ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q977V2 | MVLDNLGSSLRGSLDKLRGKSRLDEDDVQEIVKEIQRSLLSADVDVSLVMDLSDSIKTRALEEEPPGGTSARDHVLKIVYEELVDLIGESTEIPLESQTIMLAGLQGSGKTTTSAKMAWWFSKKGLRPAVIQTDTFRPGAYDQAKQMCERAEVDFYGDPDCDDPVQIAREGLEATEDADVHIVDTAGRHALEDDLIDEIEEIEGVVQPDLNLLVLDAAIGQGAKEQAQQFDESIGIGGVVITKLDGTAKGGGALTAVNETDSSIAFLGMGETVQDIERFEPNGFISRLLGMGDLKQLSERVERAMSETQAEDEDWDPEEM... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
P56005 | MFQALSDGFKNALNKIRFQDDEKALDRALDELKKTLLKNDVHHKVARELLKKVESQTKLNGIGKQQFLDALEKSLLEILSAKGSSGFTFAQTPPTVVLMAGLQGSGKTTTTAKLAHYLKTKNKKVLLCACDLQRLAAVEQLKVLGEQVGVEVFYEENKSVKEIASNALKRAKEAQFDVLLVDSAGRLAIDKELMQELKEVKEILNPHEVLYVADALSGQDGVKSANTFNEEIGVSGVVLSKFDSDSKGGIALGITYQLGLPLRFIGSGEKIPDLDVFVPERIVGRLMGAGDIVSLAEKTASVLNPNEAKDLSKKLKKGQF... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
P61011 | MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIE... | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) . As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory prote... |
Q07955 | MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT | Function: Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5... |
Q01130 | MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS | Function: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with... |
Q5R1W5 | MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKREPKSRSRSKSPPESPEEEGAVSS | Function: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with... |
Q06A98 | MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPASKRESKSRSRSKSPPKSPEEEGAVSS | Function: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with... |
P84103 | MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRSPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK | Function: Splicing factor that specifically promotes exon-inclusion during alternative splicing . Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion... |
Q08170 | MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHARGPRRDGSYGSGRSGYGYRRSGRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLDGTEVNGRKIRLVEDKPGSRRRRSYSRSRSHSRSRSRSRHSRKSRSRSGSSKSSHSKSRSRSRSGSRSRSKSRSRSQSRSRSKKEKSRSPSKEKSRSRSHSAGKSRSKSKDQAEEKIQNNDNVGKPKSRSPSRHKSKSKSRSRSQERRVEEEKRGSVSRG... | Function: Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 56678
Sequence Length: 494
Subcellular Location: Nucleus speckle
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Q8VE97 | MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHARGPRRDGSYGSGRSGYGYRRSGRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLDGTEVNGRKIRLVEDKPGSRRRRSYSRSRSHSRSRSRSRHSRKSRSRSGSSKSSHSKSRSRSRSGSHSRSKSRSRSQSRSRSKKEKSRSPSKDNKSRSRSRSPDKSRSKSKDHAEDKLQNNDSAGKAKSHSPSRHDSKSRSRSQERRAEEERRRSVSRAR... | Function: Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10 (By similarity).
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 55979
Sequence Length: 489
Subcellular Location: Nucleus speckle
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Q13243 | MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHSRSRSRSRSRTRSSSRSRSRSRSRSRKSYSRSRSRSRSRSRSKSRSVSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN | Function: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 31264
Sequence Length: 272
Subcellular Location: Nucleus
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C0H3Y2 | MSGGYSNGFALLVVLFILLIIVGAAYIY | Function: Spore protein involved in the assembly of several components of the spore coat, including CotB, CotG and CotH, and in spore germination.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 2979
Sequence Length: 28
Subcellular Location: Spore coat
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Q9US47 | MTSLIQSIPRYIYESNSLPKLIRSGLDRKSPIGLSLLKRNCRNRSFAANMSTSSKLSTNIKDLSLFDLEEFPARSYIGGKWVTAASGKTFDVENPGLNETLAPVTDMSVEETRKAIKVAHEAFLSYRNSDIKERYAILRRWYDLIMENADDLATMMTLENGKALGDAKGEVVYAAKFIDWFAGEALRISGDSSMSSNPQNRIITIKQPVGVVGIITPWNFPAAMITRKVGAALAAGCTVVIRPAAETPFTALALAKLAERAGVPAGVLNMVTANSPSEHGIELTTNPLIRKVSFTGSTNVGKILAKQSSSTLKKLSLELG... | Catalytic Activity: H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
Sequence Mass (Da): 58834
Sequence Length: 547
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
Subcellular Location: Cytoplasm
EC: 1.2.1.16
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Q9UTM8 | MAPQFKRPELFGFDKSHAQSFVQGKWISSPNNKTFEVDNPATGEIIGKVADVSVEETKKAISAANEAFKTYKNFTHVQRSQLLERWAELIMENKDDLVKMLTLENGKPLSQAEMEVTTCSGYLKWYAAEAVRTFGDVAPSSLQSQNFLISIKQPVGVSALITPWNFPAAMIARKGGAALAAGCTAIFLPAFRTPYVCLGLVRLAQEAGFPDGVLNVITSSDASAHGKELTTNPIVRKVSFTGSTNVGKILMGQSASTIKKVSMELGGNAPFIVFPDFPIDQAVESFCTIKFNSCGQVCVCPNRVYVHKNVYDEFVSKLTE... | Catalytic Activity: H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
Sequence Mass (Da): 53306
Sequence Length: 493
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
Subcellular Location: Cytoplasm
EC: 1.2.1.16
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Q9SAK4 | MVIGAAARVAIGGCRKLISSHTSLLLVSSQCRQMSMDAQSVSEKLRSSGLLRTQGLIGGKWLDSYDNKTIKVNNPATGEIIADVACMGTKETNDAIASSYEAFTSWSRLTAGERSKVLRRWYDLLIAHKEELGQLITLEQGKPLKEAIGEVAYGASFIEYYAEEAKRVYGDIIPPNLSDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALASGCTVVVKPSELTPLTALAAAELALQAGVPPGALNVVMGNAPEIGDALLTSPQVRKITFTGSTAVGKKLMAAAAPTVKKVSLELGGNAPSIVFDDADLDVAVKGTL... | Function: Oxidizes specifically succinate semialdehyde. Involved in plant response to environmental stress by preventing the accumulation of reactive oxygen species, probably by regulating proline, gamma-hydroxybutyrate (GHB) and gamma-aminobutyrate (GABA) levels . Required for the maintenance of the shoot apical meris... |
P51649 | MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSAN... | Function: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Catalytic Activity: H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
Sequence Mass (Da): 57215
Sequence Length: 535
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
Subcellul... |
D0ZVG2 | MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQ... | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues . This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation . Can ubiquitinate ubiquitin, giving rise to pol... |
Q08945 | MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKA... | Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone... |
P97027 | MAVTISIKEKAFVQEGRKNTVLENIELSIAPGEFLTLIGPSGCGKSTLLKIIAGLDSEYDGSVEINGRSVTAPGIQQGFIFQEHRLFPWLTVEQNIAADLNLKDPKVKQKVDELIEIVRLKGSEKAYPRELSGGMSQRVAIARALLREPEVLLLDEPFGALDAFTRKHLQDVLLDIWRKKKTTMILVTHDIDESVYLGNELAILKAKPGKIHKLMPIHLAYPRNRTTPDFQAIRQRVLSEFEKTEDLEYAEGSGI | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system (Probable). Is also involved in taurine transport.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sul... |
Q89ER4 | MQTALRTSLPETELASRASFAPHARVVREERVVQASGLPLSIRGLRKSFGDNEVLRGIDLHIPAGQFVAIVGKSGCGKSTLLRLIAGLDKIDAGTISLGSDVQPEDIRVMFQEPRLLPWARVLANVEVGLGRDRASKDAHARAEKALTEVGLADKRDQWPSVLSGGQKQRVALGRALVSRPRVLAFDEPLGALDALTRISMQRLLERVWRDQGFTAILVTHDVSEAVALADRVLVIEEGRIAHDVVVNAARPRERGSVELAGLEGSILSHLLSADDRT | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q0BFQ0 | MNATTSAAAYGPLAGADLEAELAQARVTDDAVRDAAIVDRDGGASVVPLARRRPGSPAPGDAVTLSGVSKRFGTRTVLDNVELGIARGSFVAIVGRSGCGKSTLLRLVAGLETPSSGALATRGEGGGTLDTRIMYQDARLLPWKTVLQNVMLGLGRGARDRARAVLDEVGLLERANDWPAQLSGGQRQRVALARALVHRPQLLLLDEPLGALDALTRIEMHALIERLWREHRFTALLVTHDVQEAVALGDRILLIEQGRVALDQQVPLDRPRARASAAFAALEDRVLQRVLAGGPGGADQEAAREVDHVRPVGQIRWAV | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q62K56 | MTGTTLAATYGPISGADLEAELAQPRIADGDAQDAAVYERDGGARALPFASGGAPPDGDRADVRRAAGAGDASVRLTRVSKRYGERAVLADVDLSIGRGSFVSIVGRSGCGKSTLLRLVAELETPSAGTLVKRGDGGGALDTRIMYQEARLLPWKTVLQNVMLGLGRRAKDDARAVLDEVGLLARANDWPAQLSGGQRQRVALARALVHRPQLLLLDEPLGALDALTRIEMHALIERLWREHRFTALLVTHDVQEAVALADRVLLIEAGRIAFDQRVPLDRPRARASAAFAALEDRVLQRVLTGSDAAPAAPNAAGPEGA... | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q8NR42 | MTATLSLKPAATVRGLRKSYGTKEVLQGIDLTINCGEVTALIGRSGSGKSTILRVLAGLSKEHSGSVEISGNPAVAFQEPRLLPWKTVLDNVTFGLNRTDISWSEAQERASALLAEVKLPDSDAAWPLTLSGGQAQRVSLARALISEPELLLLDEPFGALDALTRLTAQDLLLKTVNTRNLGVLLVTHDVSEAIALADHVLLLDDGAITHSLTVDIPGDRRTHPSFASYTAQLLEWLEITTPA | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system (Probable). Is also involved in taurine transport. Seems to not be involved in long chain aliphatic sulfonates transport (chain length of eight carbon atoms or more).
Cat... |
Q0K9I2 | MQMYPVEQAALVELEAGLARREAAQPAAEAPRKAGGVALHVRQVVKRYDGREVLHNVALDVAPGEFLAIVGRSGCGKSTLLRLVAGLEAADGGSITVDGESAAKGRARHADVRVMFQDARLLPWKRVLDNVALGLPRTRRGEAADVLAQVGLADRAREWPARLSGGQRQRVALARALVHHPQLLLLDEPLGALDALTRIEMQGLIESLWRRLGFTALLVTHDVSEAVALADRIVLIEDGRIAMDERVALARPRERGAAGFAQLEAAVLKRVMRQAPQAQVPSHAGAHADPAATTAPLNVSWAA | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q46ZU5 | MQSNPVEQAALAYAGTRLKQTDAPLSAETQPGGVALHVQQVIKRYDGREVLHRIELTAAPGEFVAIVGRSGCGKSTLLRLVAGLECADEGAITLDAQPARTLQQDIRVMFQDSRLLPWKRVLENVALGLPRERREEAAAVLAQVGLRDRADAWPARLSGGQRQRVALARSLVHHPRLLLLDEPLGALDALTRIEMQGLIESLWRRLGFTALLVTHDVSEAVALADRIVLIEDGHIAMDERVALPRPRQHGSAAFAQIEERVLRRVMQHTPDAEGVSQSEQEATADWSLVRTVESVRFAV | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q8RLB6 | MNRPSLAGAVHLHGFSRSFHGKQVLDDLGLDIAPGQFVALLGESGSGKTTLLRALAGLDVEARSSGTAVAHGNVSVLFQDSRLLPWLTVLDNLTLGLDAQAVRPAAAQLLREVGLADKAAAWPASLSGGQKQRAALARSLLREPHVLLADEPFGALDALTRLRMQGLLRRMVERVRPTVILVTHDVDESLLLADRILVLRDGKIAEDHALDLAHPRRPDHPAFMQLRATLLRSLGVEAEFV | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q9XX85 | MLLFQKTLSRVAAPISVAANLILILLIIFKSPAQMGNYKYLLIGLSIFEMSYAVLDVVSETTVLSIKKSFVVVVPYKDRSFGQETAMDINLIYCGFFGFSMGMFVVIFAYRSFLTTGNTILRKFEGFKIISWFAYPLFYAIVWILVAWGPLASFPEMDIVVRPFLLDELNMTVDEVAYTGRLFYSTIDNSLRYSAILTGVLQWVLTASSLFLVIFFGLRCYFHYGKLVQLTDVQSIRLRQLQNQLFLALVCQATVPLILMHIPVTILYTCCVLNIVFNPFSVATTIALFPAIDPLPTIFIVKNYRVALFEFVCPSCLCWS... | Function: Probable G-protein coupled receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38992
Sequence Length: 344
Subcellular Location: Cell membrane
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Q06520 | MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVVDKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol an... |
O00204 | MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPD... | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol . Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) . Preferentially sul... |
Q7ZUS4 | MEIPDFSSMKLDSRPELIDFEGVSMTRYFTDNWEKVKNFQARPDDILIATYPKAGTTWVSYILDLLYFGNESPERQTSQPIYMRVPFLEMCFQGLPLGTELADTLPTSPRPIKTHLPVQLVPKSFWEQNSKVVYVARNAKDNAVSYFHFDRMNMGQPEPGDWNTFLQKFMDGRNVFGPWYDHVNGYWKKKQTYSNILYMFYEDMVEDTGREVARLCSFLGLSTSATERERITKGVQFDVMKQNKMTNYSTLPVMDFKISPFMRKGKVGDWRNHFTVAQNEQFDEVYKQKMKNTTVKFRTEI | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a variety of xenobiotic and endogenous compounds, including 2-naphthol, hydroxychlorobiphenyls, T3 (triiodo-L-thyronine), T4 (thyroxine), estrone and DOPA.
Sequence Mass (Da): 35364
S... |
Q8WU08 | MGANTSRKPPVFDENEDVNFDHFEILRAIGKGSFGKVCIVQKNDTKKMYAMKYMNKQKCVERNEVRNVFKELQIMQGLEHPFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVHFKEETVKLFICELVMALDYLQNQRIIHRDMKPDNILLDEHGHVHITDFNIAAMLPRETQITTMAGTKPYMAPEMFSSRKGAGYSFAVDWWSLGVTAYELLRGRRPYHIRSSTSSKEIVHTFETTVVTYPSAWSQEMVSLLKKLLEPNPDQRFSQLSDVQNFPYMNDINWDAVFQKRLIPGFIPNKGRLNCDPTFELEEMILES... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 46369
Sequence Length: 396
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q12608 | MISQICNEVIGLVPKKEEPGWLSVTGHPGAVYCENSISSGPEATGADVSQAIRIAYFTPLKHIPGPWYASLTGLRLSWSVFANNRIHYVHSLHQKYGPIVRIGPQEIDVADPVAGREIHRMGSGFMKAPFYELLSPGPVDNIFNFRDPKLHAARRKLYARGFTLQSLRNEWEPKVRDIIKLTVEKIKCDAVKGEAEIMGWWTLMANEIVCQLTFGGGAGIVAKGVKEPFVLMLERRMGDLAHLLKHFAPPGYYLGRALAWFIPPLQDIFYSQERMFAAGGDVVSRAREAKKAQAEPRNLFNKALEAGNLTDTDIITDAGA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in the biosynthesis of sterigmatocystin is the production ... |
Q00668 | MLLKSIQNIVCGLVPTFFLFGSAAAELDFEQWHPAGLGDLRCGCPAMNSLANHGFINHNGSNITVNEVIPLMQEVFHLSEELATIVTGLAVLSADDPASGIFNLDMLNRHNIFEHDASLTRKDFYLGGDGHTIDQPTLDEFLSYFDGKEWIDLNDAAAARYARVLDSREKNPSFLYQDQQLITSYGETIKYFRTMVDPRSNKTSAEFVRILFTEERLPVREGWQRPREEISGFSLASDVVQLALRTPEKFIGMPFDQRPFAEQAFDPLPWQRPPIWTPPNYPGFSKRHFSELVGRFAKKALPFRA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Peroxidase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in t... |
O87278 | MPNDPLLQPYQLKHLTLRNRIIVTAHEPAYPEDGMPKERYRAYTVERARGGVAMTMTAGSAAVSKDSPPVFNNLLAYRDEIVPWIREMTDAVHEEGAVIMIQLTHLGRRTRWDKGDWLPVVAPSHHREAAHRAFPKKIEDWDIDRIIKDFADAAERMKAGGMDGVELEAYGHLIDQFASPLTNELDGPYGGSLDNRMRFCFDVLKAIRARVGDEFILGVRYTADECLPGGTDKAEGLEISKRLKESGLIDYLNIIRGHIDTDPGLTDVIPIQGMANSPHLDFAGEIRAATNFPTFHAAKIPDVATARHAIASGKVDMVGM... | Function: Possible NADH-dependent oxidase, functions as a demethylase that converts N-methylproline to proline.
Sequence Mass (Da): 74684
Sequence Length: 678
Pathway: Amine and polyamine degradation; stachydrine degradation.
EC: 1.-.-.-
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O82882 | MNTKMNERWRTPMKLKYLSCTILAPLAIGVFSATAADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAKDK... | Cofactor: Binds 1 zinc ion per subunit. Does not contain structural calcium, which is often associated with other metalloproteases.
Function: Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glyc... |
Q00675 | MQGWKTIVGKLMSRYDFPLPDLSVQAEDKILGGVPTRIYTPPDVADPPLALYFHAGGWVMGSIDEEDGFVRTLCKLARTRIFSVGYRLAPEFRFPMALDDCLTVARSVLETYPVQSICFIGASAGGNMAFSTALTLVSDGLGDRVQGVVALAPVTVHPDSVSADNRDRGEYTSYEENDRLTINTGSAMRSFFDCYGAPPDDPRLSCLLHPGLGKLNKVYMAVGDADTLRDDVRLMRDALVALEVPVKCDEYPGYPHFSWLFPSPALREHQALFFGNLLSGICWVCE | Function: Esterase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the f... |
Q00707 | MAFLSLPILTALGAVVYVLFQLVYNLYFHPLRDYPGPLLWRASSLPWKLTLLRGTMHHDLMRHHQTYGDTVRIKPDEISYANGQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTRNHARFRSLFGHAFSDKGLRAQEPTIARYADLLVEVLREVADTGKSVEMVRYFNMAIFDSIGALSFGESFDSLRNRELHPWVDTIHKNLKSVAISHVLRSMGVEFLAPYLMPAELRGKRQENYTYAIEKLKKRMQKTGDQGDFWDRVIVKSADGNQSGDGMSYGEMINNAAVMVVAGSETTSSALCGCTYLLCKFDKMD... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in the biosynthesis of sterigmatocystin is the production ... |
P9WEP8 | MPQHPKHMKSLGHLMALQRPTVWVDHFPVLEQLGEPPNPDKTLMVDIGGGFGQQSKALRSRCPNVEGKIIVQDMPQTLASAEPAEGVEFSEHDFFQPQPVKGAKFYYLRHVLHDWPDEQCVQILQQVIPAMAPESRILIDEVVIPVTGVPWQAAFMDLLMMESFASIERTRAEWEALMDKAGLKIIEEYYYDGKEQAILVVIPK | Function: Norsolorinic acid reductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in the biosynthesis of sterigmatocystin is the production of... |
Q00713 | MPSYAVLGATGNTGRAIVQVLLDRADTDTRIHICAYCRSKEKLFRVCPAAETSKSLSVFQGRLDDDSLIDECLRGTDAVFLVVAIVDNMPGCTVAMQTAEAVVASLQRLRATDPAIRLPRLVILSSASLEPTFCNDVPAPVHWVLKTAVSHLYRDLAAAEAYLRAQSDWLSATFVKPGGLVHDQARGHKVCLDRAQTPLSFLDLAAGMVEVADADDGRYHMRSVSVVPASRVAIFPWDGVYYTFTGLLFHFCPWTYRFLGEYKLQSRKERDKQA | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by... |
A1KM51 | MREYDIVVIGSGPGGQKAAIASAKLGKSVAIVERGRMLGGVCVNTGTIPSKTLREAVLYLTGMNQRELYGASYRVKDRITPADLLARTQHVIGKEVDVVRNQLMRNRVDLIVGHGRFIDPHTILVEDQARREKTTVTGDYIIIATGTRPARPSGVEFDEERVLDSDGILDLKSLPSSMVVVGAGVIGIEYASMFAALGTKVTVVEKRDNMLDFCDPEVVEALKFHLRDLAVTFRFGEEVTAVDVGSAGTVTTLASGKQIPAETVMYSAGRQGQTDHLDLHNAGLEVQGRGRIFVDDRFQTKVDHIYAVGDVIGFPALAAT... | Cofactor: Binds 1 FAD per subunit.
Function: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
Catalytic Activity: NAD(+) + NADPH = NADH + NADP(+)
Sequence Mass (Da): 50754
Sequence Length: 468
Subcellular Location: Cytoplasm
EC: 1.6.1... |
Q58CP9 | MDVCARLALWLLWGLLLHHGQSLSQSHSEKATGSGANSEESTAAEFCRIDKPLCHSEDEKLSFDAVRSIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELE... | Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activa... |
G5EF60 | MGRVSWIIALYLTINVVIVVNGDRVTRNVEVTAEEEKIRDKLGYEAIRDIHRDMDDDHSGSIDRNESTGFMKEDMQMRGSERTRRENKFHGDDDAITVDDLWEAWFESIERTWTNERLVEWLINDVNLPSIVEAVKAKKIDGKILPRFASPNSDFLNKELGIKSSVYRQKLRLNSLDVVLFGYKDNNNRTKDILLAFLALLLTSLIFLYVRQKQKAQQKVNELSNKLTELKCMETEFEDVQKMLNDERSKRSISDGVVNHTEMENLRVQLEEAERRLEANSNGSQAPLALQPLLRRTCENEMAFLEKQRQDCFKEMKEAI... | Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor which upon Ca(2+) depletion, activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, orai-1. Essential for Ca (2+) and IP3-dependent contractile... |
Q13586 | MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEE... | Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores . Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activ... |
Q9P246 | MLVLGLLVAGAADGCELVPRHLRGRRATGSAATAASSPAAAAGDSPALMTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVEESDEFIREDMKYKDATNKHSHLHREDKHITIEDLWKRWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTVSIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQY... | Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and en... |
P83093 | MLLFGLLVAGVADGCDLVPRHLRGRRASGSAGAAASPSAAAAGERQALLTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQY... | Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and en... |
Q86TL2 | MQGPAGNASRGLPGGPPSTVASGAGRCESGALMHSFGIFLQGLLGVVAFSTLMLKRFREPKHERRPWRIWFLDTSKQAIGMLFIHFANVYLADLTEEDPCSLYLINFLLDATVGMLLIYVGVRAVSVLVEWQQWESLRFGEYGDPLQCGAWVGQCALYIVIMIFEKSVVFIVLLILQWKKVALLNPIENPDLKLAIVMLIVPFFVNALMFWVVDNFLMRKGKTKAKLEERGANQDSRNGSKVRYRRAASHEESESEILISADDEMEESDVEEDLRRLTPLKPVKKKKHRFGLPV | Function: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the endoplasmic reticulum (ER) and plasma membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical ER . SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores . Acts by interacting with ... |
Q3UF25 | MQGPGGNVSRGLPSGPASTVASGAGRCESGALMHSFGIFLQGLLGVVAFSTLMLKRFREPKHERRPWRIWFLDTSKQAIGMLFIHFANVYLADLTEEDPCSLYLINFLLDATVGMLLIYVGVRAVGVLVEWQQWESLRFGEYGDPLQCGAWVGQCALYIVIMIFEKSVVFIVLLILQWKKVALLNPIENPDLKLAIVMLIVPFFVNAFMFWVVDNFLMRKGKTKAKLEERGANQDSRNGSKVRYRRAASHEESESEILISADDEMEESDAEEDLRRPVKKKHRFGLPV | Function: Acts as a regulator of store-operated Ca(2+) entry (SOCE) at junctional sites that connect the endoplasmic reticulum (ER) and plasma membrane (PM), called ER-plasma membrane (ER-PM) junction or cortical ER. SOCE is a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts by interacting with ST... |
P83094 | MRKNTIWNYSLIFFCCVLKSISTLDHGPHTVSVDSNRHNTQHQYKQNPNVASQRHSSHESGQSLHNSQSEHVTHIAASHAGSGGEHSTHLAQNLHRSSYNLLSEAMSQAVSNEFSSMGSGSADGACAADDFDCYSGSVQDRFGMEAIASLHRQLDDDDNGNIDLSESDDFLREELKYDSGYEKRQKAFHFNDDMHISVKELWEAWLRSEVHNWTIEQTTDWLAQSVQLPQYVDLFKLHKVTGAALPRLAVNNLQYVGNVLGIKDPIHKQKISLKAMDVVLFGPPRETGTRWKDYILVTLLLSAIIGCWYAYQQNKNAKRH... | Function: Plays a role in mediating Ca(2+) influx following depletion of intracellular Ca(2+) stores.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 64797
Sequence Length: 570
Subcellular Location: Cell membrane
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E1C7U0 | MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYE... | Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered ... |
P0DUE1 | MEKNGAHSFLSDTPVTSLTMSVPVLRHPHVYHAFISYCADADTSHARTILDSVESRGFTCCFAERDFLPGECTSDVVVDAIHCSKNVILVISPASLQSEWSKFEMLMAVDDSHQRNNVCLVPVLLGGVKVDDLPPPLRPLTCIELMDDFRNTDDIIQAISKPEDTWESLLPVGNLAHGFAWGYYYGYLKIILPDLDKTVRQWRRVNNAEGRMSEKLFLFFPQSCRCRDSIADESSLIKHRGHLPIITKDRAGIIERQYKNTIYSVTDDNGEDYFFAGEYIGVIHTMFEMEQNATTGLQTREKYVQSMRFYLTLKRILDTD... | Function: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (By similarity). Binds c-di-AMP, 2'3'-cGAMP, 3'3'-cGAMP and to a lesser extent c-di-GMP. Nucleotide binding has not been seen to stimulate NAD(+) hydrolase activity .
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide... |
Q39228 | MAGGFVSQTPGVRNYNYKLTPKVFVTCFIGAFGGLIFGYDLGISGGVTSMEPFLEEFFPYVYKKMKSAHENEYCRFDSQLLTLFTSSLYVAALVSSLFASTITRVFGRKWSMFLGGFTFFIGSAFNGFAQNIAMLLIGRILLGFGVGFANQSVPVYLSEMAPPNLRGAFNNGFQVAIIFGIVVATIINYFTAQMKGNIGWRISLGLACVPAVMIMIGALILPDTPNSLIERGYTEEAKEMLQSIRGTNEVDEEFQDLIDASEESKQVKHPWKNIMLPRYRPQLIMTCFIPFFQQLTGINVITFYAPVLFQTLGFGSKASL... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, methylglucose, galactose, xylose and mannose, but not fructose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57095
Sequence Length: 514
Subcellular Location: Cell membrane
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Q09821 | AKVSRKPREPRTAVTQSTRRIKRKKTLSKPRSRGGVKAPKTTMKIKRALRRNLRRKIQTSAGQPKKAKKARKHFVSYYVLKKSGQNKKTNQNKRQNQNKRQNQNKRRGQPVPEQEIMEKPTTSCKWCSQGVTRRGRRY | Function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Sequence Mass (Da): 16223
Sequence Length: 138
Domain: The N-terminal half is highly basic.
Subcellular Location: Nucleus
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Q93Y91 | MAGGGLALDVSSAGNIDAKITAAVVMSCIVAASCGLIFGYDIGISGGVTTMKPFLEKFFPSVLKKASEAKTNVYCVYDSQLLTAFTSSLYVAGLVASLVASRLTAAYGRRTTMILGGFTFLFGALINGLAANIAMLISGRILLGFGVGFTNQAAPVYLSEVAPPRWRGAFNIGFSCFISMGVVAANLINYGTDSHRNGWRISLGLAAVPAAIMTVGCLFISDTPSSLLARGKHDEAHTSLLKLRGVENIADVETELAELVRSSQLAIEARAELFMKTILQRRYRPHLVVAVVIPCFQQLTGITVNAFYAPVLFRSVGFGS... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54368
Sequence Length: 506
Subcellular Location: Membrane
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Q9SFG0 | MAVVVSNANAPAFEAKMTVYVFICVMIAAVGGLIFGYDIGISGGVSAMDDFLKEFFPAVWERKKHVHENNYCKYDNQFLQLFTSSLYLAALVASFVASATCSKLGRRPTMQFASIFFLIGVGLTAGAVNLVMLIIGRLFLGFGVGFGNQAVPLFLSEIAPAQLRGGLNIVFQLMVTIGILIANIVNYFTATVHPYGWRIALGGAGIPAVILLFGSLLIIETPTSLIERNKNEEGKEALRKIRGVDDINDEYESIVHACDIASQVKDPYRKLLKPASRPPFIIGMLLQLFQQFTGINAIMFYAPVLFQTVGFGSDAALLSA... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, 3-O-methylglucose, mannose, fructose and galactose, and, to a lower extent, xylose and ribulose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55907
Sequence Length: 507
Subcellular Location: ... |
O04249 | MAGGSFGPTGVAKERAEQYQGKVTSYVIIACLVAAIGGSIFGYDIGISGGVTSMDEFLEEFFHTVYEKKKQAHESNYCKYDNQGLAAFTSSLYLAGLVSTLVASPITRNYGRRASIVCGGISFLIGSGLNAGAVNLAMLLAGRIMLGVGIGFGNQAVPLYLSEVAPTHLRGGLNMMFQLATTIGIFTANMVNYGTQQLKPWGWRLSLGLAAFPALLMTLGGYFLPETPNSLVERGLTERGRRVLVKLRGTENVNAELQDMVDASELANSIKHPFRNILQKRHRPQLVMAICMPMFQILTGINSILFYAPVLFQTMGFGGN... | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55829
Sequence Length: 513
Subcellular Location: Cell membrane
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Q4KMD7 | MELDKDIQTTQKGFHCNLCHVNIPNRPSLEDHVKGKKHLHLLRLRAQRKTQEENSVFVSGFKADTSQTELKEYFQQFGLVTDVIMDKQKGVYAIVEFSESQDVQTTLAQPQHQLNGLKLRVKPREKKEFKLASRGKQDCKNTLISLDKLNFELCKAMSVNEQIQKVVESLELKDNEKKVRDLLVQLLQEVFTEFFPDCQIVPFGSSVNTFGLHSCDLDLFLDLENTKVFQARAKSSEQTGENQSEDCRSEDSILSDIDLSTASPAEILELVAVILRKCVPGVHKVQALSTARLPVVKFSHKELNLQGDITINNRLAVRNT... | Cofactor: Binds 1 divalent cation per subunit.
Function: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF com... |
Q9H6E5 | MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDL... | Cofactor: Binds 1 divalent cation per subunit.
Function: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs . Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1 . In addition to polyadenylation, it is also required for the 3'-e... |
A9JTS5 | MEAEESSSSVVPLPQDVQSVVRGGFRCLLCGVNIPNRPSLTDHLSGRRHVRLHEERDKRNQQQERSVYVSNFPRETSEEQLRDVFQKISPVRNIVMDKDRGLYAIVEFESKDGMCAALEEPQIKLSGKRLRVKPREKKEFQRKKGGSPRTLQPPDPEALSKELLNCADVEQQIKKLVSLCSPSHHESHLRELLLSLLQETFTEFFPGCQLLPFGSSVNGFEISGCDLDLYLDLGDDEAENVEGKAEKEIQNREESSTDMEVSMEDPETERKEEEMEIGNSKNDEDEDVTPGLSLKGLSSEEILEVVGKVLRHCVPGVHGV... | Cofactor: Binds 1 divalent cation per subunit.
Function: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF com... |
A0A348B793 | MSPTSDFVNTTSTAKGHEIIAGLTAKPVEGSTITLCKDIIREFFDKVQVPSPNFTRDPELEARVADIVRTWGNEEHLRPYVVTSLILTVTAYSHIANFETRVQITLFTIIIIAMDDPVVFDSLATREFHQRMCTGVIQDEAGMLGAFTKILESMWDHYSGFSANTIYASALRFVNASIIENETDVTTLRSHALPFVEYKRSMTATTEAYACFIWDKARFPDVKVYMQAIPDAMLYVSYVNDILSFYKEELAGETANYIHERAYVTGKSIPDTLRNLINETASAVERVRDILGEGEARAAFENFAAGYIRVHTGNPRYHLK... | Function: Terpene cyclase that catalyzes the cyclization of geranyl diphosphate (GPP) to myrcene and linalool.
Sequence Mass (Da): 37340
Sequence Length: 332
Domain: The conserved DDXXXXD and NSE/DTE motifs are important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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A0A348B794 | MSAVTQVVETAIGCVIPSCIEFGSSMRIATSLGSPSVTQSPCVNRDVEDIARTARESIRFFLAELSIECVPYTQDPALEAQVASATRCWPDRERLAPHIRTGIVIAATAYAHNSLATRTLIALYTAIGVALDEPDILESANAIGFHHSLCTETSERPSAILDEWRRILARMWDHFPRFGASCILTSTLQFLNMTMLENETKGKVLNRTAMPFVEYRRMTDGFPEVYTAFIWEKGRFPDVQVYMQAIPNAMRFINFGNDILSFYKEEAAGETGTYIHDRARLTGLSSVETLREVVEETVSAWRQVCEILGEGIARDAWNSF... | Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to a single major terpene scaffold whose chemical structure is still unknown.
Sequence Mass (Da): 38203
Sequence Length: 340
Domain: The conserved DDXXD and NSE/DTE motifs are important for the catalytic activity, presumably through ... |
K4LMW2 | MAVYVNSTTGPPSSVVRNSAGFHPSIWGDTFIPSGNSAVQKTDVDRKEEENLQLLKQEVKKMLTAGDTCQQDLICLIDDIQRLGLSYHFEAEIDTLLQHVKDSYLEYYGTKNHDNLHDVALSFRLLRQEGHNISSDVFSKFQDSDGKFNEKLVKDVRGMLSLFEAAHLSVHGENILEDALEFTTSHLNSYLNSNPNAPLADLVRRALKYPLRKSFNRMVARHYISIYHKYYWHKQVLLDLAKCDFNLVQKVHQKELGYITRWWKDLDFTNKLPFARDRVVECYFWITGVYFEPRYAAPRKFLTKVISLTSIIDDIYDVYG... | Cofactor: Binds 3 manganese or magnesium ions per subunit.
Function: Involved in the biosynthesis of kunzeaol. Produces mainly (-)-germacrene D along with gamma-cadinene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + kunzeaol
Sequence Mass (Da): 64663
Sequence Length: 561
Domain: The Asp-Asp-Xa... |
Q3SWZ3 | MRDRTHELRQGDDSSDDEDKERVALVVHPGTARLGSPDDEFFQKVRTIRQTIVKLENKVRELEKQQVTILATPLPEESMKQDLQNLRDEIKQLGRDIRAQLKAIEPQKEEADENYNSVNTRMRKTQHGVLSQQFVELINKCNLMQSEYREKNVERIRRQLKITNAGMVSDKELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKVALENQKKARKKKVFIAICLSITVLILVVIIVISTLV | Function: Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) w... |
P91409 | MHQISGINAASPEKNNSKLADVSLQQFLANVDEIRHVLTTLSADRHAIYMEQVESLAAGCSDTAKCRKLNDHVDKFIAQARGIRRRLADASEELVQYPESRVGSGRARHEQIQMLIVSLEGIMSQFADDQASYKAEAAKKIAAYLRKQNIEVTDSEIDGAIENGSLFQLTRNINLGVAQKKALFDDMKNRATDIMILEKQIREVEELFVDMQLLVQSQGETVDRIETSVIRAEEYAEQAQQNVRQAVVLRRKNRKWKIVTCIALIVLLLVVVYLLSHFLGAIIPGWK | Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 32316
Sequence Length: 287
Subcellular Location: Membrane
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Q7KVY7 | MGKDRLPELLQRSLSTNSSNSSSNGSLLLNVYSGTTEFIIGNTGGNNNSYSVVSQNSHSCSNNNSSTEPKDRSSSKMTQYGSNVDDILNPYTEIRQQLAQIAANLETMNRMAQTVNLRTFNENEMDELHNKNLRLGNQLMTRFNDFKANLPAENDYSLEARMKRTLFYGLHQTFINLWHKNELFLQNYETKVKKNLRLHTKIINSEASEQEIELLIENKTTKLFVDNFLQETEKERQTLREMMDRFNELRRLEKSIEEVHALFMRIQTLVMEQSEVIQRVEFHAQQATLHVDKGADELDQAEQHQKKARKKKIMLIVILA... | Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 38474
Sequence Length: 333
Subcellular Location: Membrane
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Q12846 | MRDRTHELRQGDDSSDEEDKERVALVVHPGTARLGSPDEEFFHKVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMRKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKVLIAICVSITVVLLAVIIGVTVVG | Function: Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) w... |
Q08850 | MRDRTHELRQGDNISDDEDEVRVALVVHSGAARLSSPDDEFFQKVQTIRQTMAKLESKVRELEKQQVTILATPLPEESMKQGLQNLREEIKQLGREVRAQLKAIEPQKEEADENYNSVNTRMKKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHEIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKIALENQKKARKKKVMIAICVSVTVLILAVIIGITITVG | Function: Plasma membrane t-SNARE that mediates docking of transport vesicles (By similarity). Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane (By similarity). In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) w... |
Q20797 | MSDFHNIRSRRRIPEASSYSTVDFDYDPDQKNHTSAVAPTSFAYSSLTTVFNASASQLWNSAQEALVSSYDTAEGTESIDADRSKVVETLESLSIFGNPLDHIIITMPSRDRTSEFRATAKSYEMKAAANGIRPQPKHEMLSESVQFNQLAKRIGKELSQTCAKMEKLAEYAKKKSCYEERSQIDHLSSIVKSDITGLNKQIGQLQEFSKRRAGNMKNQNSGHIQLVVVGLQSKLANVGKDYQSVLEISTETMKAEKNRRDKFSSGAAVPMGLPSSSSGANVRSKLLQDDEQHGSSSIALDMGALSNMQSQQTMQQRDSS... | Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 45853
Sequence Length: 413
Subcellular Location: Membrane
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Q24509 | MQTRRRLHQTDQQDYSSSSTYTIQEDQQGGAGAGSVGTGTAGGSVGLLAQSLVPPPTGHEAAIHIGDNYQSGDSISTPDYSDDKYGKAARQWNLRAFSGHALRTLSAAAAVVTGNQPGINNDSQSNYSYPASIPTSSQFYQSKEEPQETEPEPEIFVMAARDRTGEFANAIRSLQARNITRAVNIRDPRKAKQVQSYSEFMMVARFIGKNIASTYAKLEKLTMLAKKKSLFDDRPQEIQELTYIIKGDLNALNQQIARLQDISKDQRRHTNGKHLVSHSSNMVLALQSKLASMSTDFKQILEVRTENLKQQKTRRDQFSQ... | Function: Mediates endoplasmic reticulum to Golgi transport.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 51850
Sequence Length: 467
Subcellular Location: Golgi apparatus
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Q13190 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAGSSSSDIAPLPPPVTLVPPPPDTMSCRDRTQEFLSACKSLQTRQNGIQTNKPALRAVRQRSEFTLMAKRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRSRREQFSRAPVSALPLAPNHLGGGAVVLGAESHASKDVAIDMMDSRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHS... | Function: Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (D... |
Q8K1E0 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAISSSSDSTPLPTPVALVPSPPDTMSCRDRTQEFQSACKSLQSRQNGIQTSKPALHAARQCSEFTLMARRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRNRREQFSRAPVSALPLAPNNLGGGPIILGAESRASRDVAIDMMDPRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHS... | Function: Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (D... |
Q08851 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAINSSSDIAPLPTPVALVPSPPDTMSCRDRTQEFLSACKSLQSRQNGIQTNKPALHATRQCSEFTLMARRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRNRREQFSRAPVSALPLAPNNLGGGPIVLGGESRASRDVAIDMMDPRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHS... | Function: Mediates endoplasmic reticulum to Golgi transport . Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus .
Location Topology: Single-pass type IV membrane protein
Sequence Mass ... |
P83528 | MSNYRYSKLNEEEISLEDMPSSANQILTRQEQIIQEQDDELELVGNSVRTLRGMSSMIGDELDQQSTMLDDLGQEMEYSETRLDTAMKKMAKLTHLEDESSQCKMIMVLSALLFFLVFVLLV | Function: SNARE promoting movement of transport vesicles to target membranes (By similarity). Potentially functions in retrograde trafficking and in the endocytic recycling pathway (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 14035
Sequence Length: 122
Subcellular Locatio... |
C5P6D1 | MRLFQSTCVLVGTVLPLFTAFPISSPREIEIIPDKYIITFKKGIDQAAIEAHTAWVSSVQARNTARGFTTAETPGLERMFSIHNFNAYSGSFDRETIEEIRSHPNVESVEPDSMAYVTELIEQRNATYGPRRISHREIPTGDNSYWYDSKAGEGSFVYIMDTGINKAHVDFEGRAIPGVNLHDVAFDDTHGHGSHCAGIAGSKTYGVAKKATIVDVKVFTRGGGAWSLLMGGLDWSVKNITGEDRQAKSAVSISISGPTNQAMNNAVKAAVEAGVTVVVASGNDGRDAGRNSPGSAPESITVGSINSRRGMDTRSSFSNY... | Function: Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity.
Sequence Mass (Da): 43287
Sequence Length: 406
Subcellular Location: Secreted
EC: 3.4.21.-
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D4AZ75 | MQLLNFGLLLLPFVAGDLAPQPEPLLAGPSDVVPGQYIVTLKEGLTSAQIRDHKKWVSSVHRANLDSFAAGASGVETEGIMKHFHIHDLNMYSGGFDEKTVEDLSRNPYVKSVHPDQHVYLAKTVTQRQARWGLGYMSSKGKPVPLHSTLVDYSYDDKAGEGVWAYVLDTGINVNHVEFEGRGILGHNAIPNKPHTDEFGHGTYVAGIIAGKTYGVAKKANVVSAKAFDTGSSTYNYILETYDWIVRNITDSNRKNKAVINLSISGAKYQPFDDAVEKAFKAGITTVVAAGNDGKDAKNNTPASSPNAITVGAVRWENTR... | Function: Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity.
Sequence Mass (Da): 45608
Sequence Length: 421
Subcellular Location: Secreted
EC: 3.4.21.-
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A1CMQ7 | MSHEEDLIDYSDEELQTTDAAATTAAPAANGAQDKKGDLTVSGGRPDKKGSYVGIHSTGFRDFLLKGELLRAITDCGFEHPSEVQQVCIPTAILNVDVLCQAKSGLGKTAVFVLTTLHQLEPVPGECSVLVMCHTRELAYQIKNEYARFSKYLPDVKTAVFYGGTPIQKDVEVLSNKESYPNIVVGTPGRLNALVRDKKLSLRNVKAFVLDECDKMLDQIDMRRDVQEIFRATPADKQVMMFSATLSQEIRPICKKFMRNPLEVYVDDDTKLTLHGLQQYYIKLSESEKNRKLNELLDSLEFNQVIIFVKSTLRANELDK... | Function: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity).
Catalytic Activity: ... |
O13750 | MFKTQTTLLTSLRRFSSSSQLKNSKSLYEQTIPNLMINSDTKVIFQGFTGKQGTFHAQHAMDYGTKVVGGTNPKKAGTTHLGKPVFGTIEEAMKETKADASAVFVPPPLAAGAIEEAIAAEVPLIVAITEGIPQHDMLRVSDILKTQSKSRLVGPNCPGIIRPGQCKIGIMPSHIHKPGCIGIVSRSGTLTYEAVNQTTQTDLGQSLVIGIGGDPFPGTNFIDALKLFLDDPNTQGIILIGEIGGSAEEDAAEFIRAANASRSTPKPVVSFIAGATAPKGRRMGHAGAIVAGGKGTAAAKFEALEAAGVRISRSPATLGS... | Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate bind... |
P53598 | MLRSTVSKASLKICRHFHRESIPYDKTIKNLLLPKDTKVIFQGFTGKQGTFHASISQEYGTNVVGGTNPKKAGQTHLGQPVFASVKDAIKETGATASAIFVPPPIAAAAIKESIEAEIPLAVCITEGIPQHDMLYIAEMLQTQDKTRLVGPNCPGIINPATKVRIGIQPPKIFQAGKIGIISRSGTLTYEAVQQTTKTDLGQSLVIGMGGDAFPGTDFIDALKLFLEDETTEGIIMLGEIGGKAEIEAAQFLKEYNFSRSKPMPVASFIAGTVAGQMKGVRMGHSGAIVEGSGTDAESKKQALRDVGVAVVESPGYLGQA... | Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA . The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate bin... |
Q148D5 | MAASVFYSRLLAAATLRSHRPRTALPAAAQVLGSSGLFNNHGVQIQHQQQRNLSLHEYLSMELLQEAGVSIPKGHVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERRYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAETPEAIVKEPIDIVEGIKKEQAVRLAQKMGFPASIVDSAAENMIKLYDPFLKYDATMVEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKADLNYIGLDGNIGC... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
P53588 | MIGRISQPLLNTSQKFMAPAARTLMLHEHHGMKILQNYEIKVPPFGVAQDAETAFSEAKRIGGKDYVVKAQVLAGGRGKGRFSSGLQGGVQIVFTPDEVKQKAGMMIGANLITKQTDHRGKKCEEVMVCKRLFTRREYYFSITLDRNTNGPIVIASSQGGVNIEEVAATNPDAIVKMPIDVNVGITKELAHEIAVKMGFSKDCEQQASEIIEKLYQMFKGSDATLVEINPMAEDVNGDVYCMDCKLLLDSNAEFRQAKLFDLKDKKQEDELEIRAAAANLNYIRLDGTIGCMVNGAGLAMATMDIIKLHGGEPANFLDVG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
P99507 | LSLHEYMSMELLQEAGVSIP | Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate... |
Q9YI37 | RRLSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGTFEGGLKGGVKIVFSPEEAKAVSSRMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGIKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDWTQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
Q55AI5 | MLSNIVKKTIQSSKNLKSLVLNKSTSSLVYQKRFLNVHEYQAQKMMKSYGINCPVGNVAETPEEAEKIAEVMNTQDLVVKAQVLAGGRGKGIFTSGLKGGVQLCSSAEDVKKFASKMLGHTLVTKQTGEDGKVVHQVYVTERHFLRKEMYFAILMDRKAGGPVMVASPEGGVDIEGVARDNPSAIFKEPIDIMIGVQPEQTKRLAEKLGFSKKNISMAQDQMKKLYDFFIKNDCTLVEINPLAETASGDVLCMDAKLNFDDNAAFRHPDIFKLRDKSQEDPREVKAAEFDLNYIGLDGNIGCLVNGAGLAMASMDIIKLY... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
Q9P2R7 | MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGC... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA . The beta subunit provides nucleotide specif... |
P86226 | DVVIKAQVLAGGRIVFSPEEAKLITKQTGAKGRICNQVLVCERREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKKMGFPSNIVDSAAENMIKLYNLFLKINFDSNSAYRQKIFDLQDWSQEDERLHGGTPANFLDVGGGATVQQVTEAFKVQAILVNIFGGIMRLQGTRVDDAKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI | Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate... |
Q9Z2I9 | MAASMFYGRQLAAAALRSHRPQTTLRAAAQVLGNSGLFNKHGLQVQQQQQRTLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDWSQEDERDKEAANADINYIGLDGSIGC... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
P53589 | MLRAAGNLSKSMMKSQRRFLNLQEFQSKEILEKHGCSVQNFVVASNRKEAEEKWMSFGDHEYVVKAQILAGGRGKGKFINGTKGIGGVFITKEKDAALEAIDEMIGKRLVTKQTTSEGVRVDKVMIAEGVDIKRETYLAVLMDRESNGPVVVASPDGGMDIEAVAEKTPERIFKTPIDIQMGMTEGQSLKIAKDLQFEGKLIGVAAQEIKRLYDLFIAVDATQVEINPLVETADGRVFCVDAKMNFDDSAAYRQKEIFAYETFEEHDPREVDAHQFNLNYIGMDGNIACLVNGAGLAMATMDLIKLHGGEPANFLDVGGA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
Q9YI36 | EYQSKKIMADHGVTVQRFFVADSANDALEAAQRLKAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPKIVEQLAKQMIGYNLSTKQTPKDGVTVKKVMVAEALNISRETYFAILMDRACNGPVMVGSPQGGVDIEEVAVTSPELIFKEEIDIFEGIKDHQALQMAKNLGFKGPLQQQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKEIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIISLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILVN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
Q96I99 | MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDII... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
P53590 | IPAAPVAAQARKLLRDLAFRPPLLAARSQVVQLTPRRWLNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFSSGLKGGVHLTKDPEVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIEGIKDSQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specifi... |
O82662 | MRGLVNKLVSRSLSISGKWQNQQLRRLNIHEYQGAELMGKYGVNVPKGVAASSLEEVKKAIQDVFPNESELVVKSQILAGGRGLGTFKSGLKGGVHIVKRDEAEEIAGKMLGQVLVTKQTGPQGKVVSKVYLCEKLSLVNEMYFSIILDRKSAGPLIIACKKGGTSIEDLAEKFPDMIIKVPIDVFAGITDEDAAKVVDGLAPKAADRKDSIEQVKKLYELFRKTDCTMLEINPLAETSTNQLVAADAKLNFDDNAAFRQKEVFAMRDPTQEDPREVAAAKVDLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the e... |
Q8EFN8 | MNLHEYQAKSLFAEYGLPVSEGFACDTAQEAVEAAGRIGGNLWVVKCQVHAGGRGKAGGVKVTGDKEEIRAFAEYWLGKNLVTYQTDEKGQPVAKILVESCTDIANELYLGAVVDRATRRVVFMASTEGGVEIEKVAEETPELIHKAIIDPLTGPQPFQARDLGFKLGLNPTQMKQFTKIFMGLATMFVDHDFALLEINPLVITTEGNLHCLDGKIGIDGNALFRQPKIKAMHDPSQDDAREAHAAMFELNYVALDGNVGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVAEAFKIILSDSNVKAVLVNIFG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q7N3U6 | MASLPDTNKLLRNFSRCRNWEERYLYMIELGAKLPPLTDEQRQPENLIAGCQSQVWILLRMNHQNKVEFIGDSDAAIVKGLVAIVFILFQGKTTQEILDLDVTEYFGKLSLEQHLTPSRTQGLHAMIHAIRNRTSKMV | Function: Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the ... |
A0A0F6B4W4 | MHPMLTIAVRAARKAGNVIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGNIVAGNPRVVKAMLANMRDELSDALKR | Function: Associates with the boxA element in its own promoter . Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscripti... |
Q9KTY5 | MHPMLNIAIRAARKAGNHIAKSLENAEKIQTTQKGSNDFVTNVDKEAEAIIVSTIKSSYPEHCIIAEEGGLIEGKDKEVQWIIDPLDGTTNFVKGFPHFAVSIAVRFRGKTEVACVYDPMTNELFTAQRGAGAQLNNARIRVQPIKDLQGAVLATAFPFKQKQHSESFMKILSAMFVECADFRRTGSAALDLCYLAANRVDGYFELGLKPWDMAAGELIAREAGAIVTDFAGGTDYMQSGNIVASSPRGVKAILQHIRENGNSAILK | Function: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions... |
Q9PAM0 | MQKPAVNIMVKAARSAGNVLLRHINKLETLHVIQKSRMDYASDVDEMAEKVIVKELKRAYPEYGILGEEGGLQGNHRIMWVIDPLDGTSNYLRGFPHYCISIALVENGEPTDAVIFDPLRNELFTASRGAGAILNERKIRVANRKDLNGTMLNTGFSPRERSRAHAQLKCVDALLMQAEDIRRSGSAALDLAYVACGRADAYFEAGIKVWDVAAGMLLVREAGGYVCDFKGADAPRMDDKGPESCQLVAGNIKVAHALQQVIVSSGYGREFDPKR | Function: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions... |
P15715 | MARTPAKYCDLVMKGGITSGIVYPNAALALARDYRFKNIGGTSAGAIAAAACAAAAVGDRRKQMKAAIAQPEERVGFEGLAKASANLASPGFIKDLLQPAAGAGQAFRLLVTLAGNTGVLRKGVALLGSVVRIAPVETLLLLAALAGLAYAVGGQTGMIAAALPAAICAYLGGVVFAVLRIARVLRRNLMGLCTGTAPDQPARRPRMVLTDWLHETLQALSGKASGQPLTFGDLWTAERYPGEPGSDRAVTLKMITTGISHQEPRSLPFESALFWFRRKEFEALFPKVVVDWMVEKAGEPVTVAGEDYYLLPHGADMPVL... | Function: This protein is non-essential for R.meliloti growth, but induces a heat-shock response in temperature-sensitive E.coli K165 by elevating levels of sigma 32 (mechanism unknown).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68699
Sequence Length: 633
Subcellular Location: Cell membrane
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Q5ZYR3 | MFKRIALVCALFSGVCFAEGKQLLDKVVAIVNDNVITSSELNAQVELSKKQIIAQNMQMPDESVLRKQVLQHLIDVDLEMQMAKQNGITIENAEIDEAIEKIAASNHLNLSQMRDEITKQGISWQEYRQNIRKEMLISRVQQKAVGKDIIVTNEQVEQYLKTSGRIENSNLTYHLKNIVIPLSEEPTTKQLQRAKIEAENLLNKIKKGEDFSRLAIEESSGEFALEGGDLGERHLAELPEVFAKEVVHMKVGQVAGPIRAGNGFHLIKLVAVGGENQRHVITQTHVRHILLKPDASMVPSEAIKQVNNIYRQIQSGKDFA... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q60B78 | MKISSFRKGRWLGALALFAVVCWSMADAAVDRIVAVVDDGVILESELVRKVDEIKRSLRASRASLPPDSVLVRQVLERMIVDKIQIQMAEKMGIQVDDDTLRMAVSQIAQRNNLTPDQFRRSLAREGIDYGDFLDQVRSEIAMGRLRASQINNQIKISDREVEHYLEAQGGSGAVADREYRLGHILIATPREASPDEVKKARERADRVVKELKAGLDFKDASIRYSDDPQALEGGDLGWRKLSEIPSHIAEVVGGMKDGEVSDPIRSPGGYHIVKMLAMRGVGEAKLTKTHVRHILIRPNEVLSDEDAKNKLLALKTRIE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q1GZC0 | MHNHVFKTIARHGLIALFFFFSISAMAAEVAKMDRIVAIVDQGVITEKELEDRIQTVIAQLEKQGTQLPPRDVLQKQILERLINDRLQLQYAAQTGLRVDDAQLDKTIERIAEQNKLSTGEFRKALEAEGIPYRKFREDIRNEIILARLREREVDNRVNVTESEIDNFLTTQSSRNDIQDEFEVAHILIRAPEESTPEELQKLKAKAEAALKELQSGADFAQVSAGYSDAPNALEGGILGWKASSQLