ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q9CYC3 | MPSRRRGPSRQQLSRSALPSIQTLVGGGCGNGTGLRNRNGNAIGLPVPPTTALITPGPVRHCQIPDLPVDGSLFFEFLFFIYLLIVLFIQYINIYKTVWWYPYNHPASCTSLNFHLIDYYLAAFITVMLARRLVWALISEATKAGAASTVHYTALILARLVLLTLCGWVLCWTLVNLFRSHSVLNLLFLGYPFGVYVPLYCFHQDSRAHLLLTDYVVQHQAVEEAASNVGSLARSKDFLSLLLESLKEQFNNATPIPTHSCPLSPDLIRNEVECLKADFNHRIKEVLFNSLFSAYYVAFLPLCFVKSTQYYDMRWSCEHLIMVWINAFVMLTTQLLPSKYCDLLHKSAAHLGKWQKLEHGFYSNAPQHIWSENTIWPQGVLVRHSRCLYRAMGPYNVAVPSDVSHARFYFLFHRPLRVLNLLILIEGSVVFYQLYSLLRSEKWNHTLSMALILFCNYYVLFKLLRDRIVLGRAYSYPLNSYELKAN | Function: Regulates autophagy by controlling the spatial distribution and levels of the intracellular phosphatidylinositol 4-phosphate (PtdIns(4)P) pools (By similarity). Modulates (PtdIns(4)P) levels by regulating the ER-to-Golgi trafficking of the phosphatidylinositide phosphatase SACM1L (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55720
Sequence Length: 486
Subcellular Location: Endoplasmic reticulum membrane
|
Q6GL42 | MPGGRRGPSRQQLSRSALPSLQTLVGGTCGNGTGLRNRNGSAIGLSAPPITALITPEPVRHCHIPELPLDGGLLFEFLFFIYLLVALFIQYINIYKSVWWYPYNHPASCTSLNFHLIDYHLAAFITVMLARRLVWALISEASQVGTSSMVHYAALITARLVLLTLCGWVFCWTLVNLFRNHSVLNLLFLGYPFGVYVPLCCFHQDSRSQPLPTDCGYLVQDPLVDDGANGMATLVRPRDFLSLLRESLREQFNSTPSIPSHSCPLSPDLIRNEVECLKADFNRRIKEVLFNSLFSAYYVAFLPLCFVKSTQYYDMRWSCEHLIMVWINAFVMLSTQLLPPKYCDLLHRSASHLGKWQKLEHGSYSNAPQHIWSENTVWPQGVLVRHSRSLYKAVGPYNVAVPSEVSHARFYFLFHRPLRLLNLLLIIEGSLVLYQLYSLLRAEKWNHTLSIALILFCNYYVLFKLLRDRIVLGRAYSYPISSYGLKPH | Function: Regulates autophagy by controlling the spatial distribution and levels of the intracellular phosphatidylinositol 4-phosphate (PtdIns(4)P) pools (By similarity). Modulates (PtdIns(4)P) levels by regulating the ER-to-Golgi trafficking of the phosphatidylinositide phosphatase SACM1L (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55665
Sequence Length: 488
Subcellular Location: Endoplasmic reticulum membrane
|
Q7ZW11 | MAGGRRGANRTTYCRSPLSNDTGSVGNGNHSTSSPVTGVRSRTRNGSGTGMSSPPLATQTVVPLKHCKIPELSMDKNVLFELHLFACHLIALFVHYVNIYKTVWWYPPSHPPSHTSLNFHLIDYNMLVFTVIVLARRLIAAIVKEASQSGKLSFPHSVFLVTARFAVLTLAGWSLCRSLIYLFKTYSVLSLLFLCYPFGMYIPFFRLSCDFRRAGSMSPLSGIGSKDVGAAALGRGGRDYLSVLKETWKQHTSQLYSAQPMPTHACCLSPDLIRKEVEYLKMDFNWRMKEVLVSSMLSAYYVAFVPVWFVKSTQYVDKRWSCELFILVSVSTSVILMRHLLPPRYCDLLHKAAAHLGCWQKVDPSLCSNVLQHIWTEEYMWPQGVLVKHSKNVYKAMGHYNVAVPSDVSHYRFYFFFNKPLRILNILIILEGAMIFYQLYSLMCSEKWHQTISLALILFSNYYAFFKLLRDRIVLGKAYSYSASASNQKVS | Function: May protect the cells against DNA damage caused by exposure to the cold-warming stress and facilitates tissue damage repair during the recovery phase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55776
Sequence Length: 491
Subcellular Location: Endoplasmic reticulum membrane
|
Q9GZU3 | MGGRRGPNRTSYCRNPLCEPGSSGGSSGSHTSSASVTSVRSRTRSSSGTGLSSPPLATQTVVPLQHCKIPELPVQASILFELQLFFCQLIALFVHYINIYKTVWWYPPSHPPSHTSLNFHLIDFNLLMVTTIVLGRRFIGSIVKEASQRGKVSLFRSILLFLTRFTVLTATGWSLCRSLIHLFRTYSFLNLLFLCYPFGMYIPFLQLNCDLRKTSLFNHMASMGPREAVSGLAKSRDYLLTLRETWKQHTRQLYGPDAMPTHACCLSPSLIRSEVEFLKMDFNWRMKEVLVSSMLSAYYVAFVPVWFVKNTHYYDKRWSCELFLLVSISTSVILMQHLLPASYCDLLHKAAAHLGCWQKVDPALCSNVLQHPWTEECMWPQGVLVKHSKNVYKAVGHYNVAIPSDVSHFRFHFFFSKPLRILNILLLLEGAVIVYQLYSLMSSEKWHQTISLALILFSNYYAFFKLLRDRLVLGKAYSYSASPQRDLDHRFS | Function: May protect the cells against DNA damage caused by exposure to the cold-warming stress and facilitates tissue damage repair during the recovery phase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56274
Sequence Length: 492
Subcellular Location: Endoplasmic reticulum membrane
|
Q810L4 | MGGRRGPNRTSYYRNPLCEPGSSGASGGGHSSSASVSSVRSRSRTTSGTGLSSPPLAAQTVVPLQHCKIPELPVQASILFELQLFFCQLIALFVHYINIYKTVWWYPPSHPPSHTSLNFHLIDFNLLMVTAIVLGRRFIGSIVKEASQRGKVSLFRSILLFLTRFTVLTATGWSLCRSLIHLFRTYSFLNLLFLCYPFGMYIPFLQLNYDLRKTNLFTHMASMGPREAVSGLARSRDYFLTLRETWKQHTRQLYGPEAMPTHACCLSPSLIRNEVEFLKMDFNWRMKEVLVSSMLSAYYVAFVPVWFVKNTHYYDKRWSCELFLLVSISTSVILMQHLLPASYCDLLHKAAAHLGCWQKVDPALCSNVLQHPWTEECMWPQGVLVKHSKNVYKAVGHYNVAIPSDVSHFRFHFFFSNPLRILNILLLLEGAVIVYQLYSLMSSEKWHQTISLALILFSNYYAFFKLLRDRLVLGKAYSYSASPQRDLDHRFS | Function: May protect the cells against DNA damage caused by exposure to the cold-warming stress and facilitates tissue damage repair during the recovery phase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56377
Sequence Length: 492
Subcellular Location: Endoplasmic reticulum membrane
|
Q969M1 | MGNTLGLAPMGTLPRRSPRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTIHMSALGLPGYHLHAAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSLTHRLVLGGELVYHRRPGEEGAILTLAGKYSAVHWVATLNVGSGGAHASYYHRANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQANMVFRGLVDSNWCVGAVLEKKMPPLPVTLALGAFLNHWRNRFHCGFSITVG | Function: Potential channel-forming protein implicated in import of protein precursors into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33917
Sequence Length: 308
Subcellular Location: Mitochondrion outer membrane
|
A4F267 | MGNTLGLAPMGTLPRWSHRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTVHMSALGLPGYHLHTAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSITHRLVLGGELVYHRRPGEEGAILTLAGKYSALHWVATLNVGSGGAHASYYHKANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQADMVFRGLVDSNWCVGAVLEKKMRPLPVTLALGAFLNHWRNRFHCGFSITVG | Function: Potential channel-forming protein implicated in import of protein precursors into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34049
Sequence Length: 308
Subcellular Location: Mitochondrion outer membrane
|
A8MHA3 | MKILGLVTEYNPFHNGHRYHLEQSKEITKATHTVAVMSGNFLQRGEPAMVHKWERAKMAVKSGVDLIIELPTSYACATAELFAYGAITLLHRLGSVDCLCFGSEIGNVSPLLQIAEVLSTPTSRFQEVLREHVNLGGTFPVARSMALLKYLEETKEYDVASLREISDALKSPNNILGIEYLKSLKKLNSPIVPYTISRKSADYHSKDITDSSIASATAIREHLLKENHLKGIASVVPKDTLDILAHSVGIGMAPIFATDFQQILLALLRRSTPENLKNIFDVEEGLENRIYHCAHQASTLNELYEAIKSKRYTRTRIQRILMHLLLNITKKDIFYFNDHGGPQYARILAFNDKGREILQSFKSTSSIPMVSNLKNYTPQNSAADRMLAIDIRATNLYTLAFTDEKRGGALMDYRTSPFYENSKD | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 47642
Sequence Length: 424
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
P0C0A4 | MQQTKKLTQSDIIIAVMSGPFLQRGEPALISKWYRTKMALANGVDLVVELPYVFATQKAETFANGAISILNALRVSEICFGSEDGQIENFYNTISIQKNEEETFNCLVKQFMDAGNSYAKATSDAFSHILTSEKNIDMSQPNNILGFQYMKAILSQNSSIQAQTIKRFASHYHDETFNDQHIASATSIRKQLFSEEGSFTTIEPFLPQATTSLLANYKQNYGILHNWEQYFSFFKYRLMTMSPGDLRHIYEIEEGLEHRILSKIQNSSSFYSFMEALKTKRYTWTRLQRACTHILTNTTKEDIRSANIEQHAPYIRLLGMSQKGQTYLSKNKKKIELPILTHTKTFDHVALDIEKKANSVYFSIMHEPLRTQLLKQDITHHPIRYDETTTKFL | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 45273
Sequence Length: 393
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
O34513 | MKAVGLVVEYNPFHNGHLYHAQTAKLQTGCDTAVAVMSGHFLQRGEPAVVSKWARTKMALQSGVDLVIELPYLYAVQKADIFARGSVSILNELECEALFFGSENGDIKPFLETAQLIDEHKHILNDRIKEELKKGASYPAAAAIAFSSILHTESALDLSKPNNILGYQYVTSILTGGYPMKPYTTARISSDYHDADLPEGENHIASATSIRKAMIGQNLEACLRFLPAASARELAAYRKSFGLWHTPESYFSYLKYSLSTVTARELQQVYEVEEGLEHRIIRSIRKSSSYQEFMELLKTKRYTWTRLQRMNTHILTRTKKQDMQKLLDNDKAPYIRLLGMTKKGQAYLSEKKKALSVPLVSKLSSFSHPALDLDVKASRIYSLPIEEPLRTEFDLQEYGHAPIRYDEDEQHFLNV | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 46989
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
B9MRM7 | MRVAGIIVEYNPFHNGHLYHLQKTREITNADIVVGVMSGNFIQRGEPAIVNKWARTKMAILNGVDVIFELPFAYACNSAEIFAYGAISILNQLGVDFIVFGSECGDIDKLKETAKHLAFEEDDFKSSLKSYLKEGYSFPKARELALIKTCKTNIEFSSNNILGIEYIKWIYRLNSKIEPFTIRRIGASYNDPNLTQDTYASATAIRRNINNLHAIKNKMPSVSYEILLEEFESGRGPVILEDYFKLFIYNAIVVPDFLKNKIDVKEGLENRFEKYIFNSPSAKNLLENVKTKRYTLTRLQRIFIHAIVRNNFDQKALLSITPYVRVLGFNYKGKEYLNKIKDKIEYITKLNQQWLKNPQYKELLELEIRSSMLHALQYKDFHKYLQTEFKSSPIYISSRS | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 46363
Sequence Length: 400
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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Q3A287 | MRAVGLITEYNPFHNGHLHHLRASREAAGAEVAVAVMSGHFLQRGEPALLDKWRRAEMALRCGVDVVVELPFPFACASAPHFARGAVQCLDALGVDSLCFGSESGDLGALQRCAQLLEECGEQVAERTATLLRRGMHYAAARSQVCAELSGCDAATLPLHQPNNILGIEYLRALRATGSAMQPFTISRLGAGYHDDAVGPGNIASASGIRKRLAMGETVDELLPAPAVDVVAGARADRLFPDEDLLHRLLLAQIFRGRDYLQSLYQVESGIDARLTDAAATSRDWQALVDAVKVRQFTRTRIQRTLMYILNDVRGDLMASLLAAGPLYLRLLGSSPRGRAFLGAARKRRRLPMVTNLSRIYSQLKRTYGPRSEDYRLALAMLELDLRATRNYSLLLPGWSGVSRERDFFEAPLDIHSAI | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 45974
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
Q0AYW7 | MAILGIVAEYNPFHNGHLYLLEKSRQQGDFSATVVVMSGNFLQRGEPAFCDKWARAEMALTAGVDLLIELPFCFATRSAYYFAKGAVQLLQRSGVVTHLAFGSESGQLSQLQEIAGILAHEPESYKTALKKRLSQGWSFPLARSSALQEYMGGEKKQLQEILPGPNNILALEYLRVIEEEGIPLLPLTIPRQGSSFHSSDLSPYSSARAIRQALYHNLDWEKITNSISPATEKILQREIALGRAPIGPDSLEQAIMVNLRLVSTDYLREIYEVSEGLEFRIKEATNSCGTLEELRQFIKSKRYSLTRINRTLLYTLFALSKNQVELYDQHGPQYLHILGFSAKGQEILQKIKIKSKLKIFSRGSEMKQARDKNPGTALAEMIKLDCQATDVYSLLFPNPATRRAGRDFTTSPVPGT | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 46549
Sequence Length: 416
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
