ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A1U0A9 | MSPRPLIELQDITRSFGEGELAVPVLKGIDLKIWPGEFVAIMGPSGSGKSTLMNILGCLDQPSAGQYRFNGRDVSALDRDELARLRRDAFGFVFQSYNLLPGMTARENVEIPAIYAGMAPAERHARAERLLTGLGLGERLSHRPAQLSGGQQQRVSIARALMNGGQLIFADEPTGALDSKSSQEVIRLLTDLSRQGHTIILITHDPDVAKVARRQIRIADGELVEDTGAEMPSAQIPETDQNGRRHSRLGDWQEALKSAVRSLHSNLFRTALTLLGIVIGVASVITMLAIGEGARKDVVDRISTMGSDLLLVRPGGPDQR... | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Mu... |
Q5MK06 | MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHEAGHTVIMVTHDPGIAANANRVIEIRDGEIISDTSKNPEIPASNVGRIQEKASWSFYYDQFVEAFRMSVQAVLAHKMRSLLTMLGIIIGIASVVSVVALGNGSQKKILEDISSMGTNTISIFPGRGFGDR... | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Overexpression confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da)... |
Q82VK1 | MVSTDLPPLIELRGIRKRYGGGDKPEVEVLHGIDLDIRAGEFIAIVGSSGSGKSTLMHLLGCLDRPSSGSYRFAGEDVSTFGSDELAWLRRKAFGFVFQGYHLIPTESARENVEIPAIYAGLPPGERMQRAADLLGRLGLSDKLNNRPNQLSGGQQQRVSIARALMNGGHIILADEPTGALDSRSGAEVMELLRELAGAGHTVILITHDRDVAAQAQRVVEIRDGRIVADSVTDRQPSEQPLLHHAGLSSLEMTQAHEDTGTPFWQGLHETIRAAWRVMWIHRVRTSLTLLGIVIGVASVIVMLAIGEGTKQRVIDQMGS... | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72075
Sequenc... |
P42003 | MDTDDVESNTSSAMSTLGSLFSFTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLELCQYPFSAKQKEVCINPYHYKRVESPVLPPVLVPRHSEFAPGHSMLQFNHVAEPSMPHNVSYSNSGFNSHSLSTSNTSVGSPSSVNSNPNSPYDSLAGTPPPAYSPSEDGNSNNPNDGGQLLDAQMGDVAQVSYSEPAFWASIAYYELNCRVGEVFHCNNNSVIVDGFTNPSNNSDRCCLGQLSNVNRNSTIENTRRHI... | Function: Required for the function of decapentaplegic. May play an important role in mediating Dpp signaling. Involved in the BMP signaling pathway.
PTM: Phosphorylation on Ser-453 and/or Ser-455 is required for interaction with Smurf . Phosphorylation on Ser-25 by key/Nemo promotes export from nucleus and antagonizes... |
P50537 | MGELKEILKQRYHELLDWNVKAPHVPLSQRLKHFTWSWFACTMATGGVGLIIGSFPFRFYGLNTIGKIVYILQIFLFSLFGSCMLFRFIKYPSTIKDSWNHHLEKLFIATCLLSISTFIDMLAIYAYPDTGEWMVWVIRILYYIYVAVSFIYCVMAFFTIFNNHVYTIETASPAWILPIFPPMICGVIAGAVNSTQPAHQLKNMVIFGILFQGLGFWVYLLLFAVNVLRFFTVGLAKPQDRPGMFMFVGPPAFSGLALINIARGAMGSRPYIFVGANSSEYLGFVSTFMAIFIWGLAAWCYCLAMVSFLAGFFTRAPLKF... | Function: Permease for malate and other C4 dicarboxylic acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49304
Sequence Length: 438
Subcellular Location: Membrane
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Q5F398 | MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSSCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAANMWKKKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERQETMTCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQVMGMLAFPSDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTITLQAGLSAIKTPQCYKEDGSSKNPDCPVCSKS... | Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase com... |
Q7L5Y9 | MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRS... | Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase com... |
Q4VC33 | MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSSCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASMWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELVRQNKRLDAVRHARKHFSQAEGSQLDEVRQVMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNSSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRS... | Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase com... |
Q7RZH4 | MAVDKKRKNTKAPASGPKRRKTQPSSKQIKRPVSVDALAWKTVDIPEMFDDAEGFFGLEEITGVDIVKDGDVVKFMAAVPKSEAEVEDDGEEFGGFDDEETPKPAGNADQEVKTSETKAEAASTPAKEKKASKDQRKPKEQQKQQKQQKQQPKKEQPNKAANKKNAEDKKKARKNEKTTVEPKDPELETDLFTKLEELPEPEEEEIDMSEWVPLDLSPRMISSIAKLRFSKPTVIQSKAIPEIMAGHDVIGKASTGSGKTLAFGIPVIESWLSAAETRKQNKEERKGATALILSPTRELAQQIRDHLQALCKGLPTAPYI... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 89254
Sequence Length: 805
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
Q0U6X2 | MKRAHKAPKASHKAHKRQKVEKKPRPEINVPKRKIRLDDLGWNQVSMPDRLEDFEGFYGLEEIEDVHVVKDAVTGNLSFETTKTDEQIEQDIEKAWQREEEEAKFLEKITFGGEPKNGEDVVEEETAPVEDTVEATQDEDAASWGGFSDDDVAQNGDEQSEDVQMVEEDAPPTPNVVLSTTKADGDGEAEPKKMNKRERAAEKKRIAALAKKTKKPDDDEASEGKTFGPGAFDILANRADDEDDEVDVSAWEELELSTKILESLAKLKFSKPTTIQASTIPEIMAGRDVIGKASTGSGKTLAFGIPIIESYLASKSKSKD... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 90193
Sequence Length: 817
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
O74393 | MPKKAALDELKWKEVKLPDHLDDFDGFMGLEEIEGVDIKYQPKGAMKEVIYELPEVHEKKDKKPEKRKKDQKEASEKKKKGKRTSPTIEMTSLGSKVTSKNYNEFSTLEEEDEHNSHGVDVSAWAHFSLSPEMLGSLSKAGFSKPMPIQSLVIPEASIGFDIIGKADTGSGKTLAFGIPILEHCLRNVDAKYVQALVVAPTRELAHQICQHFELIKPSPNIRVMSITGGLAVQKQQRLLNKHPHVVVATPGRLWSVINENNLTGNFKKIKCLVLDEADRLLQKSHFEELSKLLEILGNPMHTQRQTFIFSATFDEGLQQR... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 73250
Sequence Length: 648
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
A7EAY2 | MDTKQKKRSHSETNGSQKAPKRQKIQKTSKKQKKAAPKKPVAVDSLPWNEVTMPDMFEDAEGFYGLEEVDDVEVVRDGDVVTFVSSKIQTKNNEDEEFEGFGDEVEDGGNAATDNTGEVKPILKPTEESTKNDVPQGNKQKIEKKAKPEKKDKKEGSNTEEGEEKVPSKKEKKQKQEKPQKQPVDKDATLKQDPLKNVFEALDEDAAGEVEVSGWVELDLSSNTLMALSKMGFSKPTPIQSEAIPEVLAGHDVVGKASTGSGKTLAFGIPIVEKWLEVYGELDEDELKKSTRPPTALILSPTRELAHQLTEHITTLCKGM... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86191
Sequence Length: 780
Domain: The Q motif is unique to and characteristic of the DEAD bo... |
P38112 | MGKKRAPQKGKTVTKPQEIIVDESKLNWKPVDIPDTLDDFGGFYGLEEIDGVDVKVVDGKVTFVTKKDSKVLKDSNKEKVGDDQESVENESGSDSESELLEFKNLDDIKEGELSAASYSSSDEDEQGNIESSKLTDPSEDVDEDVDEDVLKENVFNKDINIDDISPVNLPEWTNLAPLSMTILQSLQNLNFLRPTEIQKKSIPVIMQGVDVMGKASTGSGKTLAYGIPIVEKLISNFSQKNKKPISLIFTPTRELAHQVTDHLKKICEPVLAKSQYSILSLTGGLSIQKQQRLLKYDNSGQIVIATPGRFLELLEKDNTL... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 87048
Sequence Length: 773
Domain: The ... |
Q7WUM3 | MTLPFAEWLPKQRWYAGRSRVLASVKEASATPLGEELDLVLVDVEYTDGSSERYQVMVGWGDGPLPEYSTIASIGTADDGRDGYDALYDPRATRHLLGLVDTSATAGDVTFEKEPGVELPLEAWPRVFDAEQSNTSVIFDEDAILKLFRRVTCGVNPDIELNRVLGRAGNPHVARLLGSLQSADDSGPCSLGMVTEYAANSAEGWAMATASARDLFADAEMRADEVGGDFQGESYRLGEAVASVHRTLAEELGTGPAPFPLDAVLARVRTAAAAVPELQQFVPAITARFEALTGAEVVVQRVHGDLHLGQVLRTPEAWLL... | Function: Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. Only maltose acts effectively as phosphoryl-group acceptor, but maltotriose, maltotetraose, maltopentaose, and maltohexaose show a weak potential to replace maltose. ATP is not replaceable as phosphoryl-group donor.
