ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P06660 | MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQAVLGDESHLRIRVVPDKANKTLTVEDTGIGMTKAELVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNDDEAYTWESSAGGTFTVTPTPDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVEKATEKEVTDEDEDEAAATKNEEGEEPKVEEVKDDAEEGEKKKKTKKVKEVTQEFVVQNKHKPLWTRDPKDVTKEEYAAFYKAISNDWEEPLSTKHFSVEGQLEFRAILFVPK... | 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... |
P40292 | MSSETFEFQAEISQLLSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPTKLDTGKDLRIDIIPDKENKTLTIRDTGIGMTKADLINNLGTIARSGTKQFMEALSAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESAAGGTFTLTQDTEGEQLGRGTKIILHLKDEQTDYLNESRIKEVVRKHSEFISYPIYLHVLKETEKEVPDEEAEETKEEEDEEKKAKIEEVDDEEEEEKKKKKKTKTVKESKIEEEELNKTKPIWTRNPADITQEEYASFYKSLSNDWEDHLAVKHFSVEGQLEFRAILYV... | 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... |
O61998 | MSEEMNGETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYQALTEPAELETGKELYIKITPNKADKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVASKHNDDDCYQWESSAGGSFIIRQVNDPELTRGTKITLYIKEDQTDYLEERRIKEIVKKHSQFIGYPIKLTVEKERDKEVSDDEAEEEKKDEDKEKKEGEIEDVGEDEEEDKKDKDKKKKKIKEKYHEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFR... | 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... |
Q18688 | MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVVRPFNDPEVTRGTKIVMHIKEDQIDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVEAKDEEKKEGEVENVADDADKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPF... | 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... |
P46598 | MADAKVETHEFTAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPSQLESEPELFIRIIPQKDQKVLEIRDSGIGMTKADLVNNLGTIAKSGTKSFMEALSAGADVSMIGQFGVGFYSLFLVADHVQVISKHNDDEQYVWESNAGGKFTVTLDETNERLGRGTMLRLFLKEDQLEYLEEKRIKEVVKKHSEFVAYPIQLVVTKEVEKEVPETEEEDKAAEEDDKKPKLEEVKDEEDEKKEKKTKTVKEEVTETEELNKTKPLWTRNPSDITQDEYNAFYKSISNDWEDPLAVKHFSVEGQLEFRAILFV... | 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... |
O44001 | MENKETFAFNADIQQLMSLIINTFYSNKEIFLRELISNASDALDKIRYEAITEPEKLKTKPELFIRLIPDKANNTLTIENSGIGMTKADLVNNLGTIARSGTKAFMEALQAGGDISMIGQFGVGFYSAYLVADSVTVVSKHNDDEQYVWESAAGGSFTVQKDDKYEPLGRGTRIILHLKEDQGEYLEERRLKDLVKKHSEFISFPIELAVEKTHEREVTESEDEEEKKADEKAEEKEGEEKKEGEEKKEGEEEKKEKTGKTKKVQEVTREWEQLNKQKPLWMRKPEEVTEEEYASFYKSLSNDWEEHLAVKHFSVEGQLE... | 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... |
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... |
O43109 | MAETFEFQAEISQLLSLIINTVYSNKEIFLRELVSNASDALDKIRYESLSDPSKLDTGKDLRIDIIPDKENKTLTIQDTGIGMTKADLVNNLGTIARSGTKQFMEALTAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESSAGGTFNISPDNGPSIGRGTKIILHLKDEQTDYLNESKIKEVIKKHSEFISYPIYLHVQKETEVEVPDEEAETVEEGDDKKPKIEEVEDDEEDKEKKPKTKKVKEVKTEEEELNKQKPIWTRNPQDITQEEYAAFYKSLSNDWEDHLAVKHFSVEGQLEFKAILFVPKRAP... | 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... |
Q4UDU8 | MASKEETPDQEVYAFNADISQLLSLIINAFYSNKEIFLRELISNASDALEKIRYEAIKDPKQIEDQPDYYIRLYADKNNNTLTIEDSGIGMTKADLVNNLGTIAKSGTRAFMEALQAGSDMSMIGQFGVGFYSAYLVADKVTVVSKNNADDQYVWESSASGHFTVKRDDSHEPLKRGTRLILHLKEDQTEYLEERRLKELVKKHSEFISFPISLSVEKTQETEVTDDEAEPEEEKKLEEEDKDKEEKVEDVTDEKVTDVTEEEEKKEEKKKKKRKVTNVTREWEMLNKQKPIWMRLPTEVTNEEYASFYKNLTNDWEDHL... | 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... |
