ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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O14681 | MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTSAEKFPSPHPSPAKLKATAGH | Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38965
Sequence Length: 340
Subcellular Location: Nucleus membrane
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Q61070 | MADSVKTFLQDLGRGIKDSIWGICTISKLDARIQQKREEQRRRRASSLLAQRRPQSVERKQESEPRIVSRIFQCCAWNGGVFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRKPHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWPYYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSSSAEKFPSPHPSPAKLKAAAGH | Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38933
Sequence Length: 340
Subcellular Location: Nucleus membrane
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Q13347 | MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDNNEPYMKIPCNDSKITSAVWGPLGECIIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis . The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation . The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression .
PTM: Phosphorylated by TGF-beta type II receptor.
Sequence Mass (Da): 36502
Sequence Length: 325
Subcellular Location: Cytoplasm
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O24606 | MMFNEMGMCGNMDFFSSGSLGEVDFCPVPQAEPDSIVEDDYTDDEIDVDELERRMWRDKMRLKRLKEQDKGKEGVDAAKQRQSQEQARRKKMSRAQDGILKYMLKMMEVCKAQGFVYGIIPENGKPVTGASDNLREWWKDKVRFDRNGPAAITKYQAENNIPGIHEGNNPIGPTPHTLQELQDTTLGSLLSALMQHCDPPQRRFPLEKGVPPPWWPNGKEDWWPQLGLPKDQGPAPYKKPHDLKKAWKVGVLTAVIKHMFPDIAKIRKLVRQSKCLQDKMTAKESATWLAIINQEESLARELYPESCPPLSLSGGSCSLLMNDCSQYDVEGFEKESHYEVEELKPEKVMNSSNFGMVAKMHDFPVKEEVPAGNSEFMRKRKPNRDLNTIMDRTVFTCENLGCAHSEISRGFLDRNSRDNHQLACPHRDSRLPYGAAPSRFHVNEVKPVVGFPQPRPVNSVAQPIDLTGIVPEDGQKMISELMSMYDRNVQSNQTSMVMENQSVSLLQPTVHNHQEHLQFPGNMVEGSFFEDLNIPNRANNNNSSNNQTFFQGNNNNNNVFKFDTADHNNFEAAHNNNNNSSGNRFQLVFDSTPFDMASFDYRDDMSMPGVVGTMDGMQQKQQDVSIWF | Function: Transcription factor acting as a positive regulator in the ethylene response pathway, by promoting histone acetylation in an ENAP1-dependent manner, thus accelerating the expression of ethylene-responsive genes . Binds DNA . Is required for ethylene responsiveness in adult plant tissues. Binds a primary ethylene response element present in the ETHYLENE-RESPONSE-FACTOR1 promoter with consequence to activate the transcription of this gene.
PTM: Phosphorylated by KIN10.
Sequence Mass (Da): 71421
Sequence Length: 628
Subcellular Location: Nucleus
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Q9ZTP3 | MLRSLGLGLLLFALLALVSGDNDYVSCNCDDEGFLSVHTILECQRVSDLLIAIAYFSIPLELLYFISFSNVPFKWVLVQFIAFIVLCGMTHLLNAWTYYGPHSFQLMLWLTIFKFLTALVSCATAITLLTLIPLLLKWKVRELYLKQNVLELNEEVGLMKRQKEMSVQVRMLTREIRKSLDKHMILRTTLVELSKILDLQNSAVWMPNENRTEMHLTHELRANPMRSFRVIPINDPDVVQVRETKVVTILRKNSVLAVESSGCGGSEEFGPVAAIRMPMLHGLNFKGGTPEFVDTPYAIMVLVLPSANSRVWTDKEIEIAEVVADQVAVAISHASVLEESQLMREKLGIQNRALLRAKQNAMMASQARNTCQKVMSHGMRRPMHTILGLLSMFQSESMSLDQKIIVDALMKTSTVLSALINDVIDISPKDNGKSALEVKRFQLHSLIREAACVAKCLSVYKGYGFEMDVQTRLPNLVVGDEKRTFQLVMYMLGYILDMTDGGKTVTFRVICEGTGTSQDKSKRETGMWKSHMSDDSLGVKFEVEINEIQNPPLDGSAMAMRHIPNRRYHSNGIKEGLSLGMCRKLAQMMQGNIWISPKSHGQTQSMQLVLRFQTRPSIRRSILAGNAPELQHPNSNSILRGLRITLADDDDVNRTVTKRLLEKLGCEVTAVSSGFECLNALSNVEMSYRVVILDLQMPEMDGFEVAMKIRKFCGHHWPLIIALTASTEDHVRERCLQMGMNGMIQKPVLLHVMASELRRALQTASE | Cofactor: Binds 1 copper ion per dimer.
Function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
PTM: Autophosphorylated predominantly on Ser residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86250
Sequence Length: 766
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.11.-
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Q6FKB4 | MSLISTVDDHTQDTASVASGSSATKKKYNPKVYHDDNQPLSKEAMYRAKLKYGVYNSPISGGVGVGVTDYKAATNKAANVANDNQTTVEAYRRLYVDQGAASAALKVGTEPVREKPDVHAEKFKQNRALNLNYTSAAAKALSVGTEKLFTASEEARHAGQKTYSIVSQVSAASTSRAMDMSKVLKGAERKAESRLKERSEPERKEYVKSYSMTAGAAADYGAAGGAAGAAGAAGAASRSIDLNSDVMARVAKRSELPPKQEGPTEKERNAAKFALGAATAVKDLDPKSMLPEDFAAREQQRQEFVRHMTSQKVLSMAREKVDREMASIDKQQAERRLYDNDSYNRAAVAIAQQNYQNKLNAQSEKAGKINIGGGLFLTPQEVDNIAHGLISPVLGEVSERAEAQRAADTEIATRIATYEKDLSNWKNLQRTKQTNDKNVLEVNSKRIALEKQEAKDAAQKKYDEMIKKMDETVAEKKKQLEAAKQRLEDLQEEMNMKLGMQDQKVEEELQKWDENREKDIEAARLEQEELVKPFQDELDEAEKQHEEFLKERDGIDTEITGLQEAIEGHKKKIEIYEGDIRAHDNMHVEEGGKLENLGQNKETLANTLNNDIIILANKTKEQAELSTKQARLKQLEVDAMVNERKSELNQTEIQLKKEKLQLLESMRNKAQARGDEKIDEEKVKGLFGMTSEEYLAKHAPKKEEPAEEKLETVAEEASAMKKEKPTAAAATTAAAAAATTPKKPASAPRAAPAAASPKSEKKRKGSVFDKFFLGPRKAHMIEETRTNQKVAEEKAKMDSVSKPHLVSTTNEHAKPHAAATEEAPKKVDAPKPATEVKSSEAAEDEENKLEHTFSGFSQGSVADDKGTTSGAHSETKKDGYFKEVF | Function: Required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97546
Sequence Length: 885
Subcellular Location: Cytoplasmic granule
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Q6CTI0 | MSLVSAVTGDESRDTNGAEQSSVYQSAGKPLSKEALYRAKLKYGVFQSPAQSLKAGVVNGKDASDTAANLATSNKTTIEAYKRLLNPNASKAANAVITPKKTDQSRPASAVVSSAASSAAIAAPKAARSRTSSTASTTVTYVNSSSSSPLHSKTPKMDITKVLAGAERNAAESVHQRTNPEKVSYVRGITDRSVGKAADASFSLTSDIVSNLPTKKEYIQSAEKESHAAEWAQKAVAALKDFNPDDVTDKNWREREEERKRLIKNLTSETVLTKAKLNAQQRLDTIDRETSQRAIFRNAEYNRAAASVAQENLRKTRSSASATANKVNLGGGLWLAPDDIDNIAKGLIAPVLDEVDQRTGAQRAMDIDIQKRSVDYQQQYEEWVNIQTEKQNNDSLLQAKAFENHQKETADIEATLAKKFQNLCTQKDSEVAKLKEALEAKKAELAKLKEDNEEELKREDEMITTECADLQKSNENELEQAKKDQEELLVPFKNDLAAAEDHHTELQDQKGKIEENIQELRDSIEKHKSHVEELNAQIETQQQQLETETEALNLQSESHQQLKDGIETNYVIMAEKAKEEAKVSSEEARVKQLEVDAIINERQTELSNTEIEVKREKLKLIDAMKEVAEVKNEDKIDEEKAKAFLGTTSGEFLASQKKVEPATKLQSDPKLSEPSSKSTKIEGVTGNVKADVPASPPAHKKHSIGGLTSPLKSKKKSDKDQKGSSIKKFFGLKPSDQNKNTKTTQPTPLKSSPKPSNKPVTATVTTEKKENVEPKSTATETKPSLEPSFSGFSQGSVHNKVEQSDASEVEGGKEEPTSKDNRKSLFKEVF | Function: Required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91232
Sequence Length: 830
Subcellular Location: Cytoplasmic granule
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C5DGV3 | MSLISAAADVNDASSTTSAGSVRSSAVYRKDGKPLSQEALYRAQQKYGVFQSPARQTGSGLKDSKMASDVAANLANNNRTTIEAYKRVLDSNASRAATAVSSRSRSSSVTSNATVVTTSSKSTNAAVKALSSKPVEQPVAPKKSNMNMSKILVGAEAAAEKRIGIRMKPEKIVYVPSKESGKAAERSMSLTPEIMDKLKTKGDYEAEAEVEADPKKYASKAAFAVRDFDPNEATEKELLEREKKKQAYFGMLTSPQVLSLARANAQVKLDQIDKAAPGSLYKNEEFNKLAVALAQKNSTKRSEHHGKINMGGGLWLTQADVQNIAQGLITPVLDEVDSRALQQRAIDEDIKQRKIDFKEQNAAWIELQRNKLSNDKMYSRETRMRHKRETEGLHARTERKFQDLCASKDSEVAEMEKALQNAKDSYAALQKQMEEDLEKERLRVEAEVAALKKEQEEDLKAARVEQEQELKPYVDDVKAAEAEHERLTAERDSLNKEIEELRASIESHKVRIEELDNEISDSAAKHEEEEGKREELTKHKEEFDQEVSEKFTVIAQAAKEKAQKSSEEARLKQLEVDAMINERQSELNSTELELKKEKLSLLEAMRNVTELKGEDKLDENRVKALIGMTSEEFIAENNKSVNVSDDKFEPFNEHTASTKSIKHEEGVLGEGGAKTNSDELPVKDSAEKSSEHLNSTAEKSIEPAKASSPYPAKPSMVDAVLPKDFKPEVKPKAKPAHKTPQQGAAAGGEPASAKSGVKRSPSLKQKFMGIIKGDTKSQSKPAAAATPVHPPATVKKAAPKKAAASSEADTPAKVSPAKDTAKTEIQKIAQGGPAPAPEPEHKTAPAVDNATTKSVSTLQKPTNSGIDKSEIHKIAQGGPAPTSGHSNHTRTSVYENGDNSDDEDELPDSSEAGENGIGADKKGSLFKEVF | Function: Required for normal formation of eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on plasma membrane and mark the site of endocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101460
Sequence Length: 930
Subcellular Location: Cytoplasmic granule
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Q93YN4 | MRPILLPDPPSLSTGVPDIFEQGGSHNVVRRAVVIGNGFPGSENQCIGLVRALGLSDNHLLYRVTRPKGGLNEWLHWLPVGFHKKLDFILRHIYLYSRLMLGSKQSKYISSVPSENGGNVGLASILEADVKGIVNLARQTYEKDGPLIVIACGRDTISIASSIRRLASENVFVVQIQHPRSHLNRFDMVITPRHDYYPLTLEAQEQVPRFMRSWITPREPPQDHVVLTTGALHQIDYASLRKAASAWHDEFAALPKPLVVVNIGWPRSNCRYGADLAKQLTDSLLNVLATCGSVRITLSYKTPAKVSRVIFKELGDNPKVYIWNGQEPNPYMGHLAWGDAFVVTADSVSLISEACSTGKPVYVVGADHCKWKIAEFQKSLRERGVVRSFTGFEDMSESWSYPPLNDTAEAATRIRRELAARGWSLRS | Function: Plant-specific factor involved in mitochondria fission. Is required for the correct localization of DRP3A from the cytosol to mitochondrial fission sites. Does not seem to be required for peroxisomal division.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47605
Sequence Length: 427
Subcellular Location: Mitochondrion outer membrane
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P32801 | MSPRQLIPTLIPEWAPLSQQSCIREDELDSPPITPTSQTSSFGSSFSQQKPTYSTIIGENIHTILDEIRPYVKKITVSDQDKKTINQYTLGVSAGSGQFGYVRKAYSSTLGKVVAVKIIPKKPWNAQQYSVNQVMRQIQLWKSKGKITTNMSGNEAMRLMNIEKCRWEIFAASRLRNNVHIVRLIECLDSPFSESIWIVTNWCSLGELQWKRDDDEDILPQWKKIVISNCSVSTFAKKILEDMTKGLEYLHSQGCIHRDIKPSNILLDEEEKVAKLSDFGSCIFTPQSLPFSDANFEDCFQRELNKIVGTPAFIAPELCHLGNSKRDFVTDGFKLDIWSLGVTLYCLLYNELPFFGENEFETYHKIIEVSLSSKINGNTLNDLVIKRLLEKDVTLRISIQDLVKVLSRDQPIDSRNHSQISSSSVNPVRNEGPVRRFFGRLLTKKGKKKTSGKGKDKVLVSATSKVTPSIHIDEEPDKECFSTTVLRSSPDSSDYCSSLGEEAIQVTDFLDTFCRSNESLPNLTVNNDKQNSDMKTDRSESSSHSSLKIPTPIKAMIRLKSSPKENGNRTHINCSQDKPSSPLMDRTVGKRTVNNSGARKLAHSSNILNFKAYINSEDSDIRETVEDVKTYLNFADNGQI | Function: Important role in G1 events required for bud emergence and septin organization. Coordinates cell growth and cell division at G2/M, essential for efficient cytokinesis and for regulation of SWE1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 72150
Sequence Length: 640
EC: 2.7.11.1
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Q9F2F9 | MRVLAVATPALGHLFPAVPLLWALRARGDEVLVVTGGDALRVAEAGLPVVDALPGETLTTLFGAYQETDPAFFVALRRSPMTTLRDLAPVLAYLAGRLLEPARRAAERWRPDAILATHGQAAGAVVAAEHGIPLVEHGFGFVRSDGAQEAVRQLLAERLGPAGSEPPPERYFLDIAVPSMTSAIEGMSLRAVPYNGGAVLPLSGASVGGRPPRPRVLVTAGTQLLHTHGAGALAWLPEVAAGHEAEFLLAAGGADLRDLGRLPPHVRVLDWTPLATVLPTCSAVVHHGGSGTTLAALAAGVPQLVSPALADNHINARAVADRGAGLETAVPDATTLTALLREPAFAKAAREVADELRSLPAPADVAARLHTAFGLPTTQGDA | Function: Glycosyltransferase that transfers an L-rhamnose moiety from dTDP-L-rhamnose to the elloramycin aglycone 8-demethyl-tetracenomycin C (8DMTC) in elloramycin biosynthesis, an antitumor polyketide. Possesses donor substrate flexibility: able to transfer at least 11 different sugars to 8DMTC, such as NDP-D-glucose, as well as NDP-L-digitoxose, including both L- and D-isomeric forms of some sugars.