Catalytic Activ... |
P23917 | MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPLPWMDEDELRYREEVPCYCGKQGCIETFISGTGFAMDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNVDRLYQTVGQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWLWPQE | Function: Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine.
Catalytic Activity: ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+)
Sequence Mass (Da): 32500
Sequence L... |
P20794 | MNRYTTMRQLGDGTYGSVLMGKSNESGELVAIKRMKRKFYSWDECMNLREVKSLKKLNHANVIKLKEVIRENDHLYFIFEYMKENLYQLMKDRNKLFPESVIRNIMYQILQGLAFIHKHGFFHRDMKPENLLCMGPELVKIADFGLARELRSQPPYTDYVSTRWYRAPEVLLRSSVYSSPIDVWAVGSIMAELYMLRPLFPGTSEVDEIFKICQVLGTPKKSDWPEGYQLASSMNFRFPQCVPINLKTLIPNASNEAIQLMTEMLNWDPKKRPTASQALKHPYFQVGQVLGPSSNHLESKQSLNKQLQPLESKPSLVEVE... | Function: Essential for the regulation of ciliary length and required for the long-term survival of photoreceptors (By similarity). Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in the transcriptional coactivation of AR. Could play an important function in spermatogenesis. May play a role in chromo... |
Q7LYX6 | MREEVLKRILLIIGAILMAIICLFPFIWMIVVSFAEDPTFLGSPLVEYKSTLENYVRVLSDPTLHFPAYLKNSIIIASLVTLTTVSISSLAAYAVSRIEFKGRLLIPIFVLGLSMFPQISLVGYLFKFIEKLGWVNTYQALYFPYVAWTLPLSLWILLSYFSQLPKDLDEAAMIDGASRIKTLTTIILPLSAPALFSTALLVFIAAFNEFMFALLFTTDHRARTVPVGIALFQGVHGEIPWGSVMAASVISTIPLVIMALLFQKYIVSGLTAGALKGE | Function: Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30795
Sequence Length: 278
Subcellular Location: Cell membrane
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Q9KL07 | MAMVQGKSLKYRVWATHAALWVFLALIIFPLLMIVAISFREGNFATGSLIPDRPSLEHWKLALGIAVQNADGSVTPPPFPVMTWLWNSVKVAGITSVLIVALSTTSAYAFARMRFKGKETILKAMMIFQMFPAVLALVALYALFDKLGQYIPFLGLNTHGGLIFSYLGGIALHVWTIKGYFETIDRSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIGVVGEVPVASLLLSDVNSYTLAVGMQQYLYPQNYLWGDFAAAAVLSALPITIVFLLAQRWLVGGLTAGGVKG | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32182
Sequence Length: 296
Subcellular Location: Cell inner membrane
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Q74RF8 | MTKEEMQMAMVQPKSQRLRLLGTHFLMLCFIALIMFPLLMVIAISLRPGNFATGSLIPDQISWEHWKLALGMSVTHADGSVTPPPFPVMLWLWNSIKIALITAMGIVALSTTCAYAFARMRFRGKSALLKGMLIFQMFPAVLSLVALYALFDRIGQYMPFIGLNTHGGVIFAYMGGIALHVWTIKGYFETIDNSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDVNSYTLAVGMQQYLNPQNYLWGDFAAAAVLSAIPITTVFLLAQRWLVGGLTAGGVKG | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33187
Sequence Length: 303
Subcellular Location: Cell inner membrane
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O05250 | MKKTLKLQTRLTIFVCIVVLIALLITFFTVGAQTTKRIRDQEKATALQTAEMVAEAPMTAAALESGKKQKELQSYTKRVQKITGTEFVVVMDMNGIRKTHPDPSKIGKKFRGGDESEVLKGHVHISTASGTLGKSQRAFVPVYAENGKQVGAVAVGITVNEIDEVISHSLRPLYFIICVSIFVGVIGAVIVARTVKNIMYGLEPYEIATLLEERSAMLESTKEGILAVDEHGKIKLANAEAKRLFVKMGINTNPIDQDVDDILPKSRLKKVIETKKPLQDRDVRINGLELVFNEVPIQLKGQTVGAIATFRDKTEVKHLA... | Function: Member of a two-component regulatory system MalK/MalR. Involved in the activation of maeA, maeN and yflS in presence of malate. Probably activates MalR by phosphorylation.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequen... |
Q8FB37 | MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTSTAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQI... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-maltose(out) + H2O = ADP + D-maltose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41006
Sequenc... |
Q18788 | MKTVRFNKQALAILAACFIFLLCVVCYFSASSESHNAVVVGERARGHIAVRDVENRHLAEEKHAVIHAKTVGKIERVVSQEKVEILRPARVESKPPGEKTSTEPEETGVGKAPIQTSEGLEKLIGKIHYENKDEENDLRRQKVKEMMIHAWEGYKNYSWGANELRPMSKKPNSQNIFGGSQMPATIVDAADTLFIMDLKDKYKEARDYIENNFSMAKSTSTLSVFETTIRFLGGLLSLYALTQESFYIEKAREVGEALLPAFNTPSGIPKSNLDVASKHASNYGWANGGQSILSEIGSLHLEFLYLSRISNAPIFEKKVK... | Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[al... |
P31723 | MRLPVSFPLTVLSLLGSTIAHPYGETEAVLRSEPKSNQAKADAVKEAFQHAWNGYMKYAFPHDELTPVSNGHADSRNGWGASAVDALSTAVIMGKADVVNAILEHVADIDFSKTSDTVSLFETTIRYLAGMLSGYDLLQGPAKNLVDNQDLIDGLLDQSRNLADVLKFAFDTPSGVPYNNINITSHGNDGATTNGLAVTGTLVLEWTRLSDLTGDEEYAKLSQKAESYLLKPQPSSSEPFPGLVGSSININDGQFADSRVSWNGGDDSFYEYLIKMYVYDPKRFETYKDRWVLAAESTIKHLKSHPKSRPDLTFLSSYSN... | Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)... |
Q9FZ29 | MLNILPFFLFFLPFLIGNNRICVAVKTGFVGRNGTQFVLNGEQVYLNGFNAYWMMTTAADTASKGRATVTTALRQASAVGMNVARIWGFNEGDYIPLQISPGSYSEDVFKGLDFVVYEAGRFNIKLIISLVNNFEDYGGRKKYVEWAGLDEPDEFYTNSAVKQFYKNHVKTVLTRKNTITGRMYKDDPTIFSWELINEPRCNDSTASNILQDWVKEMASYVKSIDSNHLLEIGLEGFYGESIPERTVYNPGGRVLTGTDFITNNQIPDIDFATIHIYPDSWLPLQSSRTGEQDTFVDRWIGAHIEDCDNIIKKPLLITEF... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 46290
Sequence Length: 411
Subcellular Location: Secreted
EC: 3.2.1.78
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Q7JRE4 | MSTESLNSLSDKELHRKLIQSGFPSTPVTETTRAVLIEKLRKHTRADKLKKRSNKYVLYSKEQQESPPFPQYHQYHAPQPPQNYANGLDNNNDLDQTGGSSAYNRSLDESDSSPLQLSASKMYAPPPVVASNYDGDCSPHSLGLNGKYLQPCSMPYAIDTSNNYGKPSGKAKLSDGGVVNRLLSFRDTTIQRKFNYPTGQASRIPLRKERLTRFALSDLKSFIRNPDIRPYVIPRVLISLFLIFLTIITVLYVGKRFEQSPIDKAALKYTLCNPNDMQMISEKVNCIEKDSLRGALDMSEELFRHLNERARLHHCKDANL... | Function: Inner nuclear membrane protein . Acts as a negative regulator of the BMP (Dpp) signaling cascade during crossvein development in pupal wings and possibly during synaptic transmission at the neuromuscular junction (NMJ) . Appears to be required for pupal development and consequently transition to the adult sta... |
Q9Y2U8 | MAAAAASAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQHRSGGRGNKTRNSNNNNTAAATVAAAGPAAAAAAGMGVRPVSGDLSYLRTPGGLCRISASGPESLLGGPGGASAAPAAGSKVLLGFSSDESDVEASPRDQAGGGGRKDRASLQYRGLKAPPAPLAASEVTNSNSAERRKPHSWWGARRPAGPELQTPPGKDGAVEDEEGEGEDGEERDPETEEPLWASRTVNGSRLVPYSCRENYSDSEEEDDDDVASSRQVLKDDSLSRHRPRRTHSKPLPPLTAKSAGGRLETSVQGGGGLAMND... | Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99997
Sequence Length: 911
Subcellular Location: Nucleus inn... |
Q0JKM9 | MRLLGAHRAALLVLACVVVVVIHGLGEAEALGGGGGFVRAQGTRFVLDGNPYYANGFNAYWLMLLAADPSQRGKVSAALGEAAGHGLTVARTWAFSDGGGGNALQLSPGNYNENTFKGLDFVLSEARKYGIKVILSLVDNYDSFGGRKQYVNWARAQGQGIGSDDEFFTNPVVKGFYKNHVKTVLTRKNTITGVAYRDDPTILAWELMNEPRCQSDLSGRTVQSWITEMAAHVKSIDRNHMLEVGLEGFYGASSPSRIAAVNPSGYQLGTDFIANNQVPGIDFATVHSYPDQWLSGKDDQAQLGFMGRWLDAHIADAQAV... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 46875
Sequence Length: 432
Subcellular Location: Secreted
EC: 3.2.1.78
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Q7Y223 | MAAPTGNGPVIPILGFLTCVAFIYLSFGDLWFGLKTEGELAFVKRNGTQFVVDGKALYVNGWNSYWFMDHAVNDHSRHRVSAMLEAGAKMGLTVCRTWAFNDGGYNALQISPGRFDERVFKALDHVIAEAKTHGVRLLLSLVNNLQAYGGKTQYVNWAWQEGVGLSSSNDSFFFDPSIRRYFKNYLTVLLTRKNSLTGIEYRNDPTIFAWELINEPRCMSDVSGDTLQDWINEMTAFIKSIDNKHLLTVGLEGFYGPSSPKKLTVNPERWASELGSDFVRNSDSPNIDFASVHIYPDHWFHDQGFEEKLKFVVKWMLSHI... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 49558
Sequence Length: 433
Subcellular Location: Secreted
EC: 3.2.1.78
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Q0JJD4 | MAVGNGLILYHILGLASCIALVYFSLGEVDLRDALPSLPFSGGASRAAAASLPFVERRGKRLFLDGRPFYINGWNSYWLMDLAVEPNTRPRVSSMFRTAVSMGLTVCRTWAFNDGSYNALQLSPGHFDERVFKALDRVVAEASEHGVRLILSLANNLDAYGGKRQYVRWAWEEGVGLTASNDSFFFDPAIRDYFKVYLKTLLMRKNHLTGLEYRDDPTILAWELMNEPRCTSDPSGDTLQRWMEEMSAYVKSIDKKHLLTVGTEGFYGPTSSQEKLNINPGEWFPNNYGADFIRNSKIQDIDFASVHVYPDNWLQHASLD... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 50063
Sequence Length: 445
Subcellular Location: Secreted
EC: 3.2.1.78
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Q9FZ03 | MAYFQRLISCIFVLFLLSLAFACEARVLLDENNANDQGFVRVNGAHFELNGSPFLFNGFNSYWLMHVAAEPSERYKVSEVLREASSAGLSVCRTWAFSDGGDRALQISPGVYDERVFQGLDFVISEAKKYGIRLILSFVNNYNDFGGKAQYVQWARNAGAQINGDDDFYTNYITKNYYKNHIKKVVTRFNTITGMTYKDDSTIMAWELMNEPRNQADYSGNTLNAWVQEMASFVKSLDNKHLLEIGMEGFYGDSVPERKSINPGYQVGTDFISNHLIKEIDFATIHAYTDQWLSGQSDDAQMIFMQKWMTSHWQDAKNIL... | Function: Possesses endo-beta-mannanase activity in vitro. May be involved in seed germination by weakening the endosperm cap prior to radicle emergence.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 46835
Sequence Length: 414... |
Q9SG94 | MKCLCFVVLLAILIAQNSSDLGVKSASSDGFVSRKGVQFILNGKPFYANGFNAYWLAYEATDSTTRFKITYVFQNATIHDLTIVRTWGFRDGGYRALQIAPGVYDEKTFQGLDFAIAEAKRLGIKMIITFVNNYSDFGGRKQYVDWAKNTGQNVSSDDDFYTNPLVKQYYKNHVKTMVNRVNTFTKVEYKDEPTIMGWELMNEPQCRADPSGKTLTAWMNEMALYVKSVDSKHLLSTGLEGFYGDSSPQRKTSLNPVAANVLGTDFIANHKLDAIDFASIHSYPDLWFPNLDEKSRLNLLRKWLECHLEDAQNILKKPLI... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 46462
Sequence Length: 414
Subcellular Location: Secreted
EC: 3.2.1.78
|
Q12RA0 | MDDTKRPLYLPFAGPAILEAPLINKGSAFSEEERIFFNLEGLLPYVIETIEEQAARAYAQFSNFSNDLDKHIYLRNIQDTNETLFYRLVRNNITEMMPIIYTPTVGLACERFSKNYRRNRGLFISYSNKDRIDDILNNSTRHKVKVIVVTDGERILGLGDQGIGGMGIPIGKLSLYTSCGGISPAYTLPITLDVGTDNQELLDDPMYMGWRHRRIEGQDYADFVEAFMEAVHRRWPDVLIQFEDFAQRNAMPLLERYKDQYCCFNDDIQGTAAVTVGSLLAASKAANTQLSKQRVVFLGAGSAGCGIAEAIVAQMISEGI... | Cofactor: Divalent metal cations. Prefers magnesium or manganese.
Catalytic Activity: (S)-malate + NAD(+) = CO2 + NADH + pyruvate
Sequence Mass (Da): 62265
Sequence Length: 562
EC: 1.1.1.38
|
Q5BGG1 | MGSKTPERDGHKGQENTTGPVECPLGGMPRGMHLATDGDGTIGDSGDDDDGEAHSTALINANANGNQKKKRKSKKKGKKKAAKQSSPPRVPLSQLFLQGKYPIGEVQEYQPNVENTSRTTAEEVRYKSRSHLEDDSFLNDYRKAAEVHRQVRKWTQERVKPGQGLMEIAEDIDDGVRALLGHAGLEPGDSLKAGLGFPTGLSLNNVVAHYTPNPGQKDIILQSSDVMKVDFGVHINGWIVDSAFTMTFDPVYDNLLAAVKDATNAGLKTAGIDVRISDVSAAIQEAMESYEVEIGGKTFPVKAVRNITGHNIKHYQIHGG... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
C7Z7V7 | MGAKISEDHPPQGNGGPLSNDPCSAGGEPRGAHLSRDGDGSVGDKGGDDDDDDDEGVVGAVSLTEASDKKKKKKRKPKKKKAKKATHQSSPPRVPLSELFTPGQYPTGEFLEYEDTNTARTTAAELRALGRKQLEDPAFLDDYRRAAEVHRQVRQWAQESVKPGQTLRDIANGIEDGVRALLGNQGLEPGDGLKSGMGFPTGLCLNHETAHYTPNPGQKDVVLQYEDVMKVDFGVHINGWIVDSAFTMSFDPTYDNLLAAVKDATNSGIKVNAAIQEAMESYEVEIAGKTYPVKPVRNISAHNIQHYRIHGGKSIPFIKN... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
O28438 | MDDEVREKLIEAGKILKQAVNEAAEKIAPGVKILEVAEFVENRIIELGAKPAFPANISINSDAAHFTPKKNDERTFKEGDVVKLDVGAHIDGYIADMAVTVDLGDNTELVKAAKEALEAAMEVVRAGVSVSEIGKAIEDAITNYGFKPIVNLTGHGLLPYLNHAPPSIYNYATEKGVTLEEGMVVAIEPFATNGVGKVGERGECEIYSLLNPRPVRMKMAREILKEVEENYKTLPFAKRWLKKAPDIIISKLAREGVLRAYPVLTEVSGGLVSQWEHTLIVEDGGATITTK | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
D4B2G3 | MAAQAAPELAKLDLNKNTGSVEANAVSAGGSEKEEAENEGDSDDDRDDEQAGGSAEVNAEKKKKKKRPKKKKKTAKVQSSPPRIPLTTLFPNSNFPEGEIVEYLNENSYRTTNEEKRHLDRMNNDFLTEYRQAAEIHRQVRQYAQKELIKPGATLTDIAEGIEDGVRHLTGHMGLEEGDSLVAGMGFPTGLNINHCAAHYSPNAGNKVVLQHGDVMKVDFGVHINGRIVDSAFTVAFDPVFDPLLTAVKEATNTGIKEAGIDVRMSDIGAAIQETMESYELELNGTSYPIKAIRNLNGHTIGQYEIHGGVNGKSVPIVKG... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
H1UBK1 | MPPANGKKGKKGGAAKAVRRIQYRPKSFKHSRFVKHAHFWSAAPEEDFDAILAEMQLADAKTAAKEATKKDAKGGKGKANGSAAATAAPEEAKQAWQAEIAAMKPIDEQFPDGKFPHGIDESPYYLKGKDGRVATDRESNEEKKALDISYEEVWQDYRRSAEAHRQVRKYVKSWIKPGMTMIEICERLETTSRRLIKEQGLEAGLAFPTGCSLNHCAAHYTPNAGDTTVLQYGDVCKIDYGIHVRGRLIDSAFTVHFDPKFDPLVEAVREATNAGIKESGIDVRLCDVGEIVEEVMTSHEVELDGKSYVVKPIRNLNGHS... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q15555 | MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPAAKPGSTPSRPSSAKRASSSGSASKSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMDILYASEEHEGHTEEPEAEEQAHEQQ... | Function: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).
Sequence Mass (Da): 37031
Sequence Length: 327
Domain: Composed of two functionally independent domains. The N-terminal domain f... |
Q8R001 | MPGPTQTLSPNGENNNDIIQDNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPASKPGSTPSRPSSAKRASSSGSASRSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMEVLYASDEQEGQTEEPEAEEQAHDQQP... | Function: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).
Sequence Mass (Da): 36946
Sequence Length: 326
Domain: Composed of two functionally independent domains. The N-terminal domain f... |
Q3B8Q0 | MPGPTQTLSPNGENNNDIIQDNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPAAKPGSTPSRPSSAKRASSSGSASRSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMEVLYASDEQEGQTEEPEVEEQTHDQQP... | Function: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity).
Sequence Mass (Da): 36988
Sequence Length: 326
Domain: Composed of two functionally independent domains. The N-terminal domain f... |
Q9UPY8 | MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYDGKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAPPCILRKNPPSARNGGHETDAQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY | Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton . Promotes microtubule growth . May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes . Also acts as a regulator of minus-end micro... |
Q7YU24 | MAAYLNRTISMVTGQTGPADDDRHASSTDTVDKSGPGSPLSRFNSSLQQSGSTMAANLLPESRLYQSNDKSPLQIFVRAKKKINDIYGEIEEYVHETTTFINALHAEAEIVDKAERELFESYVYKVAAIREVLQRDHMKVAFFGRTSNGKSSVINAMLREKILPSGIGHTTNCFCQVEGSNGGEAYLMTEGSEEKLNVVNIKQLANALCQEKLCESSLVRIFWPRERCSLLRDDVVFVDSPGVDVSANLDDWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKLSKPNIFILNNRWDASANEPECQESVKSQHTER... | Function: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion . Mitochondrial fusion is the physical merging of mitochondria that gives rise to mitochondrial networks, and this process is counterbalanced by mitochondrial fission which fragments networks . Promotes, but is not required ... |
Q6NZQ8 | MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAVTCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTANKLEKNFPCNVNTEIKDAVVVPVPQTGSNTLPTAEGAPPEVIPV | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells... |
P07394 | MFPKSNIDRNYKVKLISYDKKGKLVSDDSFEQVENYLFQNRSTTYKPGYIRRDFRRPTNFWNGYRCFNQPVGTFTRKLSDGGRQVADYGIVNPNKFTANSQHLGDNMVIYPGPFSINIDQRASVEVLNKLSQSNLNIGVAIAEAKMTASLLAKQSIALIRAYTAAKRGNWREVLSQLLISEHRFRAPAKDLGGRWLELQYGWLPLMSDLKAAYDLLTQTKLPAFMPLRVTRTVGGTHNYKVRNVESAGDTWSYRHRLSVNYRIWYFISDPRLAWASSLGLLNPLEIYWEKTPWSFVVDWFLPVGNLIEAMSNPLGLDIIS... | Function: The maturation protein is required for the typical attachment of the phage to the side of the bacterial F-pili. Binds to sequences located toward each end of the genome, hence circularizing it. The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding. Maturation prote... |
P03610 | MRAFSTLDRENETFVPSVRVYADGETEDNSFSLKYRSNWTPGRFNSTGAKTKQWHYPSPYSRGALSVTSIDQGAYKRSGSSWGRPYEEKAGFGFSLDARSCYSLFPVSQNLTYIEVPQNVANRASTEVLQKVTQGNFNLGVALAEARSTASQLATQTIALVKAYTAARRGNWRQALRYLALNEDRKFRSKHVAGRWLELQFGWLPLMSDIQGAYEMLTKVHLQEFLPMRAVRQVGTNIKLDGRLSYPAANFQTTCNISRRIVIWFYINDARLAWLSSLGILNPLGIVWEKVPFSFVVDWLLPVGNMLEGLTAPVGCSYMS... | Function: The maturation protein is required for the typical attachment of the phage to the side of the bacterial F-pili . Binds to sequences located toward each end of the genome, hence circularizing it . The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding . Maturation pr... |
Q9WH76 | MQRLKKFIAKREKGDKGKMKWNSSMDYDSPPSYQDVRRGIFPTAPLFGMEDDMMEFTPSLGIQTLKLQYKCVVNINAINPFRDFREAISAMQFWEADYSGYIGKKPFYRAIILHTARQLKTSNPGILDRGVVEYHATTQGRALVFHSLGPSPSMMFVPETFTREWNILTNKGTINVKIWLGETDTLSELEPILNPVNFRDDREMIEGAAIMGLEIKKQKDNTWLISKSH | Function: Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibit interferon signaling and thus establishm... |
A7WNB1 | MNKMNQLVRFVKDTVAVRKPQSEDKSYLPIPSTIGGHEVNSPFAEPTAPSLGIIQPKCKRADWLIKSHLTITTNYEIKEWETWDRAISDILDLYDGNPVFKPILLFVYYVLAYNARKIPGPSNGVRYGAYFDELTTVWHAIPELMNQEIDYSYNHRVLHRKIQYVISFKIQMSSTKRRTSPIESFIEVTSEGLKHTPQFTTILDRARFVYSLTGGRYVIHPF | Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly.
Location Topology: Peripheral membrane protein
Sequence Mass ... |
C1JJY2 | MAYSKGVSGTLSDYTHLRTLPALLSVVFVIAGLYQFGGISDVTITWLSNYTLTSTHAMGASIGAYALAFASSETKQFDNYQDFEKVLIAAGPAVILGYEYIQPVTDLINTTSNAGPIAAFVVTVVAWGVAVR | Function: Envelope protein that may play a role in host-cell attachment and viral genome entry.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14005
Sequence Length: 132
Subcellular Location: Virion membrane
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Q82038 | MSLFKRTKKTILIPPPHLLSGDEDRVTVLNAEGEIKISGKRPTTLDEKIYYSMSLAAAILGGNLHPSFQSLTYLFQQEMEFGSTIEKVNFGSRKPAPLTPIRWQKPEKCSFRPQPLDKKIPPQIYTVSVEGATITFSGRFLFSASHVGCDDNRVKLAGLDGFITSPNYQRVKDYYAQETVLALSFEIPTKKGK | Function: Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21616
Sequence Length: 193... |
Q6WB99 | MESYLVDTYQGIPYTAAVQVDLVEKDLLPASLTIWFPLFQANTPPAVLLDQLKTLTITTLYAASQSGPILKVNASAQGAAMSVLPKKFEVNATVALDEYSKLEFDKLTVCEVKTVYLTTMKPYGMVSKFVSSAKPVGKKTHDLIALCDFMDLEKNTPVTIPAFIKSVSIKESESATVEAAISSEADQALTQAKIAPYAGLIMIMTMNNPKGIFKKLGAGTQVIVELGAYVQAESISKICKTWSHQGTRYVLKSR | Function: Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and re... |
Q9E7N9 | MSAKLNWYRITFNDTVWRFDTARGPKDGETCPLIASELFSSGLSEVFKSVTSFSEILRNMESRGYITNITLRADSDILGPGALRCEFLFPSEVFIPTSHTLKMGRSSLILEPHLVVLKECKYISSGKLDIGISSIEATSVAVLRRVKGPAFIGCMDDNPFGVLTKKPSDEKNVLASK | Function: Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19542
Sequence Length: 177... |
Q13394 | MIAAQAKLVYHLNKYYNEKCQARKAAIAKTIREVCKVVSDVLKEVEVQEPRFISSLNEMDNRYEGLEVISPTEFEVVLYLNQMGVFNFVDDGSLPGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRSRFQTLVAQAVDKCSYRDVVKMVADTSEVKLRIRDRYVVQITPAFKCTGIWPRSAAHWPLPHIPWPGPNRVAEVKAEGFNLLSKECHSLAGKQSSAESDAWVLQFAEAENRLQMGGCRKKCLSILKTLRDRHLELPGQPLNNYHMKTLVSYECEKHPRESDWDESCLGDRLNGILLQLISCLQCRRCPHYF... | Function: Putative nucleotidyltransferase required for several aspects of embryonic development including normal development of the eye . It is unclear whether it displays nucleotidyltransferase activity in vivo . Binds single-stranded RNA (ssRNA) .
Sequence Mass (Da): 40956
Sequence Length: 359
Domain: While it shares... |
Q9XTF3 | MAALASFTRNSRSYGQQPIDVTQQGQRDRSVMSLDAQGRSVSHECPTSTTLVRQLYLPQIPQSASFAAAPTSFSGASSSSSNHHHPVYHSQNSLPPNLLGSSQNSASSNSLVQGHRNPALGSGNTLTRSYHQPSSTNSSTNNLYGPLGTISRDLKQSIRDISPPVINSSANPHLVNYVQTSSFDNGSYEFPSGQAQQQRRLGGSQQHLAPLQQTASSLYSNPQSSSSQLLGQQQAVRPNYAYQQSLPRQQHINSHQTQAFFGTVRGPTNSTNIVTPLRASKTMIDVLAPVRDTVAAQATGLPNVGTSSSNGSSNSSSGVG... | Function: Required for oocyte-to-zygote transition in which it phosphorylates oocyte proteins, including mei-1, oma-1, oma-2, mex-5, and mex-6, modifying their activity and/or stability following meiosis . Through phosphorylation of P granule components including meg-1, promotes the disassembly of zygotic P granules in... |
W7MLD5 | MLTSPLRQDHLVPETLMADASPIIRPETPPDLHIPDSQATVKVSIIDTTSYMSNFPMWAFLDPLMPGHEEMKGCDFSFIIEHPKSGNKYDTLLFDLGVRKDWENLPTPFVQGIKAGGCKIEVQKDVATILKDNGRDLSEVGGIIWSHWHFDHVGDAQTFPGTTDVIVGPGFKKAHVPAWPTDPESHIDEKAWQGRTLREIDFAAEEGKGLKIGQFDALDFYGDGSFYVLNTPGHTIGHLSALARTTVDPPTFIFMGGDIAHQGGEFRPTPYMPLPAEISPNPFNRILPRPALTCPGEIFVEIHRNKSRTEPFFDPTTAEG... | Function: Gamma-lactamase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-b... |
P19999 | MLLLPLLVLLCVVSVSSSGSQTCEETLKTCSVIACGRDGRDGPKGEKGEPGQGLRGLQGPPGKLGPPGSVGAPGSQGPKGQKGDRGDSRAIEVKLANMEAEINTLKSKLELTNKLHAFSMGKKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA | Function: Calcium-dependent lectin . Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway . Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not ... |
O02659 | MSLFTSLPFLLLTAVTASCADTETENCENIRKTCPVIACGPPGINGIPGKDGRDGAKGEKGEPGQGLRGSQGPPGKMGPQGTPGIPGIPGPIGQKGDPGENMGDYIRLATSERATLQSELNQIKNWLIFSLGKRVGKKAFFTNGKKMPFNEVKTLCAQFQGRVATPMNAEENRALKDLVTEEAFLGITDQETEGKFVDLTGKGVTYQNWNDGEPNNASPGEHCVTLLSDGTWNDIACSASFLTVCEFSL | Function: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating ... |
P11226 | MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI | Function: Calcium-dependent lectin involved in innate immune defense . Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating... |
P41317 | MSIFTSFLLLCVVTVVYAETLTEGVQNSCPVVTCSSPGLNGFPGKDGRDGAKGEKGEPGQGLRGLQGPPGKVGPTGPPGNPGLKGAVGPKGDRGDRAEFDTSEIDSEIAALRSELRALRNWVLFSLSEKVGKKYFVSSVKKMSLDRVKALCSEFQGSVATPRNAEENSAIQKVAKDIAYLGITDVRVEGSFEDLTGNRVRYTNWNDGEPNNTGDGEDCVVILGNGKWNDVPCSDSFLAICEFSD | Function: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating ... |
P33032 | MNSSFHLHFLDLNLNATEGNLSGPNVKNKSSPCEDMGIAVEVFLTLGVISLLENILVIGAIVKNKNLHSPMYFFVCSLAVADMLVSMSSAWETITIYLLNNKHLVIADAFVRHIDNVFDSMICISVVASMCSLLAIAVDRYVTIFYALRYHHIMTARRSGAIIAGIWAFCTGCGIVFILYSESTYVILCLISMFFAMLFLLVSLYIHMFLLARTHVKRIAALPGASSARQRTSMQGAVTVTMLLGVFTVCWAPFFLHLTLMLSCPQNLYCSRFMSHFNMYLILIMCNSVMDPLIYAFRSQEMRKTFKEIICCRGFRIACS... | Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36601
Sequen... |
Q9MZV8 | FLDLQLNATEGNVSGPSVGNTSSPCEDMGIEVEVFLTLGLISLLENILVIGAIARNKNLHVPMYFFVCSLAVADMLVSLSNSWETITIYLIANKHLVLSDTSVRHLDNVFDSMICISLVASMCSLLAVAVDRYVTIFYALRYQHLMTGRRCGAIIAGIWALCTGCGPVFIVYYESTYVVVCLVAMFLTMLLLMASLYAHMFLQARAHVRRIAALPGYRSARQRTSMKGAVTLAMLLGVFIVCWAPFFLHLILMISCPQNLYCSCFMSHFNMYLILIMCNSVIDPLIYAFRSQEK | Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. This receptor is a possible mediator of the immunomodulation properties of melanocortins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32753
Sequen... |
A3GEV2 | MSSNTDAEIQLLQSIKEKAAAAGTQNSAASTSGSSSDSKITRESSAFSRREITNDVPIVSSAYSEVKEAPAWVKKDTPVDKYDKYGSRPAVSTSSGPSRVSRPESESTDNKYSKYISRAAEPSTRVKRSREEFEREEPDPREYGNSRIEQEKDDDGGAAIPYSNLDVSNQSYDHRTLQSREYYTFQSHISNKEERDINSIVRTHYNQRAVHSKRQVRKNSPIIKMRNFNNAIKYMLLGNYSKREQGVDRPFTFLDLCCGKGGDLNKCQFLEIDQYIGIDISDVSVKEAFQRYSQKKVRFRSAYGQKPRKDELRYDFEACF... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 60455
Sequence Length: 531
... |
O74880 | MSSSNSRVHEEQPPTENRRYARPTAQMNRVIEQQPRRRDYFQNNDNSGRRGYNRHENNGNAQDVVRSHYNARPDLGYKKRQFSPIIQLKRFNNWIKSVLIQKFAPHASDYPILVLDMGCGKGGDLIKWDKAGIDGYIGIDIAEVSVNQAKKRYREMHASFDALFYAGDCFSSSINELLPPDQRKFDVVSLQFCMHYAFESEEKVRVLLGNVSKCLPRGGVMIGTIPNSDVIVKHIKMLKPGEKEWGNDIYKVRFPESPPRSFRPPYGIQYYFYLEDAVTDVPEYVVPFEAFRAVAEGYNLELIWVKPFLDILNEEKNSET... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41441
Sequence Length: 360
... |
Q9I8S2 | MDHVLNPEEKVSQTNSESGGADGAFQHVKGEHSSPKLSASEKSLPGNTKSPLKRKAAEPDSPPKRPRLEEGHGSLVVTHYNELPETGLEIRSQSRIFHLRNFNNWMKSALIGEFVEKVQQRTRNITVLDLGCGKGGDLLKWRKGGISKLVCTDIADVSVKQCEQRYKDMKRKSRNERIFEAEFLTSDSTKELLSEKYIDPEIKFDICSCQFVYHYSFETYEQADTMLRNACERLCPGGFFIGTTPDGFELVKRLEASDTNSFGNDVYTVTFEKKGKYPLFGCKYDFSLEEVVNVPEFLVYFPVLVEMAKKYQMKLIYKKT... | Function: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine =... |
Q28FT4 | MDNILNPEDNVSQTNTETDVTDGPFQYVKEEHSSHKFTASGQNLDSPPKNKKSPLKRKAGEPESPSKRPRLEEGHGSLVVTHYNELPETGLETRSQSRIFHLRNFNNWMKSALIGEFVEKVRQRTRNIAVLDLGCGKGGDLLKWRKGGISKLVCTDIADVSVKQCEERYKDLKRKSRNERVFEAEFLTADSTKELLSEKYNDPEIKFDICSCQFVYHYSFETYEQADMMLRNACERLCPGGFFIGTTPDGFELVKRLEASDTNSFGNDVYTVKFEKKGKYPLFGCKYDFSLEEVVNVPEFLVYFPVLVEMAKKYQMKLIY... | Function: Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine =... |
Q6CC11 | MYDPARDCYQAEGESADARDAAEIAGGEFLADSATPETKSDSTKSDGNDPKQETSETKRPAYNYLPKIARKETTSGSRDAASAKPQLKRREREDVRVAGDRVAPRADMGSYVDYSEKESRERQDRDRDSRDHRDRDRDRDRGRDRYDSRDRDRYDSRDRPRDYDSRDRDRDRDRDRYDDRVRDYDSRERDRYDDRARDYDRGSRDSRDYRDRHDRERERYDSGNSRETRDVRESRERSLSPTREPKPHDPAAPAPSKQKRPSQRGGREAAAARAAQYRAEMEKREARAQAAAQQGDQVGDSLVRNHYNQAPERGVVARQS... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 70281
Sequence Length: 609
... |
P32783 | MSTKPEKPIWMSQEDYDRQYGSITGDESSTVSKKDSKVTANAPGDGNGSLPVLQSSSILTSKVSDLPIEAESGFKIQKRRHERYDQEERLRKQRAQKLREEQLKRHEIEMTANRSINVDQIVREHYNERTIIANRAKRNLSPIIKLRNFNNAIKYMLIDKYTKPGDVVLELGCGKGGDLRKYGAAGISQFIGIDISNASIQEAHKRYRSMRNLDYQVVLITGDCFGESLGVAVEPFPDCRFPCDIVSTQFCLHYAFETEEKARRALLNVAKSLKIGGHFFGTIPDSEFIRYKLNKFPKEVEKPSWGNSIYKVTFENNSYQ... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50341
Sequence Length: 436
... |
P32094 | MASLDNLVARYQRCFNDQSLKNSTIELEIRFQQINFLLFKTVYEALVAQEIPSTISHSIRCIKKVHHENHCREKILPSENLYFKKQPLMFFKFSEPASLGCKVSLAIEQPIRKFILDSSVLVRLKNRTTFRVSELWKIELTIVKQLMGSEVSAKLAAFKTLLFDTPEQQTTKNMMTLINPDDEYLYEIEIEYTGKPESLTAADVIKIKNTVLTLISPNHLMLTAYHQAIEFIASHILSSEILLARIKSGKWGLKRLLPQVKSMTKADYMKFYPPVGYYVTDKADGIRGIAVIQDTQIYVVADQLYSLGTTGIEPLKPTIL... | Function: Probably catalyzes the second reaction in the mRNA cap formation pathway (Probable). Forms a covalent complex with GTP .
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
Sequence Mass (Da): 99969
Sequence Length: 868
Domain: Th... |
P32354 | MNDPREILAVDPYNNITSDEEDEQAIARELEFMERKRQALVERLKRKQEFKKPQDPNFEAIEVPQSPTKNRVKVGSHNATQQGTKFEGSNINEVRLSQLQQQPKPPASTTTYFMEKFQNAKKNEDKQIAKFESMMNARVHTFSTDEKKYVPIITNELESFSNLWVKKRYIPEDDLKRALHEIKILRLGKLFAKIRPPKFQEPEYANWATVGLISHKSDIKFTSSEKPVKFFMFTITDFQHTLDVYIFGKKGVERYYNLRLGDVIAILNPEVLPWRPSGRGNFIKSFNLRISHDFKCILEIGSSRDLGWCPIVNKKTHKKC... | Function: Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as a key coordinator in assembling the replication fork. Proposed to fun... |
Q9LPD9 | MAGENSDNEPSSPASPSSAGFNTDQLPISTSQNSENFSDEEEAAVDTQVIRDEPDEAEDEEEEEGEDLFNDTFMNDYRKMDENDQYESNGIDDSVDDERDLGQAMLDRRAADADLDARENRLANRKLPHLLHDNDSDDWNYRPSKRSRTTVPPRGNGGDPDGNPPSSPGVSQPDISMTDQTDDYQDEDDNDDEAEFEMYRIQGTLREWVMRDEVRRFIAKKFKDFLLTYVKPKNENGDIEYVRLINEMVSANKCSLEIDYKEFIHVHPNIAIWLADAPQPVLEVMEEVSEKVIFDLHPNYKNIHTKIYVRVTNLPVNDQI... | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. May play a crucial role in the control of de-differentiation and cell proliferation processes... |
P49735 | MDNPSSPPPNTPSDAAERRDLRAAMTSPVGDFEPFENEDEILGDQTVRDEAEEEDGEELFGDNMENDYRPMPELDHYDPALLDDEDDFSEMSQGDRFAAESEMRRRDRAAGIHRDDRDLGFGQSDDEDDVGPRAKRRAGEKAAVGEVEDTEMVESIENLEDTKGHSTKEWVSMLGPRTEIANRFQSFLRTFVDERGAYTYRDRIRRMCEQNMSSFVVSYTDLANKEHVLAYFLPEAPFQMLEIFDKVAKDMVLSIFPTYERVTTEIHVRISELPLIEELRTFRKLHLNQLVRTLGVVTATTGVLPQLSVIKYDCVKCGYV... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
P49736 | MAESSESFTMASSPAQRRRGNDPLTSSPGRSSRRTDALTSSPGRDLPPFEDESEGLLGTEGPLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRQVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLP... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
P97310 | MAESSESLSASSPARQRRRISDPLTSSPGRSSRRADALTSSPGRDLPPFEDESEGLLGTEGPMEEEEDGEELIGDGMERDYRPIPELDVYEAEGLALDDEDVEELTASQREAAERTMRQRDREAGRGLGRMRRGLLYDSSEEDEERPARKRRHVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLP... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
B8BKI8 | MDDSENNAPSTPGSPGFSTDRLPPNTTTSRGATDPSSYSDDDDDDVVGAEEAEVDPNVLPEDDGVVAAEEEEDGEDLFNDNYLDDYRRMDEQDQYESVGLDDSIEDERNLDEIMADRRAAEAELDARDVRTGAAPDRKLPRMLHDQDTDEDMSFRRPKRHRANFRPPREPRTPRSDDDGDGATPSSPGRSQRGMYSGGDVPMTDQTDDDPYEDEFDEEDEMNMYRVQGTLREWVTRDEVRRFIAKKFKEFLLTYVNPKNEQGEFEYVRLINEMVLANKCSLEIDYKQFIYIHPNIAIWLADAPQSVIEVMEEVAKNVVFD... | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 108839
Sequence Le... |
Q2R482 | MDDSENNAPSTPGSPGFSTDRLPPNTTTSRGATDPSSYSDDDDDDVVGAEEAEVDPNVLPEDDGVVAAEEEEDGEDLFNDNYLDDYRRMDEQDQYESVGLDDSIEDERNLDEIMADRRAAEAELDARDVRTGAAPDRKLPRMLHDQDTDEDMSFRRPKRHRANFRPPREPRTPRSDDDGDGATPSSPGRSQRGMYSGGDVPMTDQTDDDPYEDEFDEEDEMNMYRVQGTLREWVTRDEVRRFIAKKFKEFLLTYVNPKNEQGEFEYVRLINEMVLANKCSLEIDYKQFIYIHPNIAIWLADAPQSVLEVMEEVAKNVVFD... | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. Can complement the fission yeast mcm2 mutant.
Catalytic Activity: ATP + H2O = ADP + H(+) + ph... |
P40377 | MDSFRKRGRRDSESLPFESENSSLGATPLSLPPSSPPPEFSDEAAEALVEEDIEDLDGEALDVEDEEGEDLFGEGMERDYQQNLELDRYDIEELDDDNDLEELDIGARRAVDARLRRRDIELDAAAGRTKPAAFLQDEDDDLDSNLGTGFTRHRHRIYDEYSPNVGALDESGELPLESIADVKADSIAEWVTLDPVRRTIAREFKNFLLEYTDENGTSVYGNRIRTLGEVNAESLMVNYAHLGESKPILAYFLANAPAPIFRIFDRVALEATLLHYPDYERIHSDIHVRITNLPTCFTLRDLRQSHLNCLVRVSGVVTRR... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P55861 | MADSSESFNIATSPRAGSRRDALTSSPGRDLPPFEDESEGMFGDGVVPEEEEDGEELIGDAMERDYRPISELDRYEVEGLDDEEDVEDLTASQREAAEQSMRMRDREMGRELGRMRRGLLYDSDEEEEDRPARKRRMAERAAEGAPEEDEEMIESIENLEDMKGHTVREWVSMAATRLEIYHRFKNFLRTHVDEHGHNVFKEKISDMCKENKESLPVNYEDLAAREHVLAYFLPEAPAEMLKIFDEAAKEVVLVMYPKYDRIAREIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTCCTGVLPQLSMVKYNCNKCNFI... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
P29469 | MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPDIDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERDRLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREELTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSESLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDFPTIYSLRELRESNLSSLVRV... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P49739 | MDYGGGFEDHELREAQREYLDFLDDDQDQGLYHGKVRDMIGSNEHRLIVNLNDVRRKNDKRANLMLNDAFAETIAFQRALKDLVASIDATYAKQFEEFSVGFEGSFGSKHVSPRTLTASLLGSLVCVEGIVTKCSLVRPKVMRSVHYCPATKKTLERKYSDLTSLEAFPSSSIYPTKDEENNPLETEYGLSTYKDHQTLSIQEMPEKAPAGQLPRSVDIIADDDLVDKCKPGDRVQIVGIYRCLPSKQGGFTSGTFRTILLANNIKLMSKEIAPTFSADDVAKIKKFCKAHSKDIFEHLSKSLAPSIHGHEYIKKAILCM... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
Q7ZXZ0 | MAAVTELDDQEMREAQREYLDFLDDEEDQGIYQSKVRDMISENQYRLIVNINDLRRKNEKRASLLMNNAFEGLIAFQRALKDFVASIDGTYAKQYEDFYIGLEGSFGSKHVTPRTLTSRFLSSVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERKYTDLTSLEAFPSSAVYPTKDEENNPLETEYGLSIYKDHQTITIQEMPEKAPAGQLPRSVDIILDDDLVDKVKPGDRVQVIGTYRCLPSKQNGYTSASFRTILIACNVIQMSKEVTPVFSADDLAKIKKFSKSHSKDVFEQLSRSLAPSIHGHSYIKKAILCM... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
Q8THG6 | MEVVVDVGGNPGVDCKGFCKYCYFKKVKDIQPLGCKYCLPFKKGCDYCTRSVKESYSGFKSLQMVLEETANKLYFTSGEVKKFTVSGGGDLSCYPELKSLITFLSQFNTPIHLGYTSGKGFSKPDDALFYIDNGVTEVSFTVFATDPALRAEYMKDPEPEASIQVLRDFCTHCEVYGAIVLLPGINDGEVLEKTLCDLENMGAKGAILMRFANFQENGLILNNSPIIPGITPHTVSEFTEIVRSSAEKHPSIRITGTPLEDPLIGSPFAIRNVPEALLKLPRVSKKATIITGQVAASRLTEIFEALGGTVNVIPVKKDIG... | Cofactor: Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational me... |
Q58251 | MKEANLLIDLRGEPGINCNGFCKFCYFRKVNKNNPQPFGCRYCQFTVGCDYCMYSVREINGDFIPLPFALMELQSSLLFKRYSKVNLTAGGDVSCYPQLEELCKAINNIGLKIHLGYTSGKGFDNVEIAKNLVDYGVDEVTFSVFSTNPKLRKEWMNDKNAETALKCLRYFCENCEVHCAIIVIPGVNDGEELKKTVSDLVDWGANAVILMRFANSEEQGLILGNAPLIEGIKPHSVEEFKNIVDEIHNEFGDYIRVTGTPLHDPVAGTPFALAKEENSHILERLKDKINGEATIITGNVAYPFLKKIFDETSVNVVKVN... | Cofactor: Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-274' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational me... |
P22948 | AADIFAKFKTSMEVK | Cofactor: Binds 1 coenzyme F430 non-covalently per MCR heterotrimeric complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced, probably to the Ni(I) oxidation state.
Function: Component of the methyl-coenzyme M reductase (MCR) I that ... |
P11558 | MADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKRGIPQYNPDIGTPLGQRVLMPYQVSTTDTYVEGDDLHFVNNAAMQQMWDDIRRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMVETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVGDGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDFAYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPVRVSLDVVATGAMLYDQIWL... | Cofactor: Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid . Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state .
Function: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive... |
P22949 | SDTVDIYDAGKILERVII | Cofactor: Binds 1 coenzyme F430 non-covalently per MCR heterotrimeric complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced, probably to the Ni(I) oxidation state.
Function: Component of the methyl-coenzyme M reductase (MCR) I that ... |
Q1M799 | MTLRHQIIALAIVPLVISILAITTFITWQSANLAKNSIDTFEQNMLKTKEAEILNLTNLALSAIQTIYDKAGSDDEAAKQQVAAILTSLDYGKDGYFFVYDYDGNNIVHPRQSFRHGHNWLDLTDPDGDKVIAELIATAKAGGGLHQYKWQKPSTGQIADKLSFVVSLDKWHWVVGTGVYLDDVFAQSAAANAGMRANIKRTFVIVALIDVPSVLVVFTTCMLLTFHERRMADSRLKALTQRVIDTQEEERARLARELHDGISQNLVGVRYAMDLAGRKVRTNVDDAALTIDRGVEALNGAIKEIRRLSHDLRPRVLDDL... | Function: Member of the two-component regulatory system MctS/MctR, which activates mctP expression.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50713
Sequence Length: 461
Subcellular Location: Cell membrane
EC: 2... |
A8QZJ5 | MVTLYLHVPILLLVVITARAAPKPDTHNPFDELSSVAEKQDLHYGDRSRKDPFIAQNDVGNNFRDGTQENLTKVRSKVNQYDQPFTFKCPLGETIKSIGSIHDNHYEDRQWDIDCKPAGYTMGISTWSPYANDYDGSMNFECNEGSVVTGMSSIHDNYYEDRRYQLMCSYLNNWKRGSCAWTSYTTYDASFVELTPTGKFLVGMKSQHNNYYEDRKFKMLYC | Function: Is potently cytotoxic (EC(50) value 79 ng/mL) towards L1210 mouse leukemia cells, has hemagglutination activity on sheep erythrocytes, and is lethal in crayfish. Has no phospholipase A2 activity.
PTM: Is not glycosylated.