Q8VZG2 | MEGSKLLPCVHKSPVPTSHQLYINYEILGLTKLKKHKYTQNKMSSSDSSSAESRLATAKTVLTTAASVAATAMLARSLVQDYLPDEVHHYISYGFRSIFGYFSSQMTIIIEEFEGFAHNEVFEAAEAYLATKISPSNKRIKVSKHEKENNYNVTVERDEEVVDTYNGVKFQWILHCRHVESKHFHNPRDLNSTLRSEVRSFELNFHKKFKDVALESYLPFMVKRATLMKQEKKTLKIFTLSPENMYGNYSDAWTSVTLDHPSTFKTLAMDSDVKTSVMEDLDKFVKRRDFYKRVGKAWKRGYLLYGPPGTGKSSLIAAMA... | 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 | MSKNSDALLWYHGKITREVAVQVLLRKGGRDGFFLIRDCGNAPEDYVLSMMFRSQILHFQINCLGDNKFSIDNGPIFQGLDMLISYYKVISDGLPCKLVDFCVGKIAPLYALKYGLDTRLHLACEEKNPNTVKELLQDSVIKENVNARSISGLTALHISCSNGDNDIVAMLLNAGADASAIDANGRTPVQVVCFYNHASTLHLLISKGSADFLKRSPNNGWVPLHEAAMRGSLECVKVLLSFNASMYPRSLDGDTPRDLALQYENYNVVEFFDNYPVNQPKTSITQWLHQNLDRNGALIILQNASMADGSFLIRSSIKCH... | 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... |
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. ... |
B0EXJ8 | MDVQSEEFRGAQAQIWSQSCSFITSASLKCAVKLGIPDTIDNHGKPITLSELTNALVPPVHPSKAPFIYRLMRVLAKNGFCSEEQLDGETEPLYSLTPSSRILLKKEPLNLRGIVLTMADPVQLKAWESLSDWYQNEDDSSTAFETAHGKNFWGYSSEHMEHAEFFNEAMASDSQLISKLLIGEYKFLFEGLASLVDIGGGTGTIAKAIAKNFPQLKCTVFDLPHVVANLESKENVEFVAGDMFEKIPSANAIFLKWILHDWNDEDCVKILKSCKKAIPAKGGKVIIIDMVMYSDKKDDHLVKTQTSMDMAMLVNFAAKE... | 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-hydroxytabersoni... |
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 ... |
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 CN... |
P15686 | MAGGGVVVVSGRGLSTGDYRGGLTVYVVMVAFMAACGGLLLGYDNGVTGGVVSLEAFEKKFFPDVWAKKQEVHEDSPYCTYDNAKLQLFVSSLFLAGLVSCLFASWITRNWGRKVTMGIGGAFFVAGGLVNAFAQDMAMLIVGRVLLGFGVGLGSQVVPQYLSEVAPFSHRGMLNIGYQLFVTIGILIAGLVNYAVRDWENGWRLSLGPAAAPGAILFLGSLVLPESPNFLVEKGKTEKGREVLQKLCGTSEVDAEFADIVAAVEIARPITMRQSWASLFTRRYMPQLLTSFVIQFFQQFTGINAIIFYVPVLFSSLGSA... | 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 | MSKHFFLHNEFHWQGRHDAEDGAAGSRVHHVVQQIDYTHIGENPYGVALLGFACDAGVARNKGRIGAKKSPDLIRRALANLAWHSPHPLYDLGTVVCDDDLLESSQQHCAKIIAEVLPCVPVITLGGGHEVAWASFSGLARYFEQHHPEKAPKIGIINFDAHFDLRAFSSSQADVKPSSGTPFNQIQHYCQQQGWDFHYACLGVSKASNTRALFERAEQLNVWFVEDKDLGSVNHDYHLTQLQHFIDDCDYLYLTIDLDVFPAATAPGVSAPAARGVSYDNLAPFLDRILAHRDKLMLADIAEYNPTYDVDSQTARLAAR... | 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 degradatio... |
Q20502 | MRLQVQIGTECVVVPCKPDDTIHAVAKKSVEKLRRLRPKLPLADDYFEVRRTVGNSLLDPEDLVSDVLKDSDFIIVAASVEETEDAKEAKKQEEIDNARAEIEKIDNRRRKVSFADSLAPMVLAPPTKLLILDGNSLLPEDLVRCEKGECAIQLSMESEDRIRKARTFLEKIASEHRAVYGVTTGFGTFSNVTIPPEKLKKLQLNLIRSHATGYGEPLAPNRARMLLALRINILAKGHSGISVENIKKMIAAFNAFCVSYVPQQGTVGCSGDLCPLAHLALGLLGEGKMWSPTTGWQPADVVLKKNNLEPLELGPKEGLA... | 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 in... |
Q8RFC2 | MEVFILELVLGSKNITLEDLINVTRKGYKVSISEEAYEKIDKARALVDKYVEEGKVSYGITTGFGKFAEVSISKEQTGQLQKNIVMSHSCNVGNPLPIDIAKGIVLLRAVNLAKGYSGARRIVIEKLVELLNKDVTPWIPEKGSVGSSGDLSPLAHMSLVLIGLGKAYYKGELLEAKDALAKADIEPIPALSSKEGLALTNGTQALTSTGAHVLYDAINLSKHLDIAASLTMEGLHGIIDAYDPRIGEVRGHLGQINTAKNMRNILAGSKNVTKQGVERVQDSYVLRCIPQIHGASKDTLEYVKQKVELELNAVTDNPII... | 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 in... |
A8MF65 | MNIDVWIKNITQLVTVQAHGKPKKGKEMQDVGIIQDGWIAVAGDRIVGIGSGEISADFQVGENTVIISGEGKTVTPGLIDPHTHLVHAGSRENELALKLKGVPYLEILKQGGGILSTVNATKKATMEELVAQSKKSLDRMLSYGVTTVEIKSGYGLELEAEIKQLEAIHRLQQQTPMDLVSTFMGAHAIPKEYKENPEEFIDLIIEEMLPAIKEKNLAEFCDVFCEEGVFSVDQTRRILEAARSLGFKNKIHADEIVPLGGAELAAELQTISAEHLMAASETGLKMMAESNVVPVALPGTSFNLATGKYADARKMIEYGL... | 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-formimidoy... |