Catalytic Activity: 8-demethyltetracenomycin C + dTDP-beta-L-rhamnose = 8-demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + dTDP + H(+)
Sequence Mass (Da): 39465
Sequence Length: 382
Pathway: Antibiotic biosynthesis.
EC: 2.4.1.331
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Q9AJU2 | MDSPQVARTLVDSAGGTAAHTREAIRQIGVPETAAFLADELAGRTETVTIRHAAEVQFVFDDRYAPDAADPVPWTFRVGPEGVTHRAGALPDPGAVVTQDLTELARSLYGPAADRSDATRTVWWRDHDDPRVYFDPPPVFPAVERLLAAADGRDVPGLAGLALRHGSDKWGIHTYTAAYEQHFAPFRDRAVTVVEIGVGGYDDPAAGGGSLRMWKRYFRRGLVYGVDIADKSRHREPRVHTVVADQSDPASLRDLADAIGPIDIVIDDGSHISAHVVTAFSTLFPRLNPGGLYVVEDLQTSYWPAFQGAYDDDTRTSVGFLKRLVDGLHHAEYPSRAGRPAQPTDRTVGSLHFHPNLAFVEKRANSGHGGISRLREAT | Function: O-methyltransferase involved in the biosynthesis of the permethylated L-rhamnose moiety of elloramycin, an antitumor polyketide. Mediates the methylation of the hydroxy groups at the 2'-position after the sugar moiety has been attached to the aglycon.
Catalytic Activity: 8-demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + S-adenosyl-L-methionine = 8-demethyl-8-(2-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41180
Sequence Length: 378
Pathway: Antibiotic biosynthesis.
EC: 2.1.1.305
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Q8L9Y2 | MDRSLNLLDLALGFDEQLAIPSPLNGKVILIEDCVETSGSFVLHQLMKRVLSSNSSDALIFLAFARPFSHYDRILRKLGCNLATHKSNNRLVFFDMLMVKCSDGDQMEDNVSAVAKLFREIQETVRKLQSVTSGNITVMVDDMSLLEIATTGSNSDHVLDFLHYCHTLSSESNCSLVILNHEDIYASMERPAFLLQMVCLADVVIKAEPLASGLANDVHGQLTVLNKGISNSGRGSSRNKLQNFQFRIKENGIDYFYPGCRS | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Involved in oxidative stress signaling. Prevents anthocyanins accumulation .
Sequence Mass (Da): 29125
Sequence Length: 262
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
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O74385 | MSSLHEHLRPIPEPFSLTLLLGTRETPVTFLFHYYLYHALKAKESTCFLTFSKTLDEHAISMRKWGMDIKTKKNFFFIDGFSMLFAPISKPSKVQAPETKNHIKSVFAPVIQCVEENDFEFENSTIIIEDIDILQSTHALDSTKIQQAILELRKCFSRVIVNVTLGAPLPQQKSLGSSIGHMATRCISCRPLTSGSARRITGFLRLSRMPNHFRSGICETPEDDDKELLYEVTEAGAKVYSKGQVTLQL | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs .
Sequence Mass (Da): 28173
Sequence Length: 249
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
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Q04868 | MGSVQRQDLVLFSDQSVLPAHFFQDSNSHNLFFITHQSCTQPLWMINALVETHVLGSPSSLNESSSSMLPSSTRSHAVLASFIHEQNYFTNSLNKLKIPSNNYNVLDFLSDFIVNNIHNKPRDKILSDVLAKFSAAIQNNPTDTIVIIEQPELLLSLVSGLTCSELNNKFITPLLRQCKVLIIVSNSDIFNIDEYDASVHSSNLQNFYKSSFIKSMINLNLNPLKTGFAKDVTGSLHVCRGGAPIATSNTSLHVVENEYLYLNEKESTKLFYR | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) . May also be involved in sensitivity to Pichia inositovora toxin .
Sequence Mass (Da): 30574
Sequence Length: 273
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
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A0A075FBG7 | MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTRIDDFFDHGGSREESYKILDLVQEWKEKPAEEYGSKEVEILFTAVYNTVNDLAEKAHIEQGRCVKPLLIKLWVEILTSFKKELDSWTEETALTLDEYLSSSWVSIGCRICILNSLQYLGIKLSEEMLSSQECTDLCRHVSSVDRLLNDVQTFKKERLENTINSVGLQLAAHKGERAMTEEDAMSKIKEMADYHRRKLMQIVYKEGTVFPRECKDVFLRVCRIGYYLYSSGDEFTSPQQMKEDMKSLVYQPVKIHPLEAINV | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-ene, from (+)-copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide .
Catalytic Activity: peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate
Sequence Mass (Da): 67098
Sequence Length: 580
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.189
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P28515 | MDYEGKPVEFTLGTSSGGASLAPTSSTTAASIAPFSYNTSATNYYNTTPSSYPMFLNYQYAGGTTVTTDMDAFSGMDMSMNNGVFGTQNNPSYFYPTTQLNTYGYDTLAAATTASGITVNNNQLNVNIVQGNGTIVPQPITQNIISTVSNVQSSVPINNSQPLTPTGLAGCSTSSGSSSASSSSANSTSTPKNTISKANRSSGGANNSQFSTEDRECVNCGVHNTPLWRRDGSGNYLCNACGLYFKMNHHARPLVKPKKRQQNAQKRTGIECVNCRTNTTTLWRRNGEGHPVCNACGLYFKLHKVERPITMKKDGIQTRNRKLSAKGSRRMKKENGGTPTSMGMPTTSSSISSGIELDQSGVWGMKNTQPMLMTPTAYAFPASNFYFNSIEDQLEYKTCPPMMVDFGGQMKNLNLN | Function: Transcriptional activator that binds to the consensus sequence 5'-[AT]GATA[AG]-3' and variations thereof . During embryonic development, required for specification of cell fate of major hypodermal (epidermal) cells at the blastomere stage . The requirement is true for all four lineages derived from ABarp, ABpra and C blastomeres . Required for seam cell maintenance in late embryogenesis, for proper formation of dauer larvae and locomotion . Regulates expression of bro-1, a regulator of seam cell proliferation, via a GATA-like binding motif . Probably represses expression of eff-1 to prevent fusion of seam cells with the hypodermal syncytium . Involved in regulating expression of elt-3, a probable downstream target in hypodermal development pathways, in dorsal and ventral hypodermal cells . During postembryonic development, has a role in sperm development . Specifically, binds the bipartite consensus sequence 5'-AGATCTx(8)GATAA-3' found in genes with sperm-specific expression . Furthermore, regulates timing of developmental steps, possibly in parallel with daf-12, by controlling the expression of the let-7 family of miRNAs which in turn determines the transcription of heterochronic genes such as lin-41 .
Sequence Mass (Da): 44823
Sequence Length: 416
Domain: Both zinc fingers are required for DNA binding in vitro.
Subcellular Location: Nucleus
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Q10655 | MDNNYNDNVNGWAEMEPSQPMGGLRLPTQNMDPPEQNNESQLSELPRMKIDNDYASPIERQSVITSGTNNYEPKVETVTSFFHTGIDYSNFGMLDQTTMQPFYPLYSGIPVNTLGTFSGYTNSIYDKPSLYDPSIPTINIPSTYPTVAPTYECVKCSQSCGAGMKAVNGGMMCVNCSTPKTTYSPPVAYSTSLGQPPILEIPSEQPTAKIAKQSSKKSSSSNRGSNGSASRRQGLVCSNCNGTNTTLWRRNAEGDPVCNACGLYFKLHHIPRPTSMKKEGALQTRKRKSKSGDSSTPSTSRARERKFERASSSTEKAQRSSNRRAGSAKADRELSTAAVAAATATYVSHADLYPVSSAAVTLPDQTYSNYYQWNTAATAGLMMVPNDQNYVYAATNYQTGLRPADNIQVHVMPVQDDETKAAARDLEAVDGDS | Function: Transcriptional activator that binds to the consensus sequence 5'-[AT]GATA[AG]-3' . Predominantly directs the transcription of intestinal genes such as ges-1, cpr-6, pho-1, ftn-1, vit-2 and lev-11, and itself . Required for gut-specific differentiation, specifically acting with the GATA region-binding transcription factor elt-7 to control normal gene expression and promote normal formation of the intestine . Regulates intestinal gene expression in response to hypoxia to promote longevity . Modulation of longevity may, in part, be the result of regulation of expression of daf-16 isoforms d and f in the intestine . Regulates tissue specific gene expression at basal levels and in response to bacterial infection in the intestine to control innate immunity . Plays a role in the induction of metal-responsive genes, activating gene expression from zinc-activated promoters and iron-dependent promoters and enhancers . May regulate the expression of genes that control sensitivity to oxidative stress, in a mab-3-dependent manner, and osmotic stress, in conjunction with the GATA region-binding transcription factor elt-3 . May play a role in sphingolipid signaling by regulating the expression of the sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate lyase . May act with the Notch signaling pathway to promote endodermal gene expression . Has a protective role in response to infection by Gram-negative bacteria such as S.enterica, E.coli, P.aeruginosa and B.pseudomallei, Gram-positive bacterium E.faecalis and fungal pathogen C.neoformans . An association with the 26S proteasome regulatory subunit rpt-6, in part, controls gene expression in response to infection by P.aeruginosa . Regulates gene expression during the recovery phase following a bacterial infection . May act with p38-activated transcription factors to control p38 gene induction in response to bacterial infection . Controls lysosome formation in the intestine by controlling lysosomal gene expression .
PTM: May be ubiquitinated in response to infection by B.pseudomallei.
Sequence Mass (Da): 47116
Sequence Length: 433
Subcellular Location: Nucleus
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A0QXD8 | MSNQVPEKMQAVVCHGPHDYRLEEVAVPQRKPGEALIRVEAVGICASDLKCYHGAAKFWGDENRPAWAETMVIPGHEFVGRVVELDDEAAQRWGIAVGDRVVSEQIVPCWECLFCKRGQYHMCQPHDLYGFKRRTPGAMASYMVYPAEALVHKVSPDIPAQHAAFAEPLSCSLHAVERAQITFEDTVVVAGCGPIGLGMIAGAKAKSPMRVIALDMAPDKLKLAEKCGADLTINIAEQDAEKIIKDLTGGYGADVYIEGTGHTSAVPQGLNLLRKLGRYVEYGVFGSDVTVDWSIISDDKELDVLGAHLGPYCWPAAIKMIESGALPMDEICTHQFPLTEFQKGLDLVASGKESVKVSLIPA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD-dependent reversible oxidation of erythritol and L-threitol. Involved in the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
Catalytic Activity: erythritol + NAD(+) = D-erythrulose + H(+) + NADH
Sequence Mass (Da): 39356
Sequence Length: 362
Pathway: Carbohydrate metabolism; erythritol degradation.
