITPAAGVVQGWAAILMGFISGSIPWYTMMVLH... | Function: Involved in ammonium transport . May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52393
Sequence Length: 480
Subcellular Location: Cell membrane
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Q9M6N7 | MAGAYDPSLPEVPEWLNKGDNAWQLTAATLVGLQSMPGLVILYASIVKKKWAVNSAFMALYAFAAVLLCWVLLCYKMAFGEELLPFWGKGGPAFDQGYLKGQAKIPNSNVAAPYFPMATLVYFQFTFAAITTILVAGSVLGRMNIKAWMAFVPLWLIFSYTVGAYSIWGGGFLYQWGVIDYSGGYVIHLSSGVAGFVAAYWVGPRPKADRERFPPNNVLLMLAGAGLLWMGWSGFNGGAPYAANLTSSIAVLNTNLSAATSLLVWTTLDVIFFGKPSVIGAIQGMVTGLAGVTPGAGLIQTWAAIIIGVVSGTAPWASMM... | Function: High affinity ammonium transporter that may play an important role in moving ammonium between the apoplast and symplast of cells throughout the plant. Does not transport methylammonium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50768
Sequence Length: 475
Subcellular Location: Cell mem... |
O28528 | MVGRMCVAVLIVLLLVATAGADPNGAETLKENPELPVDFVWALICGFLVMFMQAGFAMLEAGFSRAKNVANVMMKNLMDFAVGSLAFFAVGFALMMGADWQGIAGTTGWFLAGESYDVSTIELWFFMLVFAATAATIVSGSIAERPKFSVYLVYSAVVSAVIYPIYGHWLWGGGWLSSSEFMVKLGGGYGALDFAGSGVVHALGGYIALAAVMLLGPRLGKYDSDGNPRAIPGHNLAFAVIGTFILWFGWFGFNAGSTLSAHELRVSIIASNTNLAAAAGAVTAMAITWLRNGKPDVGMTCNGAVAGLVAITAPCAWVQP... | Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)). Transport is electrogenic.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49591
Sequence Length: 468
Subcellular Location: Cell membrane
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Q20605 | MNTLQNLTLKMDRQPTIRMKPDKQLDCSLSQDDGVWMMASSFIIFTMTAGFGLLESGRVSSKDEVNCMVKNVFDVIFGGLAYWMFGYGLTFGDSKHQLGRYVGFGDFFFDPERVSDDDSTDEKGISYSLFIFQMSFATTTSTIVSAGMSERIHLKSHCFISFFITLVHSVAGHWVWDQEGVFRMMGVVDSAGCSAVHLVGGVSGLVATLYLKPRRNRFAKNGIRTVSDPTKAILGFLMIWWGWLAFNTSSNYAVTHGQWTEGMRSAVGTILASAGGGVVTVIITRLSTKKIQMDMLIDGMLASLVASTGGCLYFTPWQAT... | Function: Involved in the uptake of ammonia (Probable). Implicated in aging.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56840
Sequence Length: 515
Subcellular Location: Membrane
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Q9BLG3 | MEYLELNGTKEGLSAAVDDMWVLNATYLVFYMQAGFCMLEAGVVRAKNAKSIIMKSIIDTAIGSLLFWALGFGLAFGNADKASNPVIGTSHFFLINYQNLSFFAFQWAFCATSITIVSGSLAERVHVTSCLVYTIVMSAFIYPLSAHWVWSYNGWLRMIGFNGIIDFSGSIVVHIVGGCIGLVGTYLVGPRIGRFDSESGKPKPLPGHSITIYTLGAFIIWYGFYGFNTGSTLGISGGGIAIASRSAVTMTIIACASCATTLLAIKIKSGKYDVVKSVNSLLGGLVSSAAVCSLIDPWAAFIIGCVTSFVYLGCSHLLIK... | Function: Ammonium transporter that mediates the excretion of ammonium from the prestalk cells from the slug. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development.