Sequence Mass (Da): 25665
Sequence Length: 222
Subcellular Location: Secreted
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A9WC36 | MKGILHGLRVVEGSAFVAAPLGGMTLAQLGADVIRFDPIGGGLDYKRWPVTLDGKHSLFWAGLNKGKRSIAIDIRHPRGQELLTQLICAPGEHAGLFITNFPARGWLSYDELKRHRADLIMVNLVGRRDGGSEVDYTVNPQLGLPFMTGPVTTPDVVNHVLPAWDIVTGQMIALGLLAAERHRRLTGEGQLVKIALKDVGLAMIGHLGMIAEVMINDTDRPRQGNYLYGAFGRDFETLDGKRVMVVGLTDLQWKALGKATGLTDAFNALGARLGLNMDEEGDRFRARHEIAALLEPWFHARTLAEVRRIFEQHRVTWAPY... | Function: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. This reaction involves an intramolecular CoA transferase that catalyzes the reversible transfer of the CoA moiety from the C1-carboxyl group of mesaconyl-CoA to the C4-carb... |
G0HQ31 | MGALDDLRVLDLTQVLAGPYCTMLLADMGADVVKVERPGGDLIRSNPPFVSDGDEEAYGGYFQSVNRGKRSLELDLGTDEDREAFLSLVERADVVVENFKAGTMEKFDCGYETLREHNPDLIYSSIRGFGDPRTGETHRQGQPSFDLIAQALGGVMEITGQSDGPPTKVGPGVGDLFTAVLNAVGILAAVHHRERTGEGQYVDTAMYDSMVSLCERTVYQYSCDGESPTRQGNSHPTLFPYDSFEAADGHVVIAAFADGHWETLCEAMERPDLAADYPDAGSRIANRESLRREIADWTATIDSETLLDLLEGRVPAAPVQ... | Function: Involved in the methylaspartate cycle. Catalyzes the transfer of the CoA moiety from succinyl-CoA to mesaconate to generate mesaconyl-CoA (2-methylfumaryl-CoA) and succinate . Shows also high activity with methylsuccinate as CoA-acceptor, and only low activity with glutarate, acrylate and itaconate . Cannot u... |
Q1PE15 | MVMMKKLLSNRLFNMSKTASQSLMNCRTSSSSSLAMRTRVPKDIGEATIDPEPGDLTISQRFLNKFSMNGIDTTSKMSIGESLMEKLKEMDMNKDRIRLDGLSHPKEETLGLTVQDVKKLLRAAEIEVIKTKLMETGKIWIRYSDFLGVCSDSSLDPSQGALIAKMLDDSGNVIVMGNSVCLRPHQLTKSIEGLLPLSQIHNPNDPRRKELNELEAIKTVIDQKAHSLVRRELWAGLGYLIIQTAGFMRLTFWDLTWDVMEPICFYVSSVYFMAGYTFFLKTSREPSFQGFYQSRFEAKQRKLMQSEDFDVGRYDELKKL... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
Q9LVR5 | MSSKKSLVQSLFNISKTYSRISGLTRMRPTKSGGIPPDAGDSGIRRRFLHKRAFFSPEIVPKGGNLMEKLRELTLSNNNRIRLDEMLPPPSPKKSSPEFFPAVTVEDVKKLMRAAEMELVKSKLREIGKNWVPYSEFVRVCGEYSSDPEQGNRVANMLDEAGNVIVLGKLVCLKPEELTSAMAGLIPTLEPSLDAETRQEFEQLEIIKSDIDKRADDLVRKELWAGLGLIMAQTVGFFRLTFWELSWDVMEPICFYVTSTYFMAGYAFFLRTSKEPSFEGFYKSRFETKQKRLIKMLDFDIDRFTKLQKMHRPNLTKSGR... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
Q9FJV7 | MALRRAITKRLIDCYRSDVTQQHSFFRQLSPYNMKIHRQYMTSPNGPNLTDRIVGIRIESVSPPRREETPVMGLSVSETKKLLRLYQMEKVKERLREIPKSSVSYWEFIQICCESCGNDEQGSQMAKSLDHSGCVVVLGDIVFLHPHQIAKSMEAMIKQTSVLPNDPRKEELVQLATTKKSIDIEARRIVQAELYCGLGFLAVQTIGFMRLTFWELSWDVMEPICFFVTTIHFILGYIFFLRTSTEPSFEGLFRQRFKTKQKKLMERHGFDFLRYNELNSLFTTFPCKFHYPV | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
F4I111 | MWSMGLIRRTAMSNAIRASSQRTWLGHGGLRSCVTVKTPSEDEEEKKKEITIAEAKKLMRLVNVEDMKKKLVGVADRDVVSYSTLLEASQGMGIARSPDEAHVFARVLDDAGVVLIFRDKVYLHPDKVVDLIRRAMPLDQNPEEDQIKEEFNKLRIMKEEIDVLAHRQVRKILWCGLATSMVQIGLFFRLTFWEFSWDVMEPITFFATATGIIVGYAYFLMTSRDPTYQDFMKRLFLSRQRKLLKSHKFDCERFKELERLFKMTSSCHAAASIRNRVGLELDLEDALQSRRD | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Location Topology: Multi-pass membrane pr... |
Q9NWR8 | MLQRGLWPWRTRLLPTPGTWRPARPWPLPPPPQVLRVKLCGNVKYYQSHHYSTVVPPDEITVIYRHGLPLVTLTLPSRKERCQFVVKPMLSTVGSFLQDLQNEDKGIKTAAIFTADGNMISASTLMDILLMNDFKLVINKIAYDVQCPKREKPSNEHTAEMEHMKSLVHRLFTILHLEESQKKREHHLLEKIDHLKEQLQPLEQVKAGIEAHSEAKTSGLLWAGLALLSIQGGALAWLTWWVYSWDIMEPVTYFITFANSMVFFAYFIVTRQDYTYSAVKSRQFLQFFHKKSKQQHFDVQQYNKLKEDLAKAKESLKQAR... | Function: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenerget... |
Q810S1 | MPGALSGRRMLPSGLCLGRWQLLRTIRARGRGDPRELPSTPQVLCMKLYGNPKYHQALHYGTVEPQDEITVTYKHGLPLVTLTLPSRKERCQFVVKPMLSTVGSFLQDLQNEDKGIKTAAIITADGSEIPASTLMDTLLMTDFKLIINKLRYDIRCHKKEEPSGEHMTELENTKSLVHRLFTILHLEEIQKRRERHLMAKIDHLQEQLRPLEQVKAAIEARSEANTSGLLWAGLALLSVQGGALAWLTWWVYSWDIMEPVTFFLSFANSIVFFAYFIITRQNYTYSSLRSRQFLQFFHKKSQRRCFDVEQYNKLKEDLAE... | Function: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenerget... |
Q89V40 | MERPIRHGAKTKQCRCLGTTELSMSQIDHQVHSIGPEVTGSRIFKFIAFLYGIAAYLVFFVTILYAIGFVMGLVVPKTIDTGTDTSTAEAVIINLLLMALFAVQHSVMARQRFKTWWTQFVSKPIERSTYVLFASLSLLLLFWQWRPLPTVIWEVEDPDLAVTLVTVSFAGWVLVFTSTFIINHFELFGLHQVTNHLVGKEATPPRFKTPLLYKFVRHPIYLGFIVAFWAAPVMTAGHLLFAAVTTIYIFVGIALEERDLIDLFGDEYRQYKQRVSMLIPWRRSV | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32581
Sequence Length: 285
Subcellular Location:... |
Q89I98 | MFARLAILLYAIVSYAAFTVSFLYALGFVGNYVVPKSIDVGSPTNLGEAILVNLLLMSLFAIQHSVMARPAFKRWWAKFLPLACQRSTYVLLSSLILLLLFWQWRPIPTPVWQTSGIAAWLLIGVHWLGWLIAFASTHMIDHFDLFGLRQAFVAFRGTEISGQSFRTPLLYKIVRHPLMLGFLLAFWATPAMTAGHLLFALANTAYILVALQFEERDLIAEFGATYQDYRRRVPMLVPRLFARRRTDDRKSPRPVGAPR | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29478
Sequence Length: 259
Subcellular Location:... |
B1WZQ6 | MQQQQTLSNSFLSRTFVLLYGVFCYFTFLLTCVYAVGFIGNIFLPKSLDSKSQESLVTALLIDVGLLGIFALQHSVMARKQFKAWWTRLIPKPMERSTYVLFSSLALMLVFWQWHPIGITIWNFDNLVGQIIFYSLFALGWVIVLVSTFLINHFDLFGLRQVYLYFEEKEYTPLKFKTPAFYQYVRHPLYVGWFLVFWMTPIMTVAHLVFASVTTIYILVAIQLEEKDLVAIHGEKYENYRRQVPMLIPFIGKKS | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29869
Sequence Length: 255
Subcellular Location:... |
O05883 | MKRYLTIIYGAASYLVFLVAFGYAIGFVGDVVVPRTVDHAIAAPIGQAVVVNLVLLGVFAVQHSVMARQGFKRWWTRFVPPSIERSTYVLLASVALLLLYWQWRTMPAVIWDVRQPAGRVALWALFWLGWATVLTSTFMINHFELFGLRQVYLAWRGKPYTEIGFQAHLLYRWVRHPIMLGFVVAFWATPMMTAGHLLFAIGATGYILVALQFEERDLLAALGDQYRDYRREVSMLLPWPHRHT | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28031
Sequence Length: 244
Subcellular Location:... |
A6VCX3 | MSASIRDAGVADLPGILAIYNDAVGNTTAIWNETPVDLANRQAWFDARARQGYPILVASDAAGEVLGYASYGDWRPFEGFRGTVEHSVYVRDDQRGKGLGVQLLQALIERARAQGLHVMVAAIESGNAASIGLHRRLGFEISGQMPQVGQKFGRWLDLTFMQLNLDPTRSAP | Function: Plays a role in the resistance against the toxic effects of L-methionine sulfoximine (MSX), a rare amino acid, which inhibits glutamine synthetase (GlnA). Catalyzes the acetylation of L-methionine sulfoximine (MSX). It can also use L-methionine sulfone (MSO).
Catalytic Activity: acetyl-CoA + L-methionine sulf... |
A0A0F6P9C0 | MHTRTAPRVRPPSRAAKLAGLLYSLLSYLFFLMTLLYLIGFVGNVGVPKTIDSGPGASWPLALLVDVLLITLFAVQHSVMARKSFKQWWRPVVPAPIERATYVLASSVVLVVMFWLWQPIDLRVWQVESRLGSAVLTTLFWLGWGLILVATFLISHFELFGVKQALDALRPAKPVDGSFRTPLLYKIVRHPMYMGFLMAFWATPEMTVGHLVFALTSTIYILIGTQLEEKDLVEIFGEKYRNYQKNVGMLLPSLRRNPGSQD | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29637
Sequence Length: 262
Subcellular Location:... |
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