ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O35386 | MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDF... | Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon at... |
P0DJQ3 | MERIDSHVSPRYAQIPTFMRLPHDPQPRGYDVVVIGAPYDGGTSYRPGARFGPQAIRSESGLIHGVGIDRGPGTFDLINCVDAGDINLTPFDMNIAIDTAQSHLSGLLKANAAFLMIGGDHSLTVAALRAVAEQHGPLAVVHLDAHSDTNPAFYGGRYHHGTPFRHGIDEKLIDPAAMVQIGIRGHNPKPDSLDYARGHGVRVVTADEFGELGVGGTADLIREKVGQRPVYVSVDIDVVDPAFAPGTGTPAPGGLLSREVLALLRCVGDLKPVGFDVMEVSPLYDHGGITSILATEIGAELLYQYARAHRTQL | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: amidinoproclavaminate + H2O = proclavaminate + urea
Sequence Mass (Da): 33401
Sequence Length: 313
Pathway: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 4/8.
EC: 3.5.3.22
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Q42440 | MSTGISTDLHVHFGALNFSKTYKSGLSNRTVSFSRVGYAQNRKLSCSVSNTENVAPKDDERGKDRPLVKMCGITSARDAAMAVEAGADFIGMIIWPHSKRSISLSVAKDISKVAREGGAKPVGVFVEDDENTILRAADSSDLELVQLHGNGSRAAFSRLVRKRRVIYVLNANQDGKLLNEVPEEDCHLADWILVDSATGGSGHGFNWAQFKLPSVRSRNGWLLAGGINPTNVSEALSILQPDGIDVSSGICGTDGIQKDKSKISSFITAVRSVHY | Function: Catalyzes the conversion of 5-phosphoribosylanthranilate to l-(O-carboxyphenylamino)-l-deoxyribulose-5-phosphate, which is the third step of the tryptophan biosynthetic pathway.
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass... |
P05121 | MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTD... | Function: Serine protease inhibitor. Inhibits TMPRSS7 . Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots . As PLAU inhibi... |
P05120 | MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYEL... | Function: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 46596
Sequence Length: 415
Subcellular Location: Cytoplasm
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P12388 | MEELSMANTMFALNLLKQIEKSNSTQNIFISPWSISSTLAIVLLGAGGNTEQQMAKVLQFNEIGSYGITTRNPENFSGCDFAQQIQKENYPSAILQAQAGDKIHSAFSSLSSTINTPQGDYLLESANKLFGEKSARFKEEYIQLSKKYYSTEPEAVDFLECAEEAREKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSHESIPVQMMFLHAKLNIGYIKDLKTQILELPHTGNISMLLLLPDEIEDASTGLELLESEINFANFNKWISKDTLDEDDVVVYIPKFKLAQSYEL... | Function: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. Not required for normal murine development or survival.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 46292
Sequence Length: 415
Subcellular Location: Cytoplasm
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P29524 | MEELSMANTMFALNLLKQIEQSNSTQNIFISPWSISSTLAIVFLGAQANTEEQMAKVLNFDKIGSYDLTPGNPENFHGCDFAQHIQRDNYPVAILQAQARDKIHSAFSSLSSTINTPRLGDYLLESANKLFGEKSARFKEEYIQRCKKYYSTEPEAVDFLECANEARKKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNTIYFKGRWKTPFQKRLNGLYPFRVNLNESKPVQMMYLREKLNIGYIKDLKTQILELPYIGNISMFLLLPDEIEDSSTGLEMLEREINFDNFNKWISKETLDEDDVLVYIPKFKLAQNYE... | Function: Inhibits urokinase-type plasminogen activator.
PTM: The signal sequence is not cleaved.
Sequence Mass (Da): 47248
Sequence Length: 416
Subcellular Location: Cytoplasm
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Q8LPI9 | MSTGISSDLHLHPRALNFSKTSKSGLSNRKVSFSSVGYAQNRKLSCSVSSTENVAPKDDDRGKDRPLVKMCGITSARDAAMAVEAGADFIGMIIWPHSKRSISLSVAKDISQVAREGGAKPVGVFVEDDENTILRAADSSDLELVQLHGNSSRAAFSRLVRERKVIYVLNANEDGKLLNVVPEEDGHLADWILVDSATGGRYLDQLLSFFALSHCNVFLRGTSYTITLVHETVCLSQVTEISRV | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 26525
Sequence Length: 244
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
Subcellular Location: Plastid
EC: 5.3.1.24
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Q6G5H3 | MTIHKAVKRITASEIRSRKGQEPIVSLTAYQAYSARIADPYCDLLLVGDSVGMVVHGFETTLPVSLDMMILHGQAVMRGSKRALVVVDMPFGSYEESPEQAFSNASRILAETGCSAVKLEGGVYIAETIDFLCKRGIPVMSHVGLTPQAVNRFGGFKTQGRNESNWQQIEADAAAIEKAGAFAVVVEGVVEPLAVKLTQMLSIPTIGIGASSQCDGQILVMEDMLGYGTWVPKFVRRYGVLEQEMEKAIKSYADDVKSRTFPSDEEIYKLKQKSG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q6MHI3 | MKTILDFHDKKSKKQKISMITCYDYSFARIVADSDIDCILVGDSLAMVMLGHSTTLDVSASVMAHHTAAVVRGAGDKFVIADLPFMSYRKGLTANMTAVEKVMKAGAHAVKLEGAAGNLKLVRHLVDSGVPVMGHLGLTPQSVNQLGGFKVQGRDEKAQKKILEAALQLQDAGAFSVVLECVPSKLAKEITAALEIPTIGIGAGVDCDGQVLVLQDMLGMNQGFKPKFVKTYLDGFNTIKGALNQYHQEVSTEIFPSEKESYS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q9JZW6 | MITVNTLQKMKAAGEKIAMLTAYESSFAALMDDAGVEMLLVGDSLGMAVQGRKSTLPVSLRDMCYHTECVARGAKNAMIVSDLPFGAYQQSKEQAFAAAAELMAAGAHMVKLEGGVWMAETTEFLQMRGIPVCAHIGLTPQSVFAFGGYKVQGRGGKAQALLNDAKAHDDAGAAVVLMECVLAELAKKVTETVSCPTIGIGAGADCDGQVLVMHDMLGIFPGKTAKFVKNFMQGHDSVQAAVRAYVAEVKAKTFPAAEHIFAD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q82Y18 | MDQSAAKRMTITTLQNACEQGEKIAVLTCYDATFAAVLEEAGVDILLVGDSLGNVVQGKSSTLPVTLDEMIYHVRCVERGTHRVFIMADMPFGTFQVSPQEAFGNAVRLMAAGAQMVKIEGGQHMAETVEFLSCRGIPVCAHIGLMPQFVHQLGGYRVQGKTPNDARQLREDALLLQEAGAAMLLMELIPAVLGEEITRLLSIPTIGIGAGAACSGQVLVLHDMLGISSGTLPRFVRNFMMDADSIQTAVSNYVEAVKLGAFPAYEHTF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A9A2T9 | MHKSVQDIVNMKKGKKKVSVITGYDYTLASLCDKAGIDVLLVGDSAGMVMLGYENTIPVTMDQMCMFTEAVSRARNNALLVADLPFMSYQASIEDAINNSGKLIKAGADAVKLEGGSIMAETISAIVDVGIPVMGHIGLQPQTTMLSQGYKVQGRTKDSAMQLIQDAKELEEAGVFSIALEMVSHEVAQIISETVSAPTIGIGSGVNCDGQVLVVQDLLGMYDKIKPKFAKRYMNLSEDIVKSLEDYKNDVESNTFPAEENWFSMDPEELKKLREQIGS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q3JCP9 | MGRLTLTKLQKMKRQGEKITMLTAYDASFAALLEAAGVEVLLVGDSLGMVIQGQESTLSVTMDDMVYHCRNVSRGSQCTFILSDMPFMSYATPNQAMDNAARLMREGGAQMVKLEGGRLLGEIVEHLTARGIPVCAHLGLLPQSVHRIGGYRVQGREEISARRIQEDAMILQEAGADMLILECVPARLGSKITDALKIPVISCGAGPYCDGQVLVLYDMLGISPGKSPSFSRNFLEGTSNIPNAIQAYVSAVKKNEFPLLELSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A6Q1X8 | MKKRHTVNTIKSAKNSNKLVMITAYDALFAKLFEPIVDMILVGDSLNMVFAGRSDTLSATLDQMIYHANAVCSGAPSAFVVLDMPYGTYINEKEALQNAIRIYKETDVDAVKLEGGKEKADLIKTLCQNGIAVMGHIGLLPQHVRGQGGYKVVREADRLMEDAKALEEAGVFSIIIEGVKPEVAAKVTDAVQVPVIGIGAGKETDGQVLVWSDMLGFFEDFKPKFVKQYLNGAKLVKEAVSQYAKEVKEGSFPSQEFSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q72LM0 | MRRTVKDFRNAKGQRLVYLTAYDYPTARLAEAAGVDAILVGDSLGMVVLGYPSTVPVTLEEMLHHTKAARRGAPETFLVADLPYLAYATLDRALLAAERLLKEGGADAVKLEGGEEVAEIVRGLVRAGVPVLGHVGLTPQTASQLGGYKLQGRRPEEAERILKGALALEEAGAYGVVLEMVPARLAKEVTERLSVHTVGIGAGPHTDAQVLVFHDVVGLYGDFKPRFVKRYLEAGRLIQEALSRYAQEVREGVFPGEEHSF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q8DM44 | MVRRSVTLPQLQAKKALGEPITMLTAWDYLWARLLDAAGVDVILVGDSLGMVALGYPTTLPVTLDQMIHHAQAVRRGVSHSFLVCDLPFLSYQESPEQALRSAGRLIKEAEVQAVKMEGASPVVQAATRRLVEAGIPVLGHVGLLPQRVHQLGGWRQQGNTPQDAAAILAGALALAEAGVFAVILEHIPAALAQQITAQLKIPTIGIGAGPHCDGQVLVTADVLGLSPQVPPFAKVYADLGTQAIAAIENYCQAVKSRQFP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q10WG3 | MAVTTKQLIQWKQKGRPIVALTAYDYTIAQLLDNAGVDLILVGDSLGMVTLGYETTLPVTLEEMIHHAKAVRRAVKQALMVVDLPFLTYQESPQQAIHSAGRILKETGAQAVKLESGNEAIAQTVKKLTSIGIPVMGHIGLIPQSVHQFGGYPQQGNAPDASARILTEALALAEAGAFALVLEHIKADLAKEITEKVSIPTIGIGAGAYCDGQILVINDVLGLSHWQPPFAKPYVNLRETITQAVKEYSLEVKKRKFPQPPSP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
B3E5K9 | MRKKITIPEILLMKQEGRKVTVLTAYDYPTARLVDAGGVDAILVGDSAGVVFSGHENTLPVTMDEMLYHVKAVVRARPKALVVADMPFMACQSGEIEALKNCGRMLQEGGAEAVKIEGGSNMAPIIRAVTEMDIPVMGHVGLTPQSVHRMGGYKVQGRKDQAERILEDAHAVQEAGAFAVVLEGIPAKLAARITEMLEIPTIGIGAGPACDGQVLVIHDILGLCEKYSPKFVKRYADLAPLITEAARQYVSEVKDGTFPTEEHSFS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q83GK7 | MICMSRKPSPTRRTRIHRFHKGSCGRKLVGLTCYDFSTARVLSDCELDFLLVGDSASGVIYGYENTGSVCLDEIIYLAAGVVRGAPNSFIIVDLPFGTYEKSDELAVETAIEVIKRTGASAVKLEGGARMACRISAIVRAGVPVMGHIGFTPQTINALGGYKIQGRDNADLIYLDAQAVEQAGAFAVVMEMVTEDLAKTITSEIKITTIGVGAGRYTDGQLLVINDLIGLSEKKITFAPRYASIDNTVASCVKLWRKDVLEGNFPQKDHIPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
A5CX20 | MNIEALKVFKESGEKITCLTAYDASFASVFDACGIDIILVGDSLGNVIQGDKNTLDVSMSDMIYHMQAVAKGTQNALRIADMPYQSYTYAEQTLTNAKRLIMAGAQMVKLEGGCEHEASFRILQGNDISVCGHLGLQPQSVVEIDGYRVQGRGKQGANKIIKNALALASWGVKVIVLECVPAELAKQVSQSVSIPIIGIGAGLDCDGQVLVSYDMLGVHVRHVPRFVKNFLTDNGDVKSAVNAFIKAVKDKSFPSKKYSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5... |
Q2T095 | MKVISSIQELRDQLRGQNRTAFVPTMGNLHEGHLSLMRLARQHGDPVVASIFVNRLQFGPNEDFDKYPRTLQEDIEKLQKENVYVLFAPTERDMYPEPQEYRVQPPHDLGDILEGEFRPGFFTGVCTVVTKLMACVQPRVAVFGKKDYQQLMIVRRMCQQLALPVEIVAAETVRDADGLALSSRNRYLSEAERAEAPELAKTLARVRDAVLDGERDLAAIERRAVAHLSARGWQPDYVSIRRRENLVAPSAAQIEAGDPLVVLTAAKLGATRLIDNLEI | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31400
Sequence Length: 279
Pathway: Cofactor biosynthesis; (R)-pan... |
Q1DAN8 | MAPAVLKTVADVKDWTAGLRREGHRLALVPTMGFLHEGHLSLIREGRRRADVVAVSIFVNPTQFGPKEDLSRYPRDFEGDVAKCISAGAQAIFAPAGPEVMYPQGYQTYVEVTDVSQGLCGARRPGHFRGVATVVTKLLTLFRPEVALFGEKDYQQLQVIRALNQDLHLGADIVGMPTVREPDGLAMSSRNAYLSPEERQRALALSRGLKAAQALLREGTRESEPLVAAVRRELEAAGLREDYVELVDAERLTPLASVAPGQPARLLVAAFSGTTRLIDNMQLGGEENAGRV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31778
Sequence Length: 292
Pathway: Cofactor biosynthesis; (R)-pan... |
Q82Y17 | MEIITDIAPLRARLRHEASVAFVPTMGNLHAGHLSLVRIAQKHASCSVVSIFVNRLQFAPHEDFDRYPRTWSDDCRLLEEQGADIVFMPDEKTLYPVPQEFQLLLPPVADTLEGACRPGFFRGVTTVVLKLFNIVQPHIAVFGEKDYQQLQVVHRMVDQLNLPVEIIAGETVRDEDGLALSSRNNYLDATQRQEAGELAHHLKQIRDSIASGERDFPLLEQLAAEKLSKRGWVVDYVAVRQQHTLLPVAASDSSLVILGAAWLNQTRLIDNFLLTLP | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31131
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pan... |
A6Q581 | MQIVHTPRELKEARIALKGSVGFVPTMGALHQGHLSLIEKSKEHNDYTIVSVFVNPTQFLPGEDFEKYPRRYEADKKICELAGVDILFMPQPDTIYSEDEVLVKAPHQKGYVLEGHFRPGHFDGVLQVVNKLFHIVLPTRAYFGKKDAQQLYLIQKMVQDFFMDIEIVPCEIVRDNDGLALSSRNVYLSDAERKKALLISKSLKRAAKMVQSGILDIQEIQKEMQNILQDLKVEYIAFVDRDFRPLQKIQIGKTIILVAAYVGSTRLIDNIWL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31241
Sequence Length: 273
Pathway: Cofactor biosynthesis; (R)-pan... |
Q5Z2U3 | MIDPTLRGAYRPGQLTVHHDPAVLGSVAKALRGVGRTVALVPTMGALHQGHLQIVRQAKRTNQVVIVSIFVNPLQFGAGEDLDKYPRTLDADVELLRAEGVELVFAPNAEQMYPDGPRTTVHPGPLGAELEGASRPTHFAGMLTVVAKLLQIARPHQAFFGEKDYQQLTLIRQMVRDLNFDVRIVAVPTVRESDGLALSSRNRYLDAAQRETALALSAALSAGAHAGGLGAEGVLAAARAVLDATPGLDLDYLELRSSTLGPAPASGNARLLVAAKVGTTRLIDNIAVTLGAPIDGHPNLDSQPEPAGTDPALLPPAR | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 33561
Sequence Length: 318
Pathway: Cofactor biosynthesis; (R)-pan... |
A1SDW7 | MSSAPVLAHTREELATLLAAARARGEQVGLVPTMGALHEGHASLVRAARERVTDDGRMGPVVVSVFVNPLQFGANEDLDRYPRTLEADLEVCAREGADIVFAPSVDEVYPGGPPQVTVRPGPLGKILEGKVRPGHFRGVLTVVAKLFGLVRPDVAVFGQKDYQQLALIRRMVLDLALGVEIVAAETVREDDGLALSSRNRYLEPEQREQAVALSRALLAAQENAGYGAEVALDEARAELRAAPGVDLDYLVITDPDLDELPAVVPPGTPARILVAARVGGTRLIDNLPLMLGTRGPAGEASPPNRERSEPGSAEQNKSPG... | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 35428
Sequence Length: 334
Pathway: Cofactor biosynthesis; (R)-pan... |
P40459 | MKIFHTVEEVVQWRTQELRETRFRETIGFVPTMGCLHSGHASLISQSVKENTYTVVSIFVNPSQFAPTEDLDNYPRTLPDDIKLLESLKVDVLFAPNAHVMYPQGIPLDIEEQKGPFVSVLGLSEKLEGKTRPNFFRGVATVVTKLFNIVMADVAYFGQKDIQQFIVLQCMVDELFVNTRLQMMPIVRNNNGLALSSRNKYLCPESLKISENLYRGLKAAENAIRRLAPGGRLSRSEIIDTVTQIWAPYVDSHDFKIDYVSLADFKTLDELSDVENTSEQQPIVISCAVYVTDREKPDTVVRLIDNIVI | Function: Required for pantothenic acid biosynthesis.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 35032
Sequence Length: 309
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: ste... |
Q9EYU1 | MRKLVAGKLHGIHVTEANLNYHGSITLDPDHCEAAGILPMEFVEIWNKNSGARISTYVILGERGSRCCILNGAAARTCQPDDPIIVCNSIYLDEAHITSLKPRIVTFDQDNHILDRLSYSVDIDTDGRYSFAILDEADEPLVIPALVSGA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q7NDK7 | MLRTVLLGKIHRATVTGACLEYVGSISVDSRLLAAAGILPHEQVHVVNLNNGARLVTYAIEASEGSGAVVLNGAAARLAAAGDQVIVLAYGQGTAVELEHHQPQVVYVDAQNRIVSVHRSVEHAG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
B7K6Z1 | MGKIRLMHAKLHRVRVTEANVGYIGSITIDPQLLDRVGILPLEEVDIVNLNNGKRFSTYVFPGEAGTGEVCPNGGAALLCQPGDLLIIYAYEERDRSEVLQQGHHARVIVADENNQIKQFFHQTLIPTEEGKGVSFHSDEIILNGQPKNNPILSEN | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A1WUU3 | MQLNMLKGKLHQARVTQTELEYEGSCAIDLDLLEAVGIHEYEQIHVYNIENGERFVTYAIIGERGSRMISMNGAAAHKCNEGDRVIICAYAGVPESELGEFQPRLAYLDADNRITQRRGSIPLQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q18HQ3 | MRRWLLKSKLHRARVTGTEKDYEGSISIDAALLSEADIAVGEQVQVVNVTNGERFETYTIEGESRQMELNGAAARLAETGDVIIVISYGLYVKDEQPEPTVLLLDEENRISERE | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q7VJB2 | MQFEMLYSKIHRAKVSDANLNYVGSITIDKTLAQSANLLAGMKVEIVNINNGERFSTYVIYGDKKGEICLNGAAARKVQIGDIIIIIAYATYTHNELEHYKPTIVQVNESNQILSITNEV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
P56065 | MTFEMLYSKIHRATITDANLNYIGSITIDEDLAKLAKLREGMKVEIVDVNNGERFSTYVILGKKRGEICVNGAAARKVAIGDVVIILAYASMNEDEINAHKPSIVLVDEKNEILEKG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q118E6 | MTTIKLMHAKLHRVRVTDAKPDYVGSVTIDSDLLEKVGILPLEEVQIVNLNNGQRWLTYVLPGQAGSGMVCPNGGAALLCKKDDILIIWANEQCDRAEVLENGHKAKIFVADENNHCREFLYQILNPNQGSVEFHSLPVIPEGKTSEYLQQMIETNKI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A5CW02 | MKRIFLSAKLHKVTTTAVELNYEGSCEIDGVLLDAAGIGAFEQIQIYNINNGNRFTTYTILGKDNSGIISVNGAAARKVNVGDVLIIAAYALYSEEELEGYAPRLCYVNNKNILTKISTGSKKSSLY | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q8PLK9 | MHLSLLKAKIHRATVTHSELNYEGSIAIDGLLLEATGIREFEQVHIWDVTNGARFSTYAIRAEDGSGIMSLNGGAARHVQVGDLIIVAAFASMSEDEAKTFKPNLVYVNAHNAISHTNHSIPTQAA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
Q9PGR7 | MQLSLLKAKIHRATVSHSELNYEGSIAIDGLLLEAAGLYEFEKVHIWNVTNGARFTTYAIRAEHGSGIISVNGGAARYVQVGDLVIVAAFAQMSEDEAAVFSPNLVYVDAANAMTHTNHSIPTQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
A1JJN6 | MIRTMLQGKLHRVKVTQADLHYEGSCAIDQDFLEAAGILEYEAIDIYNVDNGQRFSTYAIAAERGSRIISVNGAAARCACVGDKLIICSYVQMSDADARLHHPKVAYFEGENQLQRKAKAVPVQVA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group ... |
P53632 | MGAKSVTASSSKKIKNRHNGKVKKSKKIKKVRKPQKSISLNDENEVEILPSRNEQETNKLPKDHVTADGILVLEHKSDDDEGFDVYDGHFDNPTDIPSTTEESKTPSLAVHGDEKDLANNDDFISLSASSEDEQAEQEEEREKQELEIKKEKQKEILNTDYPWILNHDHSKQKEISDWLTFEIKDFVAYISPSREEIEIRNQTISTIREAVKQLWPDADLHVFGSYSTDLYLPGSDIDCVVTSELGGKESRNNLYSLASHLKKKNLATEVEVVAKARVPIIKFVEPHSGIHIDVSFERTNGIEAAKLIREWLDDTPGLRE... | Function: Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA... |
Q9LW57 | MATSSTFSSLLPSPPALLSDHRSPPPSIRYSFSPLTTPKSSRLGFTVPEKRNLAANSSLVEVSIGGESDPPPSSSGSGGDDKQIALLKLKLLSVVSGLNRGLVASVDDLERAEVAAKELETAGGPVDLTDDLDKLQGKWRLLYSSAFSSRSLGGSRPGLPTGRLIPVTLGQVFQRIDVFSKDFDNIAEVELGAPWPFPPLEATATLAHKFELLGTCKIKITFEKTTVKTSGNLSQIPPFDIPRLPDSFRPSSNPGTGDFEVTYVDDTMRITRGDRGELRVFVIA | Function: Required for plastoglobule development and resistance to multiple stresses. Regulates plastoglobule osmiophilic content. May be involved in the transport of lipophilic antioxidants in and out of the plastoglobule.