Q2IHZ6 | MSRPAATLVLRNAVVATCDRGPSDAGLLPGAAVAVEGRRVAWVGRERDVEAEVNLAGAQVIDARGGLVTPGLVDSHTHLVFAGERAGEFALRCAGRTYLQVALSGGGIAVTTRETRAAPDEQLLAAAAARARRLIAQGVTTLEVKSGYGLDAPEELRLLRIVHQLGRALGGDATILPTLLFHAVPPEQVGDRAGFVRDACASLIPQVARERLAQFCDVFVEDGAFAPDEARLLLQAAKDRGLVPRVHAEQLTAGGGARLAAELGCSSADHLEELDDAGIAALAQARVVAGLLPLSTLFLGSERYAPARRLLEAGVPVSLA... | 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-formimidoy... |
Q01W05 | MSDSALLNCRQLVTLAGPPGPRTGPAMRELAIIPDGAMRIRDGCIAAVGPRADIVRSLAGDTEVIDAGWRVVLPGFIDAHTHPVFAGTRAAEYEQRAEGATYAEIAAAGGGIRSTVRRTREAGDLELATAARRYTDWFLRGGTTTIEAKSGYGLSLDDELRILKTIRLLNAERRLRYVPTFLGAHEIPDEYRGEIEDYVDLVIQEMLPAVAEDNLAEYCDVFCEPNVFPLDPARAILQAAQSLGLRLRIHADQFTGDYAALLAAELGAATADHLESTTALGLAALHEAGVQPVLLPASVYNLGSARYPAARDMIARGMAV... | 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-formimidoy... |
Q8XW28 | MNTMTDAAHLAADPRYDAAREIRAPRGTELHCKSWLTEAAYRMLQNNLDPDVAENPKHLVVYGGIGRAARDWACFDKILETLRELNDDESLLVQSGKPVGVFKTHPDAPRVLIANSNLVPKWANWEHFNALDRKGLFMYGQMTAGSWIYIGSQGIVQGTYETFAEAGRQHYSDRPSALLKQGLSPEGTAPGSGRSSAQVPGSHLAGRWILTAGLGGMGGAQPLAATLAGAVSLTIECQQSSIDFRLRTRYLDKQARDIDDALNLIRHHCERGEAVSIGLLGNAAELLPELVRRARAGGLKPDLVTDQTSAHDLVNGYLPA... | 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-formimid... |
A4FNF1 | MSSARPVRAARGTTLTARSWSTEAPLRMLQNNLDPEVAERPDDLVVYGGTGKAARNWASFDAIVRELTTLSDDETLLVQSGKPVGVLRTHEWAPRVLLANSNLVGDWANWPEFRRLDALGLMMYGQMTAGSWIYIGTQGILQGTYETFAAVAERRFGGTLAGTLTITAGLGGMGGAQPLAVTMNEGVALVVECDPERAHRRVKHGYLDEVADGLDQAIEKAEAAKAQRRAYSVAVIGNAAEVLPELLRRGVRADIVTDQTSAHDPLSYLPLGVELEDWEDYASKKPEEFTDRARDSMAKHVEAMVGFMDAGAEVFDYGNS... | 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-formimid... |
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
Sub... |
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 (axi... |
A0A1L8I316 | MVTLSPAYLPSDGGTQAASAAPSVEENWVVQPSLTLLVLLLVPCVLLLFFLNCFLLFHRLPAFSLRKRASRRKVGQYPCVRVGHSGQARLEPPYMLSPGVVLREGRLGSDTISQGFEATLALEEGVCGRQNTPQSRGSCCQGGSIPSDQICCSPRPRCATPLPCCAPRRAWNAPAYVKKRLRPKVWKVREDELGSSCELDTRHNHVPPNTPAADNALGVTPKVKFCHTSSTQRKSHVGMVPFTLGGSELLEDPSVIPREDTAEHLDASSSLPGPGLDSDFGVSAGISLHILSSDSDSGSQSWTSGMEWDYYDPCYMRRNR... | 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 (axi... |
P46593 | MRLSTAQLIAIAYYMLSIGATVPQVDGQGETEEALIQKRSYDYYQEPCDDYPQQQQQQEPCDYPQQQQQEEPCDYPQQQPQEPCDYPQQPQEPCDYPQQPQEPCDYPQQPQEPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDQPDDNPPIPNIPTDWIPNIPTDWIPDIPEKPTTPATTPNIPATTTTSESSSSSSSSSSSTTPKTSASTTPESSVPATTPNTSVPTTSSESTTPATSPESSVPVTSGSSILATTSESSSAPATTPNTSVPTTTTEAKSSSTPLTTTTEHDTTVVTVTSCS... | 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 colonizatio... |
Q969A8 | MQPRQPGDEAKQLAELEVVRQMMTPTREVLLELHESFLKELQRGLEMHKRHGITWVPEECSMKMLDSCVSNLPTGAEVGEAYAIDFGGSTCRAVRCSLLGKGKMEIIQDKICLRSAEHRCAKGFMDKKAGGKELFDQFAMCIRGLMDRSGDLKKAEETNTPVPVGFTFSFPCAQAALNSSFLIEWTKGFETGRENPDRVEGKDVAVLLADALQRHNVPAVCKAIVNDTVGTLVSCAYQRVPGTPECRVGLIIGTGFNACYVEPEASNYGYTGTVVNMEAGNFHKDLPRNEIDVEVDEKTHNRGKQQFEKLVSGYYIGEIV... | 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 | MGATATDIEKVPSAGTPDEPKAGETNVYVDTEAEKSFVRKVDFFVLPMLCLMYFFDCMDRSNLANAKTDGLEEDINLKGNEYSLLILLFYIPFGLFDLPWNLLIKRYSARIMLSLRRYAVTVVWGICALCQCAANNFGGLLAIRIILGVFEAGFFAGSTFYFTLFYTRNEMGFRLAVLQSFAVLASAFSGLISFGLFQINHSAVKGWQWLFIVEGAMTLIIGVIGFWWLPDTAQSAWFLTQRERDAASARLLRDTSAEIETKLELKAAFQTWSDWKFPIWAVITFSYPVAYATAMNFFPIIVARLGYSVVKTNLWTVAPN... | 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 o... |