B7IEZ2 | MKVLGVVVEYNPFHNGHLYHLKSAKKLVKPDFTIAVMSGNFCQRGEPAIVNKFARAKMALLNGIDVVLEIPTVYALQDAGGFAFGSVGLMHKLGLVTDIVFGSESADISFLEKISKILYENSKEFDYLIKRELKKGLSYPNARKFALQKFLKTDLDTIKKLENSNDILGIEYIKAIFKYNSNIKYHVIKRVGAKYNEQNLSGKFSSATAIRNAIKFEKNIKEYVPESTYLILKDEFEKGRGPVFLENLEQFILSEFRLKARENLENIYGFSEGLDKRFIDSANISTNLKEFIENIKAKRFTFSRIRRLIFHAIFNFEKNYMEFSNKLGPQYARVLGFTTKGQEFLSYAKKKSTIPIITNPSLKNKILKDVLKNSERKWDFNISLYNWQFEKDILASNIYTLFYPNSSQRKSGMDFRKPIIIEG | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 48763
Sequence Length: 423
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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A6LP38 | MKVLGVIVEYNPFHNGHLYHLQQAKKIVSPDYVIAIMSGNFCQRGEPAIINKFARAEIALKNGIDVVFELPTVYALQDAGGFAFGAITLLDKLTVVTDVVFGSESADKNFITTVAKTLLENPDKFDNLLKIELKKGLSFPNARKFALKKFLNENEDFLKMIENSNDILGIEYVKSILKLKSKINYHLIKRIGAKYNDTELESKYSSATAIRNAIVRNNPFETYVPQTSYKVLKREFSYGRGPVSLENMEQFILTFLRLKHRKDFESIYSFTEGLDQRFIKAIKTSKKLSDFLEKVKTKRFTYSRIRRAIFHALFDFKKEYIEFSNKLGTQYARILGFTKKGQKLLSKIKKASKIPIISNPSLHEKVLKKVLTDKDRKWEVNKKLFIWQFEKDIVASNIYTMFYPQKNERKYGLDFRKPIIEGENE | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 49234
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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Q9X1K1 | MEYNPFHNGHLYHLTSARELVKPDYTIAVMSGNFCQRGEPAVIDKFARAEIALRMGVDVVLELPVVFATQDAGGFAFGAVCVLDATGVVTDVVFGSESNDIEFLQRVARILYEQPDEYQKFLHEELKKGYSFPNARKYALMRYFSMKGWNEEEVLKLEKSNDILGVEYIHSALKIGSNIRFHTIKRVGAEEKDTSFRGRFSSATAIRNLMREKRWEEVRDSLPEDSFEILMREINEGRGPVFLENMGDFLLSFFRLKNMDFFEKIHGFSEGLEKRFHVCARQTGSYRDFLECVKAKRFTFSRIRRLALFSVFEVNKEFVEKSNTKGPQYIRILGFTEKGREILSLMRKKAKLPIVTNMSLYRKVLEKTDLPVDKQLFLEQIDLDVKATNFYSMFFPSVEQRCGERDFSIHPIFLRTEM | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
Sequence Mass (Da): 48592
Sequence Length: 418
Subcellular Location: Cytoplasm
EC: 6.3.4.-
|
Q9YBQ6 | MDVELEVSGFIQRLRHSRLRGLLVVGTGDVKAWAEKLAGYAGGDCALVSPSAGRLPGICRSWAPPGSIERILGGEYAAAIIAVPGLLRPSIIAGAGETVRSGGFLAIVADPPDRWDPGPPRGTGLYREYLFSAIRDNPVHLWIDDESGRIVSESFLEYTGVGAQGWSPGRYKPSPGSGVPRRLVSACRSESQARALESLARFFRGRWRSALVRGDRGRGKSYVIGLALAYAAWRRLIGRAVLVGPTPLSVQSVMAGLLRGLDVLGLKGHRVVRTSGGEVIRVSGPWFRIAYEQPDTAEPSPLVVVDEAAAVGVARVRRLSWRSGKSLVATTIHGYEGSGRAFARLLPNILPKPFIELELREPIRYLPGDPLEEWLYTVFMLRAEPQEPGDPSAARPVEVSREVLARDREVLRSVYGILVQAHYRNTPDDLLAMLESPHHRIYALEADGTPVAVADVVLEGPDVEEEARIALERLLYMAGSPGSGVVSWRVSRIAVHEDLQRRGLGSRLLRHVEAQARESGASLVTTMFSRHDVIPFWLKNGFKPFYVSPRYNRVTGEKNVALAKPLDSAGAEILEKASKTLALKLALAGSSIYRDLAAEKLALLLHHTPATAPPLYLTRIQARHLEGFLKGEVMADQAFDAVYIALLSTLLATRSWNPVEPGLVGAVARVVQGKPYSEVASIIGASTVDEAVGKVEEYIRGILEGARSLWSGRVIP | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 77792
Sequence Length: 716
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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P76562 | MAELTALHTLTAQMKREGIRRLLVLSGEEGWCFEHTLKLRDALPGDWLWISPRPDAENHCSPSALQTLLGREFRHAVFDARHGFDAAAFAALSGTLKAGSWLVLLLPVWEEWENQPDADSLRWSDCPDPIATPHFVQHLKRVLTADNEAILWRQNQPFSLAHFTPRTDWYPATGAPQPEQQQLLKQLMTMPPGVAAVTAARGRGKSALAGQLISRIAGRAIVTAPAKASTDVLAQFAGEKFRFIAPDALLASDEQADWLVVDEAAAIPAPLLHQLVSRFPRTLLTTTVQGYEGTGRGFLLKFCARFPHLHRFELQQPIRWAQGCPLEKMVSEALVFDDENFTHTPQGNIVISAFEQTLWQSDPETPLKVYQLLSGAHYRTSPLDLRRMMDAPGQHFLQAAGENEIAGALWLVDEGGLSQQLSQAVWAGFRRPRGNLVAQSLAAHGNNPLAATLRGRRVSRIAVHPARQREGTGRQLIAGALQYTQDLDYLSVSFGYTGELWRFWQRCGFVLVRMGNHREASSGCYTAMALLPMSDAGKQLAEREHYRLRRDAQALAQWNGETLPVDPLNDAVLSDDDWLELAGFAFAHRPLLTSLGCLLRLLQTSELALPALRGRLQKNASDAQLCTTLKLSGRKMLLVRQREEAAQALFALNDVRTERLRDRITQWQLFH | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2) . Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA (Probable).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 74893
Sequence Length: 671
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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Q7VLN6 | MRQLVILSTMPPIQGGVLLNSQNFSKAKQFLGQEYPFALYDMRSENGICFNLEAFAIIVGTIQENGTLYLICPNWHSVEQQIDVDAIRWNGGVAIACPHFFQHFKRLINKFGFEVTSRPQQPFIKTAPSYPAKLIQFTDEQQNILQKLPLDPAEIHIITAARGRGKSTLAGKLAEQFAKTEQVILTAHRSSSIQKILQTASINIPFFAPDKLLNLIETKQISADHLLFIDEAACIPLPILQQLGNYFKKVILTTTTQNYEGTGRGFKLKLVKQLHRTTKEWQLFQPLRWSNHDRLEQFTNELLLLNDELIPLDQNSQFYHLLANAHYKTTATDLRRLFDADQQLFHQCYDKNQRLMAGIWAVKEGELSQDLAEAIWAGKRRPAGNLVAQYLCCQGNLIEACQLKSIRISRIAVQPDLQNQGIGSQLVTDFMQKMQKNNKNRPLDFISVSFGITPHLLTFWRRNGFQLVQITPTKEASSGYHSAMMLYPLSQQGKQFVTKAVKQFERDLALQPFYPTLKNCLAIPAQVENEMNQDDWQNLHGFAFAQRSLANCYTSLKRLYITHQAQLTILAPLFTHRYPANQKVWLQQCRIAIRPFIQ | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 68448
Sequence Length: 598
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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P44140 | MPSRQLQILIRKTLPLVPDHVLIIGESGIAFSKATNLLGQEFEHILFDGRNGIHLEALAIAAGTLKMGGTLCLVLSDWENLSQQPDQDSLRWNGNQSAIATPNFIYHFKQCIERYHFPILREESAVEFPTVFYSNEHHKNATLAQQQIIENILQAEQDIYFLTAKRGRGKSALLGMLANQIQAPVYLTAPNKSAVHSVIEFSEGDIEFIAPDELALTLQTEPEFSQSAWLLVDEAAMIPLPLLQEYSRYFQHIVFSTTIHSYEGTGRGFELKFKRKIHRTFQHFELKQPLRWQENDPLEHFIDDLLLLNAEDDFQHFDYSNITYNIEENAKNLSFPCLRGKVPEGPKGDLDIASLPQALEALLTSKGSEGKYNRQFFFRDFYGLMTIAHYRTSPLDLRRLLDGKNQRFYFAEYQQNLLGAIWALEEGNMADDELIIQIQQGKRRPKGNLVPQALCFHENLSQACKLRSLRISRIAVQPNWQQKGIGQNLMQAMENADVDFLSVSFGYTDELAKFWQKCGFVLVHLGEHQEASSGCYSAIALKGISKEGLALVDTAYKQFQRNLPLSFHPFAINFEQNQLDWQLDDFDWMSLKNFANFHRTLFSSIPAMRRLLKLAGKENFPLISAYLTKKQFPINKKKGVECLRLEIKQYLERGTL | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 75162
Sequence Length: 656
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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D4GW73 | MTELGDDPDVEALAAARREEALATNQRRLLVLAGDRDAGIDAAFDAVRGADVPDDEVTFVTAREGFRFHRVEPKRASSLLGTTRTLVVLDAHEEFSANALGRVAGAVDGGGLLVLLTPSLDDWPTRRDSFDERLAVPPFSVADVTGRFRGRLVSTLRDHPGVALVDLDSGTVERDGAYRQGISFDAAPPRVPTEKDRRSPRRAYEDCLTADQSEALAALEALTEPGTAVVVEADRGRGKSSAAGLAAGSLAAEGKDVVVTAPGERNAAEVFARAERLLSELGALRGGGAGDFDIAADRGGRVRYVPPTEAGDAAADADALVVDEAAALPVGLLESFLAAPAVAFCTTVRGYEGAGRGFTVRFRDRLDDADREVTDARLDDPIRYAAGDPVESWTFRALLLDARPPVDQLVADATPETVSYRALSPDDLLADEHLLREAFGLLVLAHYRTEPDDLARLLDAPNLTLRALTHEGRVVSVALLAREGGLDPDTRRQMYDGGRIRGNMLPDVFTSQLRDEGAGVPVGYRVMRIATHHAVRSSGLGSRLLTELRDEFADDADYLGVGFGATPELLSFWRDNGYGTVHLSTTRNDTSGEYSALMTRPLSSAGRDLRDRHANWFLGRVGDVLGDALSDLDADVARAALAAVDSFLSPDLSEYEWRVVVGASYGPGLYTTAPGAFRRLGLAHLTNPERASLTPREERLVVRKVLQTHPWDAVADELDFHSTAGAMRALGDAYEPLVDEYGTDAAREERERFR | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 81215
Sequence Length: 754
Subcellular Location: Cytoplasm
EC: 2.3.1.193
|
Q5QY69 | MAERSGYRQLQLLQDASLWREYCEARSESSIYLSNLQTHADAVLSRYRDYLGHEFEQVWIDCHDGLHADAIAALCGTVTAGGLLSILLPAESNAMSHRMERFAAKHFAESNIKPYSSVNKTETRSANETLQLTNEQNSIFNALTQSTAKPYETHIITAERGRGKSTLLGQALAQAKEHRSIIVTAPRKANAKVLLQQAPEAHFVAWDKLLEQPGNSEVTLIIDEAAGLPLWATEQLCQKFNPWLLATTVAGYEGCGRGFAVHFTDWARKTLPQVSVHQLTQPLRWPANDPLEQWLTETFLLNEQPVTQFGNRESGTFIKHASELEEALLQQCFQLLLSAHYQSSPNDLNLLLTEPGHKLAYQSTNGEVTAVAWLMSEGPILSPLKEEVRQGQRRPKGNLLPQAIGYFLQQDWAMDLHWLRVARIAVPAAKRRRKAASELLAEIYRWALDNNYQMLGTSFAWSPGLDNFWKKNGYALWRLSSRIDSVSARPAAIYALPLTNEFTELYRVCQLLGQWGQNQLQWLSGGKETLQLTEERNKIRTSLIQAYRSKTIPFDAAHFALAQWFYWQHSNHPLTELLCNSSTTLKHLGEYWGGVSQRQANENLCKEVCLLH | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 69250
Sequence Length: 612
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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Q8TYZ5 | MPDKAEVFFDEGVLDFADVDEIVLDVGEEALAEALAHRHRRMIVFQGDEGKAEAAGVVTAGAADVLFDVRDRPISVLYVTDSLKEDTYARERYEEFRRVLEGFAEEANFEYELEALTFSGSKRALGTTWDLMVIDLSYDLDPDAIGRLVETVRGGGLVIFQTPPFDRWRNMWTAFHKSLVTPPYTLDHVGKRFNRRFIRKLKEHDGVWIVDTDEWTAEPEPSEDVDLEVEVKRRERPDLDPPDDAVLPEELYRMCATEDQFRALIRFEELLESNGKTALILTADRGRGKSALLGIAVAGAGVTTDVYDVVVTASEPENVAVLFEFLLEALRELGVEYDVERDDKGNIVYVETDDFVVEYERPSEASEIECDLMVVDEAASIHVPILERILDNNDKVVYSSTIHGYEGAGRGFSVRFLQNVRKRRDVRLIEFKMHEPIRYDSDDPIERWLFDTLLLDAEPADLDKEDLECVKEMRVEFEKPDLRYWFEDPEGEEELRQFIGIYVMAHYRNRPSDVMVLADAPHHEAYALKTETGKIVTALQVAREGTIPRDVITKMRRGYRPPGNVIPDLMVQHHDALDFPRMKGLRIVRIATHPDIMRHGLGSRALKELAKIAKKKDYDWIGTGFGANEELTRFWLRNGFVPVHISPNRNPVSGEYSVAVIRPISEEAEEIINRANFEFRIKLADWLGETHRDLEPEVARLLFEPMSSLRYRPTLTEGQLRRLKKYADMVHTYEIAADAVRELAKAYFLDTEDRPELSEEEELLLITKCLQRWKWADVADVLGEEVPDLMRSLRDLVGLLYEEYKEDLQRSAAVEGIRKAVERLADKGLTGTVIVEVEEGEPKEVIIRREERLEL | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 98136
Sequence Length: 855
Subcellular Location: Cytoplasm
EC: 2.3.1.193
|
D5C1K8 | MHPILFPPTLDNIRKITASLVAAAKASGHRRALVLSGDREWCLQAAQVSLASTSLEPVLWIAAQAPENAWRMEAAKAHRSLGQEVDAIVFDAYSGFDLDAFGIITGAIRGGGLLLLLTPPLAAWPSFNDPEHARIVTAPYEVTEVTGRFLKRLVRILREAEGVIIIEQGKILPSVPFAAPARAETGGNPPSPGDSACRTEDQGRAVEAIVKVVTGQRRRPVVLTSDRGRGKSAALGIAAARLLQRGLKHIIVTGPRLDAVEPVFRHAQRLLPQATVSRAALHLPEAGMEFAPPDDLIRTSRPADLLLVDEAATIPTPLLERLLQGYSRIAFATTIHGYEGTGRGFALRFHRVLDEKTRGWKGLRLETPIRWRSGDPLEHFVFRALLLDATAAPDSAVASARPETVAVERLDRDALVRDEATLSELFGLLVLAHYQTRPYDLRHLLDGPNLSVYVMRYRGHVVATALLAAEGGFVEETARGIWEGRTRPHGHLLPESLAAHLGLAQAPRLHCARIMRIAVHPAVQGQGLGTHLVDTIIRETGGEGLDYLGSSFGATVELLRFWERLDFLPVRLSVKRGATSGAHSAIVLHPLSSSGQALVKRARERFLVHLPHQLADPLRELEPQLAAWLLRRGDPAGPLPLDSQDWSDVLAFAFGRRVYEVCIGPIWKLTWGALAAPESATLLGEVERNALIVKVLQKRSWQEAAAALELSGRAQVIEVLRRTLRPLVLHFGNEAVRREAERLAGG | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