Location Topology: Multi-pass membrane protein
Sequence ... |
B8ZYW3 | MLTALQADLASVVEGVNLVWVLTVTFLIFFMHAGFAMLEAGQVRAKNVANQLTKNLLTWSIGVIVFFLLGAAVSAIVAGLTGGPATTVADAFMGLYAPDASATTAWVDWLFGAVFAMTAATIVSGAVAGRARLRAYLTYTILIAGVIYPVVVGVTWAGGFLNGLGFHDFAGGMIVHGMGGIAGLTAAWIIGPRMNRFNADGSANVIPGHSITFAVLGTLILAFGWYGFNVGTAAAPLAYSDGGVTLGSFAYVGRVALVTTLGMAAGALGAGGVAFYKTGKVDTLYVANGVLAGLVGITAIADDIVWPGALVVGLLAGAQL... | Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46906
Sequence Length: 456
Subcellular Location: Cell membrane
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Q58739 | MWGENIATADLFANATDIHSIVQALTTLANASDVFFLVVMGVLVFMMQWGFAMLEGGQVRKKNVNNVMMKNMVDWLIGCVAWLFIGGILCSKGFDLSAFIDWWKQILGTNWPNNGLDLASWFFGLVFCATAATIVSGGVAERIKFSAYVLISLIITGLLYPLFVYLGPWGASIVPWHDYAGSLVVHGLGGFLALGAIAALGPRIGRFVDGRPVPILGHNIPMAVFGAFALAIGWYGFNVGSSLALGDISGLVCATTTMAMAGGGIGALIASRNDVLFTANGIVAGLVAICSGTDVVSPIGGLIIGLIAGLQVPIVYKLVE... | Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43786
Sequence Length: 420
Subcellular Location: Cell membrane
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Q9US00 | MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGF... | Function: Transporter for ammonium to use as a nitrogen source.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55570
Sequence Length: 512
Subcellular Location: Membrane
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Q84KJ6 | MSGDAFNMSVAYQPSGMAVPEWLNKGDNAWQMISATLVGMQSVPGLVILYGSIVKKKWAVNSAFMALYAFAAVWLCWVTWGYNMSFGHKLLPFWGKARPALGQSFLLAQAVLPQTTQFYKGGGGADAVVETPWVNPLYPMATMVYFQCVFAAITLILLAGSLLGRMNIKAWMLFVPLWLTFSYTVGAFSLWGGGFLFHWGVMDYSGGYVIHLSSGVAGFTAAYWVGPRSTKDRERFPPNNVLLMLTGAGILWMGWAGFNGGDPYSANIDSSLAVLNTNICAATSLLVWTCLDVIFFKKPSVIGAVQGMITGLVCITPGAG... | Function: Involved in ammonium transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53794
Sequence Length: 498
Subcellular Location: Membrane
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O76264 | MFKLALTLTLCLAGSLSLAQHNPHWWGNRNTIVHLFEWKWSDIAQECENFLGPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFGDMVRRCNDVGVRIYVDVLLNHMSGDFDGVAVGTAGTEAEPGKKSFPGVPYSAQDFHPTCEITDWNDRFQVQQCELVGLKDLDQSSDWVRSKPIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYSSLSNLNIDHGFPHNARPFIFQEVIDHGHETVSRDEYKDLGAVTEFRFSEEIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRDAGAVLNY... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Sequence Mass (Da): 55420
Sequence Length: 493
Subcellular Location: Secreted
EC: 3.2.1.1
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Q9ZEU2 | MLTPTQQVGLILQYLKTRILDIYTPEQRAGIEKSEDWRQFSRRMDTHFPKLMNELDSVYGNNEALLPMLEMLLAQAWQSYSQRNSSLKDIDIARENNPDWILSNKQVGGVCYVDLFAGDLKGLKDKIPYFQELGLTYLHLMPLFKCPEGKSDGGYAVSSYRDVNPALGTIGDLREVIAALHEAGISAVVDFIFNHTSNEHEWAQRCAAGDPLFDNFYYIFPDRRMPDQYDRTLREIFPDQHPGGFSQLEDGRWVWTTFNSFQWDLNYSNPWVFRAMAGEMLFLANLGVDILRMDAVAFIWKQMGTSCENLPQAHALIRAF... | Function: Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by g... |
P16266 | MPHHEFECSKVIPERKKHAVIKGKGETLADALPQGYLNTIPGSISERGCAYCGAKHVIGTPMKDVIHISHGPVGCTYDTWQTKRYISDNDNFQLKYTYATDVKEKHIVFGAEKLLKQNIIEAFKAFPQIKRMTIYQTCATALIGDDINAIAEEVMEEMPEVDIFVCNSPGFAGPSQSGGHHKINIAWINQKVGTVEPEITGDHVINYVGEYNIQGDQEVMVDYFKRMGIQVLSTFTGNGSYDGLRAMHRAHLNVLECARSAEYICNELRVRYGIPRLDIDGFGFKPLADSLRKIGMFFGIEDRAKAIIDEEVARWKPELD... | Cofactor: Binds 1 [8Fe-7S] cluster per heterodimer.
Function: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 ... |
P16268 | MSTASAAAVVKQKVEAPVHPMDARIDELTDYIMKNCLWQFHSRSWDRERQNAEILKKTKELLCGEPVDLSTSHDRCYWVDAVCLADDYREHYPWINSMSKEEIGSLMQGLKDRMDYLTITGSLNEELSDKHY | Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]... |
Q46244 | MEDPSKVQLNQLTDYIMKNCLWQFHSRKWDRERQNEGILTKTKQILLGEEVDLSTPADRCYYADALCLADAYKTEYPWINDMSKDELIQLMQQLKDRIDYVTITGSLNAELTDPRY | Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]... |
Q46084 | MTCEVKEKGRVGTINPIFTCQPAGAQFVSIGIKDCIGIVHGGQGCVMFVRLIFSQHYKESFELASSSLHEDGAVFGPCGRVEEAVDVLLSRYPDVKVVPIITTCSTEIIGDDVDGVIKKLNEGLLKEKFPDREVHLIAMHTPSFVGSMISGYDVAVRDVVRHFAKREAPNDKINLLTGWVNPGDVKELKHLLGEMDIEANVLFEIESFDSPHSADGSLVSHGNTHHRGSDRHRQCPTFPEPLRRHQGRRVSAEEIRRSRRSSARPRSHPQYRHLPAEPEEGDGKPIPQSLAHERGVAIDALADLTHMFLAEKRVAIYGAP... | Cofactor: Binds 1 [8Fe-7S] cluster per heterodimer.
Function: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein.