C8VK14 | MAPTAPPILDFSPFYGTDGAAKAKLVQQVRESCEYNGFFQITGHRIPRELQVRVMDAAKRFFALPLEEKMAIDKNLNSFNRGYELLRSQMLEVGTAPELKEGLYIGEEIGADHPYYINGRLNSGPNQWPATVPDAQEFRETSMEYYHAVYELAKDVLAVLALTLDVEESFFDPLTEGGVATMRMLHYPSQPKDEDEKLNRGIGAHTDFGCITLLLQDEVDGLQVLDAPSGQWLDVQPVLGAYVVNLGDLMMRMANDRYKSNIHRVINKSGRERYSIPFFFSGNPDHVCKCLPNCCKAGEQPKYPPITVEDMVRGAYKQSY... | 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 hx... |
C8VK15 | MDISYPVINAGGLKNIASQIIMEIELDKRENRPTDNVPPDDIGKIEVVDDAEMEQFYGSSTTDAYRLKSELVSQCMADIGMGRFQWKLFTVAGFGWIVDNFCSQGISAVQPPIQQEFSGIKQVSYSSVAYYVGMIIGASFWGISSDLIGRKPAFNSTLAIAGIFLCAAAGTSNFIAFSALWAVIGTAAGGNVVCDSMILLEFIPGSHQYLLTALSGWWNLGQLVVSLLAWVFLANFSCPTDATPDTCSRADNMGWRYTLITLGGLSLAFTFVRIFVFKMPETPRYLLSQGNDQAAVDAVNYVARQNGKPEPLTLSMLQAI... | 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 o... |
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 dephosphory... |
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... |
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 Act... |
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).... |
P42833 | MTAQIPYQHSSGYISHFHNNELDAGRGRDYNVTIKYLDDKEENIEGQAAKISHNASLHIPVLLCLVISLGGFIFGWDIGTIGGMTNMVSFQEKFGTTNIIHDDETIFVSTKKLTDLQIGLIISIFNISCGVGALTLSKIGDWIGRKGGIWFALVVYCIGITIQILSYGRWYFLTLGRAVTGIGVGVTTVLVPMFLSENSPLKIRGSMVSTYQLIVTFGILMGNILNFICERCYKDPTQNIAWQLPLFLGYIWAIIIGMSLVYVPESPQYLAKIKNDVPSAKYSFARMNGIPATDSMVIEFIDDLLENNYNNEETNNESKK... | 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 | MASEQSSPEINADNLNSSAADVHVQPPGEKEWSDGFYDKEVINGNTPDAPKRGFLGYLIIYLLCYPVSFGGFLPGWDSGITAGFINMDNFKMNFGSYKHSTGEYYLSNVRMGLLVAMFSVGCSIGGVAFARLADTLGRRLAIVIVVLVYMVGAIIQISSNHKWYQYFVGKIIYGLGAGGCSVLCPMLLSEIAPTDLRGGLVSLYQLNMTFGIFLGYCSVYGTRKYSNTAQWRIPVGLCFLWALIIIVGMLLVPESPRYLIECERHEEACVSIAKINKVSPEDPWVLKQADEINAGVLAQRELGEASWKELFSVKTKVLQR... | 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 | MNVNSSSNRGEAILAALKTQFPGAVLDEERQTPEQVTITVKINLLPDVVQYLYYQHDGWLPVLFGNDERTLNGHYAVYYALSMEGAEKCWIVVKALVDADSREFPSVTPRVPAAVWGEREIRDMYGLIPVGLPDQRRLVLPDDWPEDMHPLRKDAMDYRLRPEPTTDSETYPFINEGNSDARVIPVGPLHITSDEPGHFRLFVDGEQIVDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSVAYTNSVENALGIEVPQRAHTIRSILLEVERLHSHLLNLGLSCHFVGFDTGFMQFFRVREKSMTMAELL... | 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 | MNPSSLVLNGLTSYFENGRARVVPPVGRNILGVVNYASVCEYPTLDHGYPELEINMVAPTAEPFAEVWVTDAESEHGERDGITYAHDGEYFFCAGRVPPTGRYTEATRAAYVTMFELLEEFGYSSVFRMWNFIGDINRDNAEGMEVYRDFCRGRAEAFEQCRLEFDQFPAATGIGSRGGGIAFYLLACRSGGHVHIENPRQVPAYHYPKRYGPRAPRFARATYLPSRAADGVGGQVFVSGTASVLGHETAHEGDLVKQCRLALENIELVISGGNLAAHGISAGHGLTALRNIKVYVRRSEDVPAVREICREAFSPDADIV... | 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 Leng... |
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) si... |