PTM: Phosphorylated as part of a basal defense response.
Sequence Mass (Da): 30455
Sequence Leng... |
P00784 | MAMIPSISKLLFVAICLFVYMGLSFGDFSIVGYSQNDLTSTERLIQLFESWMLKHNKIYKNIDEKIYRFEIFKDNLKYIDETNKKNNSYWLGLNVFADMSNDEFKEKYTGSIAGNYTTTELSYEEVLNDGDVNIPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGIHYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHAVAAVGYGPNYILIKNSWGTGWGENGYI... | Function: Cysteine proteinase with a high level of diversity in substrate specificity, an amino acid bearing a large hydrophobic side chain at the P2 position is preferred.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic s... |
Q45066 | MSQPELFHDLPLEEVIGDRFGRYSKYIIQDRALPDARDGLKPVQRRILYAMHTDGNTFDKNFRKAAKTVGNVIGNYHPHGDSSVYEAMVRMSQDWKVRNVLIEMHGNNGSIDGDPPAAMRYTEARLSPIASELLRDIDKNTVEFVPNFDDTSKEPVVLPAMFPNLLVNGSTGISAGYATDIPPHHLGEVIDAVIKRIQMPSCSVDELMEVIKGPDFPTGGIIQGVDGIRKAYETGKGKIIIRGKAEIETIRGGREQIVITEIPFEVNKANLVKKMDEFRIDKKVEGISEVRDETDRTGLRVVIELKKEADAKGILNFLYK... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
O51066 | MDIRTVLKDNFLQYSSYVIKDRAIASVVDGFKPVQRRIIHSLFEMHDGNFHKVANVVGNTMKYHPHGDTSIYEALVNIANKDLFIEKQGNFGNLFTGDPASASRYIECRLTPLAFDVLYSKEITIYESSYDGRNNEPLLYPAKIPVILIQGSEGIAVGMAAKILPHNFNEILNAVKSELLGESYDIYPDFPTGGIVDVNEYADGNGKVLVRAKIETIDEKTIVIRELPFGETTESLISSIEKAIRKNYIKVSSINDFTAENVAIELSLPRGVYASEVIEKLYHYTNCQISISVNLLLLSERYPVVYTIKDLIKFHAAHLQ... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Periph... |
O54478 | MNKPVLPPPGGPDDGDRILDEPLTEALSRRYLAYALSTIGSRALPDVRDGLKPVHRRVLYAMSNMRLNPDAAARKCAKVVGEVMGNFHPHGDASIYDALVRLAQEFSQRIPLVEGQGNFGNIDGDSAAAMRYTECKMTEAAMLLLDGIDEDAVDFRPTYDGQDEEPVVLPSGFPNLLANGSSGIAVGMATSIPPHNAAELIDACQLLLANPDATTADLLEKVPGPDFPTGGVIVESRASLLETYETGRGGVRMRAKWEKEDTGRGTYQIVVTEIPYQVKKSDLVEQLADLIDSKKAALLGDVRDESAEDIRLVLEPKSKN... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
P47446 | MDQKNNNLFQKAIEEVFAVSFSKYAKYIIQDRALPDLRDGLKPVQRRILYGMFQMGLKPTTPYKKSARAVGEIMGKYHPHGDSSIYDAIIRMSQSWKNNWTTVSIHGNNGSVDGDNAAAMRYTETRLSLYGFELLKDIDKKLVSFINNFDDSEKEPTVLPTLLPNLFINGASGIAAGYATNIAPHNTNELLDSLCLRIDQPNCELKQILKIVKGPDFPTGGNVYFEKSLSDIYQAGKGKFIIQAKYEVNKNLNQIEITQIPYETLKANIVKQIEEIIFDNKLSAIESVIDSSDRNGIRIIIKHKDFLPAEKIMAFLFKHT... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
P48374 | MNTQPHASHTDSNTLMLGRYAERAYLEYAMSVVKGRALPEVSDGQKPVQRRILFAMRDMGLTAGAKPVKSARVVGEILGKYHPHGDSSAYEAMVRMAQDFTLRYPLIDGIGNFGSRDGDGAAAMRYTEARLTPIAELLLSEINQGTVDFMPNYDGAFDEPLHLPARLPMVLLNGASGIAVGMATEIPSHNLNEVTQAAIALLKKPTLETADLMQYIPAPDFAGGGQIITPADELRRIYETGKGSVRVRARYEIEKLARGQWRVIVTELPPNANSAKILAEIEEQTNPKPKAGKKQLNQDRLNTKKLMLDLIDRVRDESDG... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
Q9HUK1 | MSESLDLSLEGVERRSLAEFTEQAYLNYSMYVIMDRALPHIGDGLKPVQRRIVYAMSELGLDADSKHKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTEARLSRYSEVLLSELGQGTVDWVPNFDGTLDEPAVLPARLPNLLLNGTTGIAVGMATDVPPHNLREVASACVRLLDQPGATVAELCEHVPGPDFPTEAEIITPRADLQKVYETGRGSVRMRAVYRVEDGDIVIHALPHQVSGSKVLEQIAGQMQAKKLPMVADLRDESDHENPTRIVIIPRSNRVDVEELMT... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
Q59749 | MGQSLLPPSGGDDNIQPVDLKAALEERYLAYALSTIMHRALPDVRDGLKPVHRRIIHAMSEMGLRPNSSFKKCARIVGDVIGKFHPHGDQSVYDALVRLAQDFSQRYPVVDGQGNFGNIDGDNAAAYRYTEAKMTEVAALLLEGIDQDAVDFRPTYNEEDQEPTVLPGAFPNLLANGASGIAVGMATSIPPHNAHELCDAALHLIKHPDATVEDLLFDPANPQRGGIEGPDFPTGGVIVESRASMAESYRTGRGGFRVRARWAVEDLGRGGFQIVVTEIPYQVQKSRLIEKIAELLIARKLPLLEDIRDESAEDVRVVLV... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
Q9ZE79 | MKEAKIENIDFGNALSERYLAYALSTIMSRSLPDVRDGLKPVHRRLLYAMLQLRLEPNSGYKKCARVVGDVIGKYHPHGDVAVYDTLVRLAQHFSLRYPLIDGQGNFGSIDGDNAAAMRYTESRMTEICMLLMEDIDKDTVDFRSTYDDSDLEPVIMPASFPNLLANGSEGIAVGMATNIPPHNLHELCDALLYLIDNPQAGINDIMNFIKGPDFPTGGIIIDKAEVINAAYTTGRGSFRVRSRWEKEELSYGTYQIVVTEIPYQIQKSKLIEQIAILLKDKKIPLISSIRDESTDIIRVVIEPRDRSCDPQIVMESLFK... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane pr... |
P26973 | MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNATAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYAELLLSELGQGTADWVPNFDGTMQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAKAAITLIEQPKTTLDQLLDIVQGPDYPTEAEIITPRAEIRKIYENGRGSVRMRAVWTKEDGAVVISALPHQVSGAKVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMEQVMNHLFATTD... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA . Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Location Topology: Peripheral membrane p... |
Q99LX0 | MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVMICPDTSLEDAKTQGPYDVVVLPGGNLGAQNLSESPMVKEILKEQESRKGLIAAICAGPTALLAHEVGFGCKVTTHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAPLVLKD | Cofactor: Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.