EC: 1.1.1.-
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P53073 | MSEQEPYEWAKHLLDTKYIEKYNIQNSNTLPSPPGFEGNSSKGNVTRKQQDATSQTTSLAQKNQITVLQVQKAWQIALQPAKSIPMNIFMSYMSGTSLQIIPIMTALMLLSGPIKAIFSTRSAFKPVLGNKATQSQVQTAMFMYIVFQGVLMYIGYRKLNSMGLIPNAKGDWLPWERIAHYNNGLQWFSD | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21460
Sequence Length: 190
Subcellular Location: Endoplasmic reticulum membrane
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Q32LC4 | MAPSLWKGLVGIGLFALAHAAFSAAQHYFPSSGIKWKRKCEFLQSSSFQDKIFRSMYYVYDRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGIVHIAGEFKDMDATSELKNKTFDTLRNHPSFYVYNHRGRVLFRPSDTTNSSNQDALSSNTSLKLRKLESLRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (By similarity). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. May be involved in Mg(2+) transport (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18950
Sequence Length: 165
Subcellular Location: Endoplasmic reticulum membrane
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Q86J02 | MKKGIAKIFCVIGISIFLHTVYSALQHRKYLRLTDQPFEGVPFDIVVECIISLFLFAWGIINSQFLIPIKASTHLAKKSFDSYDYRPNFTVFNHRGKYLNEILNK | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12199
Sequence Length: 105
Subcellular Location: Endoplasmic reticulum membrane
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Q8N4V1 | MAPSLWKGLVGIGLFALAHAAFSAAQHRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGIVHIAGEFKDMDATSELKNKTFDTLRNHPSFYVFNHRGRVLFRPSDTANSSNQDALSSNTSLKLRKLESLRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes . By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors . By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (By similarity). May be involved in Mg(2+) transport (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14686
Sequence Length: 131
Subcellular Location: Endoplasmic reticulum membrane
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Q8K273 | MAPSLWKGLVGVGLFALAHAAFSAAQHRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGIVHIAGEFKDMDATSELKNKTFDTLRNHPSFYVFNHRGRVLFRPSDATNSSNLDALSSNTSLKLRKFDSLRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (By similarity). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable). May be involved Mg(2+) transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14677
Sequence Length: 131
Subcellular Location: Endoplasmic reticulum membrane
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C6Y4A7 | MESSTINAKKISVLLTLFSIIGYTAYSAHESILEIRQDGKLPLDIKCEVILVTLLFTFTTVIIASPLRSIQLNKWSHQRSDLAFLNSRTNFLRIKELKEKIEKVKN | Function: The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12136
Sequence Length: 106
Subcellular Location: Endoplasmic reticulum membrane
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P40540 | MSFVSKLLYTVSALVLFHSGFSSYEFHHLLKLNSLNNAQGAISKLPKDIMYETYAGLILFVLAVFTSFEKLQYLPIESNDGKIISQGNYLKEIALNKATNVDNLIGSNPNGEIIFTPSFVDVHMKRKICREWASNTVKKEK | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15907
Sequence Length: 141
Subcellular Location: Endoplasmic reticulum membrane
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Q1ZXH4 | MLHPQQMQEQQQQQQEAQAASIIPEHYEMEYIQRNNKTVSFCQIPISILGGAIAGVIGFSGVYGFLFYFFIYITFCSLFTLKENKNLHLYFPNPRSIWFDSIGAGLMPYILFWTFLYNIIHIY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14433
Sequence Length: 123
Subcellular Location: Endoplasmic reticulum membrane
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Q9BV81 | MAAVVAKREGPPFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTGLYGFIFYLLASVLLSLLLILKAGRRWNKYFKSRRPLFTGGLIGGLFTYVLFWTFLYGMVHVY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes . By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors . By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12017
Sequence Length: 110
Subcellular Location: Endoplasmic reticulum membrane
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F4JZC2 | MSVAPPAPSPPPFDPTKPSTPISFPIKTLQDLKSRSYFDSFHYPFNRSSVPLRRNIGALSDRPRLLVCHDMKGGYVDDKWVQGCGNNAGYAIWDWYLMDVFVYFSHSLVTLPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKELLATKESAQMYAERLAELAAALGFDGWLINIENVIDEVQIPNLMVFVSHLTKVMHSSVPGGLVIWYDSVTIDGHLAWQDQLTENNKPFFDICDGIFMNYTWKENYPKASAEIAGDRKYDVYMGIDVFGRGTYGGGQWTANVALDLLKSSNVSAAIFAPGWVYETEQPPDFYTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGLGSHTSLGGRKLSEAPWYNISCQSLQPFLEFNEGRNSETIQVTVDGREASYNGGGNVSFRGKLKRNAHFTARLFKPQLQLSAAPISIFFSVKSDKRSELSILLHFSSPSQEKKSMLMVPNESINRFGDMFLPCLLTSKQTTSGWTVHETNLVLDGHTLTEISAFCSRPDDLTEETNTLEYFALLGHISIKSQQKAKVYPLASSWVIEAHHVKFVPGDSGSKTLSCKLEWRLKHPEEDSVFPKYNVYAENLSSSEYRPRKVMEEPRSEKVFLGTAHVDAYYVSEMVVGSDVKGVRFVVQTCGEDGSWQELDASPNLVVEVERVSSKLCCCGLI | Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the production of high-mannose type N-glycans during plant development and fruit maturation.
Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
Sequence Mass (Da): 76351
Sequence Length: 680
Subcellular Location: Cytoplasm
EC: 3.2.1.96
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Q9SRL4 | MPKSNDDDVAQSEAVPLLDLVKPSLPISFPIKALQDLKSRSYFDSFHFQFNRSTVPFRRNSDCLPNRPRVLVCHDMKGGYVDDKWVQGCENEAGFAIWHWYLMDIFVYFSHSLVTIPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKEMLATKESAQMYAERLAELATALGFDGWLINIENDIDEEQIPNMKEFVSHLKKVLHLSTPGALVIWYDSVTVRGNLQWQDQLTELNKPFFDLCDGIFMNYTWKESYPNLSAEVAGDRKFDVYMGIDVFGRGSFGGGQWTVNAALDLLKRNNVSAAIFAPGWVYETAQPPNFHTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGFGYHVSLEGRQLSDSPWYNISCQSLQPLLEFNEDNKDIIQVTVDQEGKNVFDFSEQHLNNYYEYDSAREASFNGGGNIVFRGKLKGDAYFTTRLFKPHLQLSSSPITISYSVKSDETSNLGILLSFSSPSLETKSILVAPEDPIRRFDDMSLQCLTTSVQTVSEWTVHEASLVMDGHTLTEISAFCYRPENSTKSAEFVALLGHISVKDHVQNQQNPEILLPASSWVIEAHNVELVPGNSSSKILRVKLEWRQKDLEDSAFTRYNVYAENVKSTDLRPRKVLEKPKSETVLLGIAHVPAYYVAELVVESDVKAVRFMVQACGEDASLGKLDEALNLLVDLEGLSVNHD | Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the production of high-mannose type N-glycans during plant development and fruit maturation.
Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
Sequence Mass (Da): 79325
Sequence Length: 701
Subcellular Location: Cytoplasm
EC: 3.2.1.96
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A1L251 | MIARKRKSNGSETTSGKIPKDDVSSESCLDQPADESVHEVVTFEPSTLPSVHYDPDTTEPISCSLKSLDELLSWKRNEASIFNVSSVPLASRYPPLESCPRRTLVSHDMMGGYLEDRFIQGAEVETPYAFYHWEYIDIFNYFSHQMVTIPPAVWTNAAHRHGVLSIGTFITEWTDGAKTCEAFLADEESYRAAADKLVQISHCNGFDGWLINIENELSETAVNNTGPFLRYLTDQMHERVPGSVVIWYDSVLKDGKLLWQNELNDNNRMFFDACDGFFTNYNWTEQSLEGMKSYAAAQGRFADIYVGVDVFARGKVIGGKYETNKALELIRKYDLSTAIFAPDWVYECHEKADFRQNQDKFWSLLSDFLYIHRPSSNLPFVSSFCQGFGKSLYWRGKVETERSWFNLHAQEIQPLYLSESFGNGGWLRTRGCSEDAWIGGSSLMLEGMIPSGLSDVCARIFSLHVPLAARTFVSFVFKPPVGVKVSLELKTIDGPLCTFDGTEEIASRSVFPEALAESNQLVEQFAQNCGQWASDGWATRCFLLKMIGCSLREVCIRVSRDGGDEDINFNCRIGEIMLLDADNLQAPLQSVEGICVNDVVWQTGVLKGDGHTLKVLLNATLRWQYPTRQVRHFRIHWRHLRGPDPRIPSGPLTLIGRSYSALYRVVELEVPAAPGLIELVVEPVSKEGFSVPEAQWGRQTLSYSQSPSGNPSH | Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol (By similarity).
Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
Sequence Mass (Da): 80255
Sequence Length: 713
Subcellular Location: Cytoplasm
EC: 3.2.1.96
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Q8NFI3 | MEAAAVTVTRSATRRRRRQLQGLAAPEAGTQEEQEDQEPRPRRRRPGRSIKDEEEETVFREVVSFSPDPLPVRYYDKDTTKPISFYLSSLEELLAWKPRLEDGFNVALEPLACRQPPLSSQRPRTLLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAFLAGDERSYQAVADRLVQITQFFRFDGWLINIENSLSLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQDELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQAGERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALFAPGWVYECLEKKDFFQNQDKFWGRLERYLPTHSICSLPFVTSFCLGMGARRVCYGQEEAVGPWYHLSAQEIQPLFGEHRLGGDGRGWVRTHCCLEDAWHGGSSLLVRGVIPPEVGNVAVRLFSLQAPVPPKIYLSMVYKLEGPTDVTVALELTTGDAGSCHIGGISVLNAETSSRHSLRPLRVPPTKLARWVGRCGRQLSGGWVQHCYEVSLRGCLLLDLLVCFSRPPGSREEESFTCRLGEIQVVDAASLLAPLPQVQAVTISHIRWQPSASEREGPPALLQLSCTLHWSFLLSQVRCFRIHCWGGMSDDSPGRELPRPEMPMFLGLAFATQYRIVDLLVEAAGPGQDRRMEFLVEPVPKEGFRVPQAEWGRAVLLYSAPA | Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol.
Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
Sequence Mass (Da): 83987
Sequence Length: 743
Subcellular Location: Cytoplasm
EC: 3.2.1.96
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Q8BX80 | METSSVLTRGAARQRSPAAPEKQARDQTERRPGRRRQGRRINEDQEEEAVFREVVSFTPDPLPARYYDKDTTRPISFYLSTLEELLAWTPLMEDGFNVALEPLVCRRPPLSSPRPRTLLCHDMMGGYLEDRFIQGSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGRLCEAFLAGDEPSFQAVADRLVQIAQFFRFDGWLINIENSLTPAAVRNTPLFLQYLTAQLHQQVPGGLVLWYDSVVQSGQLKWQDELNDQNRVFFDSCDGFFTNYNWREDHLQRMVAQAGERLADVYVGVDVFARSNVVGGRFDTDKSLELIRKHGFSAALFAPGWVYECLEKSDFFQNQDKFWSLLERFLPTHSICSLPFVTSFCLGLGTRRVCYGKEQAVGPWYHPSAQETQPLFGEHKLAGDSRGWVKTHCCLTDAWHGGSSLLLRGLIPPEVDSVAVRLFSLHIPVPPKVFLSMVYKFEGSTDVQVALELTTGDASSCHVGGMLVLNETGSRHSPRPLRVPPTRLARWASSCGQQLSGGWIQRCYEVNLRGCLLQDLLVSFSRPPGSREEESFICRLGEIQVVDASSLLAPLPRVQNVTISQIRWLPLITGSEGLPTRLLLSCTLHWSYLLLRARCFRIHCWKRTGSSSSVAESPETEKPTFLGLAFANQYRVVDLAVEAAGFGQDGRVEFLVEPVPREGFLVPQAEWGKAVLLFSVPQ | Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol (By similarity).
Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
Sequence Mass (Da): 82945
Sequence Length: 734
Subcellular Location: Cytoplasm
EC: 3.2.1.96
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Q8T4F7 | MAMKKLYAKTSFTSKKPSSAANSTPILAYHQQQHQQPGNGICEFQVVAPGHSGELMIRRSQSMHHKMSPPVGGLGSKSEYYSIEELQELDLLDYRHPMYHHYQQQELRQRYHEHEQLVLQLPKATSPKAGPIYEAPQRSQQQQDQMLYVPTAAQRDSSSSAAATSIASSSTLTSSPSPSSSSSLIFSTLRKCVSPSNPSVNPNQPSKTQPSKLGCSMSFSIRTTTATAATAAAANAATATLSTQQQQQQAQQQHKQHLYSNIHHYLIRQQQQKQHYTLQRRHNSVKDKFIGGITTIFAEQSIIGARASVMVYDDNQKKWVPSGSSSGLSKVQIYHHQQNNTFRVVGRKLQDHEVVINCSILKGLKYNQATATFHQWRDSKFVYGLNFSSQNDAENFARAMMHALEVLSGRVANNPGGPPTNGNGYEEDMGYRTMTSEDAAILRQNNSIGGHVTPSAQTPTSQTNQNNIPQSPPTPQGHHRTSSAPPAPQPQQQQQQQQAQQMGQPGSHYGPTGNGPTSNGLPQQVNSQIPPAPQQQPQQQQFQQQQQQQQYQQMVQAGYAPSQQYQQPHYVLSNSNPNLTVHQYPTQQAQQQPPQAPQPPLQNGGMYMVGHGHLPSSASANSVVYASQQQMLPQAHPQAPQAPTMPGPGYGGPPVPPPQQQAENPYGQVPMPPPMNPSQQQQPGQVPLNRMSSQGGPGGPPAPAPPPPPPSFGGAAGGGPPPPAPPQMFNGAPPPPAMGGGPPPAPPAPPAMGGGPPPAPGGPGAPPPPPPPPGLGGAPKKEDPQADLMGSLASQLQQIKLKKNKVTTSAPENSGSSTSSGGSGNYGTIGRSSNGMASMMDEMAKTLARRRAQAEKKDPDPEAEVKKRPWEKSNTLPHKLSGGAGSGSAGSGHEGANGNSGGAGSNTTNSGGESPRPMRKRFGSASEETILKVNGDGLSLALSNGDLDTLKAEIVREMRLEIQKVKNEIIDAIKSEFNRR | Function: Functions, together with Abl, trio and fra, in a complex signaling network that regulates axon guidance at the CNS midline. Required in part for robo-mediated repulsive axon guidance. May be involved in lamellipodial dynamics.