P25016 | MVPITSLAQTLERLRRKDYSCLELVETLIARCEAAKALNALLATDWGGLRRRAKKIDRHGNAGVGLRGIPLCFKANIATGIFPTTAATPALINHLPKIPSRIAERLFSAGALPGASGNMHELSFGITSNNYATGAVRNPWNPSLIPGGSSGGVAAAVASRLMLGGIGTDTGASVRLPAALCGVVGFRPTLGRYPRDRIIPVSPTRDTAGIIAQCVADVVILDQVISGRPARILPIPLKGLRIGLPTTYFYDDLDADVAFAAETTIRLLANRGVTFVEADIPHLEDLNSGASLPIALYEFPHALKQYLDDFVGTVSFSDVI... | 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 | MVRGRHRSRDPQRRDLRGRDRRSASRTDARRQSAAERGCRRSQRGSAEGCACGRQTGPRAARSACCTACPSRSRRMSTTEGRPNFNGVPANKDFVAPSDSPVVHNLKKAGAIVIGLTNTPEFSFRGFTDNPLHGLTLNPWDPNITCGGSSGGAGSAVAAGIGTIAHGNDIGGSLRWPAHCNGVATIKPTQGRIPAFNGSATAERPMLAHLMSAQGPLARHVGDVRLALDVMSQADPRDPWWVPAPLAGPRPKGPIKVALARIPEDMDVDPSVRAALRQAADHLERSGYRVTEVDVPDIDGVWQTWCDIITNETVVMQEAG... | 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 | MHEIITLESLCQALADGEIAAAELRERALDTEARLARLNCFIREGDAVSQFGEADHAMKGTPLWGMPVSFKDNICVRGLPLTAGTRGMSGFVSDQDAAIVSQLRALGAVVAGKNNMHELSFGVTSINPHWGTVGNPVAPGYCAGGSSGGSAAAVASGIVPLSVGTDTGGSIRIPAAFCGITGFRPTTGRWSTAGIIPVSHTKDCVGLLTRTAGDAGFLYGLLSGKQQSFPLSRTAPCRIGLPVSMWSDLDGEVERACVNALSLLRKTGFEFIEIDDADIVELNQTLTFTVPLYEFFADLAQSLLSLGWKHGIHHIFAQVD... | 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... |
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: Se... |
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 repeti... |
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 ... |
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 f... |
Q8IU81 | MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPATKDLAAAAAQGPQLPPPQAQPQPSGTGGGVSGQDRYDRATSSGRLPLPSPALEYTLGSRLANGLGREEAVAEGARRALLGSMPGLMPPGLLAAAVSGLGSRGLTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYER... | 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-conj... |
Q7Z5L9 | MAAAVAVAAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAHGCFPEGRSPPGAAASAAAKPPPLSAKDILLQQQQQLGHGGPEAAPRAPQALERYPLAAAAERPPRLGSDFGSSRPAASLAQPPTPQPPPVNGILVPNGFSKLEEPPELNRQSPNPRRGHAVPPTLVPLMNGSATPLPTALGLGGRAAASLAAVSGTAAASLGSAQPTDLGAHKRPASVSSSAAVEHEQREAAAKEKQPPPPAHRGPADSLSTAAGAAELSAEGAGKSRGSGEQDWVNRPKTVRDTLLALHQHGHSGP... | 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 immatur... |
Q9H1B7 | MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAAAAAAAAQQQQQQQQQQQQQQQQQQQQQQQQQLNHVDGSSKPAVLAAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHTARLPNGLGGPNGFPKPTPEEGPPELNRQSPNSSSAAASVASRRGTHGGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPPPHALGSRGPPTPAPPGAPGGPACLGGTPGVSATSSSASSSTSSSV... | 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 syst... |
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 | MLRVFIFFVFLGSGLTGRIKPQVTCKYFISENNTWYKYNVTILNSSIILPAYNTIPSNAAGISCTCHDIDYLQKNNISIHYNTSILKTFQDIRIIRCGMKNISEIAGGFGKELKFLDLRYNDLQVIDYNILRKLIRSNTPTYLYYNNLMCGKRNCPLYYFLLKQEQTYLKRLPQFFLRRISFSNNNTYLYHFLSCGNKPGHEFLEYQTKYCRTKFPEINITVNQLIAKKNTERYKSCYPLVFISILCSCISFLFLFICLLRSICKKYSCTKQDKSSHNYIPLIPSYTFSLKKHRHPETAVVEDHTTSANSPIVYIPTTEE... | 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 leuci... |
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-cy... |
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-glyc... |
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-lin... |
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-glyc... |
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... |
F4HZG9 | MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPHLMAEGEVTPGIRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERGLCMFMPESTPKDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNVQSASQRYTNLDDFQNSASLGKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSS... | 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): 5498... |