Function: Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stres... |
Q2KHV4 | MAWRGWAQRGWGCGQAWTLPVCGGSYEELTAALAPSRLLRRRFNFFIQQKCGFRKAPRKVEPRRSDTSSEAYKRSALIPPVEETAFYPSPYPIRTLVKPLFFTVGFTGCAFGSAAIWQYESLKSKVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVFVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISTFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAG... | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cl... |
A1Z8R8 | MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMF... | Function: Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function . Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles . Essential for proteolytic processing of Pink1 and HtrA2 into their mature forms ... |
Q9H300 | MAWRGWAQRGWGCGQAWGASVGGRSCEELTAVLTPPQLLGRRFNFFIQQKCGFRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDT... | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals (By similarity). Required for the maturation of PINK1 into its 52kDa mature f... |
Q3B8P0 | MALYSWVQRGWRCGQTWAPLLGGGYRELSATQARQLLGRRFNLLLQQKCGFRKAPRKVEPRRSDTGSSGEAYKRSALIPPLEETVFYPSPYPVRTLLKPFFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGNLRKEINKWWNSLSDGQRTVTGIIAANALVFCLWRVPSLHRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSTSIVNILGQEQFVAVYLSAGVISNFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPVFTFTAGNALKAIIAMDTAG... | Function: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cl... |
Q6UWI2 | MVYKTLFALCILTAGWRVQSLPTSAPLSVSLPTNIVPPTTIWTSSPQNTDADTASPSNGTHNNSVLPVTASAPTSLLPKNISIESREEEITSPGSNWEGTNTDPSPSGFSSTSGGVHLTTTLEEHSSGTPEAGVAATLSQSAAEPPTLISPQAPASSPSSLSTSPPEVFSASVTTNHSSTVTSTQPTGAPTAPESPTEESSSDHTPTSHATAEPVPQEKTPPTTVSGKVMCELIDMETTTTFPRVIMQEVEHALSSGSIAAITVTVIAVVLLVFGVAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS | Function: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
PTM: Highly N-glycosylated and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 32289
Sequence Length: 310
Subcellular Location: Cell membrane
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Q6P9X9 | MVCKALITLCIFAAGLRVQGSPTPTLLPVSLTTKSTAPMATWTTSAQHTAMATTPVASATHNASVLRTTAASLTSQLPTHPREEAVTSPPLKREVNSTDSSPTGFSSNSSGIHLAPTPEEHSLGSPETSVPATGSQSPTLLFSQGPTSASTSPATSPSEPLSASVTSNHSSTVNNIQPTGAPMAPASPTEEHSSSHTPTSHVTEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGAAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS | Function: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
PTM: Highly N-glycosylated and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30729
Sequence Length: 296
Subcellular Location: Cell membrane
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Q8W4C3 | MQRRFLSSISATAGNTKTLNQGRWSVKQVKKSNFHVTLDEIRTSIDSSDFIALSLQNTGSYAAAWHRVSAIDTPQTSYLKAKYAAERYQILQFALCPFSLQGSKLTVHPYNFHLFPRDELKCGMPSYSFSCQASRLTAMAREGFDFNICIYEGISYLSRAQESASKFLSENPILADSVTVSSSPATVADTVFVGRIRSRVKNWRQSCIDSGSKTGDDDLVSSLRRLVLGSEQYGSRLCLTIDVCSERQVQLILEMLTEFSDDVVPLLVASKSRGTQAVRTVFMSSKEDKDLFKRELKDLEKEENRRVRGFREVVDFISSS... | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs (By similarity).
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence ... |
Q9LG26 | MRRHKRWPLRSLVCSFSSSAAETVTTSTAASATAAFPLKHVTRSNFETTLNDLRSLVKAADFVAIDLEMTGVTSAPWRDSLEFDRYDVRYLKVKDSAEKFAVVQFGVCPFRWDSRTQSFVSYPHNFFVFPRQELTFDPPAHEFLCQTTSMDFLAKYQFDFNTCIHEGISYLSRREEEEASKRLKMLHGEDGIDSSGETEELKLVRLADVLFAARMEKLLNEWRSGLLHGGNASSEFPRISNGSNQSMETVFHHMRPALSLKGFTSHQLRVLNSVLRKHFGDLVYIHSNDKSSSSRDIVVYTDSDSDKENLMKEAKDERKR... | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. Essential for early development, possibly by participating in silencing certain maternal mR... |
Q7ZU92 | MEVTRQNFKEVLPEVCNAVQEADFISIDGEFTGISDGPSVSALTNGLDTPEERYTKLRKHSMNFLLFQFGVCTFRYDQNQSTYITKAFNFYIFPKPFSRTSPDIKFICQSSSIDFLASQGFDFNKVFRSGIPYLNQEEECQLREQYEERRGQMNGAGPVSYTPPSGTGVCNVPEDQREFIRSVEEKVEALLKNTDQTLDLEPCTGFQRKLIYQTLNSKYSKGLHVEALETEKKERFIQISKVDDEERRRREQQKQQREQEELNDAVGFSRVIRAISKSGKLVVGHNMLLDVMHTIHQFCGPLPEELDDFKEVAMTVFPRL... | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation ... |
O95453 | MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFP... | Cofactor: Divalent metal cations. Mg(2+) is the most probable.
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence c... |
P21861 | MPGTAEVQVRPGVEEDLKPLTDLYNHYVRETPITFDTEPFTPEERRPWLLSHPEDGPYRLRVATDAESQEILGYATSSPYRAKPAYATSVETTVYVAPGAGGRGIGSLLYASLFDALAAEDLHRAYAGIAQPNEASARLHARFGFRHVGTYREVGRKFGRYWDVAWYERPL | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. The physiological substrate could be a structurally related compound.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin
Sequence Mass (Da): 19205
Sequence Length: 171
EC: 2.3.1.183
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P16426 | MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLDFSLPVPPRPVLPVTEI | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. Can also acetylate demethylphosphinothricin but not PTT or glutamate. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-a... |
Q57146 | MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQRDFELPAPPRPVRPVTQI | Function: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance.
Catalytic Activity: acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin
Sequence Mass (Da): 20618
Sequence Length: 183
E... |
A0A1U8QHE3 | MTCADVTDLCTQASQLVQQLRTKDGELGFMSAAVYDTAWVSMVQKTTPEGRQWLLPKCFEYILRTQLEDGSWETYASDVDGILNTAASLLALETHAESRIASTDPPVEEMKERIGRARAALSRQLQAWSVKDTVHVGFEIILPALLRLLREKGHEFEFDGRAELDRLNRIKLSKFRPEYLYSARTTALHSLEAFVGMIDFDKVAHQKVNGSFMFSPSSTAAFLMFSSSWDDECEQYLRLVLQNGAGGGTGGMPSAYPSKYFEVSWVRGQLARLESKLTELQALTTLLDNGYSTGDLGIEDTDSLGEMLRDALVKGGGIVG... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The g... |
A0A1U8QLG8 | MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEG... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors... |
C8VN86 | MPESQIIELGTLGQIPLYSLERALQDPLRAVKLRRQIVSQHQATGNIDFTTDGSALPYEGYDYKAVLGACCENVIGYMPIPVGVAGPIKINGKMVFLPMSTTEGALVASTNRGCMAINAGGGVTALVLGDGMTRAPIVRFPSLEEAGAAKQWLGSDAGFLIIEDAFNASSRFARLQNIKATAVGSDLYIRFTASTGDAMGMNMISKGVEQALEAMQKHGFESMDVVSLSGNFCADKKPAAVNWIEGRGKTVTAQATIPEHAVRETLKTSVEALVELNVSKNLVGSAVAGALGGFNAHAANVVTAIYLATGQDPAQNVQSS... | Function: 3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophospha... |
A0A1U8QXK4 | MNTLNAPRNPTRHPAMTADTLVDAPALPHQNGSTEEKLKERGSFGKLYTYKRSPRALGIQAVAKSIGLELEQVELQPANGVPDFYWNLNPLGKTPTFVGADGLVLTECMAIALHVTNEDSTTTLLGSSSLDFVQIIRWISFTNTDVVTRMASWVRPLIGYTPYSKEEVLKAQQQTTQAIGVFEDSLRDRKYLVGDRLTLADIMCVSLVSFGFAQIFDKEWREAFPYFSGWYMMVMHLPIMKAVVEEVPFVEEGLPNAPPTEPFRAP | Function: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1... |
A0A1U8QP15 | MVSLKTVQASNAGLRALPNITALFVGGTSGIGQSTLRQLARYADSPTAYIIGRNEARTRPFLSELQQLNPKGRFHFIEADVSLVRNVDAACQQILQQQKKLNFLFMTPGGISLGGRNETVEGIDYLFALRYYSRMRFIQNLLPLLEASSPSRVISVYGGGFEYSINTADLDLKHNFSLLNAYKHSITMTSLSMEHLARTHPAVSFIHVYPGLVGTNIYTNSFPAPVSTFYNYLVWPFMKPFSVDLGESGERHLFHLSSAHYPAKQGIVPQGVPLEAGEVAKGITGEPGSGAYLLNWKGDVRPSTKILAQYREQKIPQLVW... | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is need... |
A0A1U8QJR1 | MVDATSPPGVNAVVNYYVPNSDGSPPATNDMAVMLGQKDMISHKMRIRDLRPYKEEYSLDRNGFQYATIHSTLTDATDETQIKEVYYREIEKLVQDITGAKRVLAFHHAVRTRTGNEFGEQIKDRYQGVEGPAYRVHIDQTPQGALSIVQFMFPDLADDVRNGSFQVINVWRPLTRVQRDPLMVADAAEMPPEDLLLISRKYYNGLHSSNFVIKYDGRMAAGEGPTDGLSGDGKHSWWYIGDQEPTEALVFSSSGFRNGKAIIGTAHDLYSAEPMINAYERKNASSLYGHDESQI | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is need... |
C8VN91 | MDNYTWHSGTLIPSDSPSSIDRSQLYLEILGVLSVVYLLQTLVAYSKSFKAPFVGFRFWYEPKWLVGLRFSQGALAQVNEGYAKYKNAMFKVARNDSDILVIPNKYVEELRSLPDEKISAIRAHIKNLLGKYSTTLILLESDLHTRMLQTKLTPNLGSFIEVIESELLFAMDQEIPANLDDWQSVNVFHIVLRIVARISARVFLGVPACRNEEWLQTSIHYTENVFATVMLLRRFPKWMHPIVGHLLPSYWAIHRNLRTAKRIISPMVRQRRAEEAKRNPDYVKPNDLLQWMMDGANENDGQPDKLAHRQLLLSLASIHT... | Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) . Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors . The geranylgeranyl pyrophosphate (GGPP) synthase... |
Q9FE20 | MGCFSCFDSSDDEKLNPVDESNHGQKKQSQPTVSNNISGLPSGGEKLSSKTNGGSKRELLLPRDGLGQIAAHTFAFRELAAATMNFHPDTFLGEGGFGRVYKGRLDSTGQVVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEFMPLGSLEDHLHDLPPDKEALDWNMRMKIAAGAAKGLEFLHDKANPPVIYRDFKSSNILLDEGFHPKLSDFGLAKLGPTGDKSHVSTRVMGTYGYCAPEYAMTGQLTVKSDVYSFGVVFLELITGRKAIDSEMPHGEQNLVAWARPLFNDRRKFIKLAD... | Function: Protein kinase required for plant defense mechanism mediated by the disease resistance (R) protein RPS5. In case of infection by Pseudomonas syringae, AvrPphB triggers RPS5-mediated defense mechanism via the cleavage of PBS1. Both kinase activity and cleavage by avrPphB are independently required to trigger t... |
P08018 | MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHYNNINADLHARVKAFQEQRALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSKSTLKNVLDNQETQNITDVNINIDTTKITATTIGVNTGLPATDITPSVSNTASATHKAQLLNPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSGGGGLFAN... | Function: Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.
PTM: Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.
Catal... |
Q9XUV0 | MWGETFDDFENDEGEMAMAKQNLIAEPARADFTFAKLPLGIQPVDFMKTHFAETAGKSMQFRKGTTTLAFVYEPATPADKGGIIVAVDSRASSGEYISSKSVMKILDIGDRMVATMAGGAADCQFWTRIVAKYCTLYELREKTSITVSAASKYFANTLYGYRGQGLSVGSMVAGYDKKGPQIFKVDSEGDRCQLKVCSVGSGSLNAYGILDNHYKPKMTDDEARKLGLRAIMHATYRDSGSGGVCNLCHITPTEKIRLPPMDVSKLWYEFADELGRDITYNPVE | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins . This complex plays numerous essential roles within the cell by associating with different regulatory particles (By similarity). Associated with two 19S regulatory particles, forms the 26S prot... |
Q08017 | MSASRFMLRPLTRALLMHGATRTRLAGTGLGLALTLTAAPYVQAQEWTLNIPSQPLAQALQTLGQQTSLQIIYSPESLQGLRSTALNGRYQDDESLKAMLNGTGIRYQRDGNTVTVLGPATGSAMELAPTNVNASRLGATTEGSNSYTTGGVTIGKGVHSLKETPQSVTVMTRKMLDDQNLNTIEQVMEKTPGITVYDSPMGGKYFYSRGFRMSGQYQYDGVPLDIGSSYVQADSFNSDMAIYDRVEVLRGAAGMMKGAGGTAGGVNFVRKRGQDTAHTQLSLSAGTWDNYRGQVDTGGPLNDSGTIRGRAVVTEQTRQY... | Function: Specific receptor for the siderophore ferric pyoverdine (pseudobactin) M114.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90388
Sequence Length: 826
Subcellular Location: Cell outer membrane
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Q797E3 | MNFKVFLLAASTIAVGLVELIVGGILPQIANDLDISIVSAGQLISVFALGYAVSGPLLLALTAKIERKRLYLIALFVFFLSNLVAYFSPNFATLMVSRVLAAMSTGLIVVLSLTIAPKIVAPEYRARAIGIIFMGFSSAIALGVPLGILISDSFGWRILFLGIGLLALISMLIISIFFERIPAEKMIPFREQLKTIGNLKIASSHLVTMFTLAGHYTLYAYFAPFLEETLHLSSFWVSICYFLFGISAVCGGPFGGALSDRLGSFKSILLVTGSFAIIMFLLPLSTSSMIFFLPVMVIWGLLSWSLAPAQQSYLIEIAPD... | Function: Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine, 6-mercaptopurine and 2-fluoroadenine. Therefore plays a role in maintaining the cellular purine base pools and prote... |
O34987 | MKTFFQFDELGTSYRNEIIGGLTTFLSMAYILFVNPITLALESVKDFPEALRIDQGAVFTATALASAAGCILMGLIARYPIAIAPGMGLNAFFAFSVVLGMGISWQAALSGVFISGLIFVALSLTGFREKIINAIPPELKLAVGAGIGLFITFVGLQGSGIITANPSTLVTIGNIHSGPVLLTIFGVIVTVILMVLRVNAGVFIGMLLTAVAGMIFGLVPVPTQIIGSVPSLAPTFGQAWIHLPDIFSVQMLIVILTFLFVGFFDTAGTLVAVATQAGLMKENKLPRAGRALLADSSSIVIGAVLGTSTTTSYVESSSGV... | Function: Involved in the uptake of the purine bases hypoxanthine and guanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46191
Sequence Length: 440
Subcellular Location: Cell membrane
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O34978 | MFHLKEQQTSIKQEIIAGLTTFFTMVYIVVVNPVILANAGVPFDQVFTATIIASIVGTLWMALAANYPIAIAPGMGLNAYLAFHVVSASDGGITYATAFSAVFTAGVLFIILSLTPLRKQLIEAIPNNLKYGITTGIGLFIAFIGLRQAGIVAADESNLVTLGNLHSPGVILTLVGLLISVVLMVLNVSGALFIGMAATALIAFFTGQLHFSKGFMSLPHLPEGLMISNPFTAFGDVIHHGLYAVVFSFLLVTIFDTTGTMIGVAEQAGLMKNNKLPNVRKALLADSTATTVGAVFGTSPTTAFIESSAGVAAGGRTGLT... | Function: Involved in the uptake of the purine bases hypoxanthine and guanine. May work at purine concentrations higher than 100 uM.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45420
Sequence Length: 432
Subcellular Location: Cell membrane
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P42086 | MRNGFGKTLSLGIQHVLAMYAGAIVVPLIVGKAMGLTVEQLTYLVSIDIFMCGVATLLQVWSNRFFGIGLPVVLGCTFTAVSPMIAIGSEYGVSTVYGSIIASGILVILISFFFGKLVSFFPPVVTGSVVTIIGITLMPVAMNNMAGGEGSADFGDLSNLALAFTVLSIIVLLYRFTKGFIKSVSILIGILIGTFIAYFMGKVQFDNVSDAAVVQMIQPFYFGAPSFHAAPIITMSIVAIVSLVESTGVYFALGDLTNRRLTEIDLSKGYRAEGLAVLLGGIFNAFPYTAFSQNVGLVQLTGIKKNAVIVVTGVILMAFG... | Function: Transport of xanthine in the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46238
Sequence Length: 438
Subcellular Location: Cell membrane
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P40424 | MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHG... | Function: Transcription factor which binds the DNA sequence 5'-TGATTGAT-3' as part of a heterodimer with HOX proteins such as HOXA1, HOXA5, HOXB7 and HOXB8 . Binds to the DNA sequence 5'-TGATTGAC-3' in complex with a nuclear factor which is not a class I HOX protein . Has also been shown to bind the DNA sequence 5'-ATC... |
O60330 | MIPARLHRDYKGLVLLGILLGTLWETGCTQIRYSVPEELEKGSRVGDISRDLGLEPRELAERGVRIIPRGRTQLFALNPRSGSLVTAGRIDREELCMGAIKCQLNLDILMEDKVKIYGVEVEVRDINDNAPYFRESELEIKISENAATEMRFPLPHAWDPDIGKNSLQSYELSPNTHFSLIVQNGADGSKYPELVLKRALDREEKAAHHLVLTASDGGDPVRTGTARIRVMVLDANDNAPAFAQPEYRASVPENLALGTQLLVVNATDPDEGVNAEVRYSFRYVDDKAAQVFKLDCNSGTISTIGELDHEESGFYQMEVQ... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 100955
Sequence Length: 932
Subcellular Location: Cell membrane
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Q9Y5G2 | MKASSGRCGLVRWLQVLLPFLLSLFPGALPVQIRYSIPEELAKNSVVGNLAKDLGLSVRDLPARKLRVSAEKEYFTVNPESGDLLVSDRIDREQICGKQPLCVLDFDTVAENPLNIFYIAVIVQDINDNTPLFKQTKINLKIGESTKPGTTFPLDPALDSDVGPNSLQRYHLNDNEYFDLAEKQTPDGRKYPELILKHSLDREEHSLHQLVLTAVDGGDPPQSGTTQIRIKVTDANDNPPVFSQDVYRVTLREDVPPGFFVLQVTATDRDEGINAEITYSFHNVDEQVKHFFNLNEKTGEITTKDDLDFEIASSYTLSIE... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 100875
Sequence Length: 931
Subcellular Location: Cell membrane
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Q9UN71 | MGSGAGELGRAERLPVLFLFLLSLFCPALCEQIRYRIPEEMPKGSVVGNLATDLGFSVQELPTRKLRVSSEKPYFTVSAESGELLVSSRLDREEICGKKPACALEFEAVAENPLNFYHVNVEIEDINDHTPKFTQNSFELQISESAQPGTRFILGSAHDADIGSNTLQNYQLSPSDHFSLINKEKSDGSKYPEMVLKTPLDREKQKSYHLTLTALDFGAPPLSSTAQIHVLVTDANDNAPVFSQDVYRVSLSENVYPGTTVLQVTATDQDEGVNAEITFSFSEASQITQFDLNSNTGEITVLNTLDFEEVKEYSIVLEAR... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99927
Sequence Length: 923
Subcellular Location: Cell membrane
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Q9Y5G0 | MGSGAGELGRAERLPVLFLFLLSLFCPALCEQIRYRIPEEMPKGSVVGNLATDLGFSVQELPTRKLRVSSEKPYFTVSAESGELLVSSRLDREEICGKKPACALEFEAVAENPLNFYHVNVEIEDINDHTPKFTQNSFELQISESAQPGTRFILEVAEDADIGLNSLQKYKLSLNPSFSLIIKEKQDGSKYPELALEKTLDREQQSYHRLVLTALDGGHPPLSGTTELRIQVTDANDNPPVFNRDVYRVSLRENVPPGTTVLQVSATDQDEGINSEITYSFYRTGQIFSLNSKSGEITTQKKLDFEETKEYSMVVEGRDG... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99875
Sequence Length: 923
Subcellular Location: Cell membrane
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Q9PP01 | MKKFDKLGLDNIKEIFHNLSYDELNAHEKANNEGLSTDNDTFCVDTGIFTGRSPKDKYFVKQDPSSKYIAWGKVNQPITKELFDKLLTKAKQELSGKKIYVQDVFCGASLQSRKAVRFVTEIAWQAHFVKNMFIRPSQEELENFKADFIVYNACKCINEDYKQDGLNSEVFVIFNVEENIAVIGGTWYGGEMKKGIFSMMNYWLPLENKLSMHCSANVGEKDDVALFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDEGVFNFEGGCYAKTINLDPEHEPEIYGAIKRNALLENVVLRADKSVDYADASKTENTRVSYPIE... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
Q21BR2 | MQETGVRNGAYGADKFGLKNLKGVKWNLTAPHLYEDALRAGEGVLSGDGSLCVDTGIFTGRSPKDKYTVRDANTENTMWWGGNQSITAEQFENLYQDFLKHAEGMSLFAQDLYGGADPSFQIKTRVFTEMAWHSLFIRTLLRRPETAELASFVPELTIIDLASFRADPARHGCKSENVVAIDFTRKIVLIGGTQYAGEMKKSVFTTLNYYLPDKGVLPMHCSANVGPDGDTAIFFGLSGTGKTTLSADPNRTLIGDDEHGWGKDGVFNFEGGCYAKCIKLSAEAEPEIFAASNRFGAILENCVLDPITRKPDFNDGSKTE... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
Q13E86 | MQETGVHNGAHGADKFGLKNLKGIYWNFGAPQLYEHALRNGEAVLSADGALVADTGVFTGRSPKDKFTVRDATTETTMWWGGNQSITAEQFETLYQDFIKHAEGMTLFAQDLYGGADPSFQIKTRVFTELAWHSLFIRTLLRRPDRADLAAFVPELTLIDLPSFRADPKRHGCRSENVVAIDFARKIVLIGGTQYAGEMKKSVFTTLNYYLPERGVLPMHCSANVGPAGDTAIFFGLSGTGKTTLSADPNRTLIGDDEHGWGKDGVFNFEGGCYAKCIKLSPEAEPEIFAASSRFGAVLENVVLDEITRKPDFDNGSKTE... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
Q16AH6 | MTHGRVNPDFRLEDQGITGLGTVYYNLIEPDLIQYALARGEGSLGKGGSFLVTTGKFTGRSPKDKHVVKTDSVADTIWWENNREMSPEGFDQLYTDMLAHMEGRDYFVEDLTGGSDPKHAINVRMVTELAWHGLFIRHMLRRPDREDLDDFIADFTVINCPSFQADPAKHNCRSETVIAMNFDKKLILIGGTEYAGENKKSVFTLLNYLLPEKGVMPMHCSANHAVGNPVDTAVFFGLSGTGKTTLSADPARTLIGDDEHGWSDTGTFNFEGGCYAKTISLNPEAEPEIYATTEKFGTVIENMVYDAETKDLDFEDDSLT... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
Q1AY78 | MDLAVRKMTLEGLGVSQLGAVHENLPPARLVEASVRRREGMLAENGALVCLTGKRTGRSPKDRFIVENGLTRGPVDWGPVNKPFPGERFERLLAKASAYLENLEEVYVVDAYAGADPRYRLNVQVVCEYAWQALFTRQLFRRPSREELDAFEPDWTVISVPGLLTDPEEDGTESETFVGIDFGRRVVLICGTRYAGEIKKSIFSVLNFVLPTEHGVFPMHCSANVGPGGDVALFFGLSGTGKTTLSSDPERYLIGDDEHGWSDEGIFNFEGGCYAKCIDLSREKEPQIYDAIRFGAVLENVVVDRITRRVDYSDASLTEN... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
O54075 | MTAEGPLAPEDRVLDREAIGRLCVSLIAAEQQDLLREGRVGHHQMIGARLLTAGHPSPDDLLIDEDTLGLDSLLMLSLVTRVAGFFHLSDSNTEDYLLVRRRLGEWVDLIDHHHTLMGPKARFTFATSGSTAGPKPVTHSAAALLSEGQAIAKILTERPPEVRRVLSCVPAHHIYGFLWSCLFPSRRGLEAKQLANLSASGIMRHARSGDLVVGTPFIWEQFADLDYRLPGDVVGVTSGAPSTAETWRCASALGPARMLDIYGSTETGGIGWRERRDDPFRTLPDLACFHDTLSRLGRRLDLQDEIAWDKDGGFTILGRK... | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore.
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 45008
Sequence Length: 411
EC: 6.2.1.12
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P42516 | MQGLNADEVLRLLRSLIPGELATGRGQRGDPPEAQDLCADSRLDAEPIRADSLDRLNLASALNRFFRLHETGVEDRLLAVRRIGDMAELIADASQHTSGLTFSTSGSTGTPQPHHHSWAALTQEAEALANALGSHPRVIAWLPVHHLYGFVFGVALPRALGSTVIESHAAPTALFREPAPDDLIATVPARWRYLFDSNHRFPGGTGISSTAALETACRNGLLQAGLDALLEVYGATEAGGIGLRWAPSEDYRLLPHWHGDATATSSALNPDGAAVTVAPLDRLQWRDERVFRPTGRIDDIIQIGGVNVSPGHVARRLESH... | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore.
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 42439
Sequence Length: 391
EC: 6.2.1.12
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O69140 | MVRRLLISLIRAEARRGRNQILPEAAFTGDPRIDEEGLGFDSLARLDLIGAVRDFFDLSRTGIEDYVYVEPTLQGWIDRIMQHFDLLAARSETAQAVFRTSGSTGTPKPIPHPWPKLMREAASMARDQGLVPAPGGAVIGLVPAHHLFGCLFTALLPELAGAALRDLTAAPPASALRTAQPGDLIIATPHLWAHLGAAGAFPPGLRGVSSGAPMPDALWHSLLAAGLEDLTEVYGASETGGIGLRRAPGAAFTLLPFLSRSADDGISDGPAPLPLQDRLRWTGPVRFVIEGRLDQALQVGGVNVRLGHVKSVLEAEPGVE... | Function: Converts p-coumaric acid into p-coumaryl CoA. This is necessary for the activation of the photoactive yellow protein (PYP) chromophore (By similarity).
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Mass (Da): 40942
Sequence Length: 384
EC: 6.2.1.12
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A7IQE5 | MNQAAVQLPLPGFEQASGQWRSDYSRQVAGEKPVRNRSGIEVQPLYSPRDWAGERYLDDLGFPGQYPFTRGIYPSMHRGRTWTQRQLIGLGTPQDYNVRVRRIIDAGATAISLLPCCSGFRGIDCDEVDPVLLGTCGTVVNTTDHMDAALDGVPLGTISTAMNDPSPFTLLAFTLGVARRRGIDWRSITGTSNQSDYISHFIANHQFYRLSLPGSRRVLLDHIEFCRRALPNWNPLSVVGQHMQQAGATPAETMGFTLSSAIQYAQDCIERGMDVDDVLRRFTFFFDISISFFEEIAKFRAGRRIWARIARERLGAKDPA... | Function: Together with Xaut_5044, catalyzes the reversible isomerization between pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Does not exhibit isobutyryl-CoA mutase (ICM) activity.
Catalytic Activity: 3-methylbutanoyl-CoA = 2,2-dimethylpropanoyl-CoA
Sequence Mass (Da): 61992
Sequence Length: 559
EC: 5.4.99... |
Q9SWW5 | MEVASLYRRVLPSPPAVEFASAEGKRLFAEALQGGTMEGFFNLISYFQTQSEPAFCGLASLSVVLNALAIDPGRPWKGPWRWFDESMLDCCEPLHKVKAEGITFGKVVCLAHCAGARVQSFRADQTTIHDFRAHLTRCASSQDCHLISSYHRSPFKQTGTGHFSPIGGYHAEKDMALILDVARFKYPPHWVPLTLLWDAMNTTDEATGLLRGFMLVSRRSSAPSLLYTVSCGHGSWKSMAKYCVEDVPNLLKDESLDNVTTLLSRLVESLPANAGDLIKCVIEVRRKEEGESSLSKEEKERLFLKEKVLQQIRDTDLFRV... | Function: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
Catalytic Activity: [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine
Sequence Mass (Da): 55045
Sequence Length: 500
EC: 2.3.2.15
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Q9ZWB7 | MSMASLYRRSLSPPAIDFASFEGKQIFNEALQKGTMEGFFGLISYFQTQSEPAFCGLASLSMVLNSLSIDPGRKWKGPWRWFDESMLECCEPLEIVKDKGISFGKVVCLAHSSGAKVEAFRTNQSTIDDFRKYVVKCSTSDNCHMISTYHRQVLKQTGTGHFSPIGGYNAERDMALILDVARFKYPPHWVPLKLLWDAMDSIDQSTGRRRGFMLISRPHREPGLLYTLSCKDESWISIAKYLKEDVPRLVSSQHVDTIERILYVVFKSLPANFNQFIKWMAEIRRTEDVNQNLSSEEKSRLKLKQELLKQVQETKLFKHV... | Function: Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
Catalytic Activity: [Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine
Sequence Mass (Da): 51551
Sequence Length: 452
EC: 2.3.2.15
|
Q6UW60 | MRPAPIALWLRLVLALALVRPRAVGWAPVRAPIYVSSWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKVQWFQQQTLQRRVKRSVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPSKENRHGTRCAGEVAAMANNGFCGVGVAFNARIGGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTL... | Function: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization even... |
P29121 | MRPSQTELWLGLTLTLALLAVRWASAQAPIYVSSWAVRVTKGYQEAERLARKFGFVNLGQIFPDDQYFHLRHRGVAQQSLTPHWGHRLRLKKDPKVRWFEQQTLRRRVKRSLVVPTDPWFSKQWYMNKEIQQDLNILKAWNQGLTGRGVVISILDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPNDENRHGTRCAGEVSATANNGFCGAGVAFNARIGGVRMLDGAITDIVEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGLLTQEAFRRGVTKGRQGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTLSVG... | Function: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm... |
P29122 | MPPRAPPAPGPRPPPRAAAATDTAAGAGGAGGAGGAGGPGFRPLAPRPWRWLLLLALPAACSAPPPRPVYTNHWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKRQVRSDPQALYFNDPIWSNMWYLHCGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGR... | Function: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues.
Location Topology: Perip... |
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