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 ... |
Q8H0F2 | MDQLHVFFFPFLANGHILPTIDMAKLFSSRGVKATLITTHNNSAIFLKAINRSKILGFDISVLTIKFPSAEFGLPEGYETADQARSIDMMDEFFRACILLQEPLEELLKEHRPQALVADLFFYWANDAAAKFGIPRLLFHGSSSFAMIAAESVRRNKPYKNLSSDSDPFVVPDIPDKIILTKSQVPTPDETEENNTHITEMWKNISESENDCYGVIVNSFYELEPDYVDYCKNVLGRRAWHIGPLSLCNNEGEDVAERGKKSDIDAHECLNWLDSKNPDSVVYVCFGSMANFNAAQLHELAMGLEESGQEFIWVVRTCVD... | Function: Specifically glucosylates the 3'-hydroxy group of delphinidin 3,5-di-O-glucoside to produce gentiodelphin. Shows a strict specificity for UDP-glucose as donor.
PTM: The N-terminus is blocked.
Catalytic Activity: delphinidin 3,5-bis-O-beta-D-glucoside + UDP-alpha-D-glucose = delphinidin 3,3',5-tri-O-beta-D-glu... |
P01016 | DRVYIHPFHLLVYS | Function: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.
PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting en... |
P01019 | MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQ... | Function: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.
PTM: Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear leukocytes produces alanine . The resulting peptide form, angiotensin-A, has the same affinity for the A... |
Q6W4T2 | MSPLIKLAASSRLHDATHYVLCPFAGGGSGAFRHWRTLSLENEVISVMLYPGREFRIDDPTVINIGTLAEEMIQALKTCNQRIEDTIIVGHSMGAQVAYEASKKLVNQGLFLKGLIISGCQAPHIKGRRLLGECDDKTFIHNLVEIGGCDPSLAKSPEWWPIFLPALRADFTATEQYIFTSLPNDKEGLPIPTLLISGDQDREANFSEIEEWKLWCNKVVDHLVVEGGHFYITEQPQMMLECIRALSTETTA | Function: Probable thioesterase. Involved in anguibactin production, but is not essential for virulence or iron transport gene expression.
Sequence Mass (Da): 28070
Sequence Length: 252
Pathway: Siderophore biosynthesis; anguibactin biosynthesis.
EC: 3.1.2.-
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P03880 | MRILKSHPLLKIVNSYIIDSPQPANLSYLWNFGSLLALCLGIQIVTGVTLAMHYTPSVSEAFNSVEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGLYYGSYKTPRTLTWAIGTVILIVMMATAFLGYVLPYGQMSLWGATVITNLMSAIPWIGQDIVEFIWGGLYTDEPQCGDVLLKILLNAGKSPILGFAYDLFFIIVLLIGVKIAMTRGKSAGVRSLHTSEASQRLHAGDLTYAYLVGLFEGDGYFSITKKGKYLTYELGIELSIKDVQLIYKIKKILGIGIVSFRKINEIEMVALRIRDKNHLKSFILPIFE... | Function: Mitochondrial DNA endonuclease and mRNA maturase involved in intron homing and required for splicing of the cytochrome b (cobA) gene intron, containing its own coding sequence. The protein stimulates the intrinsic ribozyme activity of the intron through binding to and stabilizing specific secondary and tertia... |
Q02219 | MKRQALAAMIASLFALAACGGEQAAQAPAETPAASAEAASSAAQATAETPAGELPVIDAVTTHAPEVPPAIDRDYPAKVRVKMETVEKTMKMDDGVEYRYWTFDGDVPGRMIRVREGDTVEVEFSNNPSSTVPHNVDFHAATGQGGGAAATFTAPGRTSTFSFKALQPGLYIYHCAVAPVGMHIANGMYGLILVEPKEGLPKVDKEFYIVQGDFYTKGKKGAQGLQPFDMDKAVAEQPEYVVFNGHVGSIAGDNALKAKAGETVRMYVGNGGPNLVSSFHVIGEIFDKVYVEGGKLINENVQSTIVPAGGSAIVEFKVDI... | Cofactor: Binds 1 Cu(+) ion.
Function: Catalyzes the reduction of nitrite to nitric oxide (NO), probably with azurin as electron donor. Essential for growth and survival in oxygen-depleted environments. Can also provide protection against killing by normal human sera.