Q10439 | MSGYIRTLFIRNRFSNYRLRSQIIKYKYSNVSYLNKSALRCGQATDSTHPHILQPGELTPRISAQEYKTRRDRVASLLEDNDFMIVTSAPVRHMCGAAFYEYHQDPNFYYLTGCLEPNAVLLMFKNGASGSYDCSLYLPSKNPYIEKWEGLRTGSTLGKKLFQIENVYDSSLASSVINALGKKSNRIFYNYQTGYLSKMPAASAPEFIQDTLTKLFRTSTQRSVDELLHPLRSIKSTAELECMKEAANISSNVYREIMRKRFEKEAEMSAEFNYRFCIGGCDRSAYVPVVAGGKNGLTIHYTINNDIFRPDEMVLVDAGG... | 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 ... |
P40051 | MLHRINPVRFSMQSCQRYFSKLVSPLEQHKSNTFTNRVRIPIEAGQPLHETRPFLIKSGELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQFASGAVFYPFQQENDLFYLSGWNEPNSVMILEKPTDSLSDTIFHMLVPPKDAFAEKWEGFRSGVYGVQEIFNADESASINDLSKYLPKIINRNDFIYFDMLSTSNPSSSNFKHIKSLLDGSGNSNRSLNSIANKTIKPISKRIAEFRKIKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDKDAYIPVVATGSNSLCIHYTRNDDVMFD... | 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 ... |
Q8LE98 | MPRPRVSELSQRQAPRLRSSSSTSDSNHSNRLITTDQSFKPGVDRKSPRSGGPNSDPLGQKKLGGRISDLESQLGQAQEELRLLKEQLANAEAVKKQAQDELHKKSKKPNPLARVEESATEAERIDRDEIPGDVQKETDVFEVPVEKIAVEEEELRSGNDEAEKLVAKEDEIKMLKARLYDMEKEHESLGKENESLKNQLSDSASEISNVKANEDEMVSKVSRIGEELEESRAKTAHLKEKLESMEEAKDALEAEMKKLRVQTEQWRKAADAAAAVLSGEFEMNGRDRSGSTEKYYAGGFFDPSAGFMDPPGMADDYDDG... | 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 directional... |
Q8VYU8 | MQTPKSRPGSLELPQKKSPLPAPKVVRRLKPSGAESDPKTKTISKTQIPKVVADRRSARIPLNEIQKKRTGRIPELESTISQLQEELKKAKEELNRSEALKREAQEEAEDAKHQLMDINASEDSRIEELRKLSQERDKTWQSELEAMQRQHGMDSTALSSAINEVQKLKSKLFESESELEQSKYEVRSLEKLVRQLEEERVNSRDSSSSMEVEELKEAMNLSRQEITQLKSAVEAAETRYQEEYIQSTLQIRSAYEQTEAVKSRYSQREAELTEELNRTKDEIEGLRKELMEKVKEDESTGDLKKLESDLMEVRGSLMDK... | 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 membra... |
P21954 | MSMLSRRLFSTSRLAAFSKIKVKQPVVELDGDEMTRIIWDKIKKKLILPYLDVDLKYYDLSVESRDATSDKITQDAAEAIKKYGVGIKCATITPDEARVKEFNLHKMWKSPNGTIRNILGGTVFREPIVIPRIPRLVPRWEKPIIIGRHAHGDQYKATDTLIPGPGSLELVYKPSDPTTAQPQTLKVYDYKGSGVAMAMYNTDESIEGFAHSSFKLAIDKKLNLFLSTKNTILKKYDGRFKDIFQEVYEAQYKSKFEQLGIHYEHRLIDDMVAQMIKSKGGFIMALKNYDGDVQSDIVAQGFGSLGLMTSILVTPDGKTF... | 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
Se... |
O67480 | MNKTTFENVYYWEGKAQIPQEGQFIKLKEDKTLEVPDNPIIPFIEGDGIGPEITQAMLLIINTAVEKTYNGSKKIYWVELLAGDKAEEKTGERLPQETLDVLKESIVGIKGPLGTPVGKGVRSINSALRRAFDYYSAVRPVYWMGQATPIPNPERVDLVVFRENTDDVYAGVEFFAGTPEAKKVREFLIKEMGAKEEGFPEDVGITVKPMSEFKTKRHVRKALRYALENNKKNVAVIGKGNIMKATEGAFINWAFEVAEEPEFKGKVVTDPEAEPGEGQVKLTKVITDQMLMQLVLKPEAWDVIIAQNLNGDYVSDLAAS... | 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
|
O29610 | MQYEKVKPPENGEKIRYENGKLIVPDNPIIPYFEGDGIGKDVVPAAIRVLDAAADKIGKEVVWFQVYAGEDAYKLYGNYLPDDTLNAIKEFRVALKGPLTTPVGGGYRSLNVTIRQVLDLYANVRPVYYLKGVPSPIKHPEKVNFVIFRENTEDVYAGIEWPRGSEEALKLIRFLKNEFGVTIREDSGIGIKPISEFATKRLVRMAIRYAIENNRKSVTLVHKGNIMKYTEGAFRDWGYEVAKQEFGEYCITEDELWDKYGGKQPEGKIVVKDRIADNMFQQILTRTDEYDVIALPNLNGDYLSDAAAALIGGLGIAPGS... | 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
|
P16100 | MSTPKIIYTLTDEAPALATYSLLPIIKAFTGSSGIAVETRDISLAGRLIATFPEYLTDTQKISDDLAELGKLATTPDANIIKLPNISASVPQLKAAIKELQQQGYKLPDYPEEPKTDTEKDVKARYDKIKGSAVNPVLREGNSDRRAPLSVKNYARKHPHKMGAWSADSKSHVAHMDNGDFYGSEKAALIGAPGSVKIELIAKDGSSTVLKAKTSVQAGEIIDSSVMSKNALRNFIAAEIEDAKKQGVLLSVHLKATMMKVSDPIMFGQIVSEFYKDALTKHAEVLKQIGFDVNNGIGDLYARIKTLPEAKQKEIEADIQ... | 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 ... |