PTM: Tyrosine phosphorylated on multiple sites by Abl kinase. In vitro, phosphorylation on specific tyrosine residues inhibits interaction with Abl and Src SH3 domains.
Sequence Mass (Da): 104824
Sequence Length: 980
Domain: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
Subcellular Location: Cell projection
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Q0QLE9 | MSKTIIKNIGKIVSGDIKSPVLQADTIVVEDGLIAAIGGEELMKDAGDATIIDAAGSTVTPGLLDTHVHVSGGDYAPRQKTMDFISSALHGGVTTMISAGSPHFPGRPKDAAGTKALAITLSKSYYNARPAGVKVHGGAVILEKGLTEEDFIEMKKEGVWIVGEVGLGTIKNPEDAAPMVEWAHKHGFKVQMHTGGTSIPGSSTVTADDVIKTKPDVVSHINGGPTAISVQEVDRIMDETDFAMEIVQCGNPKIADYVARRAAEKGQLGRVIFGNDAPSGTGLIPLGILRNMCQIASMSDIDPEVAVCMATGNSTAVYGLNTGVIAPGKEADLIIMDTPLGSVAEDAMGAIAAGDIPGISVVLIDGEAVVTKSRNTPPAKRAAKIL | Cofactor: Binds 1 Fe cation per subunit.
Function: Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.
Catalytic Activity: 1,4,5,6-tetrahydro-6-oxonicotinate + 2 H2O = 2-formylglutarate + NH4(+)
Sequence Mass (Da): 39923
Sequence Length: 386
Pathway: Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 2/8.
EC: 3.5.2.18
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Q08299 | MLETDHSRNDNLDDKSTVCYSEKTDSNVEKSTTSGLRRIDAVNKVLSDYSSFTAFGVTFSSLKTALLVALFLQGYCTGLGGQISQSIQTYAANSFGKHSQVGSINTVKSIVASVVAVPYARISDRFGRIECWIFALVLYTIGEIISAATPTFSGLFAGIVIQQFGYSGFRLLATALTGDLSGLRDRTFAMNIFLIPVIINTWVSGNIVSSVAGNVAPYKWRWGYGIFCIIVPISTLILVLPYVYAQYISWRSGKLPPLKLKEKGQTLRQTLWKFADDINLIGVILFTAFLVLVLLPLTIAGGATSKWREGHIIAMIVVGGCLGFIFLIWELKFAKNPFIPRVYLGDPTIYVALLMEFVWRLGLQIELEYLVTVLMVAFGESTLSAQRIAQLYNFLQSCTNIVVGIMLHFYPHPKVFVVAGSLLGVIGMGLLYKYRVVYDGISGLIGAEIVVGIAGGMIRFPMWTLVHASTTHNEMATVTGLLMSVYQIGDAVGASIAGAIWTQRLAKELIQRLGSSLGMAIYKSPLNYLKKYPIGSEVRVQMIESYSKIQRLLIIVSISFAAFNAVLCFFLRGFTVNKKQSLSAEEREKEKLKIKQQSWLRRVIGY | Function: Involved in the transport of siderophore enterobactin and so has a role in iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66970
Sequence Length: 606
Subcellular Location: Endosome membrane
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O14682 | MSVSVHENRKSRASSGSINIYLFHKSSYADSVLTHLNLLRQQRLFTDVLLHAGNRTFPCHRAVLAACSRYFEAMFSGGLKESQDSEVNFDNSIHPEVLELLLDYAYSSRVIINEENAESLLEAGDMLEFQDIRDACAEFLEKNLHPTNCLGMLLLSDAHQCTKLYELSWRMCLSNFQTIRKNEDFLQLPQDMVVQLLSSEELETEDERLVYESAINWISYDLKKRYCYLPELLQTVRLALLPAIYLMENVAMEELITKQRKSKEIVEEAIRCKLKILQNDGVVTSLCARPRKTGHALFLLGGQTFMCDKLYLVDQKAKEIIPKADIPSPRKEFSACAIGCKVYITGGRGSENGVSKDVWVYDTLHEEWSKAAPMLVARFGHGSAELKHCLYVVGGHTAATGCLPASPSVSLKQVEHYDPTINKWTMVAPLREGVSNAAVVSAKLKLFAFGGTSVSHDKLPKVQCYDQCENRWTVPATCPQPWRYTAAAVLGNQIFIMGGDTEFSACSAYKFNSETYQWTKVGDVTAKRMSCHAVASGNKLYVVGGYFGIQRCKTLDCYDPTLDVWNSITTVPYSLIPTAFVSTWKHLPS | Function: Actin-binding protein involved in the regulation of neuronal process formation and in differentiation of neural crest cells. Down-regulates transcription factor NF2L2/NRF2 by decreasing the rate of protein synthesis and not via a ubiquitin-mediated proteasomal degradation mechanism.
PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination.
Sequence Mass (Da): 66130
Sequence Length: 589
Subcellular Location: Nucleus matrix
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A0A0F5HPP7 | MNKSQLYPDSPLTDQDFNQLDQTVIEAARRQLVGRRFIELYGPLGRGMQSVFNDIFMESHEAKMDFQGSFDTEVESSRRVNYTIPMLYKDFVLYWRDLEQSKALDIPIDFSVAANAARDVAFLEDQMIFHGSKEFDIPGLMNVKGRLTHLIGNWYESGNAFQDIVEARNKLLEMNHNGPYALVLSPELYSLLHRVHKDTNVLEIEHVRELITAGVFQSPVLKGKSGVIVNTGRNNLDLAISEDFETAYLGEEGMNHPFRVYETVVLRIKRPAAICTLIDPEE | Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous icosahedral shells 42-43 nm in diameter with an iron- and phosphorus-rich core (1Fe:1.1P) which can store over 23,000-35,000 iron atoms (with a calculated maximum of 83,000 Fe). There are 2 types of negatively charged open pores in the cryo-electron structure; a 3-fold pore where 3 hexamers meet with a minimal size of 7.2 Angstroms and a 5-fold pore where pentamers meet with a minimal size of 2.3 Angstroms. The 2-fold pore seen in other encapsulin nanocompartments is closed. Empty compartments can be generated in E.coli . Both types of pore have extra density in their centers in the structure . 2 different cargo proteins have been identified (IMEF and Fer); when both are expressed in E.coli with the shell protein only IMEF is detected within the nanocompartment. E.coli expressing all 3 genes stores the largest amount of iron and is protected from Fe/H2O2-induced oxidative stress . Part of the iron-mineralizing encapsulin-associated Firmicute (IMEF) system (Probable).
Sequence Mass (Da): 32204
Sequence Length: 282
Domain: Formed of E- and discontuous A- and P-loops. A-loops form the main pores while A- and E-loops are the most flexible parts. E- and P-loops of neighboring monomers arrange head-to-tail and form a chainmail topology.
Subcellular Location: Encapsulin nanocompartment
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Q1Q6L7 | MVMGILNTFKKVYAVTGFFALLAVFSLSQVGSSAFAACAKVDDCFSCHTTQELNAVHKNTPYQGQSCIVCHKAFAADDTCSDAKDGRFAKISSEININKEDWNKIQRAVHETTEKHLVGRKFLNIYGPLGTGAQSVPLDTYGLPSWASIDMLGEGNEAIHPLKREIAQIYLIYKDFWLFRRDIEFSKKCETPIDISAAIGAAVSVSRKEDDMVFNGLSEMGIPGLLTASGRNIMKLSDWSVIGNGFQDVVLAVEKLTSRGFNGPFALVVSPKLYAYLHRVYERTGQLEIQGVKELVNGGVYQSYVFNKDVALVIATGSLNMDLAVGSNYKVEYWGPQDLNHRFRVVGSSVLRIKCPQAICTLE | Cofactor: Binds 2 heme groups per molecule.
Function: Fusion of the shell and cargo protein of a type 1 encapsulin nanocompartment. Protein missing its signal peptide makes 33 nm particles in E.coli (called cEnc), protein missing its signal peptide and diheme domain (residues 1-86, called Enc) makes 29 nm particles. The cEnc nancompartment encloses c-type heme. The cargo protein NIR-HAO (AC P0DV45) is probably targeted to the nanocompartment by its association with the diheme domain in cEnc; removal of the diheme domain in Enc halves the amount of cargo.
Sequence Mass (Da): 40021
Sequence Length: 363
Subcellular Location: Encapsulin nanocompartment
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I6WZG6 | MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH | Function: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls . Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo . Probably involved in protection against oxidative damage from the host immune response (Probable) . A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity .
PTM: The initiator methionine is partially removed. When isolated from culture filtrate isoelectric focusing gives 3 bands, none of which are glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28830
Sequence Length: 265
Subcellular Location: Encapsulin nanocompartment
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Q1D6H4 | MPDFLGHAENPLREEEWARLNETVIQVARRSLVGRRILDIYGPLGAGVQTVPYDEFQGVSPGAVDIVGEQETAMVFTDARKFKTIPIIYKDFLLHWRDIEAARTHNMPLDVSAAAGAAALCAQQEDELIFYGDARLGYEGLMTANGRLTVPLGDWTSPGGGFQAIVEATRKLNEQGHFGPYAVVLSPRLYSQLHRIYEKTGVLEIETIRQLASDGVYQSNRLRGESGVVVSTGRENMDLAVSMDMVAAYLGASRMNHPFRVLEALLLRIKHPDAICTLEGAGATERR | Function: Shell component of a type 1, iron-storage encapsulin nanocompartment. Encapsulin nanocompartments are 32 nm in diameter with an iron- and phosphorus-rich core (4Fe:1P) about 24 nm in diameter. Upon expression in E.coli most particles are 32 nm, 20% are 18 nm. The core is filled with an average of 14 dense granules, 5-6 nm in diameter that are not evenly distributed. Each nanocompartment is estimated to hold 30,000-35,000 Fe atoms . The minor proteins EncB, EncC and EncD probably lie against the interior face of the nanocompartment (Probable).
Sequence Mass (Da): 31656
Sequence Length: 287
Domain: Has 3 domains; a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Subcellular Location: Encapsulin nanocompartment
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Q9S2N2 | MSTASSSSSLPRNPVGGHVPVAGGLHSVGLSYARELKAEAVQVFVANPRGWATPAGNPKQDEAFREACAAGSVPAYVHAPYLINFGSHTGATVERSVESLRHSLRRGRAIGALGVVVHTGSATGGRERPVALKQVREHMLPLLDELTHDDDPYLLLESTAGQGASLCSRTWDFGPYFEALDAHPKLGVCLDTCHIFAAGHDLTGPSGMHQTLDLLVDTVGEGRLRLIHANDSKDVAGAHKDRHENIGAGHIGEDPFRALMTHPATDGVPLVIETPGGKEGHAADVARLKKLRDG | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 31070
Sequence Length: 294
EC: 3.1.21.2
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A6QCI0 | MKFVGAHVSASGGVDNAPLNAMAIGAKAFAVFAKNQRQWVAKPLEEKTIEAFKKNLETAGILPKHVLPHDSYLINLGHPEEEKLEKSRAAFIDELERCNQLGLDKLNFHPGSHLVKIPKKDPEYHEKLMEAELHCLDVIAESMNLAIEATKGSDVKLVIENTAGQGTNLGYKFEHLAHLIEKVEDKSRVGVCLDTCHTFTAGYDLRTREAYDETMDAFERIVGFEYLMGMHINDSKPKLGSRVDRHASLGQGEIGWDAFCFIMNDPRMDDIPLILETIDESLWPEEIKALYALVKK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 33185
Sequence Length: 296
EC: 3.1.21.2
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Q67S99 | MKLGCHISISKGFPQAVENAHRLGCEAFQFFTKNPRGFKGKSADPEAAARGRALMAEYGLVAVAHAPYITNLSTPDPELQAISIASLKQDLENAEAYGAIGCVCHMGKHVGEGEAYGRARMVETLNRLLEAYTGSCPLLLENTAGMGSELGTHLEELMEVRSRVEQPERIAFCFDTCHAFAAGIYRPEDWEDFVAHARAIGYWGLLRAVHLNDSKFDHGSRKDRHANLGKGFLGEAGIATLLRSGAFEGLPVVLETPVKDEAEYGPEIAYARSLLQ | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 30064
Sequence Length: 276
EC: 3.1.21.2
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Q9HJS3 | MIDEAIRSISKKYTIGGHISVAGGLHNGPARAAVFGFPTFQFFSKNQMRWSSPPLKDDEAAAFKSEVRKYGIESTMIHASYLINLASADPDLYKRSMEAFHDEIDRSDKLGSTFLTVHPGSNPDRADGIRRVRDALSTIGDHAVIILIENTAGQGNVIGTRLDEVAKIIDTSDKKLGVCIDTCHAWASGYDLRDSLEKFIESLDYTIGLDRIFAFHLNDAKREMGSRIDRHELIGKGTIDGGLINLIRDDRLRAKPKIMETPFGEARFEDNLRYMSSKIGE | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 31278
Sequence Length: 281
EC: 3.1.21.2
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Q9WYJ7 | MIKIGAHMPISKGFDRVPQDTVNIGGNSFQIFPHNARSWSAKLPSDEAATKFKREMKKHGIDWENAFCHSGYLINLASPKDDIWQKSVELLKKEVEICRKLGIRYLNIHPGSHLGTGEEEGIDRIVRGLNEVLNNTEGVVILLENVSQKGGNIGYKLEQLKKIRDLVDQRDRVAITYDTCHGFDSGYDITKKEGVEALLNEIESLFGLERLKMIHLNDSKYPLGAAKDRHERIGSGFIGEEGFAVFFSFKEIQEVPWILETPGGNEEHAEDIKKVFEIIEKFGIEVD | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 32435
Sequence Length: 287
EC: 3.1.21.2
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O86954 | CHGFDSGYDITKKEGVESLLSEIENLFGLERLKMIHLNDSKYPLGAAKDRHERIGSGFIGEAGFAVFFSFKEVQRIPWILETPGGNEEHAEDIKKVFEIIEKYRIEVD | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 12331
Sequence Length: 108
EC: 3.1.21.2
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Q39131 | MARFTVLITAVVLAFLMAAPMPGVTAKKYTVGENKFWNPNINYTIWAQGKHFYLGDWLYFVFDRNQHNILEVNKTDYEGCIADHPIRNWTRGAGRDIVTLNQTKHYYLLDGKGGCYGGMKLSVKVEKLPPPPKSAPVKNIGSVSMVTGLAQFMIPVSLFAFPAMWDVISRMW | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19435
Sequence Length: 172
Subcellular Location: Cell membrane
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Q5Z9C8 | MARRDQLVSFLCFFLIVSAVAGGLCVSATVLPMRVGKQYVVGGRSGWRTPPPASVDLYAKWAAGIRFYVADSIEFVYKNDSVVKVDKFGYYHCNATAAAANDGSVLFLLDAPGFAYFSSADADHCKKGQRLMINVDSAPSPSPSPSPAPQEAATASAATSSSAATAAHALLLAAMAMMGLILGEW | Function: May act as a carbohydrate transporter . Required for male fertility and seed yield .
Location Topology: Lipid-anchor
Sequence Mass (Da): 19418
Sequence Length: 185
Subcellular Location: Cell membrane
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O82083 | MSPSCSSCVNVLLIMCLMLLSLSADAYKNYTVGESTGWFDIQERPSANYQKWADSKSFSLGDFLIFNTDSNHSVVQTYDFKTYKDCDYDNNENNDTTEWSAANPSATSPVPVSISVPLVKEGSNYFFSGNYDGEQCKFGQHFMINVTHGQGLPDSSSPDDAAAPGPSESSQSGDDEVAPDTIVPANFDHPKDIESADDDKEVHSKKSSSSTTKTSLFCFVFMGLFASF | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24904
Sequence Length: 228
Subcellular Location: Cell membrane
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A3BEP8 | MAGAVATVSVGLAWLGLMAAAASATQFRVGGGRGWSVPDANAEPYNSWAGRMRFQIGDQLLFVYPKEMDAVVVVDQGAYDACNTSSSVAGGGGGRYDDGNTVFTFDRSGPFFFISGNEANCRAGEKLVVVVMADRGGRHAPPPSPPAVPPPVAPVPMPSPASSPPSPAPAAATPSLAPSPVATTPSPSPSVSPMAPAPAPTTSTPSSPPAPAAMAPSPSTTPGGVAQPPPPPGTDGANATTPAAPAANDRSGAAAAAPVVAGVVVTSLGAYIGYAMLAI | Function: May act as a carbohydrate transporter . Promotes tolerance to salt stress in a redox-dependent manner .
Location Topology: Lipid-anchor
Sequence Mass (Da): 27350
Sequence Length: 279
Subcellular Location: Cell membrane
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A0A0P0WGX7 | MASPPPFDICGDLDDDPTPPAPTPLAAPTPNGLNDRLLRLTRTHQRGPSQNPNPNPNPNPKPPPPPPPQEPEPAKVKLAGRRRLCKLSTAGDESAGDDDSIRDILDDLTTRLDSLSVDRPTARPRPHVSPLPCALHADPDPSQSQLNDGTKPSSSFVDCDDDDDDAGGAYGGFGVKEEVTRKVFKASSSFGGRGNDDKMKAKGAYAFDTVSRKTTTESKASKFFGDYDDEDDIDQDAENGKENHADDVGWEKTEDFKMEPTGTGVTRKPYNLPGRIFNMLYPHQREGLRWLWVLHCRGTGGILGDDMGLGKTMQVSAFLAGLFHSRLIKRVLVVAPKTLLTHWTKELSVVSLKDKIRDYSGPNANARNYELKYAFKEGGILLTTYDIVRNNFKMIKGNFTNDFDDEEETLWNYVILDEGHIIKNPKTQRAQSLFEIPCAHRIVISGTPIQNNLKEMWALFYFCCPEVLGDKEQFKARYEHAIIQGNDKNATNRQKHIGSNVAKELRERIKPYFLRRMKNEVFLDSGTGEDKKLAKKNELIIWLKLTSCQRQLYEAFLNSELVHSSMQGSPLAAITILKKICDHPLLLTKKAAEGVLEGMDAMLNNQEMGMVEKMAMNLADMAHDDDDVELQVGQDVSCKLSFMMSLLQNLVSEGHNVLIFSQTRKMLNIIQEAIILEGYKFLRIDGTTKISERERIVKDFQEGPGAPIFLLTTQVGGLGLTLTKAARVIVVDPAWNPSTDNQSVDRAYRIGQMKDVIVYRLMTSGTIEEKIYKLQVFKGALFRTATEHKEQTRYFSKRDIQELFSLPEQGFDVSLTQKQLQEEHGQQLVMDDSLRKHIQFLEQQGIAGVSHHSLLFSKTAILPTLNDNDGLDSRRAMPMAKHYYKGASSDYVANGAAYAMKPKEFIARTYSPNSTSTESPEEIKAKINRLSQTLANTVLVAKLPDRGDKIRRQINELDEKLTVIESSPEPLERKGPTEVICLDDLSV | Function: DNA helicase that acts as an essential component of the spindle assembly checkpoint (By similarity). Plays an indispensable role in the development of seed endosperm . Is required to secure sister chromosome separation during endosperm syncytial mitosis, which involves extremely rapid free nuclear cycles .
Sequence Mass (Da): 110498
Sequence Length: 987
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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F4IVN9 | MMGKYLWALVYVTVMILIIVVEVESSLHRVGGGRYTWNSDVNFSDWANHQRFYSGDWLYFGFNRTRHNILQVNKSSYEQCVDNDYIFNITRGGRDVFQLLEPKPYYFICGRGYCLKGMKLAITVLPQPPPSAPTNFTSTTTPLIPPNAITAAILIFAFKALLL | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18612
Sequence Length: 163
Subcellular Location: Cell membrane
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F4K6R7 | MFLWLVIVLTISASVSSYEHKLNWVVPPANSSESFNDWASNKRFQVGDIIQFKYKKDSVMQVTKESYKQCNSSHPRFYSNTGKTRFMFDHSVPYYFISGTSGHCEKGQKMIVEVISRDHTTTSAAPPAAFAVLLCFFSLSLYFVA | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16502
Sequence Length: 145
Subcellular Location: Cell membrane
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Q38653 | MVKYTVENKIIAGLPKGKLKGANFVIAHETANSKSTIDNEVSYMTRNWKNAFVTHFVGGGGRVVQVANVNYVSWGAGQYANSYSYAQVELCRTSNATTFKKDYEVYCQLLVDLAKKAGIPITLDSGSKTSDKGIKSHKWVADKLGGTTHQDPYAYLSSWGISKAQFASDLAKVSGGGNTGTAPAKPSTPAPKPSTPSTNLDKLGLVDYMNAKKMDSSYSNRDKLAKQYGIANYSGTASQNTTLLSKIKGGAPKPSTPAPKPSTSTAKKIYFPPNKGNWSVYPTNKAPVKANAIGAINPTKFGGLTYTIQKDRGNGVYEIQTDQFGRVQVYGAPSTGAVIKK | Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 36477
Sequence Length: 341
Subcellular Location: Secreted
EC: 3.5.1.28
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Q9T1T5 | MHISEKGLVLIKRYEGLRLKAYQCRAGRWTLGYGHTHNLNIGDVITQEQAEAFLREDIAQVTALLNTQIKVPLTQNQYDAICSLVFNIGMTAFTTSTLLKKLNVGDYSGASAEFMKWSKAKVNGKRTPLPGLIKRRQAEKALFESA | Function: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 16330
Sequence Length: 146
Subcellular Location: Host cytoplasm
EC: 3.2.1.17
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P51728 | MSKKFGAMILCSAAAVAAAFFAQQKGLPTQQQNQVSPKAVSMIVNLEGCVRNPYKCPADVWTNGVGNTHNVDKTKILTIDEVATDLRRNIKEAENCINTYFNGEKMNQGQYDAMVSLAFNVGCGNIKTYYSKTQGKRVATTIYRAAQAENWILMCNRIEDFNKSGGRVLKGLQNRRAKEKALCLGE | Function: Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.
PTM: All the periplasmic cyteines of the inactive, membrane-associated endolysin are involved in disulfide bond (By similarity). In the active soluble form, disulfide bonds are isomerized and only the catalytic cysteine remains free (By similarity).
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 20553
Sequence Length: 186
Domain: The signal-anchor, which may also be an uncleaved signal sequence tethers the SAR-endolysin to the membrane until the latter is depolarized by the holin, resulting in the escape of SAR-endolysin from the membrane.
Subcellular Location: Host cell inner membrane
EC: 3.2.1.17
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Q7Y2C0 | MNKPLRGAALAAALAGLVALEGSETTAYRDIAGVPTICSGTTAGVKMGDKATPEQCYQMTIKDFQRFERIVLDAIKVPLNVNEQTALTFFCYNVGPVCTTSTAFKRFNQGRATEGCQALAMWNKVTINGQKVVSKGLVNRRNAEIKQCLEPSSQYSSLLW | Function: Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17386
Sequence Length: 160
Domain: The signal-anchor, which may also be an uncleaved signal sequence tethers the SAR-endolysin to the membrane until the latter is depolarized by the holin, resulting in the escape of SAR-endolysin from the membrane.
Subcellular Location: Host cell inner membrane
EC: 3.2.1.17
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Q16206 | MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPILPDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPATRERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALYLSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPSPPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHVRRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNISVWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDSLRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEAELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGIISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWKFCGFEGLKLT | Function: May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock.
PTM: Glycosylated.
Sequence Mass (Da): 70082
Sequence Length: 610
Subcellular Location: Cell membrane
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Q941I0 | MAAAPSESIPSVNKAWVYSEYGKTSDVLKFDPSVAVPEIKEDQVLIKVVAASLNPVDFKRALGYFKDTDSPLPTIPGYDVAGVVVKVGSQVTKFKVGDEVYGDLNETALVNPTRFGSLAEYTAAYERVLAHKPKNLSFIEAASLPLAIETAHEGLERAELSAGKSVLVLGGAGGVGTHIIQLAKHVFGASKVAATASTKKLDLLRTLGAADLAIDYTKENFEDLPEKFDVVYDAVGETDKAVKAVKEGGKVVTIVGPATPPAILFVLTSKGSVLEKLKPYLESGKVKPVLDPTSPYPFTKVVEAFGYLESSRATGKVVVYPIP | Function: Enone oxidoreductase involved in the biosynthesis of 4-hydroxy-2,5-dimethyl-3(2H)-furanone (HDMF or furaneol), the key flavor compound in strawberries. Can use both NADH and NADPH as the electron donor.
PTM: The N-terminus is blocked.
