ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6IVU5 | MGNCNGASKSNQPDSSRVTQPAAEFRRVAHSSLYGRYNCKCCWFADTNLITCNDHYLCLRCHQVMLRNSDLCNICWKPLPTTITVPVEPTAPPP | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
O73557 | MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
P18541 | MGQGKSREEKGTNSTNRAEILPDTTYLGPLSCKSCWQKFDSLVRCHDHYLCRHCLNLLLSVSDRCPLCKYPLPTRLKISTAPSSPPPYEE | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
P19326 | PDTTYLGPLNCKSCWQKFDSLVRCHDHYLCRHCLNLLLTSSDRCPLCKYPL | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
P19325 | MGQSKSKEEKGISGTSRAEILPDTTYLGPLNCKSCWQKFDSFSKCHDHYLCRHCLNLLLTSSDRCPLCKYPL | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
B0BLK7 | MGSKSSKSSGFENVPSLGLSHTNQPRVSLIREARPSLYGRYNCKCCWFQNKNLVECSDHYLCLKCISSMLRRGQNCEICGKPIPTHIAVTTAPTAPPEP | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
Q88470 | MGNCNRTQKPSSSSNNLEKPPQAAEFRRTAEPSLYGRYNCKCCWFADKNLITCSDHYLCLRCHQIMLRNSELCNICWKPLPTSIRVPLEASAPDL | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
A9JR22 | MGLRYSKEVRDRHGDKDPEGRIPITQTMPQTLYGRYNCKSCWFANKGLIKCSNHYICLRCLTSMLNRTDYCEICGEVLPKRLTFETTPTAPPYTP | Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction... |
Q60888 | MKNLSVVTQFILLGIPHTEGVETMLFVLFFSFYIFTLVGNLLILLAIVSSSRLHTPMYFFLCQLSVCDIFFPSVSSPKMLFYLSGNTPAISYAGCVSQLFFYHFLGGTECFLYTVMAYDRFVAICYPLRYSVIMSHRICAFLAMGTAVFGCIHSTFLTTLTFQLPYCGPKDVNYYFCDIPVVMKLACADTSTLEMVGFISVGLMPLSCFFFILTSYSCIVRSILQIRSTEGRHRAFSTCSAHFTAILLFYMPVIFIYLRPTPSPWLDATVQILNNLVTPMLNPLIYSLRNKEVKSSLWTVLHLLCFLPKHL | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35274
Sequence Length: 311
Subcellular Location: Cell membrane
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Q8VBW9 | MPGQNYSTISEFILFGFSAFPHQMLPALFLLYLLMYLFTLLGNLVIMAAIWTEHRLHTPMYLFLCALSISEILFTVVITPRMLSDMLSTHRSITFIACANQLFFSFTFGYTHSFLLVVMGYDRYVAICRPLHYHALMSLQGCARLVAWSWAGGSLIGMALTIIIFHLTFCESNVIHHILCHVFSLLKLACGERTAFVTIAVILVCVTPLIGCLVFIILSYIFIVAAILRIPSTEGRHKTFSTCASHLTVVIVHYGFASIIYLKSRGLYSQYTDTLMSTTYTVFTPFLSPIIFSLRNKELKNAIIKSFHRNVCQQSI | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35748
Sequence Length: 316
Subcellular Location: Cell membrane
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Q60885 | MGDDNDTDITEFILLGFSGYGFLQGHLFWGVLCIYVVTLLGNSLIVLLTLADSALHSPMYFFLRHFSVVEILYTTTIVPRMLADLRSSCPTIPLASCFTQLYFFALFGIAECCLLTAMAYDRYAAICCPLHYTTLMSQGTYTGLVGASYLAGVISGTTHSIFIFTLPFRGAKTIHHFLCDILPVLRLATASTFWGEVGNLFVTITFIFVPFLLIVASYACILVTILGVATSQGRQKLFSTCSSHLFVVILFFGTATVAYMRPQADSFGNTDQILTLVYTVVTPMCNPFVYSLRNKEVTGAMRRLMKRYLWGP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34611
Sequence Length: 312
Subcellular Location: Cell membrane
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P0C9J6 | MYFYKKYLHFFFVVSKFKFFLKMQVPFGCNMKGLGVLLGLFSLILAQQLPDLPRTQHPPKRELKYWCTYVPQCDFCWDCQNGICKNKIMETQLIDSNHSIVNCRVSRNSETQTCFYEISSKMPNHFSMSCSHPTPYIGNEIFMKKVGGDYMTLLTLKQYCLYFIISIAFAGCFVYAVRKNLRLNTTIKLLTLLSILVYLAQPVLNRPLSIFYTKQFLPRTYTPPTRELDYWCTYAKHCDFCWECRKGICKNKVLDDMPPFIIQNDYINKCSIARYFDRCMYFIEPKIPYIHYMNCSLPTYYG | Function: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35742
Sequence Length: 302
Subcellular Location: Host membrane
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P0C9J2 | MKVFLGLLLGYSTILILTYQSPATQWCFYEISLKIPNHHSMECSYPRLYKHFMFMKKWRDKNWSIIIRYYCFYLVFSFAFAGCIAFAICKNLRLCTTMKLLMLLSILVLLSQPILNN | Function: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13899
Sequence Length: 117
Subcellular Location: Host membrane
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P0C9J9 | MKVFLGLLLGYSTILILTYQSPTTQHPPKEELEYWCTYAKTCDFCWDCQNDTCINKVINESISMNSIVNCRVTRDSQSQSCFYEISLKIPNYHSMECSYPRLYKHFMSMEKWRDENWPILIRHYCFYLVFSFAFAGCVAFAICKNLRLRTTMKLLMLLSILVLLSQPILNN | Function: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20151
Sequence Length: 171
Subcellular Location: Host membrane
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P0C9K0 | MGGGDYWPIIIRHCCFYLVFSIAFVGYIVFAYYKNLHLNTTMKLIALLCILIWLSQPGLNRPLSIFYMKQNLPRTYTPPIRELEYWCTYGKHCDFCWECRNGICKNKVWDDMPLIKQNDYISQCSIARYFDRCMYFIKPKTPYIHYMDCSQPTAYKGFSH | Function: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19115
Sequence Length: 160
Subcellular Location: Host membrane
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P61981 | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
PTM... |
P68253 | AAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEITAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGG | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
PTM... |
C0H4V6 | MATSEELKQLRCDCTYRSKLAEQAERYDEMADAMRTLVEQCVNNDKDELTVEERNLLSVAYKNAVGARRASWRIISSVEQKEMSKANVHNKNVAATYRKKVEEELNNICQDILNLLTKKLIPNTSESESKVFYYKMKGDYYRYISEFSCDEGKKEASNCAQEAYQKATDIAENELPSTHPIRLGLALNYSVFFYEILNQPHQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQGDQTEEKSKDEGLE | Function: Adapter protein which binds to its partners, usually via a phosphoserine or phosphothreonine motif . Binding generally results in the modulation of the activity and/or cellular localization of the binding partner (Probable). Via its interaction with CDPK1 and PKAr, involved in merozoite microneme secretion an... |
P31947 | MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPQEPQS | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Whe... |
Q91FI1 | MELKNMELKRKLTINEINFIVDFIQPRPYIPPDIENAIIFKKKKGIIDQLVTIEIYESLIPKLKEEIEKQYVNSLIDPGECVGIIGAQSMGEYSTQATLNTFHVAGVDTGSSTGVSRFQDLINASKTVKIDNISLFFKPLFVKKNITELRKLVASKLIEVKLSHLMITSVIVKTEEISQYRQEIESCIELYNDEHFNYEDYEFCLKITLSRELLLKHRLHPSVIKNKLEEYNNDCKYAFLPISSQQILFFIFIYVNTDECIEKIIQDLMDKKICGVDGIIRYDFKRKDLFDDEWYIETTGGSFSNINCLADIFDLTKTKT... | Function: Component of the DNA-dependent RNA polymerase that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Mass (Da): 53326
Sequence Length: 462... |
Q7NXD4 | MANIDLHFHSRTSDGALTPTEVIDRAAARAPALLALTDHDCTGGLAEAAAAAARRGIPFLNGVEVSVSWGRHTVHIVGLGIDPAEPALAAGLKSIREGRLERARQMGASLEAAGIAGCFDGAMRWCDNPEMISRTHFARHLVDSGAVKDMRTVFRKYLTPGKPGYVSHQWASLEDAVGWIVGAGGMAVIAHPGRYDMGRTLIERLILDFQAAGGQGIEVASGSHSLDDMHKFALHADRHGLYASSGSDFHAPGEGGRDVGHTEDLPPICRPIWRELEARILRPAD | Cofactor: Binds 3 Mn(2+) ions per subunit.