P39126 | MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKEVYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLRPVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIRFPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELAEKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEFDVVATMNLNGDYISDALAAQ... | 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
|
P96318 | MVSHPCTADEAKPPSEGQLARFENGKLIVPDNLIVAYFKGDGIGPEIVESAKKVLDAAVDKAYGGTRRIVWWEVTAGEEAQKECGSLLPDGTLQAFKLARVNLKGPLTTPVGGGFRSLNVTLRMVLDLYSNVRPVKWYGQPTPHCHPENIDWVIFRENTEDVYAGIEWPFDSPEAQKIRDFLKKEFGIELTPDTGIGIKPISKWRTQRHVRRAMEWAIRNGYKHVTIMHKGNIMKYTEGAFRQWAYDLILSEFRDYVVTEEEVNTKYGGKAPEGKIIVNDRIADNMLQQIITRPGEYNVIVTPNLNGDYISDEANALVGG... | 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
|
Q8RQL9 | MAKIIWTRTDEAPLLATYSLKPVVEAFAATAGIEVETRDISLAGRILAQFADQLPEEQKVSDALAELGELAKTPEANIIKLPNISASVPQLKAAVKELQEQGYDLPEYEDAKDRYAAVIGSNVNPVLREGNSDRRAPVAVKNFVKKFPHRMGEWSADSKTNVATMGADDFRSNEKSVIMDEADTVVIKHVAADGTETVLKDSLPLLKGEVIDGTFISAKALDAFLLDQVKRAKEEGILFSAHMKATMMKVSDPIIFGHIVRAYFADVYAQYGEQLLAAGLNGENGLAAIYAGLDKLDNGAEIKAAFDKGLEEGPDLAMVN... | 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
|
P50216 | MAKIIWTRTDEAPLLATYSLKPVVEAFAATAGIEVETRDISLAGRILAQFPERLTEDQKVGNALAELGELAKTPEANIIKLPNISASVPQLKAAIKELQDQGYDIPELPDNATTDEEKDILARYNAVKGSAVNPVLREGNSDRRAPIAVKNFVKKFPHRMGEWSADSKTNVATMDANDFRHNEKSIILDAADEVQIKHIAADGTETILKDSLKLLEGEVLDGTVLSAKALDAFLLEQVARAKAEGILFSAHLKATMMKVSDPIIFGHVVRAYFADVFAQYGEQLLAAGLNGENGLAAILSGLESLDNGEEIKAAFEKGLE... | 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
|
Q9ZH99 | MTELTGVSIVTYQHIKVPSQGEKITVNKAVLEVPDRPIIPFIEGDGIGIDIAPVMKNVVDAAVEKSYAGKRKIEWMEIYAGEKATKVYGKDNWLPDETLEAIKEYQVAIKGPLTTPVGGGIRSLNVALRQQLDLYVCLRPVRYFTGVPSPVKTPEKVNMVIFRENSEDIYAGIEWPAGSPEAVKLINFLQNEMGVKKIRFPETAGIGIKPVSKEGTSRLVRRAIQYAIDNDRDSVTLVHKGNIMKFTEGAFKDWGYEVAVKEFGAKPLDGGPWHVFENPKTGQKITIKDVIADAFLQQILLRPAEYSVIATLNLNGDYIS... | 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
|
P08200 | MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGI... | 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
|
D4GU92 | MSYDQIEVPDDGEKITVDEETGELSVPDNPIIPIIHGDGIGTDVGPAAQKVLDAAAEATGRSVSWMRVYAGSSARDKYDENLPEDTVSAIRNHRVAIKGPLTTPVGAGFRSLNVALRKKLDLYANVRPTYHLDGVPSPVKNPSAMDMVTFRENTEDVYAGIEWEAGTDEVQKVKEFVEEEMGADGVIHDGPVGIGIKPITEFGTKRLVREAIEYALENDRPSVTLVHKGNIMKFTEGAFRDWGYELAEEEFGDVTITEDELWEEYDGERPEDKVVVKDRIADNMLQQLLTRTADYDVIATMNLNGDYMSDAAGAQIGGLG... | 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
|
P56063 | MAYNPKILQKPKEGEEITIKDNKLHVPNHPIIPFIEGDGIGSDITPAMIKVVDSAVQKAYKGEKKIAWYEVFVGEKCYQKFKDYKELSPEEQWLLPDTIEAINHYKVSIKGPLTTPIGEGFRSLNVALRQKMDLYVCLRPVRWYGSPSPVKEPQKVDMVIFRENSEDIYAGIEWQEGSAEAKKLIHFLQNELKVKKIRFPESSGIGVKPISKEGTERLVRKAIEYAIDNDKPSVTFVHKGNIMKYTEGAFMKWGYALAQKEFNAQVIDKGPWCSLKNPKNGKEIIIKDMIADAFLQQILLRPSEYSVIATMNLNGDYISD... | 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
|
P65098 | MSNAPKIKVSGPVVELDGDEMTRVIWKLIKDMLILPYLDIRLDYYDLGIEHRDATDDQVTIDAAYAIKKHGVGVKCATITPDEARVEEFNLKKMWLSPNGTIRNILGGTIFREPIVISNVPRLVPGWTKPIVIGRHAFGDQYRATNFKVDQPGTVTLTFTPADGSAPIVHEMVSIPEDGGVVLGMYNFKESIRDFARASFSYGLNAKWPVYLSTKNTILKAYDGMFKDEFERVYEEEFKAQFEAAGLTYEHRLIDDMVAACLKWEGGYVWACKNYDGDVQSDTVAQGYGSLGLMTSVLMTADGKTVEAEAAHGTVTRHYR... | 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
|
A0A096P8D3 | MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDA... | 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).