Catalytic Activity: 4-hydroxy-2,5-dimethyl-furan-3(2H)-one + NADP(+) = 4-hydroxy-5-methyl-2-methylenefuran-3(2H)-one + H(+) + NADPH
Sequence Mass (Da): 34296
Sequence Length: 323
EC: 1.3.1.105
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Q7M0V7 | MGAEVFHSLKKVLGEKGLASGVGDEGGFAPNLGSNIRRAGYTAVISHRVAKYNQLLR | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 6042
Sequence Length: 57
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
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B9EAH1 | MPIITDVYAREVLDSRGNPTIEVEVFTESGALGRALVPSGASTGEHEAVELRDGDKDRYMGKGVLKAVENVNEIIAPEIIEGDFSVLDQVSIDKMMIALDGTDNKGKLGANAILGVSIAVARAAADYLGVPLYKYLGGFNGTELPVPMMNIVNGGSHSDAPIAFQEFMVLPVGAPNFKEALRWGAEIFHNLAKILKGRNLSTAVGDEGGFAPTFEGTEDAVETILEAIKAAGLEPGKDVFLGFDCAASEFFENGVYDYAKFEGENGKKRTSSEQVDYLEELVDKYPIITIEDGMDENDWEGWKALTDRLGNKVQLVGDDLFVTNTKILERGINEGVGNSILIKVNQIGTLTETFEAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKFKGLNAFYNLNK | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 46999
Sequence Length: 434
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
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A4X3B7 | MATIEGIVAREILDSRGNPTVEVEVGLDDGTIARAAVPSGASTGAFEAVELRDGEKDRYLGKGVTQAVSNIEDKIVDELIGYEASEQRLIDQKMLDLDGTDNKSQLGANAILGVSLAVAKAAASAAELNLFRYLGGPNAHLLPVPMMNILNGGAHADSNVDIQEFMIAPIGAPTFREALRSGAEVYHALKSVLKKKDLATGLGDEGGFAPNLPTNAAALDLISEAVEKAGYRLGTDIVFALDVAATEFFENGTYTFEGVEKTAEEMSSYYTKLADAYPIVSIEDPLAEDDWSGWRTLTASVGDRIQIVGDDLFVTNPQRIARGIAENAANSVLVKVNQIGSLTETLDAVDLAHRAGFRCMMSHRSGETEDTTIADLAVATGCGQIKTGAPARSDRVAKYNQLLRIEEELADAARYAGSGAFPRYRSA | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45404
Sequence Length: 427
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
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P33675 | MTAIVSIHGRQVVDSRGNPTVEVDVTLEDGSFGRAAVPSGASTGVHEAVELRDGDKTRWGGKGVTKAVHAVNNEIANAIIGLEAEDQELIDQTMIKLDGTPNKGKFGANAILGVSLAVAKAAAEARGLPLYRYVGGTAAHVLPVPMMNIVNGGMHADNPIDFQEFMIAPVGASSINEAVRIGTEVFHTLKKELSAKGMNTNVGDEGGFAPSLDSASSALDFIVDSISKAGYKPGEDVFIALDAASSEFYNKDQNIYDLKGEGRKLTSAQLVDYYVELCGKYPIYSIEDGLAEDDFEGWKILTEKLGDKVQLVGDDLFVTNVKRLSDGIERGIANSLLVKFNQIGSLSETLAAVNMANDASYTAVMSHRSGETEDTTIADLAVATNCGQIKTGSLCRSERIAKYNQLMRIEEELGSVAKYAGRSVLRKAK | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45743
Sequence Length: 429
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
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Q8SWL3 | MKLLGFLIVGLSAISALKTKALHLTCEQELRPYSAVVDANCMAFALNGSNIHEAIKYLQAMNIKKAYVLYWNDHDLRGTPMVLYDNGALAPFDPYTNTAKYVLCVEACPCPGSKAASVGGFQAATSSEKIYVEGSARPAQCSEVCIEPVERRPHYKKIVVNPSPSNCIPCEPECYDSSSSSECNKKRCKTFPRICKEKCGSRRRGCPRKVEVLKSQKTYTFDIEKYRRRGEVVVRVCSKDSKEKFERFILSRNGEIRGNNNKNCILEPLPKCLRCPGQLHKLKKHIERKVCQEVCMYINAKCDIFVLVGDCDFYRVVVNDRRRYRNLHLKKVRGHKLRELIKHGLFGVEFGPLDLDR | Function: Spore wall protein involved in the adhesion to host cells surface glycoaminoglycans (GAGs). Microsporidian spore adherence is an integral part of activation and host cell invasion which requires the extrusion at the spore apex of a very long and coiled structure, the polar tube, through which the sporoplasm is pushed to enter into the potential host cell.
Sequence Mass (Da): 40584
Sequence Length: 357
Domain: Heparin-binding motifs (HBMs) are characterized by an XBBXBX or XBBBXXBX sequence, where X is any neutral amino acid and B is a positively charged basic amino acid, and are defined as the consensus sequence necessary for protein-heparin interactions. HBM1 motif is necessary for spore adherence to host cells.
Subcellular Location: Spore wall
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Q03415 | MDILIRPGDSLWYFSDLFKIPLQLLLDSNRNINPQLLQVGQRIQIPGYVTTSYTITQGDSLWQIAQNKNLPLNAILLVNPEIQPSRLHIGQTIQVPQRLTWRLVNGQQNYDYSMMMNDIKKLQTAYPFLQGTPIGNSVLAQPIPEILIGNGSKRIHYKASFHANEWITTPIIMTFLNDYLLALTNQTTIRGLSMGPLYNQTTLSLVPMVNPDGVNLVINGPPANEALKNKLIAWNHNSQNFSGWKANINGVDLNDQFPAKWELENARNPQTPGPRDYGGEAPLTQPEAIAMADLTRSRNFAWVLAFHTQGRVIYWGFENLEPPESQTMVEEFSRVSGYEPIQSANSYAGYKDWFIQDWRRPGFTVELGSGTNPLPISEFDTIYQEALGIFLAGLYL | Function: An endopeptidase which hydrolyzes the gamma-D-Glu-(L)meso-diaminopimelic acid bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. It is active on spore cortex peptidoglycan.
Catalytic Activity: Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted.
Sequence Mass (Da): 44724
Sequence Length: 396
Domain: LysM domains are thought to be involved in peptidoglycan binding.
EC: 3.4.19.11
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P85155 | AVVNGVNYVGETTAA | Function: Diaminopimelinoyl-alanine endopeptidase. Has antibacterial activity.
Sequence Mass (Da): 1465
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9NKX1 | MKSITKIFLILGLFAFLLVAFAPSSSVATVNLESDGYTEAEAKLIEEKGEKFTFQTEVNKLMNIIINSLYSKKEIFLRELISNASDALDKIRFLALTNADLLGEGEQSNLDIHIKIDKANNVLHITDRGVGMTKDELVRNLGTIAQSGTKEFIKKVSDSAESSNLIGQFGVGFYSLFLVADSVVVTSKSNDDDQYVWTSDSQSSYTIAKDPKGNTLGRGTRISLHIKDDSKEFLDQEVIKQLVKKYSQFINFPIYLYVSEEVEIPKEEQEDSKPITDDQVEETTTTTEEGEEETTTEEEGQTEEKKTKTVYKWEELNDSKPLWMKAAKDVTKEEYTEFFRSLSKTQDTPITYSHFKTEGDTEFRSILYIPENPPSNMFDLEAAGSGLKLFVRRVFITDNLKELVPNWLRFLVGVIDSDDLPLNVSREMLQQNKILDAIKKKVILVKFISMIKELSEDEDKTKYNEFFKKFGSSMKLGAIEDQANKKRLTKYLLFPSSKEELTTFAGYVERMKEGQDQIYFITGKSKDSVEASPLIEQAIKKGYEVLFLVDPIDEYLVPQLDKFDDKYKFTNLARSGVKFNEDKEEEDQRKQTAEEFKPLLSYLKKTLSDKLEKVVISKVLADSPSILVSNSWGVTANQERIMKAQAHQANAQPQFNSKKIMEINPSHPLIKKLLNRLNEFGEEDETTKVSAHVLYETSALTAGYSIDNPTNFADFIYKLMMINGDSLAQTNFETTKNENSGPSVSFGDDDENQQQDFQQPPQSTHDEL | Function: May play a role in late differentiation as well as in starvation response. When overexpressed, suppresses the ability to form normal fruiting bodies and impairs prespore differentiation as well as maturation into spores.
PTM: Phosphorylated.
Sequence Mass (Da): 87269
Sequence Length: 768
Subcellular Location: Endoplasmic reticulum
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Q8ZR35 | MNRQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFIGLMVGGVLADRYERKKVILLARGTCGIGFIGLCVNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVISPMLGGILLASGGVAWNYGLAAAGTFITLLPLLTLPRLPVPPQPRENPFIALLAAFRFLLASPLIGGIALLGGLVTMASAVRVLYPALAMSWQMSAAQIGLLYAAIPLGAAIGALTSGQLAHSVRPGLIMLVSTVGSFLAVGLFAIMPVWIAGVICLALFGWLSAISSLLQYTLLQTQTPENMLGRMNGLWTAQNVTGDAIGAALLGGLGAMMTPVASASVSGFGLVIIGLLLLLVLGELRRFRQTPPVSDAG | Function: Component of an export pathway for enterobactin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43089
Sequence Length: 414
Subcellular Location: Cell inner membrane
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Q99382 | MAGKAGRKQASSNAKIIQGLYKQVSLFLGMAIVRLFISRKVTIGQWIKLVALNVPMFVALYIIVLSGKPKYDGNRVVKQGIDLNDNTNLISYFFDLIYLSLFGNIGIIAFRTFKFWWCLLLCPIYAGYKLYGLKNMFMPGAQQTQADNRSKNANEGQSKSKRQMKRERRGETDSKIKYKYR | Function: Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs . Involved in vacuolar processing and morphology .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20742
Sequence Length: 181
Subcellular Location: Endoplasmic reticulum membrane
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Q12003 | MISIVLELFQNLCCCRGFSDATIRVNDKRYRIQRLLGEGGMSFVYLVQLSKNSLIIDNGIATPELYALKKIICPSVESISNGMREIENYKRFQSPYVIKSIDSQVMQEKDGSKTIYIVLPYYSLGSLQDSINRRLLEGTFVSEAECVRIMLGVTRGLLCLHDPASRQDNATSRVNVDAVSMTYSDETAMLLEDTPLEMDMLSSNSAGSIAYAHRDITPSNILFSSDGLPVIGDLGSCSQADITIENRHQLSELQEWVNDNCTLPYTPPELLNLKLNQVLSSKVDIWSLGCTFYTLMFGISPFEREEQIHGASLTYAINTGKYSFPRNSRFSEGLLSVIKKCIQVDPIQRPTTSQLLNLLQDLDT | Function: Serine/threonine-protein kinase involved in vacuolar processing and morphology.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40749
Sequence Length: 364
Subcellular Location: Vacuole membrane
EC: 2.7.11.1
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Q08651 | MLDPRILPYYDPAVERKIAVVTGGNTGIGWYTVLHLYLHGFVVYICGRNSHKISKAIQEILAEAKKRCHEDDDGSSPGAGPGPSIQRLGSLHYIHLDLTDLKCVERAALKILKLEDHIDVLVNNAGIMAVPLEMTKDGFEVQLQTNYISHFIFTMRLLPLLRHCRGRIISLSSIGHHLEFMYWKLSKTWDYKPNMLFTWFRYAMSKTALIQCTKMLAIKYPDVLCLSVHPGLVMNTNLFSYWTRLPIVGIFFWLLFQVVGFFFGVSNEQGSLASLKCALDPNLSVEKDNGKYFTTGGKESKSSYVSNNVDEAASTWIWTVHQLRDRGFDI | Function: Probable dehydrogenase required for replication of Brome mosaic virus. Involved in vacuolar processing and morphology.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37485
Sequence Length: 330
Subcellular Location: Lipid droplet
EC: 1.1.1.-
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P37690 | MTRAVKPRRFAIRPIIYASVLSAGVLLCAFSAHADERDQLKSIQADIAAKERAVRQKQQQRASLLAQLKKQEEAISEATRKLRETQNTLNQLNKQIDEMNASIAKLEQQKAAQERSLAAQLDAAFRQGEHTGIQLILSGEESQRGQRLQAYFGYLNQARQETIAQLKQTREEVAMQRAELEEKQSEQQTLLYEQRAQQAKLTQALNERKKTLAGLESSIQQGQQQLSELRANESRLRNSIARAEAAAKARAEREAREAQAVRDRQKEATRKGTTYKPTESEKSLMSRTGGLGAPRGQAFWPVRGPTLHRYGEQLQGELRWKGMVIGASEGTEVKAIADGRVILADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGSQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQPWLGR | Function: Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta-casein.
Sequence Mass (Da): 46595
Sequence Length: 419
Domain: The coiled-coil domain is necessary and sufficient for recruitment to the divisome. The LytM domain is required for proper septal peptidoglycan splitting.
Subcellular Location: Periplasm
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P03396 | MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLPNVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADRHNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEINETEPFSFTANCTGSNLGNVSGCCGEPITILPLGAWIDSTQGSFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDILKILANSSRTGIRRKRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKKHVNKIGVDSDPIGSWLRGIFGGIGEWAVHLLKGLLLGLVVILLLLVCLPCLLQFVSSSIRKMINSSINYHTEYRKMQGGAV | Function: The surface protein (SU) attaches the virus to the host cell entry receptor TVC . This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic potential. Fusion occurs at the host cell plasma membrane (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65316
Sequence Length: 601
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).