Catalytic Activity: Fe(III)-[cytochrome c] + H2O + ... |
Q9U6Y9 | MNYYVCLHQEGVNSIPKLIEKAFANNYNVVSTSINANMLPFEPHESDPTYPATILSGSDWNSKVIFTMSDVNVDSPNDKLREHAKEVFMRDVAWAEHLQNVGNLMVRLRGPENENLASIVLAKTKDDFPSGNWFIQVPITNPELATFEHRKDATAEEVAEAESNDPWNWWNNLRMVTKHSTKVKVVIELNDADRPSKETVRRWLGEPIEAIIIPSSLFVRNRSNYCVLKKEWQLIVGHFISVRANIIISTNPNDKALCQYADYVNKLINDNCDKHMLNSYENMLEIPLQPLCDNLDTYTYEVFETDPVKYKLYQDAVQAA... | Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA) (By similarity). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3. Required for arginine sym... |
O14744 | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLE... | Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA . Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRP... |
Q4R5M3 | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKRESIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLE... | Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD... |
Q8CIG8 | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIHPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDVIANAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKVQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLE... | Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA . Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRP... |
Q6YXZ7 | MPLGQRAGDKSESRYCGVEVLDFPAGEELPAVLSHSLSSSFDFLLAPLVDPDYRPTPGSVLPVAASDLVLGPAQWSSHIVGKISEWIDLDAEDEQLRLDSEITLKQEIAWASHLSLQACVLPPPKRSSCANYARVVNHILQGLTNLQLWLRIPLEKSEPMDEDHDGAKDNSDMSDTVDSWEWWNSFRLLCEHSSQLCVALDVLSTLPSMNSLGRWFGEPVRAAILQTNAFLTNARGYPCLSKRHQKLLTGFFNHSVQVIISGRSNHNVSQGGVLSGDENHTEDTAVRHALSPYLDYIAYIYQRMDPLPEQERFEINYRDF... | Function: Methylates arginine residues in proteins such as histone H4.
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 72673
Sequence Length: 649
Subcellular Location: Cytoplasm
EC: 2.1.1.320... |
Q6NWG4 | MSQHATKKRKLDRSTEDYMYFDSYSDVTIHEEMIADTVRTNTYRMGIFKNSKSIEGKVVLDVGAGTGVLSLFCAQAGARKVYAVEASSIADQAVKIVKLNQMEDRIEVIKSTLETIELAEKVDVIVSEWMGYALLHESMLNSVIFARDKWLKPGGLILPSRADLYIAPINDVVVEGRLDFWSTVKGQYGVDMSCMTDFARKCIMNKDITVNPVTVEDVLSHPCKFAELDLNTVTLEQLRDVNGSFSCVCFGSSSIHAFCVWFTVTFPAEEKALVLSTSPFKAETHWKQAVLYLDDAVDVMQDTKVEGEISLYPSEENSRH... | Function: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for... |
Q96LA8 | MSQPKKRKLESGGGGEGGEGTEEEDGAEREAALERPRRTKRERDQLYYECYSDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCAQAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIAPISDQMLEWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLARPQRFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPGGESEKPLVLSTSPFHPATHWKQ... | Function: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA . Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference fo... |
Q2RZV7 | MDALLALHRRSRRTVVGLMSGTSLDGVDAALVQLDGSGPDLTMNPEAFVHIPYPTALRDLIRTNTDPASSSVQDVTRLDARLAETYAAAVDRVAAEADVDRGTVDLVGAHGQTVCHLPEPADCAGKDVRATLQLGNPSTLATRLGVPVVGNFRAADLALGGQGAPLVPYFDRVAFTAPDEARGLLNLGGIANLTVLPAGAAPDDVRAFDTGPANMVIDALAARLFDAPHDPDGRHANAGTPDHDLLADLLEGEYFRREPPKSTGRNDFGPDYVDRLLGAAQSRTLSPEDTMATATLLTAASVYQAYAQYVRPEQAIDELI... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q07YV2 | MSKPEYFIGLMSGTSMDGVDAVLVDFSAEHPVLIASHTEAIPAHLLKGLQRLCQPETDEINRLGRLDRSVGKLFAQAVNHLLAKTTVTAAEVIAIGSHGQTVRHMPNLEMGFTLQIGDPNTIAIETNIDVIADFRRKDIALGGQGAPLVPAFHQQVFAQPGHSRVILNIGGIANITYLPGNSEQVLGFDTGPGNNLIDAFIQQNLNQPFDEDGAWADSGTTHPDLLKQLLSHSYFSLAYPKSTGRELFNRAWLEQQLADYSHLDQQDIQSTLLDLTCHSIANDINKLSPNGELFVCGGGALNKALMQRLATLVPGYKVDT... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q8EHB5 | MNKAYYIGLMSGTSMDGVDAVLVDFAGEQPQLIGTHTETIPTHLLKGLQRLCLPGTDEINRLGRLDRSVGKLFALAVNNLLAKTKIAKDEIIAIGSHGQTVRHMPNLEVGFTLQIGDPNTIATETGIDVIADFRRKDIALGGQGAPLVPAFHQQTFAQVGKKRVILNIGGIANITYLPGNSEEVLGFDTGPGNTLIDAWVQQVKNESYDKNGAWAASGKTDPQLLAQLLSHPYFSLAYPKSTGRELFNQAWLEQQLSAFNQLNEEDIQSTLLDLTCHSIAQDILKLAQEGELFVCGGGAFNAELMQRLAALLPGYRIDTT... | Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in ... |
Q7XJR2 | MATVGSLKPLHHSSCSSSFPRNPIVNRKALLGFVFDSARKNQIRCENLRYSSESDGKRRNAAAKKRNQSPERCAAEGVLTGGGGSEAIAEVRTMMPERIKVVILTACMMCLCNADRVVMSVAVVPLADKLGWSSSFLGVVQSSFLWGYIFSSVIGGALVDRYGGKRVLAWGVALWSLATLLTPWAAAHSTLALLCVRAFFGLAEGVAMPSMTTLLSRWFPMDERASAVGISMAGFHMGNVVGLLLTPLMLSSIGISGPFILFASLGLLWVSTWSSGVTNNPQDSPFITRSELRLIQAGKPVQPSTISPKPNPSLRLLLSK... | Function: Inorganic phosphate and probable anion transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55307
Sequence Length: 512
Subcellular Location: Plastid
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Q66GI9 | MCYSLSIQSSIDFHNRNALKIHGDRAILTSNLPTLRRIPFLPERDRRRKLVLCTGRVVNSLKFTGNTSVDLCGIPRHRLRVSCSDARRTPEETAAELTAQPNFSEFITSERVKVVAMLALALALCNADRVVMSVAIVPLSLSRGWSKSFSGIVQSSFLWGYLISPIAGGTLVDRYGGKVVMAWGVALWSLATFLTPWAADSSLWALLAARAMVGVAEGVALPCMNNMVARWFPPTERSRAVGIAMAGFQLGNVVGLMLSPILMSQGGIYGPFVIFGLSGFLWLLVWLSATSSAPDRHPQITKSELEYIKQKKQISTMENK... | Function: Inorganic phosphate and probable anion transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58243
Sequence Length: 533
Subcellular Location: Plastid
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Q9FKV1 | MKLSNIPQRYVIVFLTFLSTCVCYIERVGFSIAYTVAADAAGINQSSKGTILSTFFVGYACSQVPGGWAAQKIGGRKVLLLSFVLWSSTCFLVPLDPNRVGLLVVARLLVGVAQGFIFPSIHTVLAQWVPPHERSRLVSITTSGMYLGAALGMWLLPALVELRGPESVFLAEALAGVIWSLLWIRYATDPPRSEHPKAAAAGFGGALLPTNVNHHKVTHIPWKKIMLSLPVWAIVVNNFTFHYALYVLMNWLPTYFELGLQISLQGMDSSKMVPYLNMFVFSIVGGFIADYLITKRILSVTRTRKFLNTVGFLIASAALM... | Function: Inorganic phosphate and probable anion transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47166
Sequence Length: 432
Subcellular Location: Golgi apparatus membrane
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Q3E9A0 | MARLTLRPHNHFFSSPIYAHKQPFLSVYTIFPHHHQNPLIKSRVKCSASGTERVRESKKLPPKDPIEDPKPQLPIPEVLSTETGFEQNWPPWKNIPQRYKLIGATSLAFVICNMDKVNLSIAIIPMSHQFGWSSSVAGLVQSSFFWGYALSQLPGGWLSKIFGGRKVLEIGVFTWSFATALVPLLAGFMPGLIFSRILVGIGEGVSPSAATDLIARTIPVKERSRAVGFVFGGLSLGSVMGLLLAPPIIETFNWESVFYLFGLLGVGWFVGFQFLNEEEVSYKGNEISTSHKSENATKEELGSSLKEIPWKSFFQSPAVW... | Function: Inorganic phosphate and probable anion transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56683
Sequence Length: 517
Subcellular Location: Plastid
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D4GSY7 | MTTERPDAGDSGSEKPDETAAPDPAANGARRSKTRLAARSLGHGFGDGAVLEDISLAVEPGEILAVVGPSGTGKTTLFRLLAMFERPDEGTVEVGGDDVWDLPEARRLAVRRRVGMAFQTRSLFSTTVEENVSYGLRVRRSWSARVRDAVEGLFGRDEPSETVRDALRTVGMFDKVGRDAGSLSAGEAQRVAIARALAPDPDVLLLDEPTSNLDPRNTAAIESAMRAARDRGIAVALATHDMQQARRVSDRTAVILGGTCIESGPTDAVFESPDDDRVRQFVEGKLVY | Function: Part of an ABC transporter complex involved in anions import (Probable). Responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30906
Sequence Length: 288
Subcellular Location: Cell membrane
EC: 7.3.2.-
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D4GSY8 | MFALGDLNLTYLVSITAVSLYVSTAAVALSAALGLPISLAVGFRDFYGKSVVTSVISTGMGFPSVVVGLVVLLVLSRSGPLGTFELLFTPEAMILSQTILALPVLVSVSLSAVQSVPQDLRDAAFAAGGTSTDIALLVVREARYGIVTALLAAYGRAISEVGSVLIVGGNIVFSDSTSFTRTLTTAITVEARKGNIETGIALGAILLALVLGVNALGARFRDRTPGRNGRGR | Function: Part of an ABC transporter complex involved in anions import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23860
Sequence Length: 232
Subcellular Location: Cell membrane
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W6QY25 | MSAPKGPITKFPAEGLRHARRFITTHNKEGKGVFAVDDDGDHHRIMVDGLAVANIIYSTSGNPVDMNDDNDLVYARDNEVRRFAGQINLFV | Function: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors . The annullatin backbone 2-hydroxymethyl... |
Q16853 | MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQG... | Cofactor: Binds 1 copper ion per subunit.
Function: Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase... |
O08590 | MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGRLSQPLHCPSVLPSVQPQTHPGQSQPFADLSPEELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLTREYQDIQEMIFHRELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQSGDRATWFGIYYNLSGAGFYPHPIGLELLVDHKALDPALWTIQKVFYQGRYYESLTQLEDMFEAGLVNVVLVPDNGTGGSWSLKSSVPPGRAPPLQFHPEG... | Cofactor: Binds 1 copper ion per subunit.
Function: Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis (By ... |
Q93ZC5 | MIMASSAAASISMITLRNLSRNHQSHQSTFLGFSRSFHNQRISSNSPGLSTRARSTTSSTGGFFRTICSSSSNDYSRPTKIQELNVYEFNEGDRNSPAVLKLGKKPDQLCLGDLVPFTNKLYTGDLTKRIGITAGLCVLIQHVPEKKGDRFEASYSFYFGDYGHISVQGPYLTYEDTFLAITGGSGVFEGAYGQVKLRQLVYPTKLFYTFYLKGVAADLPVELTGKHVEPSKEVKPAAEAQATQPGATIANFTN | Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid.
Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate
Sequence Mass (Da): 27809
Sequence Length: 254
Subcellular Location: Plastid
EC: 5.3.99.6
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Q29437 | MFIFIFLSLWTLLVMGREEGGVGSEEGVGKQCHPSLPPRCPSRSPSDQPWTHPDQSQLFADLSREELTTVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGGQPQPNVTELVVGPLPQPSYMRDVTVERHGGPLPYYRRPVLLREYLDIDQMIFNRELPQAAGVLHHCCSYKQGGQKLLTMNSAPRGVQSGDRSTWFGIYYNITKGGPYLHPVGLELLVDHKALDPADWTVQKVFFQGRYYENLAQLEEQFEAGQVNVVVIPDDGTGGFWSLKSQVPPGPTPPLQFHPQGP... | Cofactor: Binds 1 copper ion per subunit.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
Sequence Mass (Da): 84757
Sequence Length: 762
Subcellular Location: Secreted
EC: 1.4.3.21
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A2XID3 | MAAAAPSRVSVRAAAPGQTGGFAKIRPQVVVAAAARSAGVSGRRARSVRASLFSPKPATPKDARPAKVQEMFVYEINERDRESPAYLRLSAKQTENALGDLVPFTNKLYSGSLDKRLGISAGICILIQHVPERNGDRYEAIYSFYFGDYGHISVQGPYLTYEESYLAVTGGSGVFEGAYGQVKLNQIVFPFKIFYTFYLKGIPDLPRELLCTPVPPSPTVEPTPAAKATEPHACLNNFTN | Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid (JA). Required for the production of JA in response to wounding. Necessary for flower and coleoptile development regulation by light, including blue (BL), red (RL) and far red (FR) lights. Involved in the auxin-mediate... |
P58027 | MASREKTSIEGHMFDVVVIGGGISGLSAAKLLAEHEVDVLVLEARDRVGGRTYTVRNEHVDYVDVGGAYVGPTQNRILRLSKELGLETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTMDNMGKEIPADAPWEAPHAEEWDKMTMKDLIDKICWTKTARRFASLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMERLGDRVKLKRPVTYVDQSDDNIIIETLNHELYECKYVISAIPPTLTAKIHFRPELPSERNQLIQRLPMGAIIKCMMYYKEAFWKKKDY... | Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially o... |
P21397 | MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDY... | Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues . Preferentially ... |
P21396 | MTDLEKPNLAGHMFDVGLIGGGISGLAAAKLLSEYKINVLVLEARDRVGGRTYTVRNEHVKWVDVGGAYVGPTQNRILRLSKELGIETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPLAYLDYNNLWRTMDEMGKEIPVDAPWQARHAQEWDKMTMKDLIDKICWTKTAREFAYLFVNINVTSEPHEVSALWFLWYVRQCGGTARIFSVTNGGQERKFVGGSGQVSEQIMGLLGDKVKLSSPVTYIDQTDDNIIVETLNHEHYECKYVISAIPPILTAKIHFKPELPPERNQLIQRLPMGAVIKCMVYYKEAFWKKKDY... | Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues . Preferentially ... |
Q8LPL6 | MTGMRGLSVFISDVRNCQNKEAERLRVDKELGNIRTCFKNEKVLTPYKKKKYVWKMLYIHMLGYDVDFGHMEAVSLISAPKYPEKQVGYIVTSCLLNENHDFLKLAINTVRNDIIGRNETFQCLALTLVGNIGGRDFAESLAPDVQKLLISSSCRPLVRKKAALCLLRLFRKNPDAVNVDGWADRMAQLLDERDLGVLTSSTSLLVALVSNNHEAYSSCLPKCVKILERLARNQDVPQEYTYYGIPSPWLQVKAMRALQYFPTIEDPSTRKALFEVLQRILMGTDVVKNVNKNNASHAVLFEALSLVMHLDAEKEMMSQC... | Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in ... |
O95782 | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHY... | Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... |
P17426 | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCISLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHY... | Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... |
Q8LPK4 | MTGMRGLSVFISDVRNCQNKEAERLRVDKELGNIRTCFKNEKVLTPYKKKKYVWKMLYIHMLGYDVDFGHMEAVSLISAPKYPEKQVGYIVTSCLLNENHDFLKLAINTVRNDIIGRNETFQCLALTLVGNIGGRDFAESLAPDVQKLLISSSCRPLVRKKAALCLLRLFRKNPDAVNVDGWADRMAQLLDERDLGVLTSSTSLLVALVSNNHEAYSSCLPKCVKILERLARNQDVPQEYTYYGIPSPWLQVKAMRALQYFPTIEDPSTRKALFEVLQRILMGTDVVKNVNKNNASHAVLFEALSLVMHLDAEKEMMSQC... | Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in ... |
Q0VCK5 | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLHRASPDLVPVGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLEAILNKAQEPPKSKKVQHSNAKNAVLFEAISLVTHH... | Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... |
Q86KI1 | MSMNVTNPNIAKTSMRGLTNFISDLRNSPSKENEEKRVTKEMAHIRKEFKENKNIDGYQRRKYVCKLVYMYMLGYELDFGHMEAVTLLSSTKFSEKQIGYIALGILLNEQHEMLPLIINSFKEDLLARSDYFQSLALAAICNIGGKEVAEFLSPLIQKLLIANTSSPMVKKRCALAILRMNRKHIGLVTPDSWVERLVSVLDEPDFGVLTSLMSLLIELASENPIGWEPAIPKVIHLLKKIIINKEFPKEYVYYHVTCPWLQVKLLKFLRYFPAPDDSQGGKVLGEILTAVFAQSESAKAGTVNHKNSLNAVLFEAINLI... | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Location Topology: Peripheral membrane protein
S... |
P17427 | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHD... | Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... |
P91926 | MAPVRGDGMRGLAVFISDIRNCKSKEAEVKRINKELANIRSKFKGDKTLDGYQKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYSEKQIGYLFISVLVNTNSDLIRLIIQSIKNDLQSRNPVHVNLALQCIANIGSRDMAESFSNEIPKLLVSGDTMDVVKQSAALCLLRLFRSSPDIIPGGEWTSRIIHLLNDQHMGVVTAATSLIDALVKRNPDEYKGCVNLAVSRLSRIVTASYTDLQDYTYYFVPAPWLSVKLLRLLQNYNPVTEEAGVRARLNETLETILNKAQEPPKSKKVQHSNAKNAVLFEAINLIIHS... | Function: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP-2alpha is a subunit of the plasma membrane adap... |
Q8D3I0 | MSHYLIGDIHGCYSEFKSMLDLINFNLKNDIIWIAGDFIGRGPDSLKVLRLIYKLKRNIFVVLGNHEINLLLLYAKIKKIKEEDKLTEILNAPDLKILISWLRKQPLLKIDKQKKIIMIHAGIIPKWDMSDLITNSKKVECELKSKNYKKFLKFMYIKNNEHKNIWKNNLPEIIKMRLTLNIITRIRYCISETEIDLLHKEHPEKSPNHLIPWFKFKNNITKNYSIVFGHWSSIKDYKTPKNIYGLDTGCCWKGELTALKWDNKLFFKIKSK | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 32246
Sequence Length: 272
EC: 3.6.1.41
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Q3BX84 | MSVWAIGDLQGCYDITQRLLEKINFDPAQDTLWFCGDLVNRGGQSLETLRLVHSLRAHSVVVLGNHDLSLLAIGARSEEEQRKVNPDLLRIVMAEDRDALLDWLRMQKLAHVDRTLGWMMIHAGLAPKWTTQMAEKHAREVEQQLQGGGYRKLLRNMYGDQPGWSPGLSGYDRSRAIINLFTRMRYCTPRGRIATDDKGTPGTQAQGLYPWFEVPGRVERDLKIVCGHWSALGLTITQGVHAIDTGAVWGGKLTALQLDSEELRVVQVPGREVTGPAPVARAPRRPRERQGRQRSRGNRGNAGNAAAGPKPSVDTPQD | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 35377
Sequence Length: 318
EC: 3.6.1.41
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Q8PCE5 | MSVWAIGDLQGCYDITQQLLEKIRFDPAQDTLWFCGDLVNRGGQSLETLRLVHSLRAHSVVVLGNHDLSLLAIGARSEEEQRKVNPDLQRIVLAEDRDVLLDWLRMQKLAHVDRELGWMMIHAGLAPKWTTQMAEKHAREVEQQLQGGGYRKLLRNMYGDQPGWSPGLSGYDRSRAIINLFTRMRYCTPRGRIATDDKGTPGTQAQGLYPWFEVPGRVERDLKIVCGHWSALGLTITQGVHAIDTGAVWGGKLTALQLDTDELRVVQVPGREVTAPATAPRAPRRPRERQGRQRARGGRGGGNGNGNGGNAAAPAAAPGD... | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Mass (Da): 35713
Sequence Length: 324
EC: 3.6.1.41
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Q66KI8 | MGIPCFYSSLISCLFSIITLVDVGQSSALTLSDSRLHPQSLEKSPWREFQCQHMLKHLHNGARVTVQMPPNIEGHWVSMGCEVRSGPEFITRSYRFYNNNTFKAYQHYYGNNHCTIPTYTLVIRGKIRLRQASWIIRGGTEADYQLHNVQIIPHSETVAEKLTWLVNHTCAGFVPGDMPWEPGISYDLWREEGGFKCTKALNFAMHELQLIRVEKQYMHHNLDHLVEELFLGDIHTDPSQRMYYRPSSYQPPLQNAKNHNQNCVACRIILRSDEHHPPILPAKADLPVGLNGEWVSQRCEVRPEVLFLTRHFIFNDNNHT... | Function: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58943
Sequence Length: 515
Subcellular Location: Cell membrane
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Q5P5G5 | MAIPTLEQKLTWLKPAPASSRELDLAAQIDPAQFEIGFQRTNDILDEGMDVFVRSCRCAMGVAGDSLVAIMTADGDIVNGSCGTYLHAVIPPLIIKYILETYGDEIRDGDLWFANDAVYGGVHNPDQMVCMPVYYEGKLVAWTAALVHTTETGAIEPGGMPVSATTRFEEGMNLPPMRIGENFKLREDVVSMFVAFGLRAPSMIAVDLKARCTTADRVRTRIIELCEREGADYVTGLFRKMLQVAEAGARELIEQWPDGKYRCVTFSDAVGLKQGLVRSCYMTLEKKGDRMLVDLSETGPETPSPYNAHPQAAIAHFSNY... | Cofactor: Divalent metal cations. Magnesium or manganese are required for activity.
Function: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.
... |
P11389 | TVVSQVILKADDELRYPSSGELKSITEFLQTGEQRVRIAQ | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
PTM: Contains one covalently linked bilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 4506
Sequence Length: 40
S... |
P11390 | MTIVSQVILKADDELRYPSGGELKNITDFFKTGEQRLRIAQVLSDSEKKIVDQASRKLWQRRPDFIAPGGNAYGQRQRAQCLRDYGWYLRLITYGVLAGDKEPIESIGLLGAREMYNSLGVPLPGMAEAIRTLKEASLALLSSADATVAAPYFDFLIQGMETI | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
PTM: Contains one covalently linked bilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18130
Sequence Length: 163... |
Q5P5G6 | MEAAGALWRRRMQELARGAGKPHAPLFVPLIMGCAAQIEAIPAIDMVRDGTRLRKNLSELRRMLKLDALTCAVPSCMEAEAVGVEVSQDQWPPRIGTTAQVDVTAEIDADRLAASPRIAAALDAVRQIAVDPGEPVIAAALTGPAALVAQLRAAGVEAGDEAIYDFAGRILATLARLYAEAGVNLLSWHEAARPAEEQDDFWKGALGTAGNVARFHRVPPVLVLPASLAAGPWPAQAVPCPALNHPPLPPVRTHARAWAADPAGWPCLPVEGVAERLILTDAEVPPETEIATLKAQVERVRGE | Cofactor: Divalent metal cations. Magnesium or manganese are required for activity.
Function: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates.
... |
Q9ULZ1 | MNLRLCVQALLLLWLSLTAVCGGSLMPLPDGNGLEDGNVRHLVQPRGSRNGPGPWQGGRRKFRRQRPRLSHKGPMPF | Function: Endogenous ligand for the apelin receptor (APLNR) . Drives internalization of the apelin receptor (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphoge... |
Q9R0R4 | MNLRLCVQALLLLWLSLTAVCGVPLMLPPDGTGLEEGSMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF | Function: Endogenous ligand for the apelin receptor (APLNR). Drives internalization of APLNR (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By simil... |
Q9R0R3 | MNLSFCVQALLLLWLSLTAVCGVPLMLPPDGKGLEEGNMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF | Function: Endogenous ligand for the apelin receptor (APLNR) . Drives internalization of the apelin receptor . Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR . Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an ... |
Q8W4B2 | MEATDIWGEIERSESYLVCSMYEEAESLSSSILKRIFGNIDVLSDEASQGDHQFHDMLESAGMVLVQSLHGIGRTVEIVNELRDVFGEVAAIPVQVLLTGVCLQISNGSYLGVRDILEEFFRIWVYKDNHYILNDAGVSTKGFHAKNCLDIDEYMEVVELYTFGVLAKFSNDMGLAISWVEKAALPEERRQGILRRLHSLLSLKTASSFEENSKDSSYAVVNNKKSLGNEKNDEIDSFLKLSKQHEPWSLWSSHPLSLKVGNTQFSMSRGKVAVSLVGLIICYALKRKRAALIRIIRRQMESTRKAIVDFWKLAFSYQVN... | Function: Involved in peroxisome biogenesis and matrix protein import . Required for pollen maturation and in vivo germination via its role in peroxisomal function, which partially involves jasmonic acid biosynthesis . Transported to peroxisomes via the interaction with PEX19-1 . Required for peroxisomal protein import... |
A9UGV5 | MAGQLKSKIVAVAVAAVVVVASSLVGTASAADAPAPAPTSGATATAAAAPAFAAVSVAAAALGGYLFC | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan.
Location Topology: Lipid-anchor... |
A9UGV6 | MARFSAAAVIAFAVVAAAALATVASAADAPAPAPTSGAVAAVSAPLSVCCVAGLLLALLRH | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan.
Location Topology: Lipid-anchor... |
A9UGV7 | MASRILYAAAVVAAVAVSSLAGVAYAADAPAPSPTSGAAAVSSSLVAAVLCPAVALLLGNLRQ | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan.
Location Topology: Lipid-anchor... |
P23196 | MPKRGKKGAVVEDAEEPKTEPEAKKSKAGAKKNEKEAVGEGAVLYEDPPDQKTSPSGKSATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPVELQELSGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEYDAFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLTDSFRHLYPNTAYAYTFWTYMMNARSKNVGWRLDYFLLSQSVLPALCDSKIRSKALGSDHCPITLYLAL | Function: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA... |
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