Function: Hydrolyzes 3',5'-bisphosphonucleosides (pGp, pCp, pUp, and pIp) to nucleoside 5'-phosphate and orthophosphate. Has similar catalytic efficiencies with all the bases. Also shows activity with ribonucleoside 2'-deoxyribonucleoside 3',5'-bisphosphates. Does not show act... |
P0C9P5 | MFPSLQSFAKKVLARQHVSIDHHIILERCGLWWYKAPISLDCKHMLIKLPNFADGLDLNTALMLATKENNYQLIKMFTDWGADINYGLICANTPPVREFCWELGAKYQVDKKKIMHIFFKLIHPSTTSSNIILCLKLFNDNPFSAYVIIREIKSCIHWKLKKLAEDTNVLSNISDGDMLTIYCFIVALQDNLREAISYVYQHFKYLNTWWLTCVLCYNKVFDLHHLYEKEKIRMDMDEMMRIACTKDNNFLTIYYCFILGANINLAMIASIQFYNIDNLFFCIDLGADAFEEAKALAEQRNYFLISHCLSLDIYSPDSSL... | Function: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 41533
Sequence Length: 356
Subcellular Location: Host membrane
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Q9MBC1 | VIETCRVGPPPDSVAEQSVPLTFFDMTWLHFHPMLQLLFYEFPCSKQHFSESIVPKLKQSLSKTLIHFFPLSCNLIYPSSPEKMPEFRYLSGDSVSFTIAESSDDFDDLVGNRPESPVRLYNFVPKLPPIVEESDRKLFQVFAVQVTLFPGRGVGIGIATHHTVSDAPSFLAFITAWSSMSKHIENEDEDEEFKSLPVFDRSVIKYPTKFDSIYWRNALKFPLQSRHPSLPTDRIRTTFVFTQSKIKKLKGWIQSRVPSLVHLSSFVAIAAYMWAGITKSFTADEDQDNEDAFFLIPVDLRPRLDPPVPENYFGNCLSYA... | Function: Catalyzes the transfer of the p-coumaric and caffeic acids from their CoA esters to the 3-glucosyl moiety of a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. Anthocyanins are ubiquitous colored pigments that are responsible for petal color. Does not act on delphinidin 3,... |
C8WJW0 | MYDDLKGKTVVVTGSSKGLGAAMARRFGAEGMNVVANYRSDEEGARETVRAIEEAGGAAAAVQADVSKNECVDALFDAAMFSFGGVDIWVNNAGIEVASPSDRKSIEEWQRVIDVNLTGVFAGCRRAIDHFLDRKMPGVIINLSSVHEIIPWPHFADYAASKAGVGMLTKTLALEYADRGIRVNAIAPGAMNTPINAEKFADPEARAATERLIPMGYVGAPEDVAAAAAWLASDQASYVTGTTLFVDGGMTLYPGFQFGQG | Function: Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the reduction of 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-cholan-24-oate (3-oxo-LCA) to yield isodeoxycholate... |
C8WGQ3 | MSEARHNPVLAGQTAVITGGASGIGKSIVQRFLEAGASCLAADLNEEALAALKQELAEYGDKLDVVKVDVSNRDDVEGMVDRAVQTFGQMDIIVNNAGIMDNLLPIAEMDDDVWERLMKVNLNSVMYGTRKAVRYFMERGEGGVIINTASLSGLCAGRGGCAYTASKFAVVGLTKNVAFMYADTGIRCNAICPGNTQTNIGVGMRQPSERGMAKATTGYAGATRSGTPEEISAAAAFLASDQAGFINGETLTIDGGWSAY | Function: Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the reduction of 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-cholan-24-oate (3-oxo-LCA) to yield isodeoxycholate... |
A7AZH2 | MNFGGFIMGRFDEKIMLVTGATSGIGRAVAIRAAKEGATVVAVGRNEERGAAVVAAMEEAGGKGEFMKCDVSNKDAVKALFAEIQEKYGKLDVAVNNAGIVGASKTVEELEDDDWFQVIDANLNSCFFCCREEVKLMQPSGGAIVNVSSVAGMRGFPSAAAYVASKHAVSGLTKAVAVDYATKGITCNAICPAGTDTPLTERSSADIKTRMAEIAAQGKDPMEWLKNSMLSGKTETLQKKNATPEEQAATILYFASDEARHITGSIVASDGGFTTY | Function: Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the reduction of 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-cholan-24-oate (3-oxo-LCA) to yield isodeoxycholate... |
P0DX23 | MKVLVTGATSGLGRNAVEYLRNKGISVRATGRNEAMGKLLSKMGAEFIPADLTELVSSQAKVMLAGIDTLWHCSSFTSPWGTQQAFDLANVRATRRLGEWSVAWGVRNFVHISSPSLYFDYHHHRDIQEDFRPHRFANEFARSKAASEEVINLLAQANPHTRFTILRPQSLFGPHDKVFIPRMVQMMRHYGSVLLPRGGNALVDMTYYENAVHAMWLASQPQCDHLPSARAWNISNGEPRTLRSIVQKLIDELGIKCRIRSVPYPMLDIIARSMEHFGNKSAKEPAFTHYGVSKLNFDFTLDISRAQQELGYQPIVTLDE... | Function: Catalyzes the degradation of estradiol into estrone . Can also degrade testosterone .