Subcellular Location: Virion membrane
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P0DTM5 | IPSRPVGGPCYLGKLTMLAPKHTDILKVLVNSSRTGIRRKRSTSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDQSESIQKKFQLMKEHVNKIGVDSDLIGSWLRGLFGGIGEWAVHLLKGLLLGLVVILLLVVCLPCLLQMLCGNRRKMINNSISYHTEYKKLQKACGQPESRIV | Function: The surface protein (SU) attaches the virus to the host cell entry receptor TVA . This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate to activate its fusogenic potential. Fusion occurs at the host cell plasma membrane (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26992
Sequence Length: 246
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).
Subcellular Location: Virion membrane
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P22380 | MSTGNVYQELIRRYLVVVKKLYEGKYEVSRSFSYTMFSLLVGIIGKQYVTVFYGVPVWKEAKTHLICATDNSSLWVTTNCIPSLPDYDEVEIPDIKENFTGLIRENQIVYQAWHAMGSMLDTILKPCVKINPYCVKMQCQETENVSATTAKPITTPTTTSTVASSTEIYLDVDKNNTEEKVERNHVCRYNITGLCRDSKEEIVTNFRGDDVKCENNTCYMNHCNESVNTEDCQKGLLIRCILGCVPPGYVMLRYNEKLNNNKLCSNISAVQCTQHLVATVSSFFGFNGTMHKEGELIPIDDKYRGPEEFHQRKFVYKVPGKYGLKIECHRKGNRSVVSTPSATGLLFYHGLEPGKNLKKGMCTFKGRWGLALWSLAKELNKLNDSIKVNQTCKNFTSTGEENKQNTDKQKEFAKCIKTLKIDNYTTSGDRAAEMMMMTCQGEMFFCNVTRIMRAWNDPNEKKWYPYASCQIRQIVDDWMQVGRKIYLPPTSGFNNHIRCTHRVTEMYFEMQKIDSNETKMQIKFLPPSETSNQFVAYGAHYKLVKIMPIGIAPTDVKRHTLPEHHKEKRGAVILGILGLLSLAGSAMGSVSVALTVQSQSLVTGIVEQQKQLLKLIEQQSELLKLTIWGVKNLQTRLTSLENYIKDQALLSQWGCSWAQVCHTSVEWTNTSITPNWTSETWKEWETRTDYLQQNITEMLKQAYDREQRNTYELQKLGDLTSWASWFDFTWWVQYLKWGVFLVLGIIGLRILLALWNTISRFRQGYRPVFSQDCQQNLYRKRPDNGEEESNSLELGEHNSENLKEESLNRSLIEDLTSFARE | Function: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 94410
Sequence Length: 821
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5) (By similarity).
Subcellular Location: Virion membrane
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P08810 | MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPINDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTLTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVTAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRVREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWRDLWETLRRGGRWILAIPRRIRQGLELTLL | Function: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 101252
Sequence Length: 881
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5) (By similarity).
Subcellular Location: Virion membrane
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P19503 | MGCLGNQLLIALLLLSASGIYCVQYVTVFYGIPAWRNATVPLFCATKNRDTWGTTQCLPDNGDYSELAINVTEAFDAWDNTVTEQAIEDVWNLFETSIKPCVKLTPLCITMRCNKSETDRWGLTGTPAPTTTQTTTTQASTTPTSPITAKVVNDSDPCIKINNCTGLEQEPMVSCKFNMTGLKRDKKREYNETWYSRDLVCEQNSNETDSKCYMNHCNTSVIQESCDKHYWDAIRFRYCAPPGYALLRCNDSNYSGFAPNCTKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRSNRTIISLNKYYNLTMRCRRPGNKTVLPVTIMSGLVFHSQPINERPKQAWCWFGGEWKKAIQEVKETLVKHPRYTGTNKTEQIKLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVENIQNGSRWTSQNQKERQRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIAEIDWINGNETNITMSAEVAELYRLELGDYKLVEITPIAFAPTSVKRYTTTGASRNKRGVFVLGFLGFLATAGSAMSAASVTLSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGAKNLQTRVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPRPNDTLTPNWNNMTWQEWEKQVNFLEANITQSLEEAQIQQEKNTYELQKLNSWDIFGNWFDLTSWIKYIQYGVLIVLGVIGLRIVIYVVQMLARLRQGYRPVFSSPPAYVQQIPIQTGQELPTKEGEEGDGGGRGGNRSWPWQIEYIHFLIRQLIRLLTWLFSSCRDWLLRNCQTLQPVLQSLSRTLQRAREVIRVQIAYLQYGWRYLQEAAQAWWKFVRETLASAWRDLWETLGRVGRGILAIPRRIRQGLELTLL | Function: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 102054
Sequence Length: 889
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5) (By similarity).
Subcellular Location: Virion membrane
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Q8AIH5 | MKNLIGITLILIITILGIGFSTYYTTVFYGVPVWKEAQPTLFCASDADITSRDKHNIWATHNCVPLDPNPYEVTLANVSIRFNMEENYMVQEMKEDILSLFQQSFKPCVKLTPFCIKMTCTMTNTTNKTLNSATTTLTPTVNLSSIPNYEVYNCSFNQTTEFRDKKKQIYSLFYREDIVKEDGNNNSYYLHNCNTSVITQECDKSTFEPIPIRYCAPAGFALLKCRDQNFTGKGQCSNVSVVHCTHGIYPMIATALHLNGSLEEEETKAYFVNTSVNTPLLVKFNVSINLTCERTGNNTRGQVQIGPGMTFYNIENVVGDTRKAYCSVNATTWYRNLDWAMAAINTTMRARNETVQQTFQWQRDGDPEVTSFWFNCQGEFFYCNLTNWTNTWTANRTNNTHGTLVAPCRLRQIVNHWGIVSKGVYLPPRRGTVKCHSNITGLIMTAEKDNNNSYTPQFSAVVEDYWKVELARYKVVEIQPLSVAPRPGKRPEIKANHTRSRRDVGIGLLFLGFLSAAGSTMGAASIALTAQARGLLSGIVQQQQNLLQAIEAQQHLLQLSVWGIKQLQARMLAVEKYIRDQQLLSLWGCANKLVCHSSVPWNLTWAEDSTKCNHSDAKYYDCIWNNLTWQEWDRLVENSTGTIYSLLEKAQTQQEKNKQELLELDKWSSLWDWFDITQWLWYIKIAIIIVAGLVGLRILMFIVNVVKQVRQGYTPLFSQIPTQAEQDPEQPGGIAGGGGGRDNIRWTPSPAGFFSIVWEDLRNLLIWIYQTFQNFIWILWISLQALKQGIISLAHSLVIVHRTIIVGVRQIIEWSSNTYASLRVLLIQAIDRLANFTGWWTDLIIEGVVYIARGIRNIPRRIRQGLELALN | Function: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99210
Sequence Length: 871
Domain: Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5) (By similarity).
Subcellular Location: Virion membrane
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Q86MP3 | MSKKEETIFFRIEKENRPESSKKEEDENSTEEMTTLNHASVTLDHSAFAIADKDGFKMYQLNPLHFRMYKDYVIKVGPVRLVKQDGNSRRIIYVSALAGGRFAQNNLMIFDVARNEEYFEITTPSRYGPITNIHVSPNRLVALNPNRMFVWTYPDDIKQIRSEDIRSNPKGISAMSYDPTTAACYLAYPGFKTGSVQIMHLNALTARESKSPIVIEAHLTDIAQVALNCQGTLVATGSTKGTVIRVFDARTKGPLYELRRGTVQAHLQCMAFSPCSSYLAVASDKGTLHMFGIRDAEPQKKKNVLERSRGSSSIVKIQLDRPVMAIGFGKIPETPKNLQSIIAICADATYWRHEFYKDNTGNFTSHFGSYDELIEVANDSSFFRTPVE | Function: Component of the epg-6/atg-2 complex, which is involved in the generation of autophagosomes from omegasomes and in the distribution of atg-9 and atg-13 during the autophagy-mediated degradation of protein aggregates . Binds to phosphatidylinositols on preautophagosomes, which are early autophagic structures, to promote autophagosome formation . In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P), but more weakly to phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) . Involved in autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes, which is essential for maintaining nucleotide homeostasis .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43678
Sequence Length: 388
Domain: The LRRG motif is required for recruitment to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular Location: Cytoplasm
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Q5EG71 | MAFGMLIYILLKAMGALSEEAALTASSLSTELWNSWTKNNTEAYYAEQPRLLKLMQTCLEEHHSYCINGLCAFHSELRKPICKCLAGYNGERCEHLTLNSYAHNSYERYIAVGIGIGILTSGILAIIYCYVRKRCRKLKSPYKVCMGETAL | Function: Promotes the growth of epithelial cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 17030
Sequence Length: 151
Subcellular Location: Membrane
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Q6UW88 | MALGVPISVYLLFNAMTALTEEAAVTVTPPITAQQGNWTVNKTEADNIEGPIALKFSHLCLEDHNSYCINGACAFHHELEKAICRCFTGYTGERCEHLTLTSYAVDSYEKYIAIGIGVGLLLSGFLVIFYCYIRKRCLKLKSPYNVCSGERRPL | Function: Promotes the growth of epithelial cells. May stimulate the phosphorylation of EGFR and mitogen-activated protein kinases.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 17091
Sequence Length: 154
Subcellular Location: Membrane
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P21709 | MERRWPLGLGLVLLLCAPLPPGARAKEVTLMDTSKAQGELGWLLDPPKDGWSEQQQILNGTPLYMYQDCPMQGRRDTDHWLRSNWIYRGEEASRVHVELQFTVRDCKSFPGGAGPLGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLVSGSVKLNVERCSLGRLTRRGLYLAFHNPGACVALVSVRVFYQRCPETLNGLAQFPDTLPGPAGLVEVAGTCLPHARASPRPSGAPRMHCSPDGEWLVPVGRCHCEPGYEEGGSGEACVACPSGSYRMDMDTPHCLTCPQQSTAESEGATICTCESGHYRAPGEGPQVACTGPPSAPRNLSFSASGTQLSLRWEPPADTGGRQDVRYSVRCSQCQGTAQDGGPCQPCGVGVHFSPGARGLTTPAVHVNGLEPYANYTFNVEAQNGVSGLGSSGHASTSVSISMGHAESLSGLSLRLVKKEPRQLELTWAGSRPRSPGANLTYELHVLNQDEERYQMVLEPRVLLTELQPDTTYIVRVRMLTPLGPGPFSPDHEFRTSPPVSRGLTGGEIVAVIFGLLLGAALLLGILVFRSRRAQRQRQQRQRDRATDVDREDKLWLKPYVDLQAYEDPAQGALDFTRELDPAWLMVDTVIGEGEFGEVYRGTLRLPSQDCKTVAIKTLKDTSPGGQWWNFLREATIMGQFSHPHILHLEGVVTKRKPIMIITEFMENGALDAFLREREDQLVPGQLVAMLQGIASGMNYLSNHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFQKLQAHLEQLLANPHSLRTIANFDPRMTLRLPSLSGSDGIPYRTVSEWLESIRMKRYILHFHSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Also plays a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.
PTM: Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 108127
Sequence Length: 976
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P29317 | MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.
PTM: Autophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration . Phosphorylated at Ser-897 by PKA; blocks cell retraction induced by EPHA2 kinase activity . Dephosphorylated by ACP1.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 108266
Sequence Length: 976
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P29318 | MDRRRLPLLLLCAALGSAGRLSARPGNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQESNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHLAKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNHSKEEEPPKMYCSTEGEWLVPIGKCLCNAGYEERGFACQACRPGFYKASAGNVKCAKCPPHSSTYEDASLNCRCEKNYFRSEKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGGSSKICEPCSDNVRFLPRQTGLTNTTVTVVDLLAHTNYTFEIDAVNGVSDLSTLSRQFAAVSITTNQAAPSPITVIRKDRTSRNSVSLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRAKSTNVTISGLKPDTTYVFQIRARTAARYGTSSRKFEFETSPDSFSISSENSQVVMIAISAAVAIILLTVVVYVLIGRFCGYKKSKHGTDEKRLHFGNGHLKLPGLRTYVDPHTYEDPNQAVHEFAKELDASNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKAGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDAWSYGIVLWEVMSYGERPYWEMSFQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPSSLKIITNAAARPSNLLLDQSNIDISAFRTAGDWLNGFRTGQCKGIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIVSSIKTLETHTKNSPVPV | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.