Sequence Mass (Da): 81439
Sequence Length: 746
Subcellular Location: Cytoplasm
EC: 2.3.1.193
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Q86X19 | MELPDPVRQRLGNFSRAVFSDSNRTGPESNEGPENEMVSSLALQMSLYFNTYYFPLWWVSSIMMLHMKYSILPDYYKFIVITVIILITLIEAIRLYLGYVGNLQEKVPELAGFWLLSLLLQLPLILFLLFNEGLTNLPLEKAIHIIFTLFLAFQVVAAFLTLRKMVNQLAVRFHLQDFDRLSANRGDMRRMRSCIEEI | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23046
Sequence Length: 198
Subcellular Location: Cell projection
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Q8K0U3 | MELPDPVRQRLSNLSLTVFGDSSRTGPESSDAADNEMVSSLALQMSLYFNSYFFPLWWVSCIVMLHLKYSILPDYYKFIVVTVVILITLIEAIRLYLGCMGNLQEKVPELAGFWLLSLLLQLPLILFLLLNDGLRNLPLEKAIHIIFTIFLTFQVISAFLTLKKMVNQLAARFHLQDFDQLSSSSAAVRRVRQCTEEL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22623
Sequence Length: 198
Subcellular Location: Cell projection
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Q5HZE5 | MELPDPVRQRLSNLSLTMFGDSSRTGPESSEAADNEMVSSLPLQMSLYFNSYFFPLWWVSCIVMLHLKYSVLPDYYKFIVITVVILITLIEAIRLYLGCMGNLQEKVPELAGFWLLSLLLQLPLLLFLLLNEGLKNLPLEKAIHSIFTVFLTFQVISAFLTLKKMVNQLAARFHLQDFDQLSASSATGRRARQSSEEL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22555
Sequence Length: 198
Subcellular Location: Cell projection
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Q3SZ36 | MPSAFSVSRFPVSIPAVITQTDWTEPWLVGLAGFHVLCLLLTCFSSQRYRLQVGHFLCLVTLVYCAEYINEVAAMNWRLFSKHQYFDSRGMFISLVFSAPLLLNALVIVVLWVRKTLVVMTDLRSLREQRRARARPKEE | Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16053
Sequence Length: 139
Subcellular Location: Cytoplasm
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Q96B42 | MPSAFSVSSFPVSIPAVLTQTDWTEPWLMGLATFHALCVLLTCLSSRSYRLQIGHFLCLVILVYCAEYINEAAAMNWRLFSKYQYFDSRGMFISIVFSAPLLVNAMIIVVMWVWKTLNVMTDLKNAQERRKEKKRRRKED | Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16265
Sequence Length: 140
Subcellular Location: Cytoplasm
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Q3TUD9 | MSSAYSVRSFPVSIPAVIMETDWTEPWLLGLLAFHLLCLLLTCFSSQRYKLQIGHFLCLVVLVYSAEYINEVAAVNWRLFSKYQYFDSRGMFISLVFSAPLLFNAMLIVIMWVRKTLTVMTDLKTLQEERKERRRRRKEE | Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16526
Sequence Length: 140
Subcellular Location: Cytoplasm
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Q6DGF8 | MASPYSVRVFPVSIPAVIMETDWTEPWLLGLLAFHLLCLLLTCFSAQRYKLQIGHFLCLVVLVYCAEYINEVAAMNWRLFAKYQYFDSRGMFISLVFSAPLLFNAMVIVIMWVRKTLTVMSDLKNLQERRKERKRRRKEE | Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats (By similarity). Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16548
Sequence Length: 140
Subcellular Location: Cytoplasm
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Q86YD3 | MALPPGPAALRHTLLLLPALLSSGWGELEPQIDGQTWAERALRENERHAFTCRVAGGPGTPRLAWYLDGQLQEASTSRLLSVGGEAFSGGTSTFTVTAHRAQHELNCSLQDPRSGRSANASVILNVQFKPEIAQVGAKYQEAQGPGLLVVLFALVRANPPANVTWIDQDGPVTVNTSDFLVLDAQNYPWLTNHTVQLQLRSLAHNLSVVATNDVGVTSASLPAPGLLATRVEVPLLGIVVAAGLALGTLVGFSTLVACLVCRKEKKTKGPSRHPSLISSDSNNLKLNNVRLPRENMSLPSNLQLNDLTPDSRAVKPADRQMAQNNSRPELLDPEPGGLLTSQGFIRLPVLGYIYRVSSVSSDEIWL | Function: In neurons, modulates the degradation of NMDA receptor GRIN2B subunit. Plays a role in the regulation of neuronal excitability.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39285
Sequence Length: 366
Subcellular Location: Cell membrane
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Q9DCF1 | MELPLSQATLRHTLLLLPALLSSGQGELAPQIDGQTWAERALRENEHHAFTCRVAGGSATPRLAWYLDGQLQEATTSRLLSVGGDAFSGGTSTFTVTAQRSQHELNCSLQDPGSGRPANASVILNVQFKPEIAQVGAKYQEAQGPGLLVVLFALVRANPPANVTWIDQDGPVTVNASDFLVLDAQNYPWLTNHTVQLQLRSLAHNLSVVATNDVGVTSASLPAPGLLATRIEVPLLGIVVAGGLALGTLVGFSTLVACLVCRKEKKTKGPSRRPSLISSDSNNLKLNNVRLPRENMSLPSNLQLNDLTPDLRGKATERPMAQHSSRPELLEAEPGGLLTSRGFIRLPMLGYIYRVSSVSSDEIWL | Function: In neurons, modulates the degradation of NMDA receptor GRIN2B subunit. Plays a role in the regulation of neuronal excitability.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39170
Sequence Length: 365
Subcellular Location: Late endosome
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A6H773 | MLFLALGGPWAAGLRLSGKRTALWASSALRDPRAAVSRAASCRGSSGRVGGTGLSAAAPVLRRVRAQIPVCWERGVRCSHTQLDKSEDGRLIYTGNLARTVFGVKCFSYSTSLISLAFLPYIFAQNNVIFGSLPLQILFYGTIGSFTVITPALLHFLTKGYVIRLYHEARTDTYKAITYSVVLSEKSTVFHQNDVKIPNSTHVFTTFYAKTKSLLVNPALFPNPEDYNHLMGYDKPFTFDLEEASEKKQLKEEK | Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1 through its interaction. Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis. In addition, binds the mitochondrial proton-transporting ATP synthase complexes I and may play a role in the stability of its membrane-bound subassemblies.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28139
Sequence Length: 254
Subcellular Location: Mitochondrion inner membrane
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Q5ZLJ4 | MLLRAAGCWRAAASRPGPVWLRGAEHRGLPLASRRLGLPLPLPLAAGGRRLRSGCGALPEVASFQGVAVRSLSTSAPSDHPEHGRLVYKGNLAKAVLGVRFFSYSTSIFNLFMAPYLMLKTGIGFDSLFLQAAFYGLIGFFTFVTPVTLHILTKGYVIRLYYKEEMDTYTAITYNAILAEKATVFHQKDVKIPDITKMFTTFYAKTKSMLVNPTLFPDPQDYNRLMGYDKAFCFDFEEEEKDGESK | Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1. Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27432
Sequence Length: 246
Subcellular Location: Mitochondrion inner membrane
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Q9BUB7 | MLFLALGSPWAVELPLCGRRTALCAAAALRGPRASVSRASSSSGPSGPVAGWSTGPSGAARLLRRPGRAQIPVYWEGYVRFLNTPSDKSEDGRLIYTGNMARAVFGVKCFSYSTSLIGLTFLPYIFTQNNAISESVPLPIQIIFYGIMGSFTVITPVLLHFITKGYVIRLYHEATTDTYKAITYNAMLAETSTVFHQNDVKIPDAKHVFTTFYAKTKSLLVNPVLFPNREDYIHLMGYDKEEFILYMEETSEEKRHKDDK | Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1 through its interaction . Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis . In addition, binds the mitochondrial proton-transporting ATP synthase complexes I and may play a role in the stability of its membrane-bound subassemblies .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28969
Sequence Length: 260
Subcellular Location: Mitochondrion inner membrane
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Q921N7 | MLLGLGGRWAAGLWPGRTRTTWCVAAALRGSGIAFWRAASLAEPERLRSGGHLALAESCGPPGRAQIPVCWEQCVRCFHTQVDKPENGRLIYTGNLARTIFGVKCFSYSTSVVSLAFLPYLLSQNNMMFGSLPLQVLFYGVMGSFTVITPTLLHLLTKGYVIRLYHEATSDTYRAVTYNVMLSETSTVFHQDDVTIPESAHIFTSFYAKTKSLLVNPALFLNPEDYNHLMGYDKPFTFDMEEVDEKKLHEGEK | Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1 through its interaction (By similarity). Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis . In addition, binds the mitochondrial proton-transporting ATP synthase complexes I and may play a role in the stability of its membrane-bound subassemblies (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28275
Sequence Length: 253
Subcellular Location: Mitochondrion inner membrane
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Q96NL1 | MELHYLAKKSNQADLCDARDWSSRGLPGDQADTAATRAALCCQKQCASTPRATEMEGSKLSSSPASPSSSLQNSTLQPDAFPPGLLHSGNNQITAERKVCNCCSQELETSFTYVDKNINLEQRNRSSPSAKGHNHPGELGWENPNEWSQEAAISLISEEEDDTSSEATSSGKSIDYGFISAILFLVTGILLVIISYIVPREVTVDPNTVAAREMERLEKESARLGAHLDRCVIAGLCLLTLGGVILSCLLMMSMWKGELYRRNRFASSKESAKLYGSFNFRMKTSTNENTLELSLVEEDALAVQS | Function: Plays an essential role in autophagy. TMEM74-induced autophagy may involve PI3K signal transduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33338
Sequence Length: 305
Subcellular Location: Lysosome membrane
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Q9BSE2 | MTEQETLALLEVKRSDSPEKSSPQALVPNGRQPEGEGGAESPGAESLRVGSSAGSPTAIEGAEDGLDSTVSEAATLPWGTGPQPSAPFPDPPGWRDIEPEPPESEPLTKLEELPEDDANLLPEKAARAFVPIDLQCIERQPQEDLIVRCEAGEGECRTFMPPRVTHPDPTERKWAEAVVRPPGCSCGGCGSCGDREWLRAVASVGAALILFPCLLYGAYAFLPFDVPRLPTMSSRLIYTLRCGVFATFPIVLGILVYGLSLLCFSALRPFGEPRREVEIHRRYVAQSVQLFILYFFNLAVLSTYLPQDTLKLLPLLTGLFAVSRLIYWLTFAVGRSFRGFGYGLTFLPLLSMLMWNLYYMFVVEPERMLTATESRLDYPDHARSASDYRPRPWG | Function: Contributes to the epidermal integrity and skin barrier function. Plays a role in the lamellar granule (LG) secretory system and in the stratum corneum (SC) epithelial cell formation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43520
Sequence Length: 394
Subcellular Location: Lysosome
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Q96JJ7 | MAAWKSWTALRLCATVVVLDMVVCKGFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEMPAVLVFKDETYFVYDEYEDGDLSSWINRERFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEHTRLKSIIQEVARDYRDLFHRDFQFGHMDGNDYINTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEAQGGDSILQRLKRIVFDAKSTIVSIFKSSPLMGCFLFGLPLGVISIMCYGIYTADTDGGYIEERYEVSKSENENQEQIEESKEQQEPSSGGSVVPTVQEPKDVLEKKKD | Function: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase.
