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stringlengths 6
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P06660 | MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQAVLGDESHLRIRVVPDKANKTLTVEDTGIGMTKAELVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNDDEAYTWESSAGGTFTVTPTPDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVEKATEKEVTDEDEDEAAATKNEEGEEPKVEEVKDDAEEGEKKKKTKKVKEVTQEFVVQNKHKPLWTRDPKDVTKEEYAAFYKAISNDWEEPLSTKHFSVEGQLEFRAILFVPKRAPFDMFEPSKKRNNIKLYVRRVFIMDNCEDLCPEWLAFVRGVVDSEDLPLNISRENLQQNKILKVIRKNIVKKALELFEEIAENKEDYKKFYEQFGKNVKLGIHEDSANRKKLMELLRFHSSESGEDMTTLKDYVTRMKEGQKCIYYVTGDSKKKLETSPFIEQARRRGFEVLFMTEPIDEYVMQQVKDFEDKKFACLTKEGVHFEETEEEKKQREEEKTAYERLCKAMKDVLGDKVEKVVVSERLATSPCILVTSEFGWSAHMEQIMRNQALRDSSMSAYMMSKKTMEINPAHPIVKELKRRVEADENDKAVKDLVYLLFDTALLTSGFTLDDPTSYAERIHRMIKLGLSLDDEDNGNEEAEPAAAVPAEPVAGTSSMEQVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 80758
Sequence Length: 704
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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P40292 | MSSETFEFQAEISQLLSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPTKLDTGKDLRIDIIPDKENKTLTIRDTGIGMTKADLINNLGTIARSGTKQFMEALSAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESAAGGTFTLTQDTEGEQLGRGTKIILHLKDEQTDYLNESRIKEVVRKHSEFISYPIYLHVLKETEKEVPDEEAEETKEEEDEEKKAKIEEVDDEEEEEKKKKKKTKTVKESKIEEEELNKTKPIWTRNPADITQEEYASFYKSLSNDWEDHLAVKHFSVEGQLEFRAILYVPKRAPFDLFETKKTKNNIKLYVRRVFITDDATDLIPEWLGFIKGVVDSEDLPLNLSRETLQQNKIMKVIKKNIVKKTLELFNEIAEDREQFDKFYSAFSKNIKLGIHEDAQNRQTLAKLLRYQSTKSGDEATSLADYVTRMPEHQKQIYYITGESIKAVAKSPFLDSLKQKNFEVLFLVDPIDEYAFTQLKEFDGKKLVDITKDFELEETEEEKAEREKEEKEYENLAKSLKNILGDKVEKVVVSHKLVGSPCAIRTGQFGWSANMERIMKAQALRDTSMSSYMSSKKTFEISPKSSIIKELKKKVEADGENDRTVKSITQLLFETSLLVSGFTIEEPASFAERIHKLVSLGLNIDEEAETTEEKATEEAAPAEATTGESAMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 80640
Sequence Length: 706
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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O61998 | MSEEMNGETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYQALTEPAELETGKELYIKITPNKADKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVASKHNDDDCYQWESSAGGSFIIRQVNDPELTRGTKITLYIKEDQTDYLEERRIKEIVKKHSQFIGYPIKLTVEKERDKEVSDDEAEEEKKDEDKEKKEGEIEDVGEDEEEDKKDKDKKKKKIKEKYHEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPFDLFENKKTKNAIKLYVRRVFIMENCDELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFDEIAEDKDNFKKFYEQFSKNIKLGIHEDSTNRKKLSEFLRFYTSASSEEMTSLKDYVSRMKENQKQIYFITGESREAVASSAFVERVKRRGFEVIYMTDPIDEYCVQQLKEYDGKKLVSVTKEGLELPESEEEKKKFEEDKVKFENLCKVMKDILEKKVEKVAVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHSVIKALRERVEADKNDKTVKDLVVLLFETALLSSGFSLEDPQLHASRIYRMIKLGLDITEDEEEEAIASVSGEKDECVPNLVGAEEDASRMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 82605
Sequence Length: 717
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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Q18688 | MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVVRPFNDPEVTRGTKIVMHIKEDQIDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVEAKDEEKKEGEVENVADDADKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPFDLFENKKSKNSIKLYVRRVFIMENCEELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCMELIDEVAEDKDNFKKFYEQFGKNLKLGIHEDSTNRKKLSDFLRYSTSAGDEPTSLKEYVSRMKENQTQIYYITGESKDVVAASAFVERVKSRGFEVLYMCDPIDEYCVQQLKEYDGKKLVSVTKEGLELPETEEEKKKFEEDKVAYENLCKVIKDILEKKVEKVGVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHAIMKTLRDRVEVDKNDKTVKDLVVLLFETALLASGFSLEEPQSHASRIYRMIKLGLDIGDDEIEDSAVPSSCTAEAKIEGAEEDASRMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. In response to cellular stress, up-regulated in distal tissues in a pqm-1-dependent manner, preventing protein misfolding and maintaining proteostasis . By stabilizing the receptor-type guanylate cyclase daf-11 or another signal transduction component that regulates cGMP levels, plays a role in dauer formation and chemotaxis to non-volatile and volatile attractants detected by AWC sensory neurons . Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation . Regulates yap-1 nuclear export after heat shock treatment .
Sequence Mass (Da): 80283
Sequence Length: 702
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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P46598 | MADAKVETHEFTAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPSQLESEPELFIRIIPQKDQKVLEIRDSGIGMTKADLVNNLGTIAKSGTKSFMEALSAGADVSMIGQFGVGFYSLFLVADHVQVISKHNDDEQYVWESNAGGKFTVTLDETNERLGRGTMLRLFLKEDQLEYLEEKRIKEVVKKHSEFVAYPIQLVVTKEVEKEVPETEEEDKAAEEDDKKPKLEEVKDEEDEKKEKKTKTVKEEVTETEELNKTKPLWTRNPSDITQDEYNAFYKSISNDWEDPLAVKHFSVEGQLEFRAILFVPKRAPFDAFESKKKKNNIKLYVRRVFITDDAEELIPEWLSFIKGVVDSEDLPLNLSREMLQQNKILKVIRKNIVKKMIETFNEISEDQEQFNQFYTAFSKNIKLGIHEDAQNRQSLAKLLRFYSTKSSEEMTSLSDYVTRMPEHQKNIYYITGESIKAVEKSPFLDALKAKNFEVLFMVDPIDEYAMTQLKEFEDKKLVDITKDFELEESDEEKAAREKEIKEYEPLTKALKDILGDQVEKVVVSYKLVDAPAAIRTGQFGWSANMERIMKAQALRDTTMSSYMSSKKTFEISPSSPIIKELKKKVETDGAEDKTVKDLTTLLFDTALLTSGFTLDEPSNFAHRINRLIALGLNIDDDSEETAVEPEATTTASTDEPAGESAMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 80823
Sequence Length: 707
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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O44001 | MENKETFAFNADIQQLMSLIINTFYSNKEIFLRELISNASDALDKIRYEAITEPEKLKTKPELFIRLIPDKANNTLTIENSGIGMTKADLVNNLGTIARSGTKAFMEALQAGGDISMIGQFGVGFYSAYLVADSVTVVSKHNDDEQYVWESAAGGSFTVQKDDKYEPLGRGTRIILHLKEDQGEYLEERRLKDLVKKHSEFISFPIELAVEKTHEREVTESEDEEEKKADEKAEEKEGEEKKEGEEKKEGEEEKKEKTGKTKKVQEVTREWEQLNKQKPLWMRKPEEVTEEEYASFYKSLSNDWEEHLAVKHFSVEGQLEFKALLFVPKRAPFDLFETRKKRNNIKLYVRRVFIMDDCEDIIPEWLNFVKGVVDSEDLPLNISRESLQQNKILKVIRKNLVKKCLEMFAEIEEKKENYAKFYEQFSKNLKLGIHEDSANRAKIAELLRFHSSKSGEDMVSFKEYVDRMKEGQKDIYYITGESRQTVANSPFLEKLTKKGYEVLYMTDPIDEYAVQQLKEFDNHKLRCCTKEGLEIDESEEEKKKFEELKAEFEPLLKLIKEVLHDKVDKVVLSNRITDSPCVLVTTEFGWSANMERIMKAQALRDNSMTSYMVSKKTMEVNGHHSIMIEIKNKAAVDKSDKTVKDLIWLLYDTALLTSGFSLEEPTQFAARIHRMIKLGLSIDDDEEAKDDDLPPLEEVEGAADEASKMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 82413
Sequence Length: 713
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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P20147 | KDFDGKKLKCCTKEGLDIHHSEEAKKDFETLKAEYEGLCKVIKDVLHKKVEKVVVGQRITDSPCVLVTSEFGWSANMERIMKAQALRDNSMTSYMLSKKIMEINARHPIISALKQKADADKSDKTVKYLIWLLFDTSLLTSGFALEEPTTFSKRIHRMIKLGLSIDEEENNDIDLPPLEETVDATDSKMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 21968
Sequence Length: 193
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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O43109 | MAETFEFQAEISQLLSLIINTVYSNKEIFLRELVSNASDALDKIRYESLSDPSKLDTGKDLRIDIIPDKENKTLTIQDTGIGMTKADLVNNLGTIARSGTKQFMEALTAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESSAGGTFNISPDNGPSIGRGTKIILHLKDEQTDYLNESKIKEVIKKHSEFISYPIYLHVQKETEVEVPDEEAETVEEGDDKKPKIEEVEDDEEDKEKKPKTKKVKEVKTEEEELNKQKPIWTRNPQDITQEEYAAFYKSLSNDWEDHLAVKHFSVEGQLEFKAILFVPKRAPFDLFETKKTKNNIKLYVRRVFITDDATDLIPEWLSFVKGVVDSEDLPLNLSRETLQQNKIMKVIRKNIVKKALELFTEIAEDKEQFDKFYTAFSKNIKLGIHEDSQNRNTLAKLLRFNSTKSGDEQTSLSDYVTRMPEHQKNMYYITGESIKAVSKSPFLDSLKEKGFEVLFLVDPIDEYAMTQLKEFEGKKLVDITKDFELEETEEEKKQREAEEKEYDGLAKALKNVLGDKVEKVVVSHKLVGAPCAIRTGQFGWSANMERIMKAQALRDTSMSSYMSSKKTFEISPKSPIIKELKQKVEADGENDKTVKSIVQLLFETSLLVSGFTIEEPAGFAERIHKLVALGLNLDEEPEAAADAPAADAGVAAAETSDNAMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 79323
Sequence Length: 701
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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Q4UDU8 | MASKEETPDQEVYAFNADISQLLSLIINAFYSNKEIFLRELISNASDALEKIRYEAIKDPKQIEDQPDYYIRLYADKNNNTLTIEDSGIGMTKADLVNNLGTIAKSGTRAFMEALQAGSDMSMIGQFGVGFYSAYLVADKVTVVSKNNADDQYVWESSASGHFTVKRDDSHEPLKRGTRLILHLKEDQTEYLEERRLKELVKKHSEFISFPISLSVEKTQETEVTDDEAEPEEEKKLEEEDKDKEEKVEDVTDEKVTDVTEEEEKKEEKKKKKRKVTNVTREWEMLNKQKPIWMRLPTEVTNEEYASFYKNLTNDWEDHLAVKHFSVEGQLEFKALLFVPRRAPFDMFESRKKKNNIKLYVRRVFIMDDCEELIPEWLSFVKGVVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFNELTEKKEDFKKFYEQFSKNLKLGIHEDNANRSKIAELLRFETTKSGDELVSLKEYVDRMKSDQKFVYYITGESKQSVASSPFLETLKARDYEVLYMTDPIDEYAVQQIKEFEGKKLKCCTKEGLELDEGEDEKKSFEALKEEMEPLCKHIKEVLHDKVEKVVCGTRFTDSPCALVTSEFGWSANMERIMKAQALRDSSITSYMLSKKIMEINPRHSIMKELKARAANDKTDKTVKDLVWLLYDTALLTSGFNLDEPTQFGNRIYRMIKLGLSLDDEEHVEDDSSMPPLDEPVVDSKMEEVD | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Sequence Mass (Da): 83825
Sequence Length: 722
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Subcellular Location: Cytoplasm
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Q8VZG2 | MEGSKLLPCVHKSPVPTSHQLYINYEILGLTKLKKHKYTQNKMSSSDSSSAESRLATAKTVLTTAASVAATAMLARSLVQDYLPDEVHHYISYGFRSIFGYFSSQMTIIIEEFEGFAHNEVFEAAEAYLATKISPSNKRIKVSKHEKENNYNVTVERDEEVVDTYNGVKFQWILHCRHVESKHFHNPRDLNSTLRSEVRSFELNFHKKFKDVALESYLPFMVKRATLMKQEKKTLKIFTLSPENMYGNYSDAWTSVTLDHPSTFKTLAMDSDVKTSVMEDLDKFVKRRDFYKRVGKAWKRGYLLYGPPGTGKSSLIAAMANHLNFDIYDLELTAVNNNSELRRLLIATANRSILIVEDIDCSLELKDRTSDEPPRESDDIEDPRYKKVTLSGLLNFIDGLWSSCGDERIIIFTTNYKEKLDAALLRPGRMDMHIHMSYCTPSTFKALALNYLEIKEHRLFSKIEEGIEATEVTPAEVAEQLMRNDSVDKVLEGLIEFLKVKKIENEQDKAKTEKQELENKKKTKEGTDSVVKKEVDEQLVRNDRVDKVLEGLVELLKAKKIEDDQDKAKHEEVEQH | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 66136
Sequence Length: 576
Subcellular Location: Membrane
EC: 3.6.1.-
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P53356 | MSKNSDALLWYHGKITREVAVQVLLRKGGRDGFFLIRDCGNAPEDYVLSMMFRSQILHFQINCLGDNKFSIDNGPIFQGLDMLISYYKVISDGLPCKLVDFCVGKIAPLYALKYGLDTRLHLACEEKNPNTVKELLQDSVIKENVNARSISGLTALHISCSNGDNDIVAMLLNAGADASAIDANGRTPVQVVCFYNHASTLHLLISKGSADFLKRSPNNGWVPLHEAAMRGSLECVKVLLSFNASMYPRSLDGDTPRDLALQYENYNVVEFFDNYPVNQPKTSITQWLHQNLDRNGALIILQNASMADGSFLIRSSIKCHGYYVLTLVYEKKTYHFQIKSRADRWFYIDDGPLFETLPHLVDHYMQYADGLPTLLQFPVPSAENRKRPLPPTPTKNQLKLPVPPSRPIKNNNGLPQPLPYPEFTNESDSDIFTRLECEKEKPLPKLPRPVVNHTEVPNSVNVGQKGDQTMKNNAQQNIILKESISFGKELGVGEFGSVIKGIWLSPGGKEINVAMKTLHKDKMVQGEKEFLREALVMSQLNHPCIVSLLGVCLGPPMILVQELVEMGALLDYLMDYQPEIQEVDLKLWASQIAFGMMYLELKRFVHRDLAARNILLANKKQVKISDFGLSRAVGTGSDYYQAKQGGRWPVRWYAPESINYGTFSTKSDVWSYGITLWEMFTFGDLPYGEMTGNEVVSFLEHCGRLEKPDECPIHTYSIMLSCWHIDPNKRPTFNELHSTFSTDPEYEDVRIYRDRIK | Function: May be involved in signal transduction.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 85598
Sequence Length: 757
EC: 2.7.10.2
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B1MCE2 | MTENLQDMFESSYRGEAPEQLAARPPWSIGQPQPEILKLIEQGKVHGDVLDAGCGEAATALYLAERGHTAVGLDAAPTAIQLAKGYAAERGLTNVTFDVADISNFTGYDGRFGTIIDSTLFHSMPVELREGYQQSIVRAAAPGANYIVLVFDKAAFPPDIDGPHPVSEPELREIVSKYWTVDDISPARLYANGDGFQDGGAQRFAEFREESNGWVSMAGWLLQAHRD | Function: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs (Probable). Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ) . Can also methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4-hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one .
Catalytic Activity: 2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-methionine = 2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24731
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.374
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Q7M3P9 | TTLTEPEPDLTYLTFVXIVXXEMPIFVMATANSGITSTF | Function: Metalloprotease with anticoagulant activity. Cleaves fibrinogen Aalpha (FGA), gamma (FGG) and Bbeta (FGB) chains after positions 'Asn-121', 'Lys-160' and 'Pro-102', respectively. Breaks down cross-linked and non-cross-linked fibrin clots. Prevents and reverts platelet aggregation induced by ADP and collagen. Prevents thrombin-induced platelet clotting. Does not affect plasma levels of coagulation factors prothrombin (F2), V (F5), VII (F7), VIII (F8), IX (F9), X (F10), XI (F11), XII (F12), plasma kallikrein (KLKB1) and kininogen-1 (KNG1).
Sequence Mass (Da): 4286
Sequence Length: 39
Subcellular Location: Secreted
EC: 3.4.24.-
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B0EXJ8 | MDVQSEEFRGAQAQIWSQSCSFITSASLKCAVKLGIPDTIDNHGKPITLSELTNALVPPVHPSKAPFIYRLMRVLAKNGFCSEEQLDGETEPLYSLTPSSRILLKKEPLNLRGIVLTMADPVQLKAWESLSDWYQNEDDSSTAFETAHGKNFWGYSSEHMEHAEFFNEAMASDSQLISKLLIGEYKFLFEGLASLVDIGGGTGTIAKAIAKNFPQLKCTVFDLPHVVANLESKENVEFVAGDMFEKIPSANAIFLKWILHDWNDEDCVKILKSCKKAIPAKGGKVIIIDMVMYSDKKDDHLVKTQTSMDMAMLVNFAAKERCEKEWAFLFKEAGFSDYKIYPKLDFTRSLIEVYP | Function: 16-O-methyltransferase involved in the biosynthesis of vindoline. Highly specific for 16-hydroxytabersonine. No activity with tabersonine, 3-hydroxytyramine, 4-hydroxytyramine, 5-hydroxytryptamine (5HT), 2,3-dihydro-3-hydroxytabersonine, lochnericine, hoerhammericine, 16-hydroxy-2,3-dihydro-3-hydroxytabersonine, 16-hydroxylochnericine, 16-hydroxyhoerhammericine, quercetin, kaempferol and caffeic acid as substrates.
Catalytic Activity: 16-hydroxytabersonine + S-adenosyl-L-methionine = 16-methoxytabersonine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39863
Sequence Length: 355
Pathway: Alkaloid biosynthesis; vindoline biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.94
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D3JZP7 | MRIHHPLTLAALCVVLHESLGAAQHSNNVARLEHYRIAEIEHWEKRHLRSDSRGHRHHAHHGQVIDKENNNSQEQATTGNSVETNQVPSTEPTKDKTTPMKNALFKLFREKKLKTKNAGNGHAHDDDDDSDFSDDDVPTNAPTDAPTGAPTDAPTDAPTVAPTDAPTDAPTEAPTNAPTGTDAPTDAPTDAQVVPTFD | Function: Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture (Probable). Within the host fish cells, Htp1 is involved in the uptake of the S.parasitica effector Htp3 at a neutral pH (pH 7.5) and its release from vesicles into host cytosol where it degrades nucleic acids .
Sequence Mass (Da): 21444
Sequence Length: 198
Domain: Has a conserved RxLR motif that acts to carry the protein into the host cell cytoplasm. Lacks the 'so-called' EER motif, which is found closely behind the RxLR motif in most of RxLR effector family members, but the presence of an EER motif is not always essential for the translocation of every RxLR effector into host cells, or for inducing a hypersensitive response.
Subcellular Location: Secreted
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B8E160 | MKPFTFYEAIESNKRKTWFIVFIIYFLLFFVCYAVVSYFELGEIGIIIAFLIVLFTNYYAYQKSNEIILNYSGVREPTREEYPYLLNVVEGLSIAAGIPTPKIYIMDDPSPNAFATGKDPQNSVVVVTKGLLDILNRTELEGVIAHEISHIKNYDVRLQTIAAVMVGLIVILGDGLKRSFYYSKRRRDKDENILGIVSLIIAILAPFLATLLRFALSRQREYMADASAAMLTRYPEGLASALEKIAKNFQPIKRANVMTAPLYIVNPLSSNAVSKLFSTHPPIEERIRRLRMMGERWKMLDKEG | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34628
Sequence Length: 304
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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O30795 | MLFEQIAANKRRTWFLLVAFFALLALIGAAAGYLWMNSPLGGVIIAFIIGLIYAITMIFQSTEVVMSMNGARQVSEQEAPELYHIVQDMAMVAQIPMPRVYIVEDDSPNAFATGSNPENAAVAATTGLLRLMNREELEGVIGHEVSHIRNYDIRISTIAVALASAITMISSVAGRMMWYGGGRRRNDRDDDSGLGLLMLVFSLIAIILAPLAATLVQLAISRQREFLADASSVELTRNPQGMIRALQKLDNSEPMHRHVDDASAALYISDPKKKGGLQKLFYTHPPISERVERLRKM | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32788
Sequence Length: 297
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q8IVG9 | MAPRGFSCLLLLTSEIDLPVKRRA | Function: Plays a role as a neuroprotective factor . Protects against neuronal cell death induced by multiple different familial Alzheimer disease genes and amyloid-beta proteins in Alzheimer disease . Mediates its neuroprotective effect by interacting with a receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR . Also acts as a ligand for G-protein coupled receptors FPR2/FPRL1 and FPR3/FPRL2 . Inhibits amyloid-beta protein 40 fibril formation . Also inhibits amyloid-beta protein 42 fibril formation . Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria . Also suppresses apoptosis by binding to BID and inhibiting the interaction of BID with BAX and BAK which prevents oligomerization of BAX and BAK and suppresses release of apoptogenic proteins from mitochondria . Forms fibers with BAX and also with BID, inducing BAX and BID conformational changes and sequestering them into the fibers which prevents their activation . Can also suppress apoptosis by interacting with BIM isoform BimEL, inhibiting BimEL-induced activation of BAX, blocking oligomerization of BAX and BAK, and preventing release of apoptogenic proteins from mitochondria . Plays a role in up-regulation of anti-apoptotic protein BIRC6/APOLLON, leading to inhibition of neuronal cell death . Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death . Competes with importin KPNB1 for binding to IGFBP3 which is likely to block IGFBP3 nuclear import . Induces chemotaxis of mononuclear phagocytes via FPR2/FPRL1 . Reduces aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPR2 to APP . Protects retinal pigment epithelium (RPE) cells against oxidative stress-induced and endoplasmic reticulum (ER) stress-induced apoptosis . Promotes mitochondrial biogenesis in RPE cells following oxidative stress and promotes STAT3 phosphorylation which leads to inhibition of CASP3 release . Also reduces CASP4 levels in RPE cells, suppresses ER stress-induced mitochondrial superoxide production and plays a role in up-regulation of mitochondrial glutathione . Reduces testicular hormone deprivation-induced apoptosis of germ cells at the nonandrogen-sensitive stages of the seminiferous epithelium cycle . Protects endothelial cells against free fatty acid-induced inflammation by suppressing oxidative stress, reducing expression of TXNIP and inhibiting activation of the NLRP3 inflammasome which inhibits expression of pro-inflammatory cytokines IL1B and IL18 . Protects against high glucose-induced endothelial cell dysfunction by mediating activation of ERK5 which leads to increased expression of transcription factor KLF2 and prevents monocyte adhesion to endothelial cells . Inhibits the inflammatory response in astrocytes . Increases the expression of PPARGC1A/PGC1A in pancreatic beta cells which promotes mitochondrial biogenesis . Increases insulin sensitivity .
Sequence Mass (Da): 2687
Sequence Length: 24
Domain: Largely unstructured in aqueous solution.
Subcellular Location: Secreted
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P15686 | MAGGGVVVVSGRGLSTGDYRGGLTVYVVMVAFMAACGGLLLGYDNGVTGGVVSLEAFEKKFFPDVWAKKQEVHEDSPYCTYDNAKLQLFVSSLFLAGLVSCLFASWITRNWGRKVTMGIGGAFFVAGGLVNAFAQDMAMLIVGRVLLGFGVGLGSQVVPQYLSEVAPFSHRGMLNIGYQLFVTIGILIAGLVNYAVRDWENGWRLSLGPAAAPGAILFLGSLVLPESPNFLVEKGKTEKGREVLQKLCGTSEVDAEFADIVAAVEIARPITMRQSWASLFTRRYMPQLLTSFVIQFFQQFTGINAIIFYVPVLFSSLGSANSAALLNTVVVGAVNVGSTLIAVMFSDKFGRRFLLIEGGIQCCLAMLTTGVVLAIEFAKYGTDPLPKAVASGILAVICIFISGFAWSWGPMGWLIPSEIFTLETRPAGTAVAVVGNFLFSFVIGQAFVSMLCAMEYGVFLFFAGWLVIMVLCAIFLLPETKGVPIERVQALYARHWFWNRVMGPAAAEVIAEDEKRVAAASAIIKEEELSKAMK | Function: Active uptake of hexoses.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57523
Sequence Length: 534
Subcellular Location: Membrane
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P60111 | MSKHFFLHNEFHWQGRHDAEDGAAGSRVHHVVQQIDYTHIGENPYGVALLGFACDAGVARNKGRIGAKKSPDLIRRALANLAWHSPHPLYDLGTVVCDDDLLESSQQHCAKIIAEVLPCVPVITLGGGHEVAWASFSGLARYFEQHHPEKAPKIGIINFDAHFDLRAFSSSQADVKPSSGTPFNQIQHYCQQQGWDFHYACLGVSKASNTRALFERAEQLNVWFVEDKDLGSVNHDYHLTQLQHFIDDCDYLYLTIDLDVFPAATAPGVSAPAARGVSYDNLAPFLDRILAHRDKLMLADIAEYNPTYDVDSQTARLAARLCWDIANAMNDKLEHQ | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
Catalytic Activity: H2O + N-formimidoyl-L-glutamate = formamide + L-glutamate
Sequence Mass (Da): 37499
Sequence Length: 336
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (hydrolase route): step 1/1.
EC: 3.5.3.8
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Q20502 | MRLQVQIGTECVVVPCKPDDTIHAVAKKSVEKLRRLRPKLPLADDYFEVRRTVGNSLLDPEDLVSDVLKDSDFIIVAASVEETEDAKEAKKQEEIDNARAEIEKIDNRRRKVSFADSLAPMVLAPPTKLLILDGNSLLPEDLVRCEKGECAIQLSMESEDRIRKARTFLEKIASEHRAVYGVTTGFGTFSNVTIPPEKLKKLQLNLIRSHATGYGEPLAPNRARMLLALRINILAKGHSGISVENIKKMIAAFNAFCVSYVPQQGTVGCSGDLCPLAHLALGLLGEGKMWSPTTGWQPADVVLKKNNLEPLELGPKEGLALINGTQMVTALGAYTLERAHNIARQADVIAALSLDVLKGTTRAYDPDIHRIRPHRGQNLSALRLRALLHSEANPSQIAESHRNCTKVQDAYTLRCVPQVHGVVHDTIEFVREIITTEMNSATDNPLVFADREEIISGGNFHGEYPAKALDFLAIAVAELAQMSERRLERLVNKELSGLPTFLTPDGGLNSGFMTVQLCAASLVSENKVLCHPSSVDSIPTSCNQEDHVSMGGFAARKALTVVEHVEAVLAMELLAACQGIEFLKPLISTAPLHKIYQLVRSVAPPLNEDRYMKPEIDAVLEMIRENRIWEAVLPHLETLEAMEELDPDALRQFTKTPTGIVQDRSMIPISDDEESIE | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Cys-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 74635
Sequence Length: 677
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
EC: 4.3.1.3
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Q8RFC2 | MEVFILELVLGSKNITLEDLINVTRKGYKVSISEEAYEKIDKARALVDKYVEEGKVSYGITTGFGKFAEVSISKEQTGQLQKNIVMSHSCNVGNPLPIDIAKGIVLLRAVNLAKGYSGARRIVIEKLVELLNKDVTPWIPEKGSVGSSGDLSPLAHMSLVLIGLGKAYYKGELLEAKDALAKADIEPIPALSSKEGLALTNGTQALTSTGAHVLYDAINLSKHLDIAASLTMEGLHGIIDAYDPRIGEVRGHLGQINTAKNMRNILAGSKNVTKQGVERVQDSYVLRCIPQIHGASKDTLEYVKQKVELELNAVTDNPIIFVDTDEVISGGNFHGQPMALPFDFLGIALSEMANVSERRIEKMVNPAINNGLPAFLVEKGGLNSGFMIVQYSAASLVSENKVLAHPASVDSIPTSANQEDHVSMGSVAAKKSKDIFENVRKVIGMELITACQAIDLKEAKDKLSPATKVAYDEVRKIISYVSEDRPMYIDIHAAEDLIKTNKIVENVEKAIGKLEF | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ser-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 55978
Sequence Length: 516
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 4.3.1.3
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A8MF65 | MNIDVWIKNITQLVTVQAHGKPKKGKEMQDVGIIQDGWIAVAGDRIVGIGSGEISADFQVGENTVIISGEGKTVTPGLIDPHTHLVHAGSRENELALKLKGVPYLEILKQGGGILSTVNATKKATMEELVAQSKKSLDRMLSYGVTTVEIKSGYGLELEAEIKQLEAIHRLQQQTPMDLVSTFMGAHAIPKEYKENPEEFIDLIIEEMLPAIKEKNLAEFCDVFCEEGVFSVDQTRRILEAARSLGFKNKIHADEIVPLGGAELAAELQTISAEHLMAASETGLKMMAESNVVPVALPGTSFNLATGKYADARKMIEYGLPVALATDYNPGSCPTENIQLIMSIGCLYLKMTPEEVISAVTINAAAAIDRTQEIGSIEVGKKADITIFDAPNLYYIPYHFGVNHVDTVLKSGKIVVEKGNVI | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Mass (Da): 45757
Sequence Length: 422
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Subcellular Location: Cytoplasm
EC: 3.5.2.7
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Q2IHZ6 | MSRPAATLVLRNAVVATCDRGPSDAGLLPGAAVAVEGRRVAWVGRERDVEAEVNLAGAQVIDARGGLVTPGLVDSHTHLVFAGERAGEFALRCAGRTYLQVALSGGGIAVTTRETRAAPDEQLLAAAAARARRLIAQGVTTLEVKSGYGLDAPEELRLLRIVHQLGRALGGDATILPTLLFHAVPPEQVGDRAGFVRDACASLIPQVARERLAQFCDVFVEDGAFAPDEARLLLQAAKDRGLVPRVHAEQLTAGGGARLAAELGCSSADHLEELDDAGIAALAQARVVAGLLPLSTLFLGSERYAPARRLLEAGVPVSLATNMNPGSAMSENVGLTLSLACLKLRLTPAEALVAFTAGGARALRQPDLGRVARGADADLVLWGCGSPEHLAWHMAVNHALVVVKHGRVVHEAPPAAMVDCR | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Mass (Da): 43894
Sequence Length: 421
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Subcellular Location: Cytoplasm
EC: 3.5.2.7
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Q01W05 | MSDSALLNCRQLVTLAGPPGPRTGPAMRELAIIPDGAMRIRDGCIAAVGPRADIVRSLAGDTEVIDAGWRVVLPGFIDAHTHPVFAGTRAAEYEQRAEGATYAEIAAAGGGIRSTVRRTREAGDLELATAARRYTDWFLRGGTTTIEAKSGYGLSLDDELRILKTIRLLNAERRLRYVPTFLGAHEIPDEYRGEIEDYVDLVIQEMLPAVAEDNLAEYCDVFCEPNVFPLDPARAILQAAQSLGLRLRIHADQFTGDYAALLAAELGAATADHLESTTALGLAALHEAGVQPVLLPASVYNLGSARYPAARDMIARGMAVVLATDFNPGSSPTASIPMVLSLASTQMKMTPAESITAVTVNAAHSLGRGSRIGSLEPGKAADFAIHECDDYRELAYFFGREPANAVYLAGQCVYRRSA | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Mass (Da): 44759
Sequence Length: 418
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Subcellular Location: Cytoplasm
EC: 3.5.2.7
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Q8XW28 | MNTMTDAAHLAADPRYDAAREIRAPRGTELHCKSWLTEAAYRMLQNNLDPDVAENPKHLVVYGGIGRAARDWACFDKILETLRELNDDESLLVQSGKPVGVFKTHPDAPRVLIANSNLVPKWANWEHFNALDRKGLFMYGQMTAGSWIYIGSQGIVQGTYETFAEAGRQHYSDRPSALLKQGLSPEGTAPGSGRSSAQVPGSHLAGRWILTAGLGGMGGAQPLAATLAGAVSLTIECQQSSIDFRLRTRYLDKQARDIDDALNLIRHHCERGEAVSIGLLGNAAELLPELVRRARAGGLKPDLVTDQTSAHDLVNGYLPAGWTVEQWRAAQRDPAQHAHLSAEAARSCAVHVQAMLDFQSMGIPTVDYGNNIRQVAFDQGVKNAFDFPGFVPAYIRPLFCEGRGPFRWVALSGDPEDIYKTDAKIKELFPHNAHVHRWLDMARERIAFQGLPARICWLGLGERHAAGLAFNEMVRKGELKAPIVIGRDHLDTGSVASPNRETEAMRDGTDAVSDWPLLNALLNTAGGATWVSLHHGGGVGMGYSQHAGVVIVADGTDAAARRLARVLVNDAGSGVMRHADAGYETAVACAKRNGLKLPMIG | Cofactor: Binds 1 NAD(+) per subunit.
Function: Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Mass (Da): 65180
Sequence Length: 601
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
Subcellular Location: Cytoplasm
EC: 4.2.1.49
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A4FNF1 | MSSARPVRAARGTTLTARSWSTEAPLRMLQNNLDPEVAERPDDLVVYGGTGKAARNWASFDAIVRELTTLSDDETLLVQSGKPVGVLRTHEWAPRVLLANSNLVGDWANWPEFRRLDALGLMMYGQMTAGSWIYIGTQGILQGTYETFAAVAERRFGGTLAGTLTITAGLGGMGGAQPLAVTMNEGVALVVECDPERAHRRVKHGYLDEVADGLDQAIEKAEAAKAQRRAYSVAVIGNAAEVLPELLRRGVRADIVTDQTSAHDPLSYLPLGVELEDWEDYASKKPEEFTDRARDSMAKHVEAMVGFMDAGAEVFDYGNSLRGEAQLAGYGRAFDYPGFVPAYIRPLFCEGKGPFRWAALSGDPADIAATDRAILDLFGDDDHLARWIRLAGEKVSFQGLPARICWLGYGERHLAGLRFNEMVASGELKAPLVLGRDHLDCGSVASPYRETEGMADGSDAIADWPLLNALVNTASGATWVSLHHGGGVGMGRSLHAGQVTVADGTALAAQKLERVLTNDPGMGVIRHVDAGYDRAREVATERGVRVPGLA | Cofactor: Binds 1 NAD(+) per subunit.
Function: Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Mass (Da): 59242
Sequence Length: 550
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
Subcellular Location: Cytoplasm
EC: 4.2.1.49
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Q9R4Y1 | MINGWTGNILRINLTTGAIS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Oxidoreductase with an extremely broad substrate specificity that can reduce reversibly 2-oxocarboxylates to (2R)-hydroxycarboxylates.
Catalytic Activity: A + a (2R)-2-hydroxycarboxylate = a 2-oxocarboxylate + AH2
Sequence Mass (Da): 2146
Sequence Length: 20
Subcellular Location: Cell membrane
EC: 1.1.99.30
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E9QDC5 | MSQLGSAVPSSNLPEGLPVSSLALLILVLIPCVLLLLLLNCLFVGYKLFRMTRRKRDRYGSEMSLMHSSYSTRQRITRFSDEPPVAPNRKTNYVSVSEPMLAPPITSSLTSSAERRATGQRAMFLRPDGATYAGSESLRVPHWRTSAPVLVQSSDSDMERVNTVPPNSPVLRVTPNGFSVPMTSLRRSSTMELESTSLDKIHVECESASIIPQENSCYVVSSSSSARGSGLDSDFGASAGVSLRILSMDSDGFPGSAWASALEWDYYDPSYVTQNHVPKHRPQAPPITTKQYWV | Function: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1) . Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2) . Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32250
Sequence Length: 294
Subcellular Location: Cell membrane
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A0A1L8I316 | MVTLSPAYLPSDGGTQAASAAPSVEENWVVQPSLTLLVLLLVPCVLLLFFLNCFLLFHRLPAFSLRKRASRRKVGQYPCVRVGHSGQARLEPPYMLSPGVVLREGRLGSDTISQGFEATLALEEGVCGRQNTPQSRGSCCQGGSIPSDQICCSPRPRCATPLPCCAPRRAWNAPAYVKKRLRPKVWKVREDELGSSCELDTRHNHVPPNTPAADNALGVTPKVKFCHTSSTQRKSHVGMVPFTLGGSELLEDPSVIPREDTAEHLDASSSLPGPGLDSDFGVSAGISLHILSSDSDSGSQSWTSGMEWDYYDPCYMRRNRLRRDARHNRHLPMMCSKQYWI | Function: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1) . Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2). Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37501
Sequence Length: 341
Subcellular Location: Cell membrane
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P46593 | MRLSTAQLIAIAYYMLSIGATVPQVDGQGETEEALIQKRSYDYYQEPCDDYPQQQQQQEPCDYPQQQQQEEPCDYPQQQPQEPCDYPQQPQEPCDYPQQPQEPCDYPQQPQEPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDQPDDNPPIPNIPTDWIPNIPTDWIPDIPEKPTTPATTPNIPATTTTSESSSSSSSSSSSTTPKTSASTTPESSVPATTPNTSVPTTSSESTTPATSPESSVPVTSGSSILATTSESSSAPATTPNTSVPTTTTEAKSSSTPLTTTTEHDTTVVTVTSCSNSVCTESEVTTGVIVITSKDTIYTTYCPLTETTPVSTAPATETPTGTVSTSTEQSTTVITVTSCSESSCTESEVTTGVVVVTSEETVYTTFCPLTENTPGTDSTPEASIPPMETIPAGSEPSMPAGETSPAVPKSDVPATESAPVPEMTPAGSQPSIPAGETSPAVPKSDVSATESAPAPEMTPAGTETKPAAPKSSAPATEPSPVAPGTESAPAGPGASSSPKSSVLASETSPIAPGAETAPAGSSGAITIPESSAVVSTTEGAIPTTLESVPLMQPSANYSSVAPISTFEGAGNNMRLTFGAAIIGIAAFLI | Function: Major hyphal cell wall protein which plays a role of adhesin and is required for mating, normal hyphal development, cell-to-cell adhesive functions necessary for biofilm integrity, attachment to host, and virulence. Promotes interactions with host and bacterial molecules, thus leading to effective colonization within polymicrobial communities. Plays a crucial role in gastrointestinal colonization, in mucosal symptomatic and asymptomatic infections, in vaginitis, as well as in lethal oroesophageal candidiasis, caused by the combined action of fungal virulence factors and host inflammatory responses when protective immunity is absent.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 65314
Sequence Length: 634
Subcellular Location: Secreted
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Q969A8 | MQPRQPGDEAKQLAELEVVRQMMTPTREVLLELHESFLKELQRGLEMHKRHGITWVPEECSMKMLDSCVSNLPTGAEVGEAYAIDFGGSTCRAVRCSLLGKGKMEIIQDKICLRSAEHRCAKGFMDKKAGGKELFDQFAMCIRGLMDRSGDLKKAEETNTPVPVGFTFSFPCAQAALNSSFLIEWTKGFETGRENPDRVEGKDVAVLLADALQRHNVPAVCKAIVNDTVGTLVSCAYQRVPGTPECRVGLIIGTGFNACYVEPEASNYGYTGTVVNMEAGNFHKDLPRNEIDVEVDEKTHNRGKQQFEKLVSGYYIGEIVRVAAVRVFGARAPEKASVRHSIHGETASTIRDDHSQDKAASIQAIKECWGVTMDLDDIKCIWEICRLVFDRSAAFAATLAVALCYRTGRLDTGSTVGIDGALYVKNQWYREAVEYYTKLVAGDAAKNIHYCIADDGSGKGAALIADVN | Function: Catalyzes the phosphorylation of various hexoses to hexose 6-phosphate.
Catalytic Activity: ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+)
Sequence Mass (Da): 51468
Sequence Length: 468
Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 2.7.1.1
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C8VJW1 | MGATATDIEKVPSAGTPDEPKAGETNVYVDTEAEKSFVRKVDFFVLPMLCLMYFFDCMDRSNLANAKTDGLEEDINLKGNEYSLLILLFYIPFGLFDLPWNLLIKRYSARIMLSLRRYAVTVVWGICALCQCAANNFGGLLAIRIILGVFEAGFFAGSTFYFTLFYTRNEMGFRLAVLQSFAVLASAFSGLISFGLFQINHSAVKGWQWLFIVEGAMTLIIGVIGFWWLPDTAQSAWFLTQRERDAASARLLRDTSAEIETKLELKAAFQTWSDWKFPIWAVITFSYPVAYATAMNFFPIIVARLGYSVVKTNLWTVAPNLVGAVVLLVVAKSSDIFRERSLHIIFSLTVSLVGMLILASIDVSHNKGVSYFACFLLASGAYIPTCLVHAWHNNNNTNENSRAANTGFFVGLGNIAGVLSAATFRTEYAPKYVPTLVATCACNGVCILATAFMGTWMRLENRRKDKEQGARIVAGQVETRMLADGEKSPEWRYFL | Function: Major facilitator-type transporter, part of the hnx cluster involved in the purine degradation . The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism . The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55114
Sequence Length: 495
Subcellular Location: Cell membrane
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C8VK14 | MAPTAPPILDFSPFYGTDGAAKAKLVQQVRESCEYNGFFQITGHRIPRELQVRVMDAAKRFFALPLEEKMAIDKNLNSFNRGYELLRSQMLEVGTAPELKEGLYIGEEIGADHPYYINGRLNSGPNQWPATVPDAQEFRETSMEYYHAVYELAKDVLAVLALTLDVEESFFDPLTEGGVATMRMLHYPSQPKDEDEKLNRGIGAHTDFGCITLLLQDEVDGLQVLDAPSGQWLDVQPVLGAYVVNLGDLMMRMANDRYKSNIHRVINKSGRERYSIPFFFSGNPDHVCKCLPNCCKAGEQPKYPPITVEDMVRGAYKQSYGRAEAYKKELAEKAKAHKIEAASATAMVS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-Fe(II) type oxidoreductase, part of the hnx cluster involved in the purine degradation . The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism . The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid .
Sequence Mass (Da): 39087
Sequence Length: 349
EC: 1.14.11.-
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C8VK15 | MDISYPVINAGGLKNIASQIIMEIELDKRENRPTDNVPPDDIGKIEVVDDAEMEQFYGSSTTDAYRLKSELVSQCMADIGMGRFQWKLFTVAGFGWIVDNFCSQGISAVQPPIQQEFSGIKQVSYSSVAYYVGMIIGASFWGISSDLIGRKPAFNSTLAIAGIFLCAAAGTSNFIAFSALWAVIGTAAGGNVVCDSMILLEFIPGSHQYLLTALSGWWNLGQLVVSLLAWVFLANFSCPTDATPDTCSRADNMGWRYTLITLGGLSLAFTFVRIFVFKMPETPRYLLSQGNDQAAVDAVNYVARQNGKPEPLTLSMLQAIDVRLGFTPNAEERLSTKDILKENMQEFRGEHYQALFATRKLSQHTALIWAVWLIIGIAYPLYFNFLPSYLATRFTQDSSLDLTYRNYCIQSAVGVVGPLSAAVLVNTFLGRRWMMGISSIVTGVFLFAYVGVKTPMSSLAFSCVTGLLANFANQLSEYAIMYAFTPESFPAPHRGTASGTAASLLRFGGLVASLIASETGFTTAPIYASAALWVGVGVLCFGLPFETHGHAAI | Function: Major facilitator-type transporter, part of the hnx cluster involved in the purine degradation . The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism . The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60145
Sequence Length: 553
Subcellular Location: Cell membrane
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P77625 | MRCKGFLFDLDGTLVDSLPAVERAWSNWARRHGLAPEEVLAFIHGKQAITSLRHFMAGKSEADIAAEFTRLEHIEATETEGITALPGAIALLSHLNKAGIPWAIVTSGSMPVARARHKIAGLPAPEVFVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLNEVDLVLHSLEQITVTKQPNGDVIIQ | Cofactor: Requires the presence of a divalent metal cation for activity. Can use magnesium, manganese or cobalt.
Function: Sugar-phosphate phosphohydrolase that appears to contribute to butanol tolerance . Catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate . Is also able to dephosphorylate other sugar phosphates in vitro including ribose-5-phosphate (Rib5P), 2-deoxyribose-5-phosphate, fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), and glucose-6-phosphate (Glu6P) . Selectively hydrolyzes beta-D-glucose-1-phosphate (bGlu1P) and has no activity with the alpha form .
Catalytic Activity: sugar phosphate + H2O = sugar + phosphate.
Sequence Mass (Da): 23008
Sequence Length: 216
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P77247 | MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRRNELPDTLGLRIDMVVDLWYARQPWNGPSRQEVVERVIARAISLVEETRPLLPGVREAVALCKEQGLLVGLASASPLHMLEKVLTMFDLRDSFDALASAEKLPYSKPHPQVYLDCAAKLGVDPLTCVALEDSVNGMIASKAARMRSIVVPAPEAQNDPRFVLADVKLSSLTELTAKDLLG | Cofactor: Requires the presence of a divalent metal cation for activity. Can use zinc, manganese, cobalt or magnesium.
Function: Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate . Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose . To a lesser extent, is also able to dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and glucose-6-phosphate (Glu6P) in vitro .
Catalytic Activity: sugar phosphate + H2O = sugar + phosphate.
Sequence Mass (Da): 24330
Sequence Length: 222
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Q8NR92 | MTISAQQQAVEEDLVERVLASFDSCENPRLKLVMKSLTVHLHDFIRDVRLTEEEWNYAIDFLTKVGHITDDKRQEFVLLSDTLGASMQTIAVNNEAYEDATEATVFGPFFVDDAPLVQNGDDIAFGAVGQPAWVEGTVKDTEGNPIPNARIEVWECDEDGLYDVQYADERSAGRAHLYSDENGEYHFWGLTPVPYPIPHDGPVGQMLQAVGRSPVRCAHLHFMVTAPEKRTLVTHIFVEGDPQLEIGDSVFGVKDSLIKKFVEQPAGTATPDGRDVGDQTWARTRFDIVLAPGNV | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Involved in resorcinol degradation . Catalyzes the conversion of hydroxyquinol to malelylacetate . Shows also weak activity with catechol, 3-methylcatechol and 4-methylcatechol, but cannot use 4-chlorocatechol, 4-nitrocatechol or protocatechuate (Ref.2).
Catalytic Activity: benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate
Sequence Mass (Da): 32774
Sequence Length: 295
Pathway: Aromatic compound metabolism.
EC: 1.13.11.37
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Q8NL92 | MTTTTADHNISAQQKAVEENLVNRVLQSFDACENPRLKQLMESLVVHLHDFIRDVRLTEDEWNYAIDFLTAVGHITDDKRQEFVLLSDTLGASMQTIAVNNEAYENSTEATVFGPFFLDDAPEVELGGDIAGGAQGQAAWIEGTVTDTEGNPVPNARIEVWECDEDGLYDVQYADERMAGRAYMHTDANGDYRFWGLTPVPYPIPHDGPVGNMLKAVGRSPVRCAHLHFMVTAPELRTLVTHIFVEGDPQLEIGDSVFGVKDSLIKKFEEQAPGTPTPDGRDLGDQTWARTRFDIVLAPGA | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Involved in resorcinol degradation (Ref.2). Catalyzes the conversion of hydroxyquinol to malelylacetate (Ref.2). Shows also weak activity with catechol, 3-methylcatechol and 4-methylcatechol, but cannot use 4-chlorocatechol, 4-nitrocatechol or protocatechuate (Ref.2).
Catalytic Activity: benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate
Sequence Mass (Da): 33291
Sequence Length: 301
Pathway: Aromatic compound metabolism.
EC: 1.13.11.37
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P42833 | MTAQIPYQHSSGYISHFHNNELDAGRGRDYNVTIKYLDDKEENIEGQAAKISHNASLHIPVLLCLVISLGGFIFGWDIGTIGGMTNMVSFQEKFGTTNIIHDDETIFVSTKKLTDLQIGLIISIFNISCGVGALTLSKIGDWIGRKGGIWFALVVYCIGITIQILSYGRWYFLTLGRAVTGIGVGVTTVLVPMFLSENSPLKIRGSMVSTYQLIVTFGILMGNILNFICERCYKDPTQNIAWQLPLFLGYIWAIIIGMSLVYVPESPQYLAKIKNDVPSAKYSFARMNGIPATDSMVIEFIDDLLENNYNNEETNNESKKQSLVKRNTFEFIMGKPKLWLRLIIGMMIMAFQQLSGINYFFYYGTSVFKGVGIKDPYITSIILSSVNFLSTILGIYYVEKWGHKTCLLYGSTNLLFYMMTYATVGTFGRETDFSNIVLIIVTCCFIFWFAITLGPVTFVLVSELFPLRTRAISMAICTFINWMFNFLISLLTPMIVSKIDFKLGYIFAACLLALIIFSWILVPETRKKNEQEINKIFEPE | Function: Probable glucose transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60979
Sequence Length: 540
Subcellular Location: Membrane
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P54854 | MASEQSSPEINADNLNSSAADVHVQPPGEKEWSDGFYDKEVINGNTPDAPKRGFLGYLIIYLLCYPVSFGGFLPGWDSGITAGFINMDNFKMNFGSYKHSTGEYYLSNVRMGLLVAMFSVGCSIGGVAFARLADTLGRRLAIVIVVLVYMVGAIIQISSNHKWYQYFVGKIIYGLGAGGCSVLCPMLLSEIAPTDLRGGLVSLYQLNMTFGIFLGYCSVYGTRKYSNTAQWRIPVGLCFLWALIIIVGMLLVPESPRYLIECERHEEACVSIAKINKVSPEDPWVLKQADEINAGVLAQRELGEASWKELFSVKTKVLQRLITGILVQTFLQLTGENYFFFYGTTIFKSVGLTDGFETSIVLGTVNFFSTIIAVMVVDKIGRRKCLLFGAASMMACMVIFASIGVKCLYPHGQDGPSSKGAGNAMIVFTCFYIFCFATTWAPVAYIVVAESFPSKVKSKAMSISTAFNWLWQFLIGFFTPFITGSIHFYYGYVFVGCLVAMFLYVFFFLPETIGLSLEEIQLLYEEGIKPWKSASWVPPSRRGASSRETEAKKKSWKEVLKFPKSFN | Function: Probable glucose transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62931
Sequence Length: 567
Subcellular Location: Membrane
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P77329 | MNVNSSSNRGEAILAALKTQFPGAVLDEERQTPEQVTITVKINLLPDVVQYLYYQHDGWLPVLFGNDERTLNGHYAVYYALSMEGAEKCWIVVKALVDADSREFPSVTPRVPAAVWGEREIRDMYGLIPVGLPDQRRLVLPDDWPEDMHPLRKDAMDYRLRPEPTTDSETYPFINEGNSDARVIPVGPLHITSDEPGHFRLFVDGEQIVDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSVAYTNSVENALGIEVPQRAHTIRSILLEVERLHSHLLNLGLSCHFVGFDTGFMQFFRVREKSMTMAELLIGSRKTYGLNLIGGVRRDILKEQRLQTLKLVREMRADVSELVEMLLATPNMEQRTQGIGILDRQIARDLRFDHPYADYGNIPKTLFTFTGGDVFSRVMVRVKETFDSLAMLEFALDNMPDTPLLTEGFSYKPHAFALGFVEAPRGEDVHWSMLGDNQKLFRWRCRAATYANWPVLRYMLRGNTVSDAPLIIGSLDPCYSCTDRVTLVDVRKRQSKTVPYKEIERYGIDRNRSPLK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Possible component of hydrogenase 4.
Sequence Mass (Da): 63383
Sequence Length: 555
EC: 1.-.-.-
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O30478 | MNPSSLVLNGLTSYFENGRARVVPPVGRNILGVVNYASVCEYPTLDHGYPELEINMVAPTAEPFAEVWVTDAESEHGERDGITYAHDGEYFFCAGRVPPTGRYTEATRAAYVTMFELLEEFGYSSVFRMWNFIGDINRDNAEGMEVYRDFCRGRAEAFEQCRLEFDQFPAATGIGSRGGGIAFYLLACRSGGHVHIENPRQVPAYHYPKRYGPRAPRFARATYLPSRAADGVGGQVFVSGTASVLGHETAHEGDLVKQCRLALENIELVISGGNLAAHGISAGHGLTALRNIKVYVRRSEDVPAVREICREAFSPDADIVYLTVDVCRSDLLVEIEGVVM | Function: Involved in the biosynthesis of BC325, a rapamycin analog containing a 3-hydroxybenzoate starter unit. Catalyzes the hydrolysis of chorismate via an intramolecular mechanism to yield 3-hydroxybenzoate (3HBA).
Catalytic Activity: chorismate = 3-hydroxybenzoate + pyruvate
Sequence Mass (Da): 37429
Sequence Length: 340
EC: 4.1.3.45
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Q8W191 | MSLQRPNGNSSSSSSHKKHKTEESDEELLMVPDMEAAGSTCVLSSSADDGVNNPELDQTQNGVSTAKRRRGRNPVDKEYRSLKRLLRNRVSAQQARERKKVYVSDLESRANELQNNNDQLEEKISTLTNENTMLRKMLINTRPKTDDNH | Function: Transcription factor that promotes photomorphogenesis in light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in the blue light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevents the activation of light-induced genes.
PTM: Ubiquitinated by COP1. Ubiquitination takes place in darkness and leads to its subsequent degradation, thereby preventing the activation of photomorphogenesis signals.
Sequence Mass (Da): 16899
Sequence Length: 149
Subcellular Location: Nucleus
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P25016 | MVPITSLAQTLERLRRKDYSCLELVETLIARCEAAKALNALLATDWGGLRRRAKKIDRHGNAGVGLRGIPLCFKANIATGIFPTTAATPALINHLPKIPSRIAERLFSAGALPGASGNMHELSFGITSNNYATGAVRNPWNPSLIPGGSSGGVAAAVASRLMLGGIGTDTGASVRLPAALCGVVGFRPTLGRYPRDRIIPVSPTRDTAGIIAQCVADVVILDQVISGRPARILPIPLKGLRIGLPTTYFYDDLDADVAFAAETTIRLLANRGVTFVEADIPHLEDLNSGASLPIALYEFPHALKQYLDDFVGTVSFSDVIKEIRSPDVANIVNAQIDGHQISNAEYELARQSFRPRLQAAYRNYFRLYRLDAILFPTAPLAAKAIGQDSSVIHNGSMVNTFKIYVRNVDPSSNAGLPGLSLPVGLTPDRLPVGMEIDGLAGSDHRLLAIGAALEKAINFRSFPDVLN | Function: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA).
Sequence Mass (Da): 49942
Sequence Length: 467
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 3.5.1.-
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P19922 | MVRGRHRSRDPQRRDLRGRDRRSASRTDARRQSAAERGCRRSQRGSAEGCACGRQTGPRAARSACCTACPSRSRRMSTTEGRPNFNGVPANKDFVAPSDSPVVHNLKKAGAIVIGLTNTPEFSFRGFTDNPLHGLTLNPWDPNITCGGSSGGAGSAVAAGIGTIAHGNDIGGSLRWPAHCNGVATIKPTQGRIPAFNGSATAERPMLAHLMSAQGPLARHVGDVRLALDVMSQADPRDPWWVPAPLAGPRPKGPIKVALARIPEDMDVDPSVRAALRQAADHLERSGYRVTEVDVPDIDGVWQTWCDIITNETVVMQEAGMLKVTSEDFHKAWGGMKTKANVLDLKAWMQATAARNGHIRAWQLFFEEYPVVLAPTTVKPTPGPRDDTVSADRVKEIFWGEIRFISAINVLGLPGAVVPVTLHDGKPIGVQLIAGRYREDLALDAAAAIEKRAGVLAHRLWETME | Function: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA).
Sequence Mass (Da): 50266
Sequence Length: 465
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 3.5.1.-
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P06618 | MHEIITLESLCQALADGEIAAAELRERALDTEARLARLNCFIREGDAVSQFGEADHAMKGTPLWGMPVSFKDNICVRGLPLTAGTRGMSGFVSDQDAAIVSQLRALGAVVAGKNNMHELSFGVTSINPHWGTVGNPVAPGYCAGGSSGGSAAAVASGIVPLSVGTDTGGSIRIPAAFCGITGFRPTTGRWSTAGIIPVSHTKDCVGLLTRTAGDAGFLYGLLSGKQQSFPLSRTAPCRIGLPVSMWSDLDGEVERACVNALSLLRKTGFEFIEIDDADIVELNQTLTFTVPLYEFFADLAQSLLSLGWKHGIHHIFAQVDDANVKGIINHHLGEGAIKPAHYLSSLQNGELLKRKMDELFARHNIELLGYPTVPCRVPHLDHADRPEFFSQAIRNTDLASNAMLPSITIPVGPEGRLPVGLSFDALRGRDALLLSRVSAIEQVLGFVRKVLPHTT | Function: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA).
Sequence Mass (Da): 48578
Sequence Length: 455
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 3.5.1.-
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P0C612 | NWSWCSGSGEGCDYHSECCGERCCIESMCIGDGVACWP | Function: Iota-conotoxins bind to voltage-gated sodium channels (Nav) and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. Produces general excitatory symptoms (By similarity).
Sequence Mass (Da): 4122
Sequence Length: 38
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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A0A125S9E0 | MKLALTFLLILMILPLMTGEKTSDDLELRGVESLRAIFRDRRCSDNIGATCSDRFDCCGSMCCIGGQCVVTFAECS | Function: Probable neurotoxin.
Sequence Mass (Da): 8346
Sequence Length: 76
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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P0C607 | MKLCATFLLVLVTLPLVTGEKSSERSLSGAILRGVRRTCSRRGHRCIRDSQCCGGMCCQGNRCFVAIRRCFHLPF | Function: Both natural (L-Leu form) and synthetic (D-Leu from) peptides equally cause sensitivity to touch and body tremor. Neither L-Leu form nor D-Leu form is active on nerve-muscle preparation.
Sequence Mass (Da): 8377
Sequence Length: 75
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q7Z094 | GPSFCKADEKPCEYHADCCNCCLSGICAPSTNWILPGCSTSSFFKI | Function: Iota-conotoxins bind to voltage-gated sodium channels and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels. This toxin acts on Nav1.6/SCN8A > Nav1.2/SCN2A > Nav1.7/SCN9A sodium channels. Produces general excitatory symptoms upon intracorporeal injection and repetitive action potentials in the frog cutaneous pectoris muscle. Natural peptide (with D-Phe) is active on nerve, but not on muscle. Synthetic peptide (with L-Phe) is not active on both nerve and muscle.
PTM: The natural D-Phe-44 form of the peptide is more potent than the L-Phe-44 form.
Sequence Mass (Da): 4936
Sequence Length: 46
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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P84197 | CQAYGESCSAVVRCCDPNAVCCQYPEDAVCVTRGYCRPPATVLT | Function: Neurotoxin. Elicits hypersensibility when injected intracranially in mice. May act via potassium channel currents.
Sequence Mass (Da): 4703
Sequence Length: 44
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q7Z091 | GCKKDRKPCSYHADCCNCCLSGICAPSTNWILPGCSTSTFT | Function: Iota-conotoxins bind to voltage-gated sodium channels (Nav) and act as agonists by shifting the voltage-dependence of activation to more hyperpolarized levels (By similarity). Both natural (L-Thr form) and synthetic (D-Thr form) peptides cause paralysis and death following intracranial injection and grooming and hypersensitivity upon intraperitoneal injection into mice. The L-Thr form of the peptide is 7-fold more potent than the D-Thr form. Both natural peptide (L-Thr form) and synthetic peptide (D-Thr form) are active on nerve, and on muscle.
PTM: Position 41 corresponds to a L-threonine, and not a D-threonine as firstly supposed.
Sequence Mass (Da): 4373
Sequence Length: 41
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q7M4K5 | ECKTNKMSCSLHEECCRFRCCFHGKCQTSVFGCWVDP | Function: Causes hyperactivity, circular motion, convulsion, urination and death, when injected into 13- to 15-day-old mice. Causes gasping, backward swimming or swimming in a vertical direction and death, when intraperitoneally injected into goldfish.
Sequence Mass (Da): 4304
Sequence Length: 37
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q8IU81 | MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPATKDLAAAAAQGPQLPPPQAQPQPSGTGGGVSGQDRYDRATSSGRLPLPSPALEYTLGSRLANGLGREEAVAEGARRALLGSMPGLMPPGLLAAAVSGLGSRGLTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYERRHGSGEWRQLGELLTDGVRSFREPAPAEALPQQYPEPAPAALCGPPPRAPSRNLAPTPRRRKASPEPEGEAAGKMTTEEQQQRHWVAPGGPYSAETPGVPSPIAALKNVAEALGHSPKDPGGGGGPVRAGGASPAASSTAQPPTQHRLVARNGEAEVSPTAGAEAVSGGGSGTGATPGAPLCCTLCRERLEDTHFVQCPSVPGHKFCFPCSREFIKAQGPAGEVYCPSGDKCPLVGSSVPWAFMQGEIATILAGDIKVKKERDP | Function: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 61688
Sequence Length: 584
Subcellular Location: Nucleus
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Q7Z5L9 | MAAAVAVAAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAHGCFPEGRSPPGAAASAAAKPPPLSAKDILLQQQQQLGHGGPEAAPRAPQALERYPLAAAAERPPRLGSDFGSSRPAASLAQPPTPQPPPVNGILVPNGFSKLEEPPELNRQSPNPRRGHAVPPTLVPLMNGSATPLPTALGLGGRAAASLAAVSGTAAASLGSAQPTDLGAHKRPASVSSSAAVEHEQREAAAKEKQPPPPAHRGPADSLSTAAGAAELSAEGAGKSRGSGEQDWVNRPKTVRDTLLALHQHGHSGPFESKFKKEPALTAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGPPKINGEAQPWLSTSTEGLKIPMTPTSSFVSPPPPTASPHSNRTTPPEAAQNGQSPMAALILVADNAGGSHASKDANQVHSTTRRNSNSPPSPSSMNQRRLGPREVGGQGAGNTGGLEPVHPASLPDSSLATSAPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDS | Function: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities . Represses the NFAT1-dependent transactivation of NFAT-responsive promoters . Acts as a coactivator of VEGFA expression in cardiac and skeletal muscles . Plays a role in immature B-cell differentiation .
PTM: Phosphorylation at Ser-360 is required for nuclear targeting.
Sequence Mass (Da): 61025
Sequence Length: 587
Domain: The C-terminal RING-type zinc finger domain is sufficient for interaction with IRF2.
Subcellular Location: Cytoplasm
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Q9H1B7 | MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAAAAAAAAQQQQQQQQQQQQQQQQQQQQQQQQQLNHVDGSSKPAVLAAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHTARLPNGLGGPNGFPKPTPEEGPPELNRQSPNSSSAAASVASRRGTHGGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPPPHALGSRGPPTPAPPGAPGGPACLGGTPGVSATSSSASSSTSSSVAEVGVGAGGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWASKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGALPPAAPSGRGAAASLRKRKASPEPPDSAEGALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHAAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP | Function: Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins . Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway . Probably plays a role in the development of the central nervous system and in neuronal maintenance (Probable). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 82659
Sequence Length: 796
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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O72899 | MEKLFTGTYGVFLESNDSDFEDFINTIMTVLTGKKESKQLSWLTIFIIFVVCIVVFTFLYLKLMC | Function: Late protein which probably plays a role in virus entry into the host cell.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7573
Sequence Length: 65
Subcellular Location: Virion membrane
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P27945 | MLRVFIFFVFLGSGLTGRIKPQVTCKYFISENNTWYKYNVTILNSSIILPAYNTIPSNAAGISCTCHDIDYLQKNNISIHYNTSILKTFQDIRIIRCGMKNISEIAGGFGKELKFLDLRYNDLQVIDYNILRKLIRSNTPTYLYYNNLMCGKRNCPLYYFLLKQEQTYLKRLPQFFLRRISFSNNNTYLYHFLSCGNKPGHEFLEYQTKYCRTKFPEINITVNQLIAKKNTERYKSCYPLVFISILCSCISFLFLFICLLRSICKKYSCTKQDKSSHNYIPLIPSYTFSLKKHRHPETAVVEDHTTSANSPIVYIPTTEEKKVSCSRRK | Function: Viral TLR3 homolog that probably prevents TLR3 dimerization and subsequent induction of IFN . Inhibits dsRNA-stimulated activation of NF-kB and IRF3 .
PTM: Highly glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38542
Sequence Length: 329
Domain: Contains putative leucine-rich repeats (LRR) and a C-terminus cysteine-rich capping motif similar to domain structure of host TLR3.
Subcellular Location: Host endoplasmic reticulum membrane
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P41437 | MSSRAIGAPQEGADMKNKAARLGTYTNWPVQFLEPSRMAASGFYYLGRGDEVRCAFCKVEITNWVRGDDPETDHKRWAPQCPFVRNNAHDTPHDRAPPARSAAAHPQYATEAARLRTFAEWPRGLKQRPEELAEAGFFYTGQGDKTRCFCCDGGLKDWEPDDAPWQQHARWYDRCEYVLLVKGRDFVQRVMTEACVVRDADNEPHIERPAVEAEVADDRLCKICLGAEKTVCFVPCGHVVACGKCAAGVTTCPVCRGQLDKAVRMYQV | Function: RING-finger E3 ubiquitin ligase required to prevent cellular apoptosis in infected cells. Ubiquitinates and subsequently targets host pro-apoptotic cellular proteins such as HID for degradation by the proteasome.
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30076
Sequence Length: 268
EC: 2.3.2.27
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Q05718 | MTPHRLLPPLLLTLLLAARPGGALARCPGCGQGVSAGCPGGCAEEEDGGPAAEGCAEAGGCLRREGQQCGVYTPNCAPGLQCQPPEKEDLPLRALLQGRGRCGRARTPSGENPKESKPQAGTARSQDVNRRDQQRNSGTSTTPSRSNSGGVQDTEMGPCRKHLDSVLQQLQTEVFRGAHTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVERMGQPLPGSSEGGDGSSLCPTGSSG | Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Activates the MAPK signaling pathway and induces cell migration.
PTM: O-glycosylated.
Sequence Mass (Da): 24967
Sequence Length: 237
Subcellular Location: Secreted
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P24592 | MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG | Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Activates the MAPK signaling pathway and induces cell migration .
PTM: O-linked glycans consist of hexose (probably Gal), N-acetylhexosamine (probably GalNAc) and sialic acid residues. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylated on one site only in the region AA 143-168 in cerebrospinal fluid.
Sequence Mass (Da): 25322
Sequence Length: 240
Subcellular Location: Secreted
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P35572 | MTWDGLPTQPLLMLLMLLFAAGSESALAGCPGCGPGVQEEDAGSPADGCAETGGCFRREGQPCGVYIPKCAPGLQCQPRENEETPLRALLIGQGRCQRARGPSEETTKESKPHGGASRPRDRDRQKNPRTSAAPIRPSPVQDGEMGPCRRHLDSVLQQLQTEVFRGGANGLYVPNCDLRGFYRKQQCRSSQGNRRGPCWCVDPMGQPLPVSPDGQGSSQCSARSSG | Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Activates the MAPK signaling pathway and induces cell migration.
PTM: O-glycosylated.
Sequence Mass (Da): 24193
Sequence Length: 226
Subcellular Location: Secreted
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Q16270 | MERPSLRALLLGAAGLLLLLLPLSSSSSSDTCGPCEPASCPPLPPLGCLLGETRDACGCCPMCARGEGEPCGGGGAGRGYCAPGMECVKSRKRRKGKAGAAAGGPGVSGVCVCKSRYPVCGSDGTTYPSGCQLRAASQRAESRGEKAITQVSKGTCEQGPSIVTPPKDIWNVTGAQVYLSCEVIGIPTPVLIWNKVKRGHYGVQRTELLPGDRDNLAIQTRGGPEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQASASAKITVVDALHEIPVKKGEGAEL | Function: Binds IGF-I and IGF-II with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion.
PTM: N-glycosylated.
Sequence Mass (Da): 29130
Sequence Length: 282
Subcellular Location: Secreted
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P81726 | NDVDVVMDASSKPIFPGGEYYIMPAIWGPPGGGVRLAKTRNSDCPVTVLQDYGEVIFGQPVKFTLPGRGSGLIITNTPVEEFIKKPECASSSKWSVFVDDEIEKACVGIGGHEDHPGEQVFSGTFTIQKSRTPYNSYKLVFCESDSSTCSDIGRYDNNEGGRRLILTHHNPFQVVFMDASTFDGTIRSDG | Function: Inhibits subtilisin-type microbial serine proteases incuding proteinase K, subtilisin BPN', subtilisin Carlsberg and subtilisin E in a non-stoichiometric manner. Weakly inhibits A.oryzae protease and some metalloproteases including pronase E. Does not inhibit trypsin, chymotrypsin, S.griseus alkaline protease or A.lyticus lysyl endopeptidase. CLSI-II has a wider inhibitory specificity than CLSI-III.
PTM: The N-terminal Asn is removed in about 50% of both the CLSI-II and CLSI-III chains.
Sequence Mass (Da): 20750
Sequence Length: 190
Subcellular Location: Secreted
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F4HZG9 | MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPHLMAEGEVTPGIRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERGLCMFMPESTPKDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNVQSASQRYTNLDDFQNSASLGKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIPSSFDCPERFQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLLNNHCHDNSARTSPVSLCKVKGLHTNRNPRRLF | Cofactor: Binds 2 manganese ions per subunit.
Function: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Sequence Mass (Da): 54982
Sequence Length: 493
Subcellular Location: Mitochondrion
EC: 3.4.11.-
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Q10439 | MSGYIRTLFIRNRFSNYRLRSQIIKYKYSNVSYLNKSALRCGQATDSTHPHILQPGELTPRISAQEYKTRRDRVASLLEDNDFMIVTSAPVRHMCGAAFYEYHQDPNFYYLTGCLEPNAVLLMFKNGASGSYDCSLYLPSKNPYIEKWEGLRTGSTLGKKLFQIENVYDSSLASSVINALGKKSNRIFYNYQTGYLSKMPAASAPEFIQDTLTKLFRTSTQRSVDELLHPLRSIKSTAELECMKEAANISSNVYREIMRKRFEKEAEMSAEFNYRFCIGGCDRSAYVPVVAGGKNGLTIHYTINNDIFRPDEMVLVDAGGEFGGYVTDISRTWPINGKFSTVQRDLYQAVLNVQKKCIKYCCTSNGWSLADIHFESVKLMHEELKQVGIHGTKREITDILYPHSIGHEIGLEIHDCSTNNGYQPLRKNQVITIEPGLYVPEEDGWPQWAQGIAIRIEDSVIVGDDKPFVLTSAAPKEIEEIEALKK | Cofactor: Binds 2 manganese ions per subunit.
Function: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Catalytic Activity: The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55141
Sequence Length: 486
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.11.26
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P40051 | MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTWPNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQELKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITIEPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLENVMQNGLSTKFEEDQVAPL | Cofactor: Binds 2 manganese ions per subunit.
Function: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Catalytic Activity: The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57990
Sequence Length: 511
Subcellular Location: Nucleus
EC: 3.4.11.26
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Q8LE98 | MPRPRVSELSQRQAPRLRSSSSTSDSNHSNRLITTDQSFKPGVDRKSPRSGGPNSDPLGQKKLGGRISDLESQLGQAQEELRLLKEQLANAEAVKKQAQDELHKKSKKPNPLARVEESATEAERIDRDEIPGDVQKETDVFEVPVEKIAVEEEELRSGNDEAEKLVAKEDEIKMLKARLYDMEKEHESLGKENESLKNQLSDSASEISNVKANEDEMVSKVSRIGEELEESRAKTAHLKEKLESMEEAKDALEAEMKKLRVQTEQWRKAADAAAAVLSGEFEMNGRDRSGSTEKYYAGGFFDPSAGFMDPPGMADDYDDGLGSGKRKSSGMKMFGELWRKKGQK | Function: Acts as a scaffold, mediating interaction of ROPs with different proteins. Required for primary and adventitious root maintenance, but not for their formation. Promotes the stabilization of ARAC11 on the plasma membrane of the pollen tube initiation site but not the activation of ARAC11. Regulates directionality of polar auxin transport, and is required for the formation of a stable auxin maximum and tip localized auxin gradient during embryogenesis, organogenesis, and meristem activity. Involved in exocytosis and in the recycling of PIN proteins back to the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38358
Sequence Length: 344
Domain: Interactions with ROPs and SEC3A require an intact C-terminal coiled-coil domain.
Subcellular Location: Cell membrane
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Q8VYU8 | MQTPKSRPGSLELPQKKSPLPAPKVVRRLKPSGAESDPKTKTISKTQIPKVVADRRSARIPLNEIQKKRTGRIPELESTISQLQEELKKAKEELNRSEALKREAQEEAEDAKHQLMDINASEDSRIEELRKLSQERDKTWQSELEAMQRQHGMDSTALSSAINEVQKLKSKLFESESELEQSKYEVRSLEKLVRQLEEERVNSRDSSSSMEVEELKEAMNLSRQEITQLKSAVEAAETRYQEEYIQSTLQIRSAYEQTEAVKSRYSQREAELTEELNRTKDEIEGLRKELMEKVKEDESTGDLKKLESDLMEVRGSLMDKEMELQILRSAMEKKVETANTEAMEAELKRVKIQCEQWRKAAETAASILNNDEERTDSIETSKMLKKFGVLLKKNHK | Function: ROP effector binding specifically activated ROPs and linking them to the microtubule cytoskeleton. Involved in ROP-regulated polar growth. Involved in local disassembly of cortical microtubules when associated with ARAC10 and KIN13A and conversely mediates also the elimination of ARAC10 from the plasma membrane by the cortical microtubules. Accumulates at the plus end of shrinking microtubules. Targets KIN13A to microtubules.
Sequence Mass (Da): 45680
Sequence Length: 396
Domain: The N-terminal part (1-122) is necessary and sufficient for homooligomerization and for binding to microtubules while the C-terminal domain is anchored to the plasma membrane .
Subcellular Location: Cell membrane
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P21954 | MSMLSRRLFSTSRLAAFSKIKVKQPVVELDGDEMTRIIWDKIKKKLILPYLDVDLKYYDLSVESRDATSDKITQDAAEAIKKYGVGIKCATITPDEARVKEFNLHKMWKSPNGTIRNILGGTVFREPIVIPRIPRLVPRWEKPIIIGRHAHGDQYKATDTLIPGPGSLELVYKPSDPTTAQPQTLKVYDYKGSGVAMAMYNTDESIEGFAHSSFKLAIDKKLNLFLSTKNTILKKYDGRFKDIFQEVYEAQYKSKFEQLGIHYEHRLIDDMVAQMIKSKGGFIMALKNYDGDVQSDIVAQGFGSLGLMTSILVTPDGKTFESEAAHGTVTRHYRKYQKGEETSTNSIASIFAWSRGLLKRGELDNTPALCKFANILESATLNTVQQDGIMTKDLALACGNNERSAYVTTEEFLDAVEKRLQKEIKSIE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Mitochondrial IDP1 may regulate flux through the tricarboxylic acid cycle and respiration. Its probably critical function is the production of NADPH.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 48190
Sequence Length: 428
Subcellular Location: Mitochondrion
EC: 1.1.1.42
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O67480 | MNKTTFENVYYWEGKAQIPQEGQFIKLKEDKTLEVPDNPIIPFIEGDGIGPEITQAMLLIINTAVEKTYNGSKKIYWVELLAGDKAEEKTGERLPQETLDVLKESIVGIKGPLGTPVGKGVRSINSALRRAFDYYSAVRPVYWMGQATPIPNPERVDLVVFRENTDDVYAGVEFFAGTPEAKKVREFLIKEMGAKEEGFPEDVGITVKPMSEFKTKRHVRKALRYALENNKKNVAVIGKGNIMKATEGAFINWAFEVAEEPEFKGKVVTDPEAEPGEGQVKLTKVITDQMLMQLVLKPEAWDVIIAQNLNGDYVSDLAASLIGGPGFVPSGNIGDGYALFESTHGTAWDIAGKGIANPLSLTLSGAMMLEYIGWKEAAQKVYDAVRRTLAEHIGTPDIASGFQKQGIEAKAVGTMEFAEEISKRIE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 46925
Sequence Length: 426
EC: 1.1.1.42
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O29610 | MQYEKVKPPENGEKIRYENGKLIVPDNPIIPYFEGDGIGKDVVPAAIRVLDAAADKIGKEVVWFQVYAGEDAYKLYGNYLPDDTLNAIKEFRVALKGPLTTPVGGGYRSLNVTIRQVLDLYANVRPVYYLKGVPSPIKHPEKVNFVIFRENTEDVYAGIEWPRGSEEALKLIRFLKNEFGVTIREDSGIGIKPISEFATKRLVRMAIRYAIENNRKSVTLVHKGNIMKYTEGAFRDWGYEVAKQEFGEYCITEDELWDKYGGKQPEGKIVVKDRIADNMFQQILTRTDEYDVIALPNLNGDYLSDAAAALIGGLGIAPGSNIGDGIGVFEPVHGSAPKYAGQNKVNPTAEILTGALMFEYIGWKDASEMIKKAVEMTISSGIVTYDIHRHMGGTKVGTREFAEAVVENLQSL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 45842
Sequence Length: 412
EC: 1.1.1.42
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P16100 | MSTPKIIYTLTDEAPALATYSLLPIIKAFTGSSGIAVETRDISLAGRLIATFPEYLTDTQKISDDLAELGKLATTPDANIIKLPNISASVPQLKAAIKELQQQGYKLPDYPEEPKTDTEKDVKARYDKIKGSAVNPVLREGNSDRRAPLSVKNYARKHPHKMGAWSADSKSHVAHMDNGDFYGSEKAALIGAPGSVKIELIAKDGSSTVLKAKTSVQAGEIIDSSVMSKNALRNFIAAEIEDAKKQGVLLSVHLKATMMKVSDPIMFGQIVSEFYKDALTKHAEVLKQIGFDVNNGIGDLYARIKTLPEAKQKEIEADIQAVYAQRPQLAMVNSDKGITNLHVPSDVIVDASMPAMIRDSGKMWGPDGKLHDTKAVIPDRCYAGVYQVVIEDCKQHGAFDPTTMGSVPNVGLMAQKAEEYGSHDKTFQIPADGVVRVTDESGKLLLEQSVEAGDIWRMCQAKDAPIQDWVKLAVNRARATNTPAVFWLDPARAHDAQVIAKVERYLKDYDTSGLDIRILSPVEATRFSLARIREGKDTISVTGNVLRDYLTDLFPIMELGTSAKMLSIVPLMSGGGLFETGAGGSAPKHVQQFLEEGYLRWDSLGEFLALAASLEHLGNAYKNPKALVLASTLDQATGKILDNNKSPARKVGEIDNRGSHFYLALYWAQALAAQTEDKELQAQFTGIAKALTDNETKIVGELAAAQGKPVDIAGYYHPNTDLTSKAIRPSATFNAALAPLA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 80390
Sequence Length: 741
Domain: This molecule consists of two distinct domains, a small domain and a large domain. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.
Subcellular Location: Cytoplasm
EC: 1.1.1.42
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P39126 | MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKEVYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLRPVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIRFPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELAEKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEFDVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPSSVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIKNMD | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 46418
Sequence Length: 423
EC: 1.1.1.42
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P96318 | MVSHPCTADEAKPPSEGQLARFENGKLIVPDNLIVAYFKGDGIGPEIVESAKKVLDAAVDKAYGGTRRIVWWEVTAGEEAQKECGSLLPDGTLQAFKLARVNLKGPLTTPVGGGFRSLNVTLRMVLDLYSNVRPVKWYGQPTPHCHPENIDWVIFRENTEDVYAGIEWPFDSPEAQKIRDFLKKEFGIELTPDTGIGIKPISKWRTQRHVRRAMEWAIRNGYKHVTIMHKGNIMKYTEGAFRQWAYDLILSEFRDYVVTEEEVNTKYGGKAPEGKIIVNDRIADNMLQQIITRPGEYNVIVTPNLNGDYISDEANALVGGIGMAAGLDMGDGIAVAEPVHGSAPKYAGKNVINPTAEILSGMYLLSDFVGWPEVKLLVEYAVKQAIAHKQVTYDLAREMGGVTPISTTEYTDVLVDYIRHADLKALKGQ | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 47620
Sequence Length: 429
EC: 1.1.1.42
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Q8RQL9 | MAKIIWTRTDEAPLLATYSLKPVVEAFAATAGIEVETRDISLAGRILAQFADQLPEEQKVSDALAELGELAKTPEANIIKLPNISASVPQLKAAVKELQEQGYDLPEYEDAKDRYAAVIGSNVNPVLREGNSDRRAPVAVKNFVKKFPHRMGEWSADSKTNVATMGADDFRSNEKSVIMDEADTVVIKHVAADGTETVLKDSLPLLKGEVIDGTFISAKALDAFLLDQVKRAKEEGILFSAHMKATMMKVSDPIIFGHIVRAYFADVYAQYGEQLLAAGLNGENGLAAIYAGLDKLDNGAEIKAAFDKGLEEGPDLAMVNSAKGITNLHVPSDVIIDASMPAMIRTSGKMWNKDDQTQDALAVIPDSSYAGVYQTVIEDCRKNGAFDPTTMGTVPNVGLMAQKAEEYGSHDKTFRIEADGKVQVVASNGDVLIEHDVEKGDIWRACQTKDAPIQDWVKLAVNRARLSGMPAVFWLDPARAHDRNLTTLVEKYLADHDTEGLDIQILSPVEATQHAIDRIRRGEDTISVTGNVLRDYNTDLFPILELGTSAKMLSVVPLMAGGGLFETGAGGSAPKHVQQVIEENHLRWDSLGEFLALAESFRHELNTRNNTKAGVLADALDRATEKLLNEEKSPSRKVGEIDNRGSHFWLATYWADELANQTEDAELAETFAPVAEALNNQAADIDAALIGEQGKPVDLGGYYAPSDEKTSAIMRPVAAFNEIIDSLKK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 79285
Sequence Length: 729
EC: 1.1.1.42
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P50216 | MAKIIWTRTDEAPLLATYSLKPVVEAFAATAGIEVETRDISLAGRILAQFPERLTEDQKVGNALAELGELAKTPEANIIKLPNISASVPQLKAAIKELQDQGYDIPELPDNATTDEEKDILARYNAVKGSAVNPVLREGNSDRRAPIAVKNFVKKFPHRMGEWSADSKTNVATMDANDFRHNEKSIILDAADEVQIKHIAADGTETILKDSLKLLEGEVLDGTVLSAKALDAFLLEQVARAKAEGILFSAHLKATMMKVSDPIIFGHVVRAYFADVFAQYGEQLLAAGLNGENGLAAILSGLESLDNGEEIKAAFEKGLEDGPDLAMVNSARGITNLHVPSDVIVDASMPAMIRTSGHMWNKDDQEQDTLAIIPDSSYAGVYQTVIEDCRKNGAFDPTTMGTVPNVGLMAQKAEEYGSHDKTFRIEADGVVQVVSSNGDVLIEHDVEANDIWRACQVKDAPIQDWVKLAVTRSRLSGMPAVFWLDPERAHDRNLASLVEKYLADHDTEGLDIQILSPVEATQLSIDRIRRGEDTISVTGNVLRDYNTDLFPILELGTSAKMLSVVPLMAGGGLFETGAGGSAPKHVQQVQEENHLRWDSLGEFLALAESFRHELNNNGNTKAGVLADALDKATEKLLNEEKSPSRKVGEIDNRGSHFWLTKFWADELAAQTEDADLAATFAPVAEALNTGAADIDAALLAVQGGATDLGGYYSPNEEKLTNIMRPVAQFNEIVDALKK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 80081
Sequence Length: 738
EC: 1.1.1.42
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Q9ZH99 | MTELTGVSIVTYQHIKVPSQGEKITVNKAVLEVPDRPIIPFIEGDGIGIDIAPVMKNVVDAAVEKSYAGKRKIEWMEIYAGEKATKVYGKDNWLPDETLEAIKEYQVAIKGPLTTPVGGGIRSLNVALRQQLDLYVCLRPVRYFTGVPSPVKTPEKVNMVIFRENSEDIYAGIEWPAGSPEAVKLINFLQNEMGVKKIRFPETAGIGIKPVSKEGTSRLVRRAIQYAIDNDRDSVTLVHKGNIMKFTEGAFKDWGYEVAVKEFGAKPLDGGPWHVFENPKTGQKITIKDVIADAFLQQILLRPAEYSVIATLNLNGDYISDALAAEVGGIGIAPGANLSDTVGLFEATHGTAPKYAGQDKVNPGSLILSAEMMLRYLGWKEAADLVVQGIEGAIESKTVTYDFARLMTGAKEVSTSQFGKAIIKHIL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 46636
Sequence Length: 427
EC: 1.1.1.42
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P08200 | MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKLLKCSEFGDAIIENM | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
PTM: Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK).
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 45757
Sequence Length: 416
EC: 1.1.1.42
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D4GU92 | MSYDQIEVPDDGEKITVDEETGELSVPDNPIIPIIHGDGIGTDVGPAAQKVLDAAAEATGRSVSWMRVYAGSSARDKYDENLPEDTVSAIRNHRVAIKGPLTTPVGAGFRSLNVALRKKLDLYANVRPTYHLDGVPSPVKNPSAMDMVTFRENTEDVYAGIEWEAGTDEVQKVKEFVEEEMGADGVIHDGPVGIGIKPITEFGTKRLVREAIEYALENDRPSVTLVHKGNIMKFTEGAFRDWGYELAEEEFGDVTITEDELWEEYDGERPEDKVVVKDRIADNMLQQLLTRTADYDVIATMNLNGDYMSDAAGAQIGGLGIAPGANFGEGLCLAEPVHGSAPKYAGEDKVNPTAMILSGRLMFEYMGWKDAGKLIRDAVEKTISDGDVTYDLERQIEGGNKLATSEYADKVVENIKELA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 45810
Sequence Length: 419
EC: 1.1.1.42
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P56063 | MAYNPKILQKPKEGEEITIKDNKLHVPNHPIIPFIEGDGIGSDITPAMIKVVDSAVQKAYKGEKKIAWYEVFVGEKCYQKFKDYKELSPEEQWLLPDTIEAINHYKVSIKGPLTTPIGEGFRSLNVALRQKMDLYVCLRPVRWYGSPSPVKEPQKVDMVIFRENSEDIYAGIEWQEGSAEAKKLIHFLQNELKVKKIRFPESSGIGVKPISKEGTERLVRKAIEYAIDNDKPSVTFVHKGNIMKYTEGAFMKWGYALAQKEFNAQVIDKGPWCSLKNPKNGKEIIIKDMIADAFLQQILLRPSEYSVIATMNLNGDYISDALAAMVGGIGIAPGANLNDTVGMFEATHGTAPKYAGLDKVNPGSIILSAEMMLRHMGWVEAADLIVSAMEKAIKSKKVTYDFARLMDGAKEVKCSEFASVMIENM | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 47531
Sequence Length: 425
EC: 1.1.1.42
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P65098 | MSNAPKIKVSGPVVELDGDEMTRVIWKLIKDMLILPYLDIRLDYYDLGIEHRDATDDQVTIDAAYAIKKHGVGVKCATITPDEARVEEFNLKKMWLSPNGTIRNILGGTIFREPIVISNVPRLVPGWTKPIVIGRHAFGDQYRATNFKVDQPGTVTLTFTPADGSAPIVHEMVSIPEDGGVVLGMYNFKESIRDFARASFSYGLNAKWPVYLSTKNTILKAYDGMFKDEFERVYEEEFKAQFEAAGLTYEHRLIDDMVAACLKWEGGYVWACKNYDGDVQSDTVAQGYGSLGLMTSVLMTADGKTVEAEAAHGTVTRHYRQYQAGKPTSTNPIASIFAWTRGLQHRGKLDGTPEVIDFAHKLESVVIATVESGKMTKDLAILIGPEQDWLNSEEFLDAIADNLEKELAN | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Mass (Da): 45514
Sequence Length: 409
EC: 1.1.1.42
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A0A096P8D3 | MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable).
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 52553
Sequence Length: 470
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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A5CV36 | MPQHTELVVLLDDDGETIGTAPKATVHTRDTALHLAFSCHVFDAQGRILVTRRAIGKLTWPGVWTNSFCGHPAPDEDMREAVHRRAEQELGLELESVELVLPDFRYRATDAAGVVENEICPVFRAVAASPVDPRPEEVGEYQWVDPEQLIPAVAHTPWAFSPWLTLQLPLLYPEHAAHSGLAETAAAAAAVPAA | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 21180
Sequence Length: 194
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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P60923 | MNDVELVVLADEFGKPSGTAVKSEVHTTDTPLHFAFSCYVRNNKGDLLITRRALSKKTWPGVWTNSACGHLMPGETPEQAVARRVPHEIGISQDKLVNIACVLPDFSYRAVDSRGIVEWEICPVFTAAVTDDALLPEAEEVDSLVWVEPSKLIHAVHSAPFAFSPWMVEQLQHEALRTALTTS | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 20193
Sequence Length: 183
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
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Q8NN99 | MTTEVELVVLADSEGNPIGTAPKATVHTKDTPLHFAFSTYILNPRGELLVTRRALSKKTWPGVWTNSMCGHPGPDETNADAIRRRGVDELGLEVDSFLDIQEILPDYQYRAVDASGIVEWELCPVHLVRLAVGEFVEPLDDEVEEFEWAEPQKLFDAVDATPFVFSPWLVDQLSAPELRQAILEAFDAE | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 21121
Sequence Length: 189
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
Q6A5Z1 | MSHHDGENEGTSADSGYDDFVILLDDDGNHIGTAPRATVHSQHTPRHLAFSCHVLDVGGRVLVTRRALTKVAWPGVWTNTCCGHPRVGETIIDAAVRRTHQELGLDLDPRRMRVVLPDFSYRATDSGGIVEDEFCPVVVARLSLPEELVELNPDPDEVEEVAWVGWQDMYDLARSMPALLSPWAVEQMLEFGPDLPVVR | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 22101
Sequence Length: 199
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
Q9NH02 | MATKSNEENIAEFKGHNEIQIELMKEECIVVDNDDKPIRPGSKKETHLMVNINNGLLHRAFSIFLFNGEGKLLLQQRALEKITFPGYWTNTVCSHPLWIVGSELVEENAQGVKIAAKRKLNHELGVPLDQVNIDDFTFMTKIHYKSESKEDPQWGEHEIDHILIMQKDGITINAEPNEVMDYKYVSQEELDQLFKDEDEGKVKVTPWFRLIALNHLKPWWNNLNNLKPLVEPTNTIHRY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 27771
Sequence Length: 239
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
EC: 5.3.3.2
|
A8LQ20 | MKDLVPAWIDGALRPVGKLEAHQRGLRHKAVSVFVMRGPETLIQRRALDKYHTPGLWANTCCTHPLWDESPADCAVRRLREELGITGLYPAHRDRIEYRADVGNGLIEHEVVDLFIAEAPANLKVAPNPEEVAEVKWVDLYELNAQVKRRPERYTPWLRIYLAEHSERIFGTVATS | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 20112
Sequence Length: 176
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.3.2
|
P36177 | MVRSSCLQCDQPSQGSNSTFGCGGPLAAVCATGLLVLVLYSPSSQTANWSAQGISTKALYPAVPVPSTLLPGSAPAKHQLHVWRAHAMSEATTNNSFKQSLFGYNAISSIWLQLAGVAATFFAFGALMAAVTQRKEIAVFSASGQAAEPEGAEPLKRPFPSPAAKPKPLFSTPANSFSNIFQAPPSLRTDSTYGRGPRSTSFTDISNWPSNNALRNPQSVIDIGGGVDFLGDRSPGNPFTRLRGSPSSTLSNLGMGLGLGLGKGKGFGKGFGKGRGFPVEEEVEEEQEVLSWADRRRALADPDAPPMNEDIKYPQLRLVRAVPGGRDEKLGVMSRQEALELAEAEDIDLVLVSIDTDPPVAKLVNYSKLKYESEKKKKDSHKKGKVKEVKELKVSHKIGQHDYDVRVKQARKFLEGGHRIKVSMEFKGRENQFVEIGRAVMKRFQNDLADMGKADAVPKKLGTRLILNLAPAGEALKVIAERRAERDRKAAAEEEGEGDDLDFVDENEDEDVEGEGEEEEAEELEEETAEGTEVPTRS | Function: Involved in chloroplast protein synthesis. It enhances the poly(A,U,G)-dependent binding of the initiator tRNA to chloroplast 30S subunits.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 58255
Sequence Length: 538
Subcellular Location: Plastid
|
Q5B948 | MASNDKGLEEIPDSQIESNYDEITDSFDSMELKPELLRGVYAYGFERPSAIQQRAILPIVKGNDVIAQAQSGTGKTATFSISALQKLDPNVKACQALIVAPTRELAQQIQKVVIAIGDFMNIQCHACIGGTAVRDDMNALREGPQIVVGTPGRIHDMIQRRVLKTDQMKMFILDEADEMLSRGFTEQIYDIFQLLPQSTQVVLLSATMPQDVLEVTTKFMRDPVRILVKKQELTLEGIKQFYIAVEKEEWKLDTLSDLYETVTITQAVIFCNTRRKVDWLTDKLTARDFTVSAMHGDMEQAQRDVIMKEFRSGSSRVLIATDLLARGIDVQQVSLVINYDLPANRENYIHRIGRGGRFGRKGVAINFVTADDVRMMREIEQFYSTQIEEMPMNVADLI | Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 44937
Sequence Length: 398
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
Q8SQM5 | MKQVTEQAEDFVDTRSSGTEIREFEDLRSDSSQIRMFDTWEDYGLKEDLLKGIYSIGFETPSFIQKAAIQPIIDGRDIRAQAQSGTGKTGAFAVAALQICDMSQDVTQILVLASTREIAAQNAARFEDLGCFMGARVALLSGGSPIAADKVALEKKPHIVVGTPGRVEHMININELSMDNIKLFVIDEADEMLKAGFQEQVKSIFRRITNKDEVQIAMFSATYDEEELRVSEEILINPVIIDLRYNDQTLKGIRQYFIDLRKEPPFRKGREDYLLPKLVTLYDIFRKQRLGQSIVFINSKEDARIVYDWLIRHEWECELISAELTQAERERTLNRFRGGTGRCLISSGLLSRGIDIQNLSVVFCLDVPSFERKSTYIHRIGRSGRYGRKGIAINIVYEHELKNLKAIERFYNTTIKELPADFSFQ | Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 48490
Sequence Length: 425
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
P47943 | MVDQLEDSVIETNYDEVIDTFDDMNLKPELLRGIYAYGFERPSAIQQRAIMPILGERDVLAQAQSGTGKTATFSISVLQKIDTSLKQCQALILAPTRELAQQIQKVVVALGDLMNVECHACIGGTLVRDDMAALQAGVHVVVGTPGRVHDMIQRRALPTDAVQMFVLDEADEMLSRGFKDQIYDIFQLLPPTAQVVLLSATMPQDVLEVTTKFMRDPIRILVKKDELTLEGIKQFYVAVEKEEWKLDTLCDLYETVTVTQAVIFCNTRRKVDWLTEQLTERDFTVSSMHGDMDQAQRDTLMHEFRTGSSRILITTDLLARGIDVQQVSLVINYDLPANRENYIHRIGRGGRFGRKGVSINFVTNDDVRMMREIEQFYNTHIEEMPMNIADLI | Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 44436
Sequence Length: 392
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
Q38F76 | MAQQGKVEPQDQDSFLDDQPGIRPIPSFDDMPLHQNLLRGIYSHGFEKPSSIQQRAIVPFTRGGDIIAQAQSGTGKTGAFSIGLLQRLDFRHNVLQGLVLSPTRELAMQTAEVITRIGEFLAEGSSSFCATFVGGTRVQDDYRKLQSGTIVAVGTPGRVVDVTKRGAMRTESLRVLVLDEADEMLSQGFAEQIYDIFRFLPKEIQVALFSATMPDDVLELTKKFMRDPTRILVKRESLTLEGIKQFFIAVEEEHKLDTLMDLYETVSIAQSVIFANTRRKVDWLASQLNSSNHTVSCMHSEMSKQEREKVMGTFRNGSSRVLVTTDLVARGIDVHHVNIVINFDLPTNKENYLHRIGRGGRYGRKGVAINFVTQKDVEVLREIESHYHTQIEELPVDFAAYLGE | Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 45362
Sequence Length: 404
EC: 3.6.4.13
|
Q4P331 | MSKPEDTSAAAAAPAGEAGNNLNIADGEIESNWETVIDNFDNMELKEELLRGVYAYGFERPSAIQARAIVPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIKAVQALILAPTRELAQQIQKVVIALGDYMKIDCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDTQCVLLSATMPQEVLEVTKKFMRDPIRILVKRDELTLEGIKQFYVAVEKEDWKLDTLCDLYETVTITQAVIFCNTRRKVDWLTDKLTSREFTVSAMHGDMEQAQREVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPLNVADLI | Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 46245
Sequence Length: 411
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
P23301 | MSDEEHTFETADAGSSATYPMQCSALRKNGFVVIKSRPCKIVDMSTSKTGKHGHAKVHLVAIDIFTGKKLEDLSPSTHNMEVPVVKRNEYQLLDIDDGFLSLMNMDGDTKDDVKAPEGELGDSLQTAFDEGKDLMVTIISAMGEEAAISFKEAARTD | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts . Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome . Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step . Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity .
PTM: Lys-51 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Sequence Mass (Da): 17114
Sequence Length: 157
Subcellular Location: Cytoplasm
|
Q93VP3 | MSDDEHHFEASESGASKTYPQSAGNIRKGGHIVIKNRPCKVVEVSTSKTGKHGHAKCHFVAIDIFTAKKLEDIVPSSHNCDVPHVNRVDYQLIDITEDGFVSLLTDSGGTKDDLKLPTDDGLTAQMRLGFDEGKDIVVSVMSSMGEEQICAVKEVGGGK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Regulates cytokinin-mediated root protoxylem specification and represses secifically the expression of AHP6 . Regulates the induction of programmed cell death caused by infection with virulent pathogen .
PTM: Lys-51 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Sequence Mass (Da): 17140
Sequence Length: 159
Subcellular Location: Cytoplasm
|
Q20751 | MSDDHHDDEHFHTGDSGAAATFPKQCSALRKNEHVMIKGRPCKIVEMSTSKTGKHGHAKVHMVAIDIFTSKKLEDICPSTHNMDVPVVKRREYLLMAIDDGYCSLMDPESCEQKDDLKLPDTELGQQIRDAYEKDEGSVLVQVVSAIGEEAILGWKVSTKE | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Acts in somatic tissues and its function in the soma is essential for normal growth and reproduction .
PTM: Lys-54 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain and leads to the formation of a hypusine residue. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Sequence Mass (Da): 17953
Sequence Length: 161
Subcellular Location: Cytoplasm
|
Q07460 | MADELDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFNGKKYEDICPSTHNMDVPNIKRNDYQLIGIQDGYLSLLTESGEVREDLKLPEGDLGKEIEGKFNANEDVQISVISAMNEECAVAIKPCK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity).
PTM: Lys-50 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain and leads to the formation of a hypusine residue. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16720
Sequence Length: 153
Subcellular Location: Cytoplasm
|
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