PTM: Autophosphorylates upon activation by EFNA5.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 109910
Sequence Length: 983
Subcellular Location: Cell membrane
EC: 2.7.10.1
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O13146 | MALFRIYSFLAPFHILVLCQALRNYPDNEVTLLDSMSAPGDLGWEAYPSEGWEEISVMDERNIPMRTYQVCNVMEANQNNWLRTGLIQREGAQRVYVEIKFTLRDCNSLPGVPGTCKETFNVYYHESNNAVAAPLRHIRESQYIKIDTIAADESFTQTDVGDRVMKLNTEVRDISGLSKRGLYLAFQDLGACIALVSVRVFYKRCPLAVLNLARFPDTVTGGDSALVEVRGTCVEDAEELEGPRMFCSADGGWLVPIGRCVCRPGFEEVDGHCQPCRSGFYKASAMDAYCVKCPPHSYSHQDKASECVCERGFYRAESDPRSMACTRPPSAPGNPISMVNETAVTLEWSPPRDSGGRGDVSYSVHCRKCSGETGASERCVPCGSGAHFNPRQFGLTHPRVLVTELQPHTNYTFSVEALNGVSDLSPSPRQLVSVNVTTSQTVSVILKERKGTDSVTLAWQGPEPVDGTVVEYEVTYYEKNQQDQNYTVLKTKSNSMTVDGLKPGTTYIFRVRARTDGGYGNYKGEIELETSHEDMLAVGDPNQQTILAISVAGGAVLLVLLVACFIVSGRRCGYIKAKQDPEEEKMQFQHGRVKLPETRTYIHPHTYEDPNQAVRDFAKEIEVSNIRIERVIGAGEFGEVCSGRLRLPSKREIQVAIKSLKAGYSEHQRRDFLSEASIMGQFDHPNIIRLEGVVTRCKPVMIVTEYMENGSLDTFLKKHDGQFTVIQLLGMLRGIAAGMQYLSEMNYVHRDLAARNILVNRNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVISYGERPYWEMSNQDVIKAVDEGYRLPAPMDCPVVLHQLMLDCWEKNRSDRPKFGQIVNTLDRLIRNPSSLKQLANSAVWEDPVTPEAAVNTVEDWLDLIKMGQYKEHFSSAGYVTLDSVLYVSSSELDKMGVELAGHQKKILSSIQCLQAHHGTQVQV | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially efna5. Upon activation by efna5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation probably through activation by efna1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).
PTM: Autophosphorylates upon activation by efna5.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 109655
Sequence Length: 981
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P29320 | MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.
PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 110131
Sequence Length: 983
Subcellular Location: Cell membrane
EC: 2.7.10.1
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O08680 | MDCHLSILILFGCCVLSCSRELSPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFLEHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCTCNAGYEERGFICQACRPGFYKALDGVAKCTKCPPHSSTQEDGSMNCRCENNYFRAEKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDITFNIICKKCGWNVRQCEPCSPNVRFLPRQLGLTNTTVTVTDLLAHTNYTFEIDAINGVSELSSPPRQFAAVSITTNQAAPSPVMTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTTYVFQIRARTAAGYGTNSRKFEFENSPDSFSISGENSHVVMIAISAAVAIIVLTVVTYVLVGRFCGYHKSKHSSDEKRLHFGNGHLRLPGLRTYVDPHTYEDPTQAVHEFAKELDATNIAIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPVRWTSPEATAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPLPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDIATFHTTGDWLNGMRTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV | Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).
PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 110228
Sequence Length: 984
Subcellular Location: Cell membrane
EC: 2.7.10.1
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C7LZP1 | MDPDDAPPIRRSGFVAVIGRTNVGKSSLVNALAGERATIVSRHPNTTRRSVRVISRVGDAELVLVDTPGIAAAHDELSARLRRWVDDEWDGADRALLVVDAERGVGARERELASRLKPSDVAVVARIDRVRRARTLAVLAELAQVPLAEYFVASVRTGEGIEELRSYLASSLPEGPALYEAGVALDLPRATYVAEVVREEFLHHLRDELPQALACQVESWSDDGVEVVVYVERPSQRAIVLGHEGRVLAAVRRQAQRRLRAYPPLTLRVKVQRDWRRSARMLDELGL | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31806
Sequence Length: 287
Subcellular Location: Cytoplasm
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B3ETC6 | MHTSPHQAGFVTIIGKPNVGKSTLMNRLVGERLSIITPKAQTTRHSICGIVSDTDFQIIFTDTPGILKPAYELQESMMHMLQHALVDTDVLLWLVDIKEKEVPPIVEKVLAQGRIPVLLLINKIDLIAGQEALESLVEYWKQKVNVAQIIPIAALQGFQIEQLLKHILVYLPAHPPFYPKDMLTDRPERFFVAEIIREQILYKYQQEIPYAVEVVIEEFKEEASLIRISAMIYVEKKSQKGILIGKQGESLKQVGIAARQALEKFLEKQVFLQQHVKVLPGWRSQNKLLQRFGYES | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33784
Sequence Length: 296
Subcellular Location: Cytoplasm
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O67800 | MKVGYVAIVGKPNVGKSTLLNNLLGTKVSIISPKAGTTRMRVLGVKNIPNEAQIIFLDTPGIYEPKKSDVLGHSMVEIAKQSLEEADVILFMIDATEGWRPRDEEIYQNFIKPLNKPVIVVINKIDKIGPAKNVLPLIDEIHKKHPELTEIVPISALKGANLDELVKTILKYLPEGEPLFPEDMITDLPLRLLAAEIVREKAMMLTREEVPTSIAVKINEIKPGDANPNMLVIKGEIIVDRENLKPIIIGKKGQRLKEIGKRARQELELILGRPVYLELWVKVVPDWRRRPEYVRLFGYAL | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). The GTPase is stimulated about 6-fold in the presence of a 12 nucleotide 16S rRNA C-terminal fragment. Mutations in the rRNA sequence obviate stimulation. RNA-binding depends on GTP-binding by the GTPase domain. May function as a checkpoint for assembly of the 30S ribosomal subunit.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33888
Sequence Length: 301
Subcellular Location: Cytoplasm
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P42182 | MTNESFKSGFVSIIGRPNVGKSTFLNRVIGQKIAIMSDKPQTTRNKVQGVLTTGTSQTIFIDTPGIHKPKHKLGDFMMKVAQNTLKEVDLILFMINAEEGYGKGDEFIIEKLQTMSTPVFLIVNKIDKIHPDQLLLLIDEYRKRYPFKEIVPISALEGNNIETLLAQIEAYLPEGPQFYPSDQVTDHPERFIISELIREKVLHLTREEIPHSIAVAIESIKGQDNGSVHVAATIVVERDSQKGIVIGKKGSLLKEVGKRARADIEALLGSRVYLELWVKVQKDWRNKMSQLRDFGFKEDEY | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Binds both GDP and GTP. Complements an E.coli era disruption mutant.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34074
Sequence Length: 301
Subcellular Location: Cytoplasm
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Q2KWX8 | MSSQAFRTGFVAIVGRPNVGKSTLTNALIGSKISIVSRKAQTTRHRIHGVLTREHEQFVFVDTPGFQTRHGGAMNRMMNRVVTQALADVDVVVHVVEAGKWSEGDAKLLPLLPKAERTILAISKIDALKSRDELFPFVAKIMAQHAYGAVVPVSATKNHQLDQLLEEIAQRLPEGEPMFEEDTLTDRSMRFIAAELVREKIFRLVGDELPYGCTVVIEQWEETDAHARIAACVVVERDSHRPILLGAGGQHMKRIATEARQDIAKLLDKPVHLEVYIKVRKGWSDREGALRDLGYE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33058
Sequence Length: 296
Subcellular Location: Cytoplasm
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O51604 | MKSGFAAILGRPSTGKSTLLNSICGHKISIISPIPQTTRNNIKGIFTDDRGQIIFIDTPGFHLSKKKFNIAMMKNIHSSIGEVELILYIIDIQDKPGEEENKMLEIIKNSKIKFLVILNKIDLKNTKIKEITQFLKEKGIEDSNIIKISAEKKINTEELKNKIYENFSEGPLYYPQEYYTDQEINFRISEIIREKAIENLKEELPYSLYVDIDTLENKKGSLFIRANIFVANESQKGIIVGKNGKEIKSIGERARKTIAKIFETKCNLFLQVKLKKNWNKEDKLIKRLIN | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33355
Sequence Length: 290
Subcellular Location: Cytoplasm
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Q9K0C7 | MDIETFLAGERAAGGYRCGFVAIVGRPNVGKSTLMNHLIGQKISITSKKAQTTRNRVTGIYTDDTAQFVFVDTPGFQTDHRNALNDRLNQNVTEALGGVDVVVFVVEAMRFTDADRVVLKQLPKHTPVILVVNKIDKDKAKDRYALEAFVAQVRAEFEFAAAEAVSAKHGLRIANLLELIKPYLPESVPMYPEDMVTDKSARFLAMEIVREKLFRYLGEELPYAMNVEVEQFEEEDGLNRIYIAVLVDKESQKAILIGKGGERLKKISTEARLDMEKLFDTKVFLKVWVKVKSGWADDIRFLRELGL | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34617
Sequence Length: 307
Subcellular Location: Cytoplasm
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Q82SJ6 | MNAPGYKTGYISIVGRPNVGKSTLLNHLIKQKISITSRKAQTTRHRIHGILTDAQSQFIFVDTPGFQTRHRSQLNQVMNRVVLQSMQDVDVVVFVVEAGRFGREDEQVLEQLPRNLPVVLVINKIDLLPDKLQLLPFMQKMADVFEFSAIVPVSALQNRQLSALIEAIRQHLPGNPFLFAEDEITDRSERFLAAELLREKVFRQIGEEVPYSVSVVIEQFTVEGNLRRIHACILVERENQKAIIIGKQGKKLKDMATQARKDMEMLFGSKVYLEVWVKVKSGWADDITALKSLGYE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33666
Sequence Length: 296
Subcellular Location: Cytoplasm
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Q9CPH8 | MNEIKTADNAKTYCGFIAIVGRPNVGKSTLLNKILGQKISITSRKAQTTRHRIVGIHTDGPYQAVYVDTPGLHIEEKRAINRLMNRAASSAIGDVDLIIFVVDGTHWNEDDEMVLNKLRAAKAPVVLAINKIDNIKNKEEMLPFITELTSKFDFAHVVPISAQGGKNIAELEKIVRESLHEGTHHFPEEYVTDRSQRFMASEIIREKLMRFTGDELPYSVTVEIEQFKLNERGTYEINGLILVEREGQKKMVIGNKGQKIKQIGIEARADMERLFDNKVHLELWVKVKSGWADDERALRSLGYMDE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34714
Sequence Length: 306
Subcellular Location: Cytoplasm
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A1APR8 | MKNNVNRFGYVSIVGRPNVGKSTLLNRIIGEKIAITSDKPQTTRNRIQGIHNIANGQIVFIDTPGIHACHSRLNKGMVDAALAALRGVDLLLLVVDAGGAIDDRLVRDVLGGTGTPVMLVLNKVDLLADKRVLLERMAAWSQLYPFREILPISAGSGEGVDGLIETVCGYLPEGQPLFPDDILTDLPERFIVAEMIREKIFRLTRDEIPYSTAVTVESFTERPNGVVAISAAICLERPNQKGIIIGKKGEMLKKIGSQARHDIERLLGTRVFLELFVKIEENWSERTSKLREFGYE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32742
Sequence Length: 296
Subcellular Location: Cytoplasm
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P14290 | MDVPFLDLQAAYLELRSDIDQACRRVLGSGWYLHGPENEAFEAEFAAYCENAHCVTVGSGCDALELSLLALGVGQGDEVIVPSHTFIATWLAVSRVGAVPVPVEPEGVSHTLDPALVEQAITPRTAAILPVHLYGHPADLDALRAIADRHGLALVEDVAQAVGARHRGHRVGAGSNAAAFSFYPGKNLGALGDGGAVVTTDPALAERIRLLRNYGSKQKYVHEVRGTNARLDELQAAVLRVKLRHLDDWNARRTTLAQHYQTELKDVPGITLPETHPWADSAWHLFVLRCENRDHLQRHLTDAGVQTLIHYPTPVHLSPAYADLGLPPGSFPVAESLAGEVLSLPIGPHLSREAADHVIATLKAGA | Function: Sensor protein that transfers the signal of environmental stimuli to the regulatory region of target genes to activate or repress transcription of erythromycin biosynthesis genes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39410
Sequence Length: 366
Subcellular Location: Cell membrane
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P38767 | MSKQFSHTTNDRRSSIIYSTSVGKAGLFTPADYIPQESEENLIEGEEQEGSEEEPSYTGNDDETEREGEYHSLLDANNSRTLQQEAWQQGYDSHDRKRLLDEERDLLIDNKLLSQHGNGGGDIESHGHGQAIGPDEEERPAEIANTWESAIESGQKISTTFKRETQVITMNALPLIFTFILQNSLSLASIFSVSHLGTKELGGVTLGSMTANITGLAAIQGLCTCLDTLCAQAYGAKNYHLVGVLVQRCAVITILAFLPMMYVWFVWSEKILALMIPERELCALAANYLRVTAFGVPGFILFECGKRFLQCQGIFHASTIVLFVCAPLNALMNYLLVWNDKIGIGYLGAPLSVVINYWLMTLGLLIYAMTTKHKERPLKCWNGIIPKEQAFKNWRKMINLAIPGVVMVEAEFLGFEVLTIFASHLGTDALGAQSIVATIASLAYQVPFSISVSTSTRVANFIGASLYDSCMITCRVSLLLSFVCSSMNMFVICRYKEQIASLFSTESAVVKMVVDTLPLLAFMQLFDAFNASTAGCLRGQGRQKNRWVHQPSRILLPRCAHGICVSIPVSSGCRRLMVGYN | Function: Probable transporter involved in ethionine resistance. Overproduction leads to accumulation of S-adenosylmethionine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64209
Sequence Length: 581
Subcellular Location: Membrane
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