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 51872
Sequence Length: 454
Domain: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.4.1
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Q8BXZ1 | MANAVGRRSWAALRLCAAVILLDLAVCKGFVEDLNESFKDNRKDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFDHVRKRHRVFFVYIGGESPLKEKYIDAASELIVYTYFFSASEDVVPEYVTLKEMPAVLVFKDDTYFVYDEYEDGDLSSWISRERFQNYLTMDGFLLYELGDTGKLVAIAVIDEKNTSLEHTRLKSIIQEVARDFRDHFHRDFQFGHMDGNDYINTLLMDELTVPTIVVLNTSNQQYFLLDRHIKDASDMVQFINSILDGTVPAQGGDSIFQRLKRIVFDAKSTIVSIFKSSPLMGCFLFGLPLGVISIMCYGIYTADTDGGYIEERYEVSKSEMENQEQIEESKEQESSSGGSLAPTVQEPKDVLEKKKD | Function: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 51848
Sequence Length: 456
Domain: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.4.1
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Q6GNG3 | MAAAGLCFILAIVSSTSLLASVPVSALVEDLDDSFKENRKDDIWLVDFYAPWCGHCKKLEPVWNEVGIEIRTSGSPIRVGKIDATVYSSIASEFGVRGFPTIKALKGDMAYNYRGPRTKEDIVEFANRVAGPLIRPLPSQQMFDHVKKRHPVLFVYVGVESTLKEKFIEVASELIVYTYFFSASEDVLPKYVTLNEVPAVLVFKDSTYFVYDEYEDGDLSSWVNKERFEGYLHIDGFTLYELGDTGKLVAVAVIDEKNNSIEHTRIKSIAQDVAKNNRNNFHRDFQFGHMDGNDYINSLLMDELSIPTFVVLNTSNQQYFLPSKHIENPEEMIQFINSILDGTAEAQGGDGILQRIKRVFYDAKSTVVSVFKSSPLLGCFLFGLPLGVISIMCYGICTADTEDGSEEMTRKDVIDQNASDEGSDEEEEKGREITDVSDEDQQEKDFMEKKID | Function: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50861
Sequence Length: 452
Domain: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.3.4.1
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Q9Y275 | MDDSTEREQSRLTSCLKKREEMKLKECVSILPRKESPSVRSSKDGKLLAATLLLALLSCCLTVVSFYQVAALQGDLASLRAELQGHHAEKLPAGAGAPKAGLEEAPAVTAGLKIFEPPAPGEGNSSQNSRNKRAVQGPEETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL | Function: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.
PTM: The soluble form derives from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31223
Sequence Length: 285
Subcellular Location: Cell membrane
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Q9WU72 | MDESAKTLPPPCLCFCSEKGEDMKVGYDPITPQKEEGAWFGICRDGRLLAATLLLALLSSSFTAMSLYQLAALQADLMNLRMELQSYRGSATPAAAGAPELTAGVKLLTPAAPRPHNSSRGHRNRRAFQGPEETEQDVDLSAPPAPCLPGCRHSQHDDNGMNLRNIIQDCLQLIADSDTPTIRKGTYTFVPWLLSFKRGNALEEKENKIVVRQTGYFFIYSQVLYTDPIFAMGHVIQRKKVHVFGDELSLVTLFRCIQNMPKTLPNNSCYSAGIARLEEGDEIQLAIPRENAQISRNGDDTFFGALKLL | Function: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.
PTM: The soluble form derives from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34192
Sequence Length: 309
Subcellular Location: Cell membrane
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Q46731 | MITSALHRAADWAKSVFSSAALGDPRRTARLVNVAAQLAKYSGKSITISSEGSEAMQEGAYRFIRNPNVSAEAIRKAGAMQTVKLAQEFPELLAIEDTTSLSYRHQVAEELGKLGSIQDKSRGWWVHSVLLLEATTFRTVGLLHQEWWMRPDDPADADEKESGKWLAAAATSRLRMGSMMSNVIAVCDREADIHAYLQDKLAHNERFVVRSKHPRKDVESGLYLYDHLKNQPELGGYQISIPQKGVVDKRGKRKNRPARKASLSLRSGRITLKQGNITLNAVLAEEINPPKGETPLKWLLLTSEPVESLAQALRVIDIYTHRWRIEEFHKAWKTGAGAERQRMEEPDNLERMVSILSFVAVRLLQLRESFTLPQALRAQGLLKEAEHVESQSAETVLTPDECQLLGYLDKGKRKRKEKAGSLQWAYMAIARLGGFMDSKRTGIASWGALWEGWEALQSKLDGFLAAKDLMAQGIKI | Cofactor: Binds 2 magnesium ions per subunit.
Function: Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).
Sequence Mass (Da): 53306
Sequence Length: 476
EC: 3.1.-.-
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P53322 | MSNKFTMESPKHLVDDVLFISPTNDGSEEKPTEVTFQEDEGHDASLHNRSHDKKSELATEREIMATTTDDDGIPSPSHPMEKRVLRKMDIYLIPLMGMLYFLSNLDKSNIGNAEVAGLSKDIHLVGTQYNTCVTVFFATYVLFDPIGTNLLKIMGPPLMMSICLTCFGAISLGTAWVKNYAQLIVVRLLLGAFEGMIYPAINMYLSVCYRREQYALRFAFVFSAACLSSSFGGLIAYGCSKISGSLKDWQYIYIVEGCISLGFVPFYAFGLSKNLEDSWFFNKEEKEYISERYKTMNTFDPDEKFEWFQVWQAVKDVKTWASAVALFGIDLTTFGLTVFLPIIITSMGFTNVRAQLMTVPIYFLTAIVFFICAVWSDRIKLRSPFILGACLTTSIGIAIVLGSQVHGVRYFGVYILCMGIYVNAACNCLWLSGNTGNYFKRATALGINLFFGSGSGLVSGQIFVAKDKPRYIKGLSISLAFQVFSIFMTVVQIFLYKRENDKKKAIIDRCNELGEPIPYDERLSDKNPEFKYMY | Function: Involved in the uptake of nicotinic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60135
Sequence Length: 534
Subcellular Location: Membrane
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P31015 | MPKGEPFKIKMVEPIRLIPREDREAAIKAAHYNPFLLRSSDVYIDLLTDSGTGAMSQFQWSAMMLGDESYAGASSYYRLKEAVTDITGYEYVLPTHQGRGAEKSAFAQLITRPGMYVLSNMFFDTTRGHVQLAGGRPIDLLLDVPTEEYHPFKGNMDTARLEAFIQEHGAENIACIVMTVTNNSAGGQPVSMANIRETSRIARKYGILLLFDVARYAENCHFIRMREEGYADKAPIDIAREMFSYGDGLMMSAKKDALVNIGGLLAFKDEELYTRVGGTVVPFEGFLTYGGLAGRDLEAMAVGLREALDPDYLAYRVGQVEYLGNLLRSAGIPIQWPVGGHAVFIDAAKFLPHIPWDQFPGHALTVALYQEGGVRTVEVGSLVMGRDPETGENVRSPFEFTRLAIPRRVYTNLHLEDVAETVINAFQKREQIRGVKFTREPKVLRHFTAHFDLV | Catalytic Activity: H2O + L-tryptophan = indole + NH4(+) + pyruvate
Sequence Mass (Da): 50661
Sequence Length: 454
Pathway: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1.
EC: 4.1.99.1
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Q894M8 | MIIYYLKLEGFNMKIKYVAEPFRIKMVEPIKMLTREERELKIAEAKYNTFNLRGEDVYIDLLTDSGTNAMSDDQWAGVMKGDEAYAGGKSYFKLVDAVKDIFGYKFVQPVHQGRAAEKVLFGLLLGEGKYSISNMHFDTTRAHVELSGARAIDCVVPEASDPTVRIPFKGNMDVEKLEKLIKEHGADKIGVVVMTITNNSAGGQPVSIENMKETAEICKKYNIRLCIDAARYAENAYFIKQREPGYENKSIKEIIKEIFSYADIFTMSAKKDAIVNMGGLLGIKEDEELFQLCKGRTISFEGFITYGGLSGRDLESLAIGLYEGIDENYLRYRIGQMEYLAARLDEAGIAYQSPVGGHGVFVDAKSMFPHIPYNEFPGQVLAVELYKEAGIRTCEIGSYMLGNDPDTGEQLKADFEFTRLAIARRVYTQAHIDIMADALITIKERANTVKGYRITWEPPILRHFQASLEPLK | Catalytic Activity: H2O + L-tryptophan = indole + NH4(+) + pyruvate
Sequence Mass (Da): 53131
Sequence Length: 472
Pathway: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1.
EC: 4.1.99.1
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Q7TQP6 | MGNYKSRPTQTCSDEWKKKVSESYAIIIERLEDNLQIKENEFQELRHIFGSDEAFSEVSLNYRTERGLSLLHLCCVCGGNKSHIRALMLKGLRPSRLTRNGFPALHLAVYKDSPELITSLLHSGADVQQVGYGGLTALHIAAIAGHPEAAEVLLQHGANVNVQDAVFFTPLHIAAYYGHEQVTSVLLKFGADVNVSGEVGDRPLHLASAKGFFNIVKLLVEEGSKADVNAQDNEDHVPLHFCSRFGHHNIVSYLLQSDLEVQPHVINIYGDTPLHLACYNGNFEVAKEIVQVTGTESLTKENIFSETAFHSACTYGKNIDLVKFLLDQNAVNINHRGRDGHTGLHSACYHGHIRLVQFLLDNGADMNLVACDPSRSSGEKDEQTCLMWAYEKGHDAIVTLLKHYKRPQEELPCNEYSQPGGDGSYVSVPSPLGKIKSMTKEKADVLLLRAELPSRFHLQLSEIEFHEIIGSGSFGKVYKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCQLNHPCVVQFVGACLDDPSQFAIVTQYISGGSLFSLLHEQKRILDLQSKLIIAVDVAKGMEYLHSLTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQPGNLRWMAPEVFTQCTRYTIKADVFSYSLCLWELLTGEIPFAHLKPAAAAADMAYHHIRPPIGYSIPKPISSLLIRGWNACPEGRPEFSEVVSKLEECLCNVELMSPASSNSSGSLSPSSSSDCLLSRGGPGRSHVAALRSRFELEYALNARSYAGWSQSVGTHSNPGLSLEEMNRSTQYSTVDKYGYVSDPMSLTHLHSRQDDSNFEDSN | Function: May play a role in cardiac physiology.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 92732
Sequence Length: 835
Subcellular Location: Nucleus
EC: 2.7.11.1
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Q15025 | MEGRGPYRIYDPGGSVPSGEASAAFERLVKENSRLKEKMQGIKMLGELLEESQMEATRLRQKAEELVKDNELLPPPSPSLGSFDPLAELTGKDSNVTASPTAPACPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVEPHPEHLCGAYPYAYPPMPAMVPHHGFEDWSQIRYPPPPMAMEHPPPLPNSRLFHLPEYTWRLPCGGVRNPNQSSQVMDPPTARPTEPESPKNDREGPQ | Function: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating TAX1BP1 and A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG . Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection.
PTM: Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.
Sequence Mass (Da): 71864
Sequence Length: 636
Subcellular Location: Cytoplasm
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Q9WUU8 | MEGRGPYRIYDPGGSTPLGEVSAAFERLVEENTRLKGKMQGIKMLGELLEESQMEASRLRQKAEELVKDSELSPPTSAPSLVSFDDLAELTGQDTKVQVHPATSTAATTTATATTGNSMEKPEPASKSPSNGASSDFEVVPTEEQNSPETGSHPTNMMDLGPPPPEDSNLKLHLQRLETTLSVCAEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHMEPHPEHVCGAYPYAYPPMPAMVPHHAYKDWSQIRYPPPPVPMEHPPPHPNSRLFHLPEYTWRPPCAGIRNQSSQVMDPPPDRPAEPESADNDCDGPQ | Function: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating TAX1BP1 and A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG (By similarity). Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases.
PTM: Phosphorylation at Tyr-565 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.
Sequence Mass (Da): 73050
Sequence Length: 647
Subcellular Location: Cytoplasm
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Q8NFZ5 | MSRDPGSGGWEEAPRAAAALCTLYHEAGQRLRRLQDQLAARDALIARLRARLAALEGDAAPSLVDALLEQVARFREQLRRQEGGAAEAQMRQEIERLTERLEEKEREMQQLLSQPQHEREKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQSEHTDGHTSVQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKYLAADALELMVPGGWRPGTGSQQPEPPAEGGHPGAAQRGQGDLQCPHCLQCFSDEQGEELLRHVAECCQ | Function: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes.
PTM: In vitro phosphorylated by CHUK.
Sequence Mass (Da): 48700
Sequence Length: 429
Subcellular Location: Cytoplasm
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Q99JG7 | MSSGDPRSGRQDGAPRAAAALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEEGASETQLRQEVERLTERLEEKEREMQQLMSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKCLDERQCAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRRQVPLEPELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKIMSLMYQVSQRQDSREPGPCRIHTGNKTAKYLEMDALEHVTPGGWRPESRSQQMEPSAEGGHVCTAQRGQGDLQCPHCLRCFSDEQGEAFLRHLSECCQ | Function: Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes.
PTM: In vitro phosphorylated by CHUK.