Catalytic Activity: 17beta-estradiol + NAD(+) = estrone + H(+) + NADH
Sequence Mass (Da): 38027
Sequence Length: 337
EC: 1.1.1.51
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P14060 | MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIV... | Function: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydrox... |
P22071 | MPGWSCLVTGAGGFVGQRIIRMLVQEKELQEVRALDKVFRPETKEEFSKLQTKAKVTMLEGDILDAQYLRRACQGISVVIHTAAVIDVSHVLPRQTILDVNLKGTQNILEACVEASVPAFIYCSTVDVAGPNSYKKIILNGHEEEHHESTWSDAYPYSKRMAEKAVLAANGSILKNGGTLHTCALRPMYIYGERSPFLSVMILAALKNKGILNVTGKFSIANPVYVGNVAWAHILAARGLRDPKKSQNVQGQFYYISDDTPHQSYDDLNCTLSKEWGLRLDSSWSLPLPLLYWLAFLLETVSFLLRPFYNYRPPFNCHLV... | Function: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, dehydroepiandrosterone (DHEA) to 4-androstene... |
Q84P26 | MANSQRSSSLIDPRNGFCTSNSTFYSKRKPLALPSKESLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRT... | Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Catalytic Activity: (E)-4-coumarate + ATP + CoA ... |
Q8GVF9 | METELHLAAGYCAATGVYRSGHPPQFAAAAALSFPEYILPHMLLPGRRARPAFVDASTGAALSFAGLRALSLRVARALAAAGLRRGRVALLLSPNSLHFPALSLAVLSLGAVLSAANPLLTPDELARQADDAKPFLALVTGELAPKLRSIAPDVKLVLVEQLLADVAAEVDDDETLDLPAANIGRDDAALLFYSSGTTGRSKGVVSTHGNAIAMAASLERAWGGGGGGGEKPQQYDDHDEAYGCVLPMFHMFGFSSFVMGTAALGATAVVVPGRFSVEKTMAAVEEYGVTRLLVVPPMVVKMVAAAAGDGEPSRRRLRLR... | Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Catalytic Activity: (E)-4-coumarate + ATP + CoA ... |
Q84P23 | MLTKTNDSRLIDRSSGFDQRTGIYHSLRPSLSLPPIDQPLSAAEFALSLLLKSSPPATAGKNIEALTYLVNSSSGDNLTYGELLRRVRSLAVSLRERFPSLASRNVAFILSPSSLDIPVLYLALMSIGVVVSPANPIGSESEVSHQVEVSEPVIAFATSQTVKKLQSSSLPLGTVLMDSTEFLSWLNRSDSSSVNPFQVQVNQSDPAAILFSSGTTGRVKGVLLTHRNLIASTAVSHQRTLQDPVNYDRVGLFSLPLFHVFGFMMMIRAISLGETLVLLGRFELEAMFKAVEKYKVTGMPVSPPLIVALVKSELTKKYDL... | Function: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors . Converts 12-oxo-phytodienoic acid (OPDA) into OPDA-CoA . Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification... |
Q7XXL2 | MGDAAVPAMVVEEEEQEHVFRSRFPPVAVPDGVTVPEFVLDGAEAYADRVALVEAAAGGRSYTYGEVARDTARFARALRSVGVRKGHVVVVALPNLAVYPVVSLGIMSAGAVFSGVNPRALAAEIKKQVEDSEAKLVVANEVAFDKVKDAGVPVIGVGDRERMPGAISWDGLLAAADRTGAGVVPVDAAQQSDLCALPYSSGTTGVSKGVMLSHRNLVSNLCSSMFAVAPETAGQVVTLGLMPFFHIYGITGICCATLRHKGTVVVMDRFDLRTFLRALVDHRVMFAPLVPPVMLAMVKSPVADEFDLSDLALKSVMTAA... | Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Catalytic Activity: (E)-4-coumarate + ATP + CoA ... |
Q9SMT7 | MDSDTLSGLLENVAKKFPDRRALSVSGKFNLTHARLHDLIERAASRLVSDAGIKPGDVVALTFPNTVEFVIMFLAVIRARATAAPLNAAYTAEEFEFYLSDSDSKLLLTSKEGNAPAQEAASKLKISHVTATLLDAGSDLVLSVADSDSVVDSATELVNHPDDGALFLHTSGTTSRPKGVPLTQLNLASSVKNIKAVYKLTESDSTVIVLPLFHVHGLLAGLLSSLGAGAAVTLPAAGRFSATTFWPDMKKYNATWYTAVPTIHQIILDRHASHPETEYPKLRFIRSCSASLAPVILSRLEEAFGAPVLEAYAMTEATHL... | Function: Oxalyl-CoA synthetase acting exclusively against oxalate . Follows a two-step reaction mechanism, wherein oxalate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield oxalyl-CoA (By similarity). No activity with malonate, succinate, malate, acetate, formate, lac... |
P41636 | MANGIKKVEHLYRSKLPDIEISDHLPLHSYCFERVAEFADRPCLIDGATDRTYCFSEVELISRKVAAGLAKLGLQQGQVVMLLLPNCIEFAFVFMGASVRGAIVTTANPFYKPGEIAKQAKAAGARIIVTLAAYVEKLADLQSHDVLVITIDDAPKEGCQHISVLTEADETQCPAVKIHPDDVVALPYSSGTTGLPKGVMLTHKGLVSSVAQQVDGENPNLYFHSDDVILCVLPLFHIYSLNSVLLCALRAGAATLIMQKFNLTTCLELIQKYKVTVAPIVPPIVLDITKSPIVSQYDVSSVRIIMSGAAPLGKELEDAL... | Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Catalytic Activity: (E)-4-coumarate + ATP + CoA ... |
Q13541 | MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI | Function: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interacti... |
Q13542 | MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI | Function: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation . Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contr... |
P70445 | MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI | Function: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation . Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contr... |
Q9XZ56 | MSASPTARQAITQALPMITRKVVISDPIQMPEVYSSTPGGTLYSTTPGGTKLIYERAFMKNLRGSPLSQTPPSNVPSCLLRGTPRTPFRKCVPVPTELIKQTKSLKIEDQEQFQLDL | Function: Repressor of translation initiation that regulates eIF4E1 activity by preventing its assembly into the eIF4F complex . Hypophosphorylated form competes with eIF4G1 and strongly binds to eIF4E1, leading to repress translation . In contrast, hyperphosphorylated form dissociates from eIF4E1, allowing interaction... |
Q8IH18 | MDTSKISARYSKVDLLALRYEGKSRQRPQCSTRLELQTLGFWKINLNTAALTVSSAYSNQNKNRLSPEADNSSLICSNSSSISSRRAMRNRERANNYYQRFVPTDSLLISGEDKDKDALSHGQPYKLNIIDHRSISSSHLMPAFAKRRFVISKGSNSEESNEGINTCASKGKAASSPSRKGSELDTAETCLNFVQPDHDQCMSSSPTFSTSRQERRIGSGRLLPRSDNWDYKNEKTVEASIENEKETSPNGSGSTSSLNQHNQSQHRSRTFSGRLVERVPEVTDRRFQYDSKKSFDRQGINNRRISGKEPFSTQSRSKRG... | Function: eIF4E1-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) (By similarity). Probably plays a role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation (By similarity). Acts as a binding platform for... |
Q9NRA8 | MDRRSMGETESGDAFLDLKKPPASKCPHRYTKEELLDIKELPHSKQRPSCLSEKYDSDGVWDPEKWHASLYPASGRSSPVESLKKELDTDRPSLVRRIVDPRERVKEDDLDVVLSPQRRSFGGGCHVTAAVSSRRSGSPLEKDSDGLRLLGGRRIGSGRIISARTFEKDHRLSDKDLRDLRDRDRERDFKDKRFRREFGDSKRVFGERRRNDSYTEEEPEWFSAGPTSQSETIELTGFDDKILEEDHKGRKRTRRRTASVKEGIVECNGGVAEEDEVEVILAQEPAADQEVPRDAVLPEQSPGDFDFNEFFNLDKVPCLA... | Function: EIF4E-binding protein that regulates translation and stability of mRNAs in processing bodies (P-bodies) . Plays a key role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation . Acts as a binding platform for multiple RNA-binding proteins: prom... |
Q5ZKF6 | MVPELQKSTVRIQQPERVMGVIRAIKEQGCSKLQVISDFDMTLSRFGCNGRRCPTSHNILDNSHVISEDGKKKLKDLLHHYYPIEIDPNRTLEEKRPLMVEWWTRAHELLSQQKIQKGDIAQIVRESDVMLRDGFNELFDQLHKYSVPMFIFSAGVGDVLEEIIRQANVFYPNVNVVSNYMDFDDSGVLKCFKSPLIHTYNKNNSVLQGTAYFQQLSTRTSIILLGDSMGDLTMADGVPSVENILKIGFLNDKVEEQRGRYLDAYDIVLESDETLDVVNGILRYILMET | Function: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor... |
Q9W197 | MGFDEKREPTGGRLRLQDIPALTQDHCRMRDPAEVERIINEFVIGGPERMQIVSDFDYTITKQRTEDGGAVPSSFGIFNACQSLPENFKAETDKLYHKYRPIEIDPHMPIAEKVQYMIEWWTKSGELTSGFPFDQSEIDQIASKYTHALRDRTHEFFADLQRLGIPTLVFSAGLGNSVVSVLRQANVLHPNVKVVSNFLQFRDGLLDGFQQPMIHTFNKNETVLNETSEYYDLVHTRDHIIVMGDSIGDADMASGVPASSHIMKIGFLFDHVEANMKKYMDTFDIVLVDDQTMDVPRTLLSLIEKQHKLNLEAPKQSSL | Function: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate . Also able to mediate hydrolysis of diphosphate (m(7)GDP) to 7-methylguanosine and 2 inorganic phosphate with lower activity . The specific activity for m(7)GMP may protect cells against undesired s... |
Q969T7 | MAEEVSTLMKATVLMRQPGRVQEIVGALRKGGGDRLQVISDFDMTLSRFAYNGKRCPSSYNILDNSKIISEECRKELTALLHHYYPIEIDPHRTVKEKLPHMVEWWTKAHNLLCQQKIQKFQIAQVVRESNAMLREGYKTFFNTLYHNNIPLFIFSAGIGDILEEIIRQMKVFHPNIHIVSNYMDFNEDGFLQGFKGQLIHTYNKNSSACENSGYFQQLEGKTNVILLGDSIGDLTMADGVPGVQNILKIGFLNDKVEERRERYMDSYDIVLEKDETLDVVNGLLQHILCQGVQLEMQGP | Function: Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate . The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids . Also has weak activity for CMP . UMP and purine nucleotides are p... |
Q09315 | MSNKVARRLGKCLFVSGRRFESRQSILQLRTETLTDTPLSATLDQSQFSMFKAAEIVNAAAACAEAECIEQLKKTDVVPLLMNYLLGEEQILVADPTAVAAKLRKMVVGGAGKTVVISDFDYTLSRFANEQGERLSTTHGVFDDNVMRLKPELGQKFVDLKNKYYPIEFSPNLTMEEKIPHMEKWWGTSHSLIVNEKFSKNTIEDFVRQSRIVFKDGAEDFIEALDAHNIPLVIFSAGIGNIIEYFLQQKLGAIPRNTHFISNMILFDEDDNACAFSEPLIHTFCKNSSVIQKETSFFHDIAGRVNVILLGDSMGDIHMD... | Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 42146
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q54XC1 | MAENNNNNNNNNNNNVSTPPHQKPHLTTGLRTSSSGLLMDKRRQDEEKFSAEQVAMGKKSPTKLFSAYSLNDLSNPPTDEELNNYKDLPASSLPPIHKREKLRRVFVNRDIKLDRIEFFGFDMDYTLAVYNSPDFEELAYDMVLDKLIDIGYPKSIRKLKYDPNFPTRGLFLDRELGNLLKIDSFGNIIICVHGRTTLSKNRTAEFYPSMRVSSDEIARNRFYLLNTLFTLPEACLYADLVDHLERESGLRLTEEVADEQQQMNSPPLSSLGSESVRIDESNHQPEGDLSFSNLFQDVRTACDLVHNDGSLKTRVLDDLP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acce... |
P49902 | MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates . In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acc... |
Q3V1L4 | MTTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acce... |
D3ZMY7 | MMTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLNFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates . In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acc... |
P29240 | MPRVPSASATGSSALLSLLCAFSLGRAAPFQLTILHTNDVHARVEETNQDSGKCFTQSFAGVARRWTKIEELRARDKNVLLLDAGDQYQGTIWFNYYKGAEAAHFIEAVGYNAMALGNHEFDNGAEGLLDPFLLNVSFPVLSANLEQGEDQVPSLIGYYKPSTVLDVNGEKIGVVGYTSKETPTLSSPGPHLIFKDEIQAVQHEVDILVSQGIDKIIALGHSGFETDKLIAQKVRGVDVVVGGHSNTFLYTGKAPSNDVPVGPYPFLVNSDDQRTIPVVQAYAYGKYLGYLKLTFDKGEVIKREGNPILLNSSIIQDPVL... | Function: Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 63613
Sequence Length: 577
Subcellular Location: Cell membrane
EC: 3.1.3.5
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P44569 | MLLSKKSASFALSAFAMLFTSVALAKEAPQAHKAVELSILHINDHHSYLEPHETRINLNGQQTKVDIGGFSAVNAKLNKLRKKYKNPLVLHAGDAITGTLYFTLFGGSADAAVMNAGNFHYFTLGNHEFDAGNEGLLKLLEPLKIPVLSANVIPDKNSILYNKWKPYDIFTVDGEKIAIIGLDTVNKTVNSSSPGKDVKFYDEIATAQIMANALKQQGINKIILLSHAGSEKNIEIAQKVNDIDVIVTGDSHYLYGNDELRSLKLPVIYEYPLEFKNPNGDPVFVMEGWAYSAVVGDLGVKFSPEGIASITRKIPHVLMS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Degrades NAD into adenosine and nicotinamide riboside, the latter being subsequently internalized by a specific permease. Also endowed with NAD(P) pyrophosphatase activity. Exhibits a broad substrate specificity, recognizing either mono- or dinucleotide nicotinamides... |
P21589 | MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGGVARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYKGAEVAHFMNALRYDAMALGNHEFDNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKETPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNVISSHGNPILLNSSIPEDPSI... | Function: Catalyzes the hydrolysis of nucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside, with AMP being the preferred substrate . Shows a preference for ribonucleotide monophosphates over their equivalent deoxyribose forms . Other substrates include IMP, UMP, GMP, CMP, dAMP, dCMP... |
Q676U5 | MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDA... | Function: Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP) . Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support eithe... |
Q9J552 | MGQHVSNITVIATPQAPETKYLRVEYTGGYDDEYIRFFEAENIHSGDIGSEISPPFCLTRDTTVKQCASFLSPEAKKKFVIVPGEPCKSLSFRPGSILDLQKIPYGTESYVLDGTRCRFINIDYLYTDPDIKRCCNKESDKDCPEIFSNNYETDHCDTIMSSICLQTPGSLPCREWLEKKREVAFDTYMKVCSDHLDANYCSDFVDYTRPDNFGYSDAAILSYCSKHRNNPNCWCVTTPKNDKLFSLELALGPKVCWLHECTDKSKDRKYLLFDQDVQRTNCKYIGCNINVDTLRLRNSVAELIAKCGGSIAEDTVLGDD... | Function: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation) (By similarity).
PTM: Most cysteines are linked by disulfide bonds. They are created by the viral disulfide bond f... |
D4AZY1 | MLVQGTIICALVANAIASSIPSSFLLPEPSGPFKVQREILELTDWSRKDINSTLPRRLMVSRFNPIPEKHCIRTEDVPTFPPASAKLEDAILQAASGGHWVDGLLAASRIRVCADVKKGYQTDSHGDNHGIPILLFSPGGNTTRLVYSSIAQTISSAGYTVITMDHPHDTDIVEFLNGDIITGGEVTFSNPSVLPFWNDVRVQDTVFVLNQALKTSPHARIGMLGHSFGGSAVLSSMVKDGRISAGINFDGGLWGDAVNTGLGGRKKPQPYLQWGAYTHNRHNDTSWETLWKAMERLHPHAWKKELGIPAGRHNTFSDFP... | Catalytic Activity: a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+)
Sequence Mass (Da): 42265
Sequence Length: 387
Subcellular Location: Secreted
EC: 3.1.1.47
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Q9J551 | MDNNYLNYYNVFEEFDAGAGIKEKELFTEEQQLSFLPKKGLGNGGFDGVERLYSNIINNNDIKSLLALIMLVFAINTNSLVALIFIILSAIFVPVPALIIAYCIALHLKNGSDATHVGISILLMLASAVTIYLTSTSKISKGFKRAIDVVLLVILGFYIVKIYGIDRQISIPSRRYCRQMSGPSSLENLNAFQTHSNY | Function: Envelope protein which participates in virus morphogenesis. Needed for an early step in viral crescent membrane formation by interacting with D13 scaffold protein. Its interaction with D13 scaffold protein leads to the formation of rigid, crescent-shaped membranes that assemble around the cytoplasmic virus fa... |
Q9J550 | MSYITVIDDKLYSSLRKLVGYSPLYLFNDKGDFVEVMKNSEFRFLIPSGYFSNSNVPLYGLTFSYGRNWMKDRQKIILPELYPIQRRVIEEIILQFSRKCKEKRPLYTTLHLACGFGKTVTASYLIGTHKKNAVVSVPNKLILKQWENSISSLKVSYYVSYEGVSKLLKVLTSKSFSILVVVDKHFSNKEFCELVYENYDVFILDEAHIYNLMNESIMTSFLCYYPPRICYFLTATPRQQNAVYCNSIINFIKFSPLQKILYVIRELYNEYTNPSIRAHVSQLQTTANKYHLYTEKALAEDIHRNKTIVDKIIETFKTNQ... | Function: DNA helicase which seems to act as a postreplicative transcription termination factor. Involved in ATP-dependent release of nascent RNA. Forms a stable complex with single-stranded DNA, and to a lesser extent RNA (By similarity).
Sequence Mass (Da): 53501
Sequence Length: 462
Subcellular Location: Virion
EC: ... |
Q9V3R1 | MWTLTCQQFIALILLGTLVPSESFLCKHCFRKNLEKVHESFRDILSPPIFGVNPQPLIEVQQPKVTPKPESSQVIHVHQPQVILKPIYYPKVDTISTKNQIGIHGPYSQYPSLLPSANLLGIPNQQLINAQDVLSDKDQKQTQVQNNNLHIRFGVSALREGRNNPSLETISRDKVDKISPALQLQLLRYADSQSQSQTQSQSASQSESNASSQFQAQEQSNRLLENPPVSESQSQSESQSQSESQKQSQSQSQRQQQIQTQLQILRQLQQKSNEQSAAQSASQIQSQRQSDSQSNLQLQEQSQSQSEQGKPIQSQIQILQ... | Function: Responsible for physiological and behavioral changes in mated female flies. Associates with sperm and localizes to specific regions of the female reproductive tract, including the sperm storage organs. It accelerates sperm accumulation into storage but does not mediate the entry of the first sperm into storag... |
E2DWQ7 | MRLAIMLSATAVAINFATCSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTKRADAKKLAKQLMGNDKLADAAYIWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY | Function: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways . Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein s... |
A0A4Z3 | MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRP... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addit... |
P0C2L1 | ADNRRPIWNLGHMVNALKQIPTFLXDGANA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM... |
P0A0C2 | MNIVENEICIRTLIDDDFPLMLKWLTDERVLEFYGGRDKKYTLESLKKHYTEPWEDEVFRVIIEYNNVPIGYGQIYKMYDELYTDYHYPKTDEIVYGMDQFIGEPNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHEGKKEDCYLMEYRYDDNATNVKAMKYLIEHYFDNFKVDSIEIIGSGYDSVAYLVNNEYIFKTKFSTNKKKGYAKEKAIYNFLNTNLETNVKIPNIEYSYISDELSILGYKEIKGTFLTPEIYSTMSEEEQNLLKRDIASFLRQMHGLDYTDISEC... | Function: Involved in resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region. The C-terminal region is a kinase that phosphorylates several 4,6-disubstituted aminoglycosides.
Catalytic Activity: a gentamycin + GTP = a gentamyci... |
P23181 | MLRSSNDVTQQGSRPKTKLGGSSMGIIRTCRLGPDQVKSMRAALDLFGREFGDVATYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREEVMHFDIDPSTAT | Function: Responsible for gentamicin resistance and has a limited substrate range.
Catalytic Activity: acetyl-CoA + gentamicin C = CoA + H(+) + N(3)-acetylgentamycin C
Sequence Mass (Da): 19442
Sequence Length: 177
EC: 2.3.1.60
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P0A256 | MHTRKAITEAIRKLGVQTGDLLMVHASLKAIGPVEGGAETVVAALRSAVGPTGTVMGYASWDRSPYEETLNGARLDDKARRTWPPFDPATAGTYRGFGLLNQFLVQAPGARRSAHPDASMVAVGPLAETLTEPHELGHALGEGSPVERFVRLGGKALLLGAPLNSVTALHYAEAVADIPNKRWVTYEMPMLGRNGEVAWKTASEYDSNGILDCFAIEGKPDAVETIANAYVKLGRHREGVVGFAQCYLFDAQDIVTFGVTYLEKHFGATPIVPAHEAAQRSCEPSG | Function: Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
Catalytic Activity: a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-acetyl-2-deoxystreptamine antibiotic + CoA + H(+)
Sequence Mass (Da): 30609
Sequence Length: 286
EC... |
P29808 | MTDLNIPHTHAHLVDAFQALGIRAGQALMLHASVKAVGAVMGGPNVILQALMDALTPDGTLMMYAGWQDIPDFIDSLPDALKAVYLEQHPPFDPATARAVRENSVLAEFLRTWPCVHRSANPEASMVAVGRQAALLTANHALDYGYGVESPLAKLVAIEGYVLMLGAPLDTITLLHHAEYLAKMRHKNVVRYPCPILRDGRKVWVTVEDYDTGDPHDDYSFEQIARDYVAQGGGTRGKVGDADAYLFAAQDLTRFAVQWLESRFGDSASYG | Function: Resistance to antibiotics containing the 2-deoxy-streptamine ring including dibekacin, gentamicin, kanamycin, sisomicin, tobramycin and neomycin, but not to amikacin or netilmicin . Acetylates a broad range of both 4,5- and 4,6-disubstituted aminoglycosides, including neomycin, paromomycin, ribostamycin, siso... |
P08988 | MQYEWRKAELIGQLLNLGVTPGGVLLVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMPSWSGLDDEPFDPATSPVTPDLGVVSDTFWRLPNVKRSAHPFAFAAAGPQAEQIISDPLPLPPHSPASPVARVHELDGQVLLLGVGHDANTTLHLAELMAKVPYGVPRHCTILQDGKLVRVDYLENDHCCERFALADRWLKEKSLQKEGPVGHAFARLIRSRDIVATALGQLGRDPLIFLHPPEGGMRRMRCRSPVDWLSS | Function: Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
Catalytic Activity: a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-acetyl-2-deoxystreptamine antibiotic + CoA + H(+)
Sequence Mass (Da): 28491
Sequence Length: 261
EC... |
P29809 | MDEKELIERAGGPVTRGRLVRDLEALGVGAGDTVMVHTRMSAIGYVVGGPQTVIDAVRDAVGADGTLMAYCGWNDAPPYDLAEWPPAWREAARAEWPAYDPLLSEADRGNGRVPEALRHQPGAVRSRHPDASFVAVGPAAHPLMDDHPWDDPHGPDSPLARLAGAGGRVLLLGAPLDTLTLLHHAEARAEAPGKRFVAYEQPVTVGGRRVWRRFRDVDTSRGVPYGRVVPEGVVPFTVIAQDMLAAGIGRTGRVAAAPVHLFEAADVVRFGVEWIESRMGGAAGGA | Function: Resistance to neomycin.
Catalytic Activity: a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-acetyl-2-deoxystreptamine antibiotic + CoA + H(+)
Sequence Mass (Da): 30455
Sequence Length: 286
EC: 2.3.1.81
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Q89VT8 | MNIAVLPNSPDTAPQIADPLDHLADKLFHSMGSDGVYARTALYESIVERLAALITSHREAGTEALRFPPVMSRAQLEKSGYLKSFPNLLGCVCGLHGTEREINAAVSRFDAGGDWTTSLSPADLVLSPAACYPVYPIAASRGPLPKGGLRFDVAADCFRREPSKHLDRLQSFRMREYVCIGTPDDVSDFRERWMVRAQAIARDLGLTFRVDYASDPFFGRVGQMKAVSQKQQQLKFELLIPLRSEEQPTACMSFNYHREHFGTTWGIQDANGEPAHTGCVAFGMDRLAVAMFHTHGTDLSAWPAKVRDILGLQPHVAAGA... | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Catalyzes the ATP-dependent activation of L-glycine and its transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein bsr0959 of yet unknown function. May participate in nonribosomal peptide synthesis or related processes. ... |
Q7CWR3 | MTVFSAIPPISCWFTGRTPASWDKTMDMQTSFLDRLFEEGLLIETGVDGLYGRSGQFEDVIAAFERLIDRTGGADGAEAIRFPPGINRAYFEKSGYMKSFPQLAGTVHSFCGCELDHVSLLKSMDEGGDWTKDQKATDIVLTPAACYPLYPTIAKRGALPAGGGLYDIQSYCFRHEPSKDPARQQLFRMREYVCMGTESDVTEFRQTWMDRGVEMMKAVGLDVTIDIANDPFFGRAGKMLANNQRDQNLKFELLIPVTSATNPTACMSFNYHQDAFGQKWGLNLENGDVAHTACVGFGLERIALALFAHHGLDVKKWPAK... | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Catalyzes the ATP-dependent activation of L-alanine, and to a lesser extent of L-glycine and L-serine, and their transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein Atu2571 of yet unknown function. May participate in ... |
P46481 | MGIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGTAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLL... | Function: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. Substrates are p-hydroxybenzoic acid (pHBA), 6-hydroxy-2-naphthoic and 2-hydroxycinnamate.
Location Topology: Multi-pass membrane protein
Sequenc... |
C5BC09 | MLYPRAIRLRFACKLTLASVLSLLLGFYFGLPMPRWSALTAALVAAAPAFAAGGEPFSGAIRYRGWLRIIGTVLGSLCALLLMMLLIRAPLLMILLCCLWAGVCTWLSSLVRMENSYALGLSGYTALIIVVSCLGEPQFILQLALERCGEIVLGIVCAVLVDTLLAPRSVKGEVDRVVGGMLLGQLRLLQCCVDGRDGDAIDRSWHRLIRESHTLEEMRASLALESSRWPRACRRLTALHTLSLTLITRACEIFLTQCQTPMALPAPFLALIAAPVDTPEEAYQRLKQLRRLLVAHGEHQLPPALIGWIGGASRLQLLVK... | Function: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70170
Sequence Length: 648
Subcellular Location: Cell inner membrane
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P80387 | ILMDSPEDADLYHSEEIKAPEKEEFLAWQHDLEVNDKASAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFLVDGQWTHDPSEPVVTSQLGTVNNIIQVKK | Function: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein... |
Q5R801 | MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQRDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI | Function: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein... |
P54619 | METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQ... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
Q09138 | METVTSSDSSSAVENEHPQDTPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQ... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
P80385 | MESVAAESAPAPENEHSQETPESNSSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLEAIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQA... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
Q9UGJ0 | MGSAVMDTKKKKDVSSPGGSGGKKNASQKRRSLRVHIPDLSSFAMPLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPRPSSPMSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESYKHEPERLENRIYASSSPPDTGQRFCPSSFQSPTRPPLASPTHYAPSKAAALAAALGPAEAGMLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTI... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
Q91WG5 | MGSAAMDTKKKKEVSSPGGSSGKKNPSLKRRSLRVHIPDLSSFAMPLLDGDVENSEKHSSRKVDSPFSSGSPSRGLFSRGPQPRPSSPVSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPSTSPGGIRFFSRSRKTSSVSSSPSTPTQVTKQHPFPLESYKQEPERPESRIYASSSPPDTGQRFCLAFQSPARPPLASPTYHAPLRTAVLAAAPGPAEAGMLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDF... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
Q9UGI9 | MEPGLEHALRRTPSWSSLGGSEHQEMSFLEQENSSSWPSPAVTSSSERIRGKRRAKALRWTRQKSVEEGEPPGQGEGPRSRPAAESTGLEATFPKTTPLAQADPAGVGTPPTGWDCLPSDCTASAAGSSTDDVELATEFPATEAWECELEGLLEERPALCLSPQAPFPKLGWDDELRKPGAQIYMRFMQEHTCYDAMATSSKLVIFDTMLEIKKAFFALVANGVRAAPLWDSKKQSFVGMLTITDFILVLHRYYRSPLVQIYEIEQHKIETWREIYLQGCFKPLVSISPNDSLFEAVYTLIKNRIHRLPVLDPVSGNVLH... | Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote... |
Q8RXN0 | MEIEASRQQTTVPVSVGGGNFPVGGLSPLSEAIWREKAPTEFVGDVSARLTWQDLTVMVTMGDGETQNVLEGLTGYAEPGSLTALMGPSGSGKSTMLDALASRLAANAFLSGTVLLNGRKTKLSFGTAAYVTQDDNLIGTLTVRETIWYSARVRLPDKMLRSEKRALVERTIIEMGLQDCADTVIGNWHLRGISGGEKRRVSIALEILMRPRLLFLDEPTSGLDSASAFFVTQTLRALSRDGRTVIASIHQPSSEVFELFDRLYLLSGGKTVYFGQASDAYEFFAQAGFPCPALRNPSDHFLRCINSDFDKVRATLKGSM... | Function: Required for the cuticle, root suberin and pollen coat development by controlling cutin and maybe wax transport to the extracellular matrix . Involved in developmental plasticity and stress responses. Together with ABCG9 and ABCG14, required for vascular development by regulating lipid/sterol homeostasis . Ma... |
Q9C8K2 | MELESTSNGRRPPPPAEIGRGAYLAWEDLTVVIPNFSGGPTRRLLDGLNGHAEPGRIMAIMGPSGSGKSTLLDSLAGRLARNVIMTGNLLLNGKKARLDYGLVAYVTQEDILMGTLTVRETITYSAHLRLSSDLTKEEVNDIVEGTIIELGLQDCADRVIGNWHSRGVSGGERKRVSVALEILTRPQILFLDEPTSGLDSASAFFVIQALRNIARDGGRTVVSSIHQPSSEVFALFDDLFLLSSGETVYFGESKFAVEFFAEAGFPCPKKRNPSDHFLRCINSDFDTVTATLKGSQRIRETPATSDPLMNLATSEIKARL... | Function: Involved in the secretion of cuticular wax from epidermal cells to the cuticle, especially in the transport of aldehydes, alcohols and acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76451
Sequence Length: 687
Subcellular Location: Cell membrane
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Q08641 | MGVADLIKKFESISKEEGDATVDTNSSSKPLKSNDETKELHQQESTAVPQEVDVNEEFENEPETINSSRTAEKPLETNLPKPETNEEDEEEGSMSENKIYSKGENADINVNDFQEYKEMENTGAEVLASSVEESDAIQEGVAEETEGIATPKQKENEKNDESEEESANNASEPAEEYSQSEEDADIEQSNGKETENAENASQQANDGSTSTTTSKNKKKKNKKKNKKKRNGNVNTNANVDDSTKTGENDDTTGDTTSSTTSAIQEVNDLEVVDDSCLGIDQQHNREHLKALTQDVKEETLENIAHEGRGDNTGDQNAVEK... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) . N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite ... |
O65934 | MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLD... | Function: Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence.
PTM: Phosphorylated by PknF. Can probably be phosphorylated in vivo by other kinases... |
P31941 | MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN | Function: DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selecti... |
Q9UH17 | MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYK... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce ... |
Q9NRW3 | MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce ... |
Q8IUX4 | MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRS... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against viruse such as HIV-1 or HIV-2 . After the penetration of retroviral nucleocapsids into target cells of i... |
Q7YR25 | MNPQIRNMVEQMEPDIFVYYFNNRPILSGRNTVWLCYEVKTKDPSGPPLDANIFQGKLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQQALRILCQERGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISNNKHVSLCIFAARIYDDQGRC... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also simian foamy virus (SFV). After... |
Q694C5 | MKPHFRNTVERMYRGTFFYNFNNRPILSRRNTVWLCYEVKTRGPSMPTWGAKIFRGQLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQEALRILCQKRGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISKKKHVSLCIFAARIYDDQGRR... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-se... |
Q9HC16 | MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGR... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against Vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infec... |
Q694B8 | MKPQTRNTVVRMDPDTFFYNFYNRPILSHRNTVWLCYEVKMKTNDPSRPPLVANIFQGQVSFNPEHHAEMYFLSWFRGNLLPACKRSQITWFVSWNPCLYCVAKVAEFLAEHPKVTLTVSTARLYCYRKKDWRRALRKLSQTGARVKIMDYEEFQHCWDNFVDNQREPFEPWNALPKHYTLLRITLGEVLRHRMDPVTFTYNFTNDPSVLGQHQSYLCYKVEHLRNGTWVPLHQHRGFILNEASNSVSFPEGRHAELCLLDLISFWKLKQAQRYRVTCFISWSPCFSCAEKVAEFLQENPHVNLHISAARIYDYQRGYKK... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-se... |
Q694C2 | MQPQYRNTVERMYRGTFFYNFNNRPILSRRNTVWLCYEVKTRGPSMPTWDTKIFRGQVLRSKAKYHPEMRFLHWFREWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGLHATMKIMNYNEFQDCWNKFVDGGGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHLSLCIFAARIYDDQGR... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-se... |
Q7YR23 | MVEPMDPRTFVSNFNNRPILSGLNTVWLCCEVKTKDPSGPPLDAKIFQGKVYSKAKYHPEMRFLRWFHKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGPHATMKIMNYNEFQDCWNKFVDGRGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRYQEGLRAL... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs). After the penetration of retroviral nuc... |
Q55DA0 | MDQVSIEMSSTPRPTMVKSKSQLSLRRSLTITFKDLAYSVTVKKKKMQILKGVSGTVTPGELVAVFGPSGSGKTTLLDILANRKESGEISGAVLINGNEIDDDYKRLCSYVVQEDVLLPTITVRETLRFYADLKLPKSWTEKEKHERIEQILEQIGLSHRADAKIGGVLPGGIVLRGLSGGEKRRVSIGCGLVTSPSIVLLDEPTSGLDTTSAMAVMKTLVELTQQKSVTVICTIHQPRSEIFKLFTKIMVLAEGRLVYYGNRPVEHFTEIGFPFPDQTNPADYILDAVTTIKEEGRADEIADRLQSSYLDQANQESSST... | Function: May be involved in cell migration.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68269
Sequence Length: 615
Subcellular Location: Membrane
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G4MMH2 | MLSLKAVLRFASVAVAVVLPTLAQAQAPEPSLSVRSPPVSYNNTLVKQRADPQILKHTNGRYYFIATVPEYDRVVMRQADSIQGLSTAEERLIWARSQSKAGVGYVWAPELHKIGDKWYIYFALGRTAPFDVRPFVLEGTGSDDPMAASWAEKGFITTDFDTFSLDATTFEVNGVRYLSWAQADPRFDNGGGTSLFLARMTNPWTIQRPSIVISRPDQPWERIGHNVNEGSWGMVRNGKVFVTYSAAATDANYCMGLLTADQNADLMNPASWSKSKDPVFVSNTATSQFGPGHSAFTVSDDNQSDVLVYHARQYKDIRGE... | Function: Secreted arabinofuranosidase that causes degradation of rice cell wall components during infection. Required for virulence.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Mass (Da): 52455
Sequence Length: 486
Domain: Organized into ... |
A1CQC3 | MTTFTKLSEQETPSIAVHASRRISKINPNIYAGFTEHMGRCIYGGIYDPGNPLSDENGFRKDVLEALKELNIPVVRYPGGNFMATYHWIDGVGPKDQRPSRPELAWLGTETNQFGTDEFMKWCELLGTEPYFCLNFGTGTLDEALAWVEYCNGTRDTYYANLRRKNGREEPYNIKYWALGNEVWGPWQVAQTTKEEYAHKAYQWAKALKLLDPTLKLILCGQDGTASWDYYTLKHCILPVNSPLSTSAVPLIDMHSIHLYTSSSSHLPNVTAPLAAERAIEITSSLIDLAMIENGVPNTQLRPTICFDEWNVWDPIRAEG... | Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha... |
Q5BDV3 | MTTFTKLSEQEAPGISIHPDRRISKINPNIYAGFAEHMGRCIYGGIYDPGNPLSDENGFRKDVLEALKELKVPVIRYPGGNFTATYHWIDGVGPRDQRPARPELAWLGTETNQFGTDEFLKWCEVLGTEPYLCLNMGTGTLDEALAWVDYCNGTRDTYYANLRRKNGREEPYNVKYWALGNEVWGPWQVEQSTKEEYAHKAYQWAKALKLLDPSIELILCGKEGPTSWDYYTLKQTMLPVHSPLSTSAVPLIDMHSIHLYTAHSSHLPNVTAPLAAERAIEITSSLIDLARVENGVPPEQRRPTICFDEWNVWDPIRAEG... | Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.... |
P46133 | MSMSSIPSSSQSGKLYGWVERIGNKVPHPFLLFIYLIIVLMVTTAILSAFGVSAKNPTDGTPVVVKNLLSVEGLHWFLPNVIKNFSGFAPLGAILALVLGAGLAERVGLLPALMVKMASHVNARYASYMVLFIAFFSHISSDAALVIMPPMGALIFLAVGRHPVAGLLAAIAGVGCGFTANLLIVTTDVLLSGISTEAAAAFNPQMHVSVIDNWYFMASSVVVLTIVGGLITDKIIEPRLGQWQGNSDEKLQTLTESQRFGLRIAGVVSLLFIAAIALMVIPQNGILRDPINHTVMPSPFIKGIVPLIILFFFVVSLAYG... | Function: Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl-glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p-aminobenzoate and glutamate. It seems also to increase the se... |
P0CU79 | MFAVIFETRPQPSQFDTYLTIAKSLRPELANIDGFIENIRYKSLSRPGWILSLSFWRDEKSLVRWRTTATHHMAQEKGRDGVLEDYHLRVGQVTASVRSNEVKRVETVDAREQDDVTAVGAAKTVQLVRFQMDRGAGIDAAAGKLGLNPEEPRGLLAWDIMEAVLSPGDMILLASWETGSSSVSIPGADSDEVQVLRDYGKYDRREAPQFYPPAS | Function: Monooxygenase that converts the endogenous (and likely the host) jasmonate (JA) to its hydroxylated derivative 12-hydroxyjasmonate (12OH-JA), also known as tuberonic acid, a compound that attenuates or disables jasmonate-based host innate immunity and which is essential for proper initiation and elaboration o... |
Q9HFS9 | MYSLLTALSVPLLAGLAHGYANPGSCSGSCNVHDPALIVRESDGKYFRFSTGNEISYASASSINGPWTAIGSVVPAGSKIDLSGNTDLWAPDLSYVDGTYYCLYSVSTFGSQDSAIGVASSTTMELNTWTDHGSVGVASSSSKNYNAIDGNLLVDGSSYYLQFGSFWGDIYQVKMASPLKTAGSASYNIAYNATGTHSEEGSYLFKYGSYYYLFFSSGTCCGYDTSRPAQGEEYKIMVCRSTSATGGFVDKNGNACTESGGTIVLASHGTVYGPGGQGVYDDPTYGPVLYYHYVDTTIGYADDQKLFGWNTIDFSSGWPV... | Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Catalytic Activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Sequence Mass (Da): 34097
Sequence Length: 321
Pathway: Glycan metabolism;... |
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