Ca... |
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 = di... |
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 = di... |
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 = di... |
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 = di... |
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
Sequ... |
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 = di... |
P36177 | MVRSSCLQCDQPSQGSNSTFGCGGPLAAVCATGLLVLVLYSPSSQTANWSAQGISTKALYPAVPVPSTLLPGSAPAKHQLHVWRAHAMSEATTNNSFKQSLFGYNAISSIWLQLAGVAATFFAFGALMAAVTQRKEIAVFSASGQAAEPEGAEPLKRPFPSPAAKPKPLFSTPANSFSNIFQAPPSLRTDSTYGRGPRSTSFTDISNWPSNNALRNPQSVIDIGGGVDFLGDRSPGNPFTRLRGSPSSTLSNLGMGLGLGLGKGKGFGKGFGKGRGFPVEEEVEEEQEVLSWADRRRALADPDAPPMNEDIKYPQLRLVR... | 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 | MASNDKGLEEIPDSQIESNYDEITDSFDSMELKPELLRGVYAYGFERPSAIQQRAILPIVKGNDVIAQAQSGTGKTATFSISALQKLDPNVKACQALIVAPTRELAQQIQKVVIAIGDFMNIQCHACIGGTAVRDDMNALREGPQIVVGTPGRIHDMIQRRVLKTDQMKMFILDEADEMLSRGFTEQIYDIFQLLPQSTQVVLLSATMPQDVLEVTTKFMRDPVRILVKKQELTLEGIKQFYIAVEKEEWKLDTLSDLYETVTITQAVIFCNTRRKVDWLTDKLTARDFTVSAMHGDMEQAQRDVIMKEFRSGSSRVLIA... | 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 ... |
Q8SQM5 | MKQVTEQAEDFVDTRSSGTEIREFEDLRSDSSQIRMFDTWEDYGLKEDLLKGIYSIGFETPSFIQKAAIQPIIDGRDIRAQAQSGTGKTGAFAVAALQICDMSQDVTQILVLASTREIAAQNAARFEDLGCFMGARVALLSGGSPIAADKVALEKKPHIVVGTPGRVEHMININELSMDNIKLFVIDEADEMLKAGFQEQVKSIFRRITNKDEVQIAMFSATYDEEELRVSEEILINPVIIDLRYNDQTLKGIRQYFIDLRKEPPFRKGREDYLLPKLVTLYDIFRKQRLGQSIVFINSKEDARIVYDWLIRHEWECELI... | 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 ... |
P47943 | MVDQLEDSVIETNYDEVIDTFDDMNLKPELLRGIYAYGFERPSAIQQRAIMPILGERDVLAQAQSGTGKTATFSISVLQKIDTSLKQCQALILAPTRELAQQIQKVVVALGDLMNVECHACIGGTLVRDDMAALQAGVHVVVGTPGRVHDMIQRRALPTDAVQMFVLDEADEMLSRGFKDQIYDIFQLLPPTAQVVLLSATMPQDVLEVTTKFMRDPIRILVKKDELTLEGIKQFYVAVEKEEWKLDTLCDLYETVTVTQAVIFCNTRRKVDWLTEQLTERDFTVSSMHGDMDQAQRDTLMHEFRTGSSRILITTDLLAR... | 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 ... |
Q38F76 | MAQQGKVEPQDQDSFLDDQPGIRPIPSFDDMPLHQNLLRGIYSHGFEKPSSIQQRAIVPFTRGGDIIAQAQSGTGKTGAFSIGLLQRLDFRHNVLQGLVLSPTRELAMQTAEVITRIGEFLAEGSSSFCATFVGGTRVQDDYRKLQSGTIVAVGTPGRVVDVTKRGAMRTESLRVLVLDEADEMLSQGFAEQIYDIFRFLPKEIQVALFSATMPDDVLELTKKFMRDPTRILVKRESLTLEGIKQFFIAVEEEHKLDTLMDLYETVSIAQSVIFANTRRKVDWLASQLNSSNHTVSCMHSEMSKQEREKVMGTFRNGSSR... | 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 ... |
Q4P331 | MSKPEDTSAAAAAPAGEAGNNLNIADGEIESNWETVIDNFDNMELKEELLRGVYAYGFERPSAIQARAIVPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIKAVQALILAPTRELAQQIQKVVIALGDYMKIDCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDTQCVLLSATMPQEVLEVTKKFMRDPIRILVKRDELTLEGIKQFYVAVEKEDWKLDTLCDLYETVTITQAVIFCNTRRKVDWLTDKLTSREFTVSAMHGDMEQAQREVIM... | 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 ... |
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 p... |
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 t... |
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 t... |
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 t... |
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