Sequence Mass (Da): 49094
Sequence Length: 430
Subcellular Location: Cytoplasm
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Q13470 | MLPEAGSLWLLKLLRDIQLAQFYWPILEELNVTRPEHFDFVKPEDLDGIGMGRPAQRRLSEALKRLRSGPKSKNWVYKILGGFAPEHKEPTLPSDSPRHLPEPEGGLKCLIPEGAVCRGELLGSGCFGVVHRGLWTLPSGKSVPVAVKSLRVGPEGPMGTELGDFLREVSVMMNLEHPHVLRLHGLVLGQPLQMVMELAPLGSLHARLTAPAPTPPLLVALLCLFLRQLAGAMAYLGARGLVHRDLATRNLLLASPRTIKVADFGLVRPLGGARGRYVMGGPRPIPYAWCAPESLRHGAFSSASDVWMFGVTLWEMFSGGEEPWAGVPPYLILQRLEDRARLPRPPLCSRALYSLALRCWAPHPADRPSFSHLEGLLQEAGPSEACCVRDVTEPGALRMETGDPITVIEGSSSFHSPDSTIWKGQNGRTFKVGSFPASAVTLADAGGLPATRPVHRGTPARGDQHPGSIDGDRKKANLWDAPPARGQRRNMPLERMKGISRSLESVLSLGPRPTGGGSSPPEIRQARAVPQGPPGLPPRPPLSSSSPQPSQPSRERLPWPKRKPPHNHPMGMPGARKAAALSGGLLSDPELQRKIMEVELSVHGVTHQECQTALGATGGDVVSAIRNLKVDQLFHLSSRSRADCWRILEHYQWDLSAASRYVLARP | Function: Involved in negative regulation of cell growth. Has tumor suppressor properties. Plays a negative regulatory role in the Ras-MAPK pathway. May function in signaling pathways utilized broadly during fetal development and more selectively in adult tissues and in cells of the lymphohematopoietic system. Could specifically be involved in phospholipid signal transduction.
PTM: Autophosphorylated on tyrosine residues.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 72468
Sequence Length: 666
Subcellular Location: Cytoplasm
EC: 2.7.10.2
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Q9H2S6 | MAKNPPENCEDCHILNAEAFKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVPKKAYDMEHTFYSNGEKKKIYMEIDPVTRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLISVSELQDFEEEGEDLHFPANEKKGIEQNEQWVVPQVKVEKTRHARQASEEELPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV | Function: May be an angiogenesis inhibitor.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 37130
Sequence Length: 317
Subcellular Location: Membrane
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Q8NFQ8 | MADSGLREPQEDSQKDLENDPSVNSQAQETTIIASNAEEAEILHSACGLSKDHQEVETEGPESADTGDKSESPDEANVGKHPKDKTEDENKQSFLDGGKGHHLPSENLGKEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEASDGTGASQEPPTTDSQEAQSPGHSSAGQEGEDTLRRRLLAPEAGSHPQQTQKLEEIKENAQDTMRQINKKGFWSYGPVILVVLVVAVVASSVNSYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVADAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCLF | Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51263
Sequence Length: 470
Subcellular Location: Endoplasmic reticulum membrane
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Q6P752 | MSQTLKSQDTNMSDSGYRDPVEDSQNVLGNDPSVNSQAQDPIVTPSNTVEAQTLHPTSDLKEDHHEIGAKGQEHADTGDRAESSEEPALEKPPLDKAELERSPSSQDTEQRHHPYSEHVGGDTLVLDPNYSQSDLGGRADAHLESSSAAPTEGAGEGGEAGAHLESSCAALPVGADEGGRANAHLESSSAAPTEGAGEGGEADVHLESSSAVPPEEAHLESSSAAPSEGAGEGGEADAHLESSSAAPSEGAGEGGETAQNLLAVDSTDAQSPCHSSAGPGSQDSLRRRLPVTEAERHEEETQLVTEKEEVAQETLRKTEKKSLWTYGSMFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFSQLREKFPGQSAFLWQRGRKFLQKHLNASNPSEPATVIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSYGFENGHKAAVVHHFESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPRETEEKVRDLLWAKFTDSGTPSSFSHMDSDKLSGLWSRISHLVLPVQPVKNIEERGCLL | Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61698
Sequence Length: 578
Subcellular Location: Endoplasmic reticulum membrane
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Q6INE3 | MATSISTQRGQVFIGELPQDFLRISPTQQQQQIQLDAQAAQQLQYSGVMATMGRLSITVVQAKLAKNYGMTRMDPYCRIRLGYAVYETPTAHNGAKNPRWNKVIQCTIPPGVDSFYIEIFDERAFSMDDRIAWTHITIPETLKEGKHVDEWFSLSGKQGDDKEGMINLVMSYTSVPAMMPAQPVVLMPTVYQQGVGYVPIADPIYNPGMPMAAPPPAVNPQHETREEDIQSIKDMFPTMDPEVIRSVLEAQGGNRDAAVNSLLQMVEDS | Function: Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance.
Sequence Mass (Da): 29983
Sequence Length: 269
Domain: Both ATG8-interaction motifs (AIM1 and AIM2) are required for the association with ATG8 family proteins.
Subcellular Location: Cytoplasm
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P40310 | MTRFMNSFAKQTLGYGNMATVEQESSAQAVDSHSNNTPKQAKGVLAEELKDALRFRDERVSIINAEPSSTLFVFWFVVSCYFPVITACLGPVANTISIACVVEKWRSLKNNSVVTNPRSNDTDVLMNQVKTVFDPPGIFAVNIISLVLGFTSNIILMLHFSKKLTYLKSQLINITGWTIAGGMLLVDVIVCSLNDMPSIYSKTIGFWFACISSGLYLVCTIILTIHFIGYKLGKYPPTFNLLPNERSIMAYTVLLSLWLIWGAGMFSGLLHITYGNALYFCTVSLLTVGLGDILPKSVGAKIMVLIFSLSGVVLMGLIVFMTRSIIQKSSGPIFFFHRVEKGRSKSWKHYMDSSKNLSEREAFDLMKCIRQTASRKQHWFSLSVTIAIFMAFWLLGALVFKFAENWSYFNCIYFCFLCLLTIGYGDYAPRTGAGRAFFVIWALGAVPLMGAILSTVGDLLFDISTSLDIKIGESFNNKVKSIVFNGRQRALSFMVNTGEIFEESDTADGDLEENTTSSQSSQISEFNDNNSEENDSGVTSPPASLQESFSSLSKASSPEGILPLEYVSSAEYALQDSGTCNLRNLQELLKAVKKLHRICLADKDYTLSFSDWSYIHKLHLRNITDIEEYTRGPEFWISPDTPLKFPLNEPHFAFMMLFKNIEELVGNLVEDEELYKVISKRKFLGEHRKTL | Function: Outwardly rectifying potassium channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77408
Sequence Length: 691
Subcellular Location: Cell membrane
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Q9LFL3 | MGDNLMDKVTAFGERLKIGGSEVSNKISAGVSSMSFKVKELFQGPNPTDKIVEDATTENLEEPDWDMNLEICDMINQETINSVELIRGIKKRIMMKQPRIQYLALVLLETCVKNCEKAFSEVAAERVLDEMVKLIDDPQTVVNNRNKALMLIEAWGESTSELRYLPVFEETYKSLKARGIRFPGRDNESLAPIFTPARSTPAPELNADLPQHVHEPAHIQYDVPVRSFTAEQTKEAFDIARNSIELLSTVLSSSPQHDALQDDLTTTLVQQCRQSQTTVQRIIETAGENEALLFEALNVNDELVKTLSKYEEMNKPSAPLTSHEPAMIPVAEEPDDSPIHGREESLVRKSSGVRGGFHGGGGSGDDMMDDLDEMIFGKKNGCDSSTNPDHDPKKEQSSSKNDDLIRF | Function: Might contribute to the loading of the ESCRT machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45311
Sequence Length: 407
Subcellular Location: Membrane
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Q9LNC6 | MDKLKIAEWGEKLKTGGAQMSRMVSEKVKDMLQAPTLESKMVDEATLETLEEPNWGMNMRICAQINNDEFNGTEIVRAIKRKISGKSPVSQRLSLELLEACAMNCEKVFSEVASEKVLDEMVWLIKNGEADSENRKRAFQLIRAWGQSQDLTYLPVFHQTYMSLEGENGLHARGEENSMPGQSSLESLMQRPVPVPPPGSYPVPNQEQALGDDDGLDYNFGNLSIKDKKEQIEITRNSLELLSSMLNTEGKPNHTEDDLTVSLMEKCKQSQPLIQMIIESTTDDEGVLFEALHLNDELQQVLSSYKKPDETEKKASIVEQESSGSKDTGPKPTEQEEQEPVKKTGADDDKKHSEASGSSNKTVKEEKQAVKIELGLSSDEDEK | Function: Binds ubiquitin in vitro . Might contribute to the loading of the ESCRT machinery (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42797
Sequence Length: 383
Subcellular Location: Cytoplasm
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Q6NQK0 | MANDAAACAERATNDMLIGPDWAINIELCDLINMDPSQAKEAVKVLKKRLGSKNSKVQILALYALETLSKNCGENVYQLIIDRGLLNDMVKIVKKKPELNVREKILTLLDTWQEAFGGRGGRYPQYYNAYNDLRSAGIEFPPRTESSLSFFTPPQTQPDEDAAIQASLQGDDASSLSLEEIQSAEGSVDVLMDMLGAHDPGNPESLKEEVIVDLVEQCRTYQRRVMTLVNTTTDEELLCQGLALNDNLQHVLQRHDDIANVGSVPSNGRNTRAPPPVQIVDINHDDEDDESDDEFARLAHRSSTPTRRPVHGSDSGMVDILSGDVYKPQGNSSSQGVKKPPPPPPHTSSSSSSPVFDDASPQQSKSSEVIRNLPPPPSRHNQRQQFFEHHHSSSGSDSSYEGQTRNLSLTSSEPQKEEKPEDLLFKDLVEFAKTRSSKANNNNRSL | Function: Might contribute to the loading of the ESCRT machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49255
Sequence Length: 446
Subcellular Location: Cytoplasm
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Q9FFQ0 | MAAELVSSATSEKLADVDWAKNIEICELAARDERQAKDVIKAIKKRLGSKNPNTQLYAVQLLEMLMNNIGENIHKQVIDTGVLPTLVKIVKKKSDLPVRERIFLLLDATQTSLGGASGKFPQYYTAYYELVNAGVKFTQRPNATPVVVTAQAVPRNTLNEQLASARNEGPATTQQRESQSVSPSSILQKASTALEILKEVLDAVDSQNPEGAKDEFTLDLVEQCSFQKERVMHLVMTSRDEKAVSKAIELNEQLQRILNRHEDLLSGRITVPSRSTTSNGYHSNLEPVRPISNGDQKRELKASNANTESSSFISNRAHLKLEEEDEEEEPEQLFRRLRKGKARARPEDEEEPSPPQGLPGSAIHNERLNRPLIRPLPSEEASRGGDSHSQSPPVVIPPPPAKHVEREKFFKENKGDGALGLPGHMRGLSLHSRDGSSSRSGSVDFSD | Function: Might contribute to the loading of the ESCRT machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49423
Sequence Length: 447
Subcellular Location: Cytoplasm
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O80910 | MASSSASATVAVDKATSDLLLGPDWTTNMEICDSVNSLHWQAKDVVKAVKKRLQHKSSRVQLLALTLLETLVKNCGDYLHHQVAEKNILGEMVKIVKKKADMQVRDKILVMVDSWQQAFGGPEGKYPQYYWAYDELRRSGVEFPRRSPDASPIITPPVSHPPLRQPQGGYGVPPAGYGVHQAGYGVPQAGYGIPQAGYGVPQAGYGIPQVGYGMPSGSSRRLDEAMATEVEGLSLSSIESMRDVMDLLGDMLQAVDPSDREAVKDEVIVDLVERCRSNQKKLMQMLTSTGDDELLGRGLDLNDSLQILLAKHDAIASGSPLPVQASGSPLSVQASKPADSSPKSSEAKDSSSIAGSSSPIPATVSTGKSPIDEEYEEEEDEFAQLARRHSKPPASVTTDPTSLESHNAASNALALALPDPPPPVNTTKEQDMIDLLSITLCTPSTPPAPSSQPSPPPPAGSDQNTHIYPQPQPRFDSYVAPWAQQQQPQQPQAQQGYSQHQQHQQQQGYSQPQHSQQQQGYSQLQQPQPQQGYSQSQPQAQVQMQPSTRPQNPYEYPPPPWASTSANAYYTPRANASASYTDTSALAGRSLQQSNSFPTRAGDPQATSTASNSGVSVGQKPFVPSYRLFEDLDVFGSADGKHNKPANSSNGSQNLSGSQTQQSMIGGRKMI | Function: Acts as a gatekeeper for degradative protein sorting to the vacuole. Plays a role in recognition of ubiquitinated PIN2 auxin carrier at the plasma membrane and further to its endocytic sorting. Binds ubiquitin in vitro . Might contribute to the loading of the ESCRT machinery (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72318
Sequence Length: 671
Subcellular Location: Endosome
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F4KAU9 | MRPSCASSSSSSASPSLRLSSVTVAVDKATSELLRTPDWTIIIAICDSLNSNRWQCKDAIKAVKRRLQHKSSRVQLLTLTLLEAMLKNCGDFVHSHIAEKHLLEDMVKLVRKKGDFEVRNKLLILLDTWNEAFSGVACKHPHYNWAYQELKRCGVKFPQRSKEAPLMLEPPPPVTQSSSSSSMNLMSIGSFRRLDETMATEIESLSLSSLESMRNVMDLVNDMVQAVNPSDKSALKDELIVDLVEQCRSNQKKLIQMLTTTADEDVLARGLELNDSLQVVLARHDAIASGVSLPLLLQAPEPRETSSSLKTCGAAALESADSESSSSSSSSESETDEVEDVKDDFIQLAKRHALLNALHSDEEEETLLLGNDNEKTAEAEAKTQCKDLALFDTTTTTTTKSEQDIIELLSLTLSTTALPSPQTQPQTQHPSFFADDNILMNSYVVPWAQSQEEPQVPKMTQFAPSGPQFQPWPLQQQQPYSYGYPQPQWSGGQVNSNDTTFWSQGGNENMVFERNLQVSNSFPARATGTSGAATAATVDRQP | Function: Might contribute to the loading of the ESCRT machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59768
Sequence Length: 542
Subcellular Location: Membrane
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Q9C9Y1 | MVHPLVDRATSDMLIGPDWAMNLEICDMLNHEPGQTREVVSGIKKRLTSRTSKVQLLALTLLETIITNCGELIHMQVAEKDILHKMVKMAKRKPNIQVKEKILILIDTWQESFSGPQGRHPQYYAAYQELLRAGIVFPQRPQITPSSGQNGPSTRYPQNSRNARQEAIDTSTESEFPTLSLTEIQNARGIMDVLAEMMNAIDGNNKEGLKQEVVVDLVSQCRTYKQRVVHLVNSTSDESMLCQGLALNDDLQRLLAKHEAIASGNSMIKKEEKSKKEVPKDTTQIIDVGSSETKNGSVVAYTTNGPKIDLLSGDDFETPNADNSLALVPLGPPQPSSPVAKPDNSIVLIDMLSDNNCESSTPTSNPHANHQKVQQNYSNGFGPGHQEQSYYGQGSSAPVWNLQITQQPSSPAYGNQPFSPNFSPPASPHYGGQNNNVLALPPPPWEAQSPSSSPQYSPTHPMQVTQVVITTHTHQPLGYNPQGGSPHATNNNNNNMFGMFLPPMTGGHMPPPFGHNGHVTNNNYNPNMYGGYGGQAQPPQQYLVEQQMYGMSLQDNGNNNTNPYQVSSHQPPPMMKPMNKKPEDKLFGDLVELSKFKKPTSGRAGSM | Function: Might contribute to the loading of the ESCRT machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66686
Sequence Length: 607
Subcellular Location: Membrane
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P43768 | MTAELNFLDLFLKASIVVQLVIVILISFSIISWAIIIQRSRILTNALKEARTFEDRFWSGEDLNKLYEGLSNRRDGLTGSEQIFCVGFKEFSRLKQVNPDAPEAIIKGTMRAMNLAMNREIESLENRVPFLATVASVSPYIGLFGTVWGIMHAFMALSGAKQATLQMVAPGIAEALIATAIGLFAAIPAVMAYNRLSLRVNAIEQDYGNFIDEFTTILHRQAFGKAPH | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25287
Sequence Length: 228
Subcellular Location: Cell inner membrane
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P50598 | MEPNVVDHTSMWSLISNASIVVQLVMLTLVAASVTSWIMIFQRGNAMRAAKKALDAFEERFWSGIDLSKLYRQAGSNPDPDSGVEQIFRAGFKEFSRLRQQPGVDPDAVMEGVARAMRVAISREEEKLEASLPFLATVGSTSPYVGLFGTVWGIMNSFRGLATVQQATLATVAPGIAEALIATAIGLFAAIPAVIAYNRFSARSEMLIGRYYTFADEFQAILHRKVHTSDD | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25282
Sequence Length: 231
Subcellular Location: Cell inner membrane
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P0ABV8 | MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSNDNPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEIIKALNLLHSAGVKSVGLMTQPI | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15383
Sequence Length: 142
Subcellular Location: Cell inner membrane
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P43769 | MARRQRKAIKSEINIVPFLDVLLVLVLIFMATAPIISQSVQVELPDSVQSQEVSNEDKVPVILEVAGIGKYAISIGGERQEGLTEEMVTQLSRQEFDKDNNTLFLVGGAKEVPYEEVIKALNLLHLAGIKSVGLMTNPI | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15258
Sequence Length: 139
Subcellular Location: Cell inner membrane
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P50599 | MARVRHKRKPVAEMNVVPYIDVMLVLLVIFMVTAPMLNQGVKVDLPKVSSEALPQDNNKQVLTLSVKADGSYYWNVGSEVDTEKQTDSAVSLEQMTDAVTKIMSARPDTQVFIRGDKAVNYGAVVGAMGALQQAGVPNVGLITEAP | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15788
Sequence Length: 146
Subcellular Location: Cell inner membrane
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P83588 | SPVCTPSGQPCQPNTQPCCNNAEEEQTINCNGNTVYRCA | Function: Potent inhibitor of insect, but not mammalian, voltage-gated calcium channels (Cav).
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 4173
Sequence Length: 39
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9FEG2 | MTDSGLMMPAEIAGILTTAITSWWDDVNESTQWQDGIFFALCGAYALVSAVALVQLIRIQMRVPEYGWTTQKVFHLMNFVVNGVRAVLFGFHMQVFLVHPKALCWVLLDLPGLLFFSAYTLLVLFWAEIYHQARSLPTDKLRITYISVNVAVYLAQIGIWAYIWVHDNSTVELVGKIFIAVVSFIAALGFLLYGGRLFFMLRRFPIESKGRRKKLHEVGSVTAICFTCFLIRCVVVAVSAFDKDLTLDVLDHPVLNLIYYMVVEVLPSALVLFILRKLPPKRVSAQYHPIQ | Function: Necessary for the efficient intracellular multiplication of tobamoviruses, probably being a membrane anchor promoting the formation of the replication complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33009
Sequence Length: 291
Subcellular Location: Vacuole membrane
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Q54GH3 | MVTELVDKATNELLIQTDWTTVLQISDILNRDPIHARGVVRQVTKKLKDRSRVILLALELADSLLQNCHCTHVYFAERTFQTELCRLIMNKKTKLNVKEKTLEIVESWGNAFQARHDVPGFYETYSFIKRSGYKFPPKPSDAPILNFNNSPAKRTVSTTILTNNSHSTTPPQANVPSFNNVSSVGSNNAGGGGSSSQPIKNQEISSIKGSTSVFNEMISFLNVEDEDPQENDLIKELFETCKQSQIRVKEMIESGSTNERDLNVLLKLNDEINNALNDHEACIKRRRAFVENGYKPVPPPQQQQQQQQQQQQQQQQQQQQQSHSNNHNGTTTTTTTNNNNKNPSYLTKHKELEEIDFFKAPDGISPYSVQQQLQPFQQQQFNSTYNPFAQPQPQQFQQQPQQQLQQQPQQQQGFNQRIQQPQQQADAFDLFVANRQQSNNNNNNNNINNTTSSFGANNPFANNSSNNNNTNGAIQPYIPNTAKSLPPVSQQLQQPMQNQFSPQPQKFVGSSITPSAPPPFKPNTTQSNPFNTSPPLNNMNNHNNNMMQQQQPQQQQQQQPQQQFNPMYNNNAMAPSYPNYNAIGADNQHNTNPYGMMNHQQQQQQQQQQQPMMNQMNNFSAPTYSQFTNYAQPNQQPYNNNYGGMNQSNMYPNNNMSGKSSLI | Function: May contribute to the sorting of ubiquitinated proteins and transfer them for further sorting/trafficking processes to the endosomal multivesicular bodies (MVBs) pathway. Binds to phospholipids, such as phosphatidylinositol PtdIns(3)P and PtdIns(3,5)P2. These phospholipids are involved in the recruitment of the ESCRT machinery to endosomal membranes (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75375
Sequence Length: 663
Domain: The VHS domain binds phosphatidylinositol PtdIns(3)P and PtdIns(4)P.
Subcellular Location: Cytoplasm
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O60784 | MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDALRAVKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHVLVASQDFVESVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVTIYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETQSGQDSVGTDSSQQEDSGQHAAPLPAPPILSGDTPIAPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEELLIVNDNLNNVFLRHERFERFRTGQTTKAPSEAEPAADLIDMGPDPAATGNLSSQLAGMNLGSSSVRAGLQSLEASGRLEDEFDMFALTRGSSLADQRKEVKYEAPQATDGLAGALDARQQSTGAIPVTQACLMEDIEQWLSTDVGNDAEEPKGVTSEEFDKFLEERAKAADRLPNLSSPSAEGPPGPPSGPAPRKKTQEKDDDMLFAL | Function: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways . Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures . Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes . MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN . Binds to polyubiquitinated proteins via its GAT domain . In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes . The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin . Mediates clathrin recruitment to early endosomes by ZFYVE16 . Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking . Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation . PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation . Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling .
PTM: Monoubiquitinated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53818
Sequence Length: 492
Domain: The GAT domain and the VHS domain are required for the interaction with polyubiquitinated proteins.
Subcellular Location: Cytoplasm
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Q57815 | MVKLPAISKKPREIAKQKIIELAKKMYEDLMKGKRPKITMPIRSLSNAMFDKEKGSFTLVGKEKARTLTVNQAKIFAQTTKMLEFAKQLLETDDFSTLREAYYVSKNWGEARFDDQQASNNVIEDLEAALGVLREHLGFIPEEDGSSVVGPLKIIEETPEGELVVDCTKLGTGAYNIPNDVTKLNLETDADFILAIETSGMFARLNAERFWDKHNCILVSLKGVPARATRRFIKRLHEEHDLPVLVFTDGDPYGYLNIYRTLKVGSGKAIHLADKLSIPAARLIGVTPQDIIDYDLPTHPLKEQDIKRIKDGLKNDDFVRSFPEWQKALKQMLDMGVRAEQQSLAKYGLKYVVNTYLPEKIKDESTWLP | Cofactor: Mg(2+) is directly coordinated by Glu-197 and Asp-249 as well as indirectly coordinated through 2 water molecules by Asp-251 .
Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 41829
Sequence Length: 369
EC: 5.6.2.2
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Q8PUB7 | MEGEKGSKTRKGDALAREKLLEIAEKIYNQFEEEVVPSVSLPSRTKANLEYSDESDVWVYGDRESERSAKTVKGAFQLLKTTYATDFLINEHLARNRGSTLRELYYISEGWDYAKFKEQGESDRLIEDLEILTSLQREYFHMRPEEDGATMFGPIEITEQTKRGERNIHCQKDVGEGGYQIPFNVENIEFQKHDASMIIAIETGGMYARLMENGFDEAYNAILVHLKGQPARSTRRIIKRMNEELGIPVAVFTDGDPWSYRIYASVAYGAIKSAHLSEFMATPAAKFLGLQPSDIVEYELSTDKLTEQDVSALRSELSDPRFESDYWKEQIQLQLDIGKKAEQQAFAGKGLDFVTEVYLPNRLKEMGMI | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 42127
Sequence Length: 369
EC: 5.6.2.2
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O27089 | MNRREIAINKLKSLGDVILDDVTQGRIPRIKVPSRGTSNIIYDEDKRHYVLGDRYGTRSMGNVKQIKKIGQMLYTANFCKDLVAREKTATLRELYYISEGWEVDFADQQESNIVGEDLEVTLGMTREELGLMPEEDGASVYGALTVREGDIEIDALRSGKSGYNISPTIDEVEFVDHDVERVIAVETMGMFHRLVQEKAYKKFDALIVGLKGQAARATRRFIKRVNEELNLPVYICNDGDPWGFHIAMVIISGSAKLAHVNHQLATPDAKFLGVTASDIINYDLPTDPLKDVDVVRLKELLQDPRYRGDFWKTEIKKMLTIGKKAEQQSFSKYGLEYVVDTYLPEKLEAVENQ | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 40029
Sequence Length: 353
EC: 5.6.2.2
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A2XFC1 | MSEKKRRGGAGAGAASGSASKKPRVSTAASYAESLRSKLRPDASILATLRSLASACSKSKPAGSSSSSSSASKALAAEDDPAASYIVVADQDSASVTSRINRLVLAAARSILSGRGFSFAVPSRAASNQVYLPDLDRIVLVRRESARPFANVATARKATITARVLSLVHAVLRRGIHVTKRDLFYTDVKLFGDQAQSDAVLDDVSCMLGCTRSSLHVVASEKGVVVGRLTFADDGDRIDCTRMGVGGKAIPPNIDRVSGIESDALFILLVEKDAAFMRLAEDRFYNRFPCIILTAKGQPDVATRLFLRRLKVELKLPVLALVDSDPYGLKILSVYMCGSKNMSYDSANLTTPDIKWLGVRPSDLDKYRVPEQCRLPMTDHDIKVGKELLEEDFVKQNEGWVKELETMLRTRQKAEIQALSSFGFQYLTEVYLPLKLQQQDWI | Function: Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity). May be involved in cell proliferation and stress tolerance.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 48242
Sequence Length: 442
Subcellular Location: Nucleus
EC: 5.6.2.2
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O59209 | MKLKRQKPKEKFSYDPQKVLKKLEDLAWKILEEAKSGKNPYFDVPTRGLNNVYFDEESRLIRLGDRLSRRYFLNVAHARKFMQTLILMAYIKRLVSEGKHASLREAYYANKHTVPGTRENTFEDQSESDPIIEDLERMLGVLREEMHITADRRGYIYGDIVIKDGEDEFNASKLGTGGWAVPGTVEHIQFPEINVDYVLVVETAAMADRLIEEKYPKRENCLIVATQGQASRGVRRLIHRLHYEEGLPIIVFTDGDPYGWYIYSTIKRGSINLAYLSEKLATPDAKFVGMTMDDIKEYNLENVTEKLKGIPPDKKGGPTGDYKRLIEELNYPWFQDKEWQRQLKLALKWGVRIEQQALANKSLEFVAKEYLPEKIREGKLLP | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 44296
Sequence Length: 382
EC: 5.6.2.2
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O05208 | MSSEFISKVDKEARRKAANILRDKFLNLVEQLKKGEPLVMEIPMRTLSNAIYDEKRKLLLLGEKKLRRNFLDLNEAKRFMQTVLMASIIYDALVSDEYPTIRDLYYRGKHSLLLKSIEGNKIVSEENTWDEQKESDSVIVDIEVFTSLLREEMLILSKEKGKVVGNLRIRSGNDVIDLSKTGHGAYAIEPTPDLIDFIDVDAEFVLVVEKDAVFQQLHRAGFWKQYKSILITSAGQPDRATRRFVRRLNEELKLPVYILTDADPYGWYIFSVFRIGSISLSYESERLATPDAKFLGVSMGDIFGNSRKKPYLSEAERKNYIIKAKDADIKRAEEIKNYEWFKTKAWQEEINTFLQRKAKLEIEAMASKGLKFLAFQYIPEKITNKDYIA | Function: Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity; it cannot introduce DNA supercoils . ATP is absolutely required for DNA cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands .
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 45055
Sequence Length: 389
EC: 5.6.2.2
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Q9YE64 | MSAVAKRTRRARARAEEAARPGSTGEKYREMSVAEFFAKNKELAGFANPTRALYQTIRELVENSLDATDAKGILPWIHISIRQIEGSEGRGGRPRYTVTVEDNGIGVPVTSMAMAFGKVLFSSKYVIRQTRGMYGLGVKAAILYGQMTAGTPVEVYSATKGSQYVYMMKLVIDVQRNEPRILERGEWNKRGSWHGTRVTLSLEGDWSRAKSKILEYIKRTAVIAPYAEIILETPDGEIYYFPRSTRKLPKPPRESKPHPHGVDIEQLKSMLRSTRASTLREFLVKEFQSIGDKTAQDFLEKYGLDPDLKPRELLKKGRDKLLRRLADALMEYPFRAPKSDYLSPIGSDIIEIGLRRMFNPEWVGAVSRSPKAYRGHPFIVEVGIAYGGGIEARSEPLLLRYANKIPLLYEEREDVSYKVVSSINWRQYNVDFPAPLVVLVHIASTKVPYKGVGKESVSDVPEIEAEIRNAVQEVARRLRLYLSRKAREEEAIRRSVTLAKYIPEVAVSLAYFLRPPSKWQPPKPEEVKKIQEALIKIVARHIELPPVDGKTEDPEAIVRRIVESVELE | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 64354
Sequence Length: 568
EC: 5.6.2.2
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Q9C5V6 | MAGDDLVETKKGSSKNSKDSNESKLKQKSPAEFFAENKNIAGFDNPGKSLYTTVRELVENALDSAESISELPEVEVTIEEIVKSKFNSMIGLIDRERVDTQLYDDYETEKARGKRLAKEARASEIQAKNLASGKKNKEPGVSKVLKARGEASYYKVTCKDNGKGMPHDDIPNMFGRVLSGTKYGLKQTRGKFGLGAKMALIWSKMSTGLPIEISSSMKSQNYVTFCRLDIDIHRNIPHIHLHEKKGNKEKWHGAEIQVVIEGNWTTYRSKILHYMRQMAVITPYAQFLFRFISETPEKNVTIKFTRRTDVMPPIPIETKHHPSSVDLLLIKRLITDTSKKTLLQFLQNEFVNINKTLAARLIGEMGPDFGPSMAVKSVTSQQMVRIHQLFRQAKFDDPSGDCLSPAGEYNLRLGIIKELHPDMVATYSGSAQVFEGHPFIVEAGVSLGGRDVKQGINIFRFANRIPLLFEQGADVVTRTALKRINWNSYKINQTQDKIGVFVSIVSTKIPFKGTGKEYIGDDISEIATAVKSAIQQCCIQLKSKIVKRLQAREQQERKRSLSRYIPDATGAVYEVLKQMTEEHKTKRKRYGEEDIVMLDKVSKQIITKETLKEKLAEHVEQVDYEMALEYATQSGVSEEPRENIYLQHLDPNKSNFIDLHSPTFVFRLML | Function: Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity. The B subunit binds ATP. Involved in cell-elongation processes.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 75852
Sequence Length: 670
Subcellular Location: Nucleus
EC: 5.6.2.2
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O29605 | MSGKHREISVAEFFEKNKHILGYSNPAKAIITVVKEAVDNALDACEEAGILPDIFVRISKVDDHFKIVVEDNGPGIPREQIPKVFGKLLYGSRFHEIRQSRGQQGIGISAAVLYAQLTTGKPATVISKTPDEDRAKKVVLYINTKKNEPEIVEEGEEEWYLPSGTKIELEVAGNYVRERKQSVYEYLRETSVINPHAKITFVEPDGTINEFKRVTDDIPQPPKSIKPHPHGIELGTLMSMLKSTRATTLRRFLKEEFVRVGEKIADDVLRKAGFSGDETPQEMGRDDAAKLLNAFRQTDFLPPPTDCLSPIGEAMIAKSLMAEFQPEFVYAVTRKPKVYSGHPFLVEVGLAYGGEIKSEKVTLLRYANKIPLLYQQGGCALTKAVESVNWKSYGMVQNRGELPSAPAVILIHLASTNIPYTSESKESVAAIPEIIDETRLALQEVGRRLKEYLERKSRQQKKKKKEEMIGKVLPLIAKKVCEILEKEPLEIDRIVARIMGYLHVERIVEERDGVKVVTIRVSNFTRSKKSIKLYEMCSGNVEADGAKVSGSGYSTVTWSLEVKPDEEVEVSYRLKGRIINKNPLVEGVEEDLLSGAEVMNFA | Function: Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 67400
Sequence Length: 602
EC: 5.6.2.2
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Q8N2E6 | MAAATRGCRPWGSLLGLLGLVSAAAAAWDLASLRCTLGAFCECDFRPDLPGLECDLAQHLAGQHLAKALVVKALKAFVRDPAPTKPLVLSLHGWTGTGKSYVSSLLAHYLFQGGLRSPRVHHFSPVLHFPHPSHIERYKKDLKSWVQGNLTACGRSLFLFDEMDKMPPGLMEVLRPFLGSSWVVYGTNYRKAIFIFIRWLLKLGHHGRAPPRRSGALPPAPAAPRPALRAQRAGPAGPGAKG | Function: Salusins -alpha and -beta may be endocrine and/or paracrine factors able to increase intracellular calcium concentrations and induce cell mitogenesis. Salusins may also be potent hypotensive peptides.
PTM: Amidation of salusin-alpha(29-Gly) by peptidylglycine alpha-amidating monooxygenase, PAM, converts Lys-241-Gly-242 to Lys-241-NH2 and gives raise to salusin-alpha.
Sequence Mass (Da): 26262
Sequence Length: 242
Subcellular Location: Secreted
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N4WQZ8 | MVYNPTATFHKKTLTRMKTGLGSNGDILFIQTRALRDQLSSSFRFVYSNGPFFSDPGPGVLPVYKDAGPFRSWLRRPLQNRAQEPRLHMEAIRKCLEGTMKEDEQSGASGQWVGLMGFSQGARLAASVLFESQRRQNIQEKGGIVRGYEGDNIETKLWDQRWQFAVLFSGPAPLIAFCPENDHLSSQSTAEHDPMYRALDNVNCSGELHITKPTLHVIGVKDEWAPSQRELYEKYCSKESSTLVEWEGAHRIPIESSIVKDLCARILVMSKQADFVES | Function: Probable esterase; part of the Tox1A locus, one of the 2 loci that mediate the biosynthesis of T-toxin, a family of linear polyketides 37 to 45 carbons in length, of which the major component is 41 carbons, and which leads to high virulence to maize . One of the PKSs (PKS1 or PKS2) could synthesize a precursor, used subsequently by the other PKS as starter unit, to add additional carbons . Variability in the length of the final carbon backbone C35-47 could be achieved by varying the number of condensation cycles, or use of different starter or extender units or might be due to decarboxylation of the penultimate product, catalyzed by DEC1 . Additional proteins are required for the biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9 .
Sequence Mass (Da): 31373
Sequence Length: 278
Pathway: Mycotoxin biosynthesis.
EC: 3.1.2.-
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Q00357 | MDEQIVSASSNVKDGVEKQPVKDREDVDANVVPPHSTPSLPKISLISLFSIVMSLGAAAFLGALDATVVAVLTPTLAQEFHSVDAVAWYGAIYLLMSGTTQPLFGKLYNEFSPKWLFITCLIVLQLGSLVCALARNSPTFIVGRAVAGIGAGGILSGALNIVALIVPLHHRAAFTGMIGALECVALIIGPIIGGAIADNIGWRWCFWINLPIGAAVCAILLFFFHPPRSTYSASGVPRSYSEILGNLDYIGAGMIISSLVCLSLALQWGGTKYKWGDGRVVALLVVFGVLFLSASGHQYWKGEKALFPTRLLRQRGFLLSLFNGLCFGGVQYAALYYLPTWFQAIKGETRVGAGIQMLPIVGAIIGVNIVAGITISFTGRLAPFIVIATVLASVGSGLLYTFTPTKSQARIIGYQLIYGAGSGAGVQQAFIGAQAALDPADVTYASASVLLMNSMSGVITLCVCQNLFTNRINALTEVLPGVTKETLQSGFAFLRSTLTPAEFGVAIQTFNSAIQDAFLVAIVLSCASVLGWPFLSWASVKGQKKMNK | Function: MFS-type transporter; part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid . HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize . TOXA acts as a HC-toxin efflux pump which contributes to self-protection against HC-toxin and/or the secretion of HC-toxin into the extracellular milieu .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58045
Sequence Length: 548
Subcellular Location: Membrane
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P11439 | MHLTPHWIPLVASLGLLAGGSFASAAEEAFDLWNECAKACVLDLKDGVRSSRMSVDPAIADTNGQGVLHYSMVLEGGNDALKLAIDNALSITSDGLTIRLEGGVEPNKPVRYSYTRQARGSWSLNWLVPIGHEKPSNIKVFIHELNAGNQLSHMSPIYTIEMGDELLAKLARDATFFVRAHESNEMQPTLAISHAGVSVVMAQAQPRREKRWSEWASGKVLCLLDPLDGVYNYLAQQRCNLDDTWEGKIYRVLAGNPAKHDLDIKPTVISHRLHFPEGGSLAALTAHQACHLPLETFTRHRQPRGWEQLEQCGYPVQRLVALYLAARLSWNQVDQVIRNALASPGSGGDLGEAIREQPEQARLALTLAAAESERFVRQGTGNDEAGAASADVVSLTCPVAAGECAGPADSGDALLERNYPTGAEFLGDGGDISFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTGLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPREDLK | Function: An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes the transfer of the ADP ribosyl moiety of oxidized NAD (NAD(+)) onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis . Has an LD(50) of 65 ng/ml against the human lung epithelial cell line C38 .
PTM: The 8 cysteines participate in intrachain disulfide bonds.
Catalytic Activity: diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide
Sequence Mass (Da): 69284
Sequence Length: 638
Domain: Domain I (which is divided into 2 non-contiguous regions Ia and Ib) is required for binding to cells, but not for ADPRT activity (Probable) . A subtilisin-digested fragment starting about residue 417 and extending to the C-terminus has full ADPRT activity .
EC: 2.4.2.36
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M2WKH6 | MKAIKVNAGRTAAVQPARMPKLRDGYLLCKVHCVALNPADWKYLDFIGVQGVTLGADLSGVVEEIDPSCGAHFEKGDRIAAFVHGGNVSQPDDGAFAEYCLVKADLALKVPDAMSDEDAATLGVAVATCGQALYQGLELPLPGGAPYDGFLLVYGGSTSTGTLAIQYARLSGCKVIATASPHNWPLLKELGVEETFDYKDPDCAKKVRGIPICKAGYLTDGALIRAFTSDSLVLALDCIAEGDSAKICEDSISESKGGTICYLFQAKHSRADIVDKRVFAYTVFGEAFDKFGQSWPARAEDFARGKEFAALASQMLSDGQLRPHPVRLGKDGLEGVLDGLQQLRERKVSGAKLVYRVVETP | Function: Oxidoreductase; part of the hps1-dma1 gene cluster that probably mediates the biosynthesis a derivative of cyclopiazonic acid (CPA) (Probable). The hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) nps1 might incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway (By similarity). In addition, the cluster also includes the tryptophan dimethylallyltransferase dma1, the FAD-dependent oxidoreductase toxD, the cytochrome P450 monooxygenase cyp3.1 and the methyltransferase DOTSEDRAFT_139328; the latter 2 being not present in all CPA-producing fungi but involved in additional modifications that occur in biosynthesis of a range of CPA and CPA-like products (Probable). Further studies are required to clarify whether the CPA-like hps1-dma1 cluster is functional or a non-functional relic reflecting evolution of D.septosporum (Probable).
Sequence Mass (Da): 38571
Sequence Length: 361
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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O74205 | MGTTSPNSEKRQITDINERRKLQNRVAQRKYRTRQKTRMKLAEAVLNDYTYIHPTLGTIQSKKKSPLTMECDRSSASYPDLSSYAEICSETRSETQATRARQLTSQRTCFRESVDNNQADSHAQLSRCLNRQEMFYGISGETEFSEGDTRDRVECIDPNLTRGWLDMDLRSGTPNSSTVVDCGLCTVGANSQPPTRTNVQEAIETLELFEPNDQRKTENLPREPCGSCPSSSHGYSPTSGNPSTLLLTPSESLMNSVIVTSDSPLLAADDKSPGDLVISEANTHGPKEDQFSPLMTAISLGRLDIARILLQSGAPLDIPDDSGKTALHRAVGRRELHMVEALLNLGAEMLATDHEGNSLLHIAVKTNSLSITRLLLERYKSCRELKDAQLGHGCRQHGNQVHSESWIDLRNREGMTAVHLSVIFNRPEILQLLVKYSANVN | Function: Transcription factor, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid . HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize . TOXE is a pathway-specific transcription factor which coordinates the expression of genes involved in HC-toxin biosynthesis . Binds to the tox-box, a 10-bp motif with the consensus 5'-ATCTCNCGNA-3', which is found in the promoter of all genes involved in HC-toxin biosynthesis . Required for pathogenicity of the fungus on maize .
Sequence Mass (Da): 48983
Sequence Length: 441
Domain: Contains a basic DNA-binding region at the N-terminus which is usually found in bZIP transcription factors, but does not contain the characteristic leucine zipper domain. Instead, four C-terminal ankyrin repeats were identified that were shown to confer protein-protein interaction of regulatory proteins.
Subcellular Location: Nucleus
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Q9Y885 | MAIPLPAFYKWDVYDSKLNNVHGHVECRYTAQTGYWSDPCFVQSPFLSVHGLAPGLNYGQQVYEGIQARRTARNEILIFRPGASADRMAKSATAVSMPPVPYELFVRSVHMAVALNADYVPPHDFHGSMYIRPCQFGSSCQIGLQPPDEFIFCVFVQPHIALHGHGSLRALIAEDFDRAATRGTGHVKIGGNYAPVIRWTQSAKKEENGGWDVLLHVDSKTQTRIDEFSTSAFIGTKYAEEQNEPPQIILPESAAAIQSITSDSVAWLAKSFGWNIVKQPVTIDELASLSEVMAVGTAAGLVPVSCIRHNSTNRTFEFPSAGPMYRQLKETLDNIQRGRSSDSFGWCEKLRYAEFVQ | Function: Aminotransferase, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid . HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize . TOXF contributes to the synthesis of 2-amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 .
Sequence Mass (Da): 39618
Sequence Length: 357
Pathway: Mycotoxin biosynthesis; HC-toxin biosynthesis.
EC: 2.6.1.-
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Q9UW18 | MSNMVLNGNIDKSDRNSILDILQSLENIAWGQPGSARCDFRSDVITRPSLRMLSAVLKTTLGDDVFREDLTTAHFEAHVAEISGREEGMFVITGTMANQLCLHALVSTRPCGILLSSESHAIHYEAGGSSMLSGAMLQPVQPSNGKYLRVEDLEEHAILTDDVHKCPTSIVSMENTAGGAVVPVHELRRIRDWAKQNNVRTHLDGARLFEAVATGAGTLKEYCSLIDLVSVDFSKNLGAPMGAMILGDKKLIQQMRRTRKGIGGGMRQGGVITAAAREALFENFGLGAEIESQTLLQVHKVAKRLGEEWTRKGGKLSKEIETNIIWLDLDAVGIKKSQFIDKGREYGVILDGCRIVCHHQIDIYAVEALIDVFHDILKADPIKNKNSDR | Function: Alanine racemase, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid . HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize . TOXG catalyzes the conversion of L-alanine into D-alanine, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 .
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 42697
Sequence Length: 389
Pathway: Mycotoxin biosynthesis; HC-toxin biosynthesis.
EC: 5.1.1.1
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Q4WQZ7 | MERQPKSLCDATQLLETANIISDTVQTIIAEWSAEAKAPQGSGKQNAPMLPSRELFDAQRTILAAVGKLTELVSDPSARILEVATQFQESRSLYIAAERRIPDLLAAGDEGGVHIDQISQKAKIEPRKLARILRYLCSIGIFKQTGPDTFANNRISAALVSNEPLRAYVQLVNSEGFTASDRLPHTLLHPDTGPSYDVAKTAWQNAVCTKKTRWEWLEERVAPEQLLESGGHYPGIPSLVMGLPPREDDGLVARPELEIMGLSMVGGGRVFGTAHVYDFPWASLGDALVVDVGGGVGGFPLQLSKVYPQLRFIVQDRGPVVKQGLEKVWPRENPEALHQGRVQFVEHSFFDTNPTEGADIYFLRYVLHDWSDDYCVRILAAIRSSMAAHSRLLICDQVMNTTIGDPDLDSAPSPLPANYGYHTRFSHSRDITMMSCINGIERTPAEFKGLLQAAGLKLKKIWDCRSQVSLIEAVLPEMNGFR | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC . The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC . The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone . The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin . Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin . Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin . Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death . The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway .
Sequence Mass (Da): 53244
Sequence Length: 482
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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M2U578 | MEQLSYQSKLICSDESRHTGCFTTLPIRIHPRDDLADAASRRFVQDWAREMRDGREQSTHFSFSPVGNWSSLIYPEAIPERLGVLAYLSDLGLIHDDGGEGLSIEDAQAEHGELCAALDPSDISSAAPGSRAMKTKKLVSQCMLECISLDRELGLKMLAAFRDVWLAISERNSDKEAQTMEEYLKYRSDNGGMLVFWPMLQFSLGMSISEAEEALVQPIIDAATEGLLLANDYFSWEREYRELQSGQSKRIVSAVDLFIRTKGLSIDDAKEEVKRKIIAAERDFCQRRDDLYTNHPNIPLKLKRWIDCAGLAVSGNHYWCSACPRQNAWKDMSSQSLNGAKRKTSHGATIGMHEAPFKKRKDSSFFGSQPSDDEPSLSEVSSYPFYKPSGLALEAPSKYVSDMPSKGVRSTLIEALNTWLHVPSERLDSIMSVINTLHNASLILDDLEDNSPLRRGYPATHILFGHSQSINTANFMFVRAVQEVAQNLSPNALVALLEELKGLYLGQSWDLYWKHNLACPSEAEYVNMIDHKTGGMFRMLLRIMQAESDVTPQPDFHRLTLLFGRFFQIRDDYMNFQDYTAQKGLCEDLDEGKFSYPVVYCLENHPEYRGYFLSMFRQRPTIATVNACPLSGESKQYLTACLKKSGAFNKTIACLTDMERDLEFEINRLEQQTGETNPMLRLCLAKLSVKGIGRIGEVSPSTSK | Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of terpestacin . The bifunctional terpene synthase tpcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene preterpestacin I . The C-terminal prenyltransferase (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into preterpestacin I . The cytochrome P450 monooxygenase tpcB then hydroxylates preterpestacin I to yield 24-hydroxypreterpstacin I (renamed as preterpestacin II) whereas the cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin III) . Finally, the FAD-dependent monooxygenase tpcD converts preterpestacin III into terpestacin .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 79402
Sequence Length: 704
Domain: The conserved DDXXD motifs as well as the NSE/DTE motif are important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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Q4WQZ6 | MLALHQTQRDVPCSEVHDALGLQGARSIYFGRPTGRSILSDPIRPRPMPTVTVIIYSDIRFLLEFPSVFLCAYVLPVQRTVIMANEKRGGYRQINQALNICAWEGYLNEQHARLPTLEDVEQISPRVLRVLGQNEGKVRRADGYYTCSSRLIEGPQFTLQGTNTYIVGTGRHRLLIDTGQGIPEWASLISSTLAGSSIELSHVLLTHWHGDHTGGVPDLLRMYPDLSDSIYKHTPGKGQKPISDGQTFRVEGATVRAVHTPGHSHDHMCFILEEENAMFTGDNVLGHGSSAVEVLSTWMSSLRMMQSLRCAVGYPAHGAVIRDLPSKLDLELTQKARREDRVVETLKQMKTETQRNGARGKGSVTVQQLVTAMHGHDLDEQVRTMALEPFVDEVLRKLAQDDRVAFEVRGGQKKWFAIEYT | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC . The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC . The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone . The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodin anthrone to emodin . Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin . Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin . Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death . The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway .
Catalytic Activity: atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate + H(+) + holo-[ACP]
Sequence Mass (Da): 47062
Sequence Length: 421
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.2.-
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M2V0Z8 | MAVISLLQGLSVGQQIGTAAAISVFVLTSIVVYGCYLHPLSHVPGPFLAKFSPIWGMRALYRMKFNSELQALHEKYGPVVRVAPNEVSFATLEAETAIYANQEDGRFSKAGTFLTLFSDLVLNAPTLITIPDPALHKRLHKVIQQAFTPQALASQEPIQKLHIEKAIPDFDETADKGYHIDLADKLETMFWEIIGDLAFGEPLMAGKRPTYEKLKQLGKGSMPMVEALSFMLVMPGVAPTLEMARSFLSAMPMSSQLSKLVPSTKLRDCVERKDGREDFLSAIMGSEKQGLTLDADAFFSNAMGLTLAGYQTTATTLASTFYHVLRYTDAYKTLCTEIRSAFNDEAEITGERLARLPFLNACIRETLRLLPPANGKTAQRTAPSCTIADTYIPAGTIVSADLYTIQRSPKYFVDPARFHPERWLEDAEKNGFNGDNRSASRPFLIGSRACIGRHMAQQSIRLIMATLLWRYDFELLDPDGFIWERDAGSSLIYTDYKLPVHVKRFQ | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of terpestacin . The bifunctional terpene synthase tpcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene preterpestacin I . The C-terminal prenyltransferase (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into preterpestacin I . The cytochrome P450 monooxygenase tpcB then hydroxylates preterpestacin I to yield 24-hydroxypreterpstacin I (renamed as preterpestacin II) whereas the cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin III) . Finally, the FAD-dependent monooxygenase tpcD converts preterpestacin III into terpestacin .
Sequence Mass (Da): 56314
Sequence Length: 506
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.-.-.-
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M2UJ60 | MAILSSALVTIDLPVTLVSLLVGSIFYFCYLTVYRLFLSPIAHFPGPKLAAWTYWYEFWYDVIAEPEYTFKIGRLHKIYGPVVRINPDEIHIADPDFYDTIYAGSGRKRDKWDWITRSFGVDESLIGTLKHDEHRVRRASLSPYFSKQSVRALQPLIDRNMAILLDRLREFAKSGSPLKLDDAYAALTNDIVEDYAFGRSDHRLEAPDFDPSFRDAMLQGGKAGHVLKHFTWLMDLLKKLPDSLLLKLSPAMGAYSQLQTSVKRQVAEIQHAHQMHTYDKTRRTIFHEILNSKLSDYDKSTDRLWQEGEVVVAAGTITTAWALGVSTYFVLATPDILRKLKTELEAAIPDPSQPLNLITLEALPFLTGVVQEGVRLSHAISHRLHRICPDETLIYQDNDNQREWRIPPGTPLSMTSNLVHHDERVFPDSHAFKPERWLDNARLERYLVSFGKGGRACLGINLAYAELYLTLAALFRVYGTEQVKGKDDVGTLQLFETSAADLVITSDTVVPVMPEDSKGLRVKVS | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of terpestacin . The bifunctional terpene synthase tpcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene preterpestacin I . The C-terminal prenyltransferase (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into preterpestacin I . The cytochrome P450 monooxygenase tpcB then hydroxylates preterpestacin I to yield 24-hydroxypreterpstacin I (renamed as preterpestacin II) whereas the cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin III) . Finally, the FAD-dependent monooxygenase tpcD converts preterpestacin III into terpestacin .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59551
Sequence Length: 525
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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M2T7Z1 | MQLLGTLSWLYAIQASIGSSKAVTADYGSCHDACTLLSGTLSVELGGSHVSDYKHYPTIANGSSVASLFWAQQQQSAQPACLVHVYSPQDVATVISVSRSTNCPFAVRGGGHSDIPGASNINGGITVNMAALSNVELHESEGLARVGAGARWGDVYKELEKSNKTVVGGRLTGVGVGGLVLGGGLSHFSGLHGWACDNVRNYEVVLANGTLVIASNSSNPDLYRALRGGGNSFGVVTRFDLDVFQQGPMWGGLHVWPFQPSVTSAITRGFVEFAHNAPSDPHVSLFAGLGYKQGGFAWAVGQYDALGRVEPPIFTQFKDDVEVYGTAKIVSTARLTSLSDLADELNQSEPAGIRSRFTTATFTADAELLILIVEFFEEQVQKALDKGLDKDQRFAPMLGIQPLTQNLLRAQETRGGNVMGLRDLDAPLVVCSFGWEWSYESDDKVVIDGIKAVLDHSVSAAKEKGLYHPFKYMNYAALDQDPIESYGKENIEFLKRVRAMYDPEGVFTNLVPGGHKIN | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of terpestacin . The bifunctional terpene synthase tpcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene preterpestacin I . The C-terminal prenyltransferase (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into preterpestacin I . The cytochrome P450 monooxygenase tpcB then hydroxylates preterpestacin I to yield 24-hydroxypreterpstacin I (renamed as preterpestacin II) whereas the cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin III) . Finally, the FAD-dependent monooxygenase tpcD converts preterpestacin III into terpestacin .
Sequence Mass (Da): 55674
Sequence Length: 518
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.-.-.-
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Q4WQZ2 | MPDIQPITVYGKGGPNPPRVAIILAELDLPHKVIEVPLSKVKEPDYVAINPNGRIPAIYDPNTDLTLWESGAIVEYLVSHYDPDHRISFPAGSNLAALATQWLFFQASGQGPYYGQASWFKKFHHEKVPSAIERYVKEINRVTGVLEGHLSRQKVAADGDGPWLVGGKCSFADLAWIPWQVIVTAIIQPEDGYTVEDYPHVKNWLDRMMARPGVQKGMADIFPST | Function: Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC . The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC . The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone . The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin . Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin . Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin . Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death . The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway .
Sequence Mass (Da): 25031
Sequence Length: 225
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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Q4WQZ0 | MLEKVFHEKSFADQYTYGAKISELYAETLITESGIAKSHQRPLIILDNACGTGSISSTLQRTLDERNKRSLKLTCGDLSEGMVDYTKQRMQAEGWNNAEAKIVNAQDTGLPSDHYTHVYTAFAFNMFPDYKAALRECLRILQPGGTLATSTWKTANWCTIMKPVIATMPGQLSYPTMDEINTMLNKGWDRESDVRAEFEQAGFDHVNITTVEKQCLLPVQEFGEACKILLPYILSKFWTQEQRDQYEADVPSYLMRYLEREYGKDGLAPMKGVAIIASGRKP | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC . The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC . The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone . The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin . Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin . Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin . Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death . The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway .
Sequence Mass (Da): 31896
Sequence Length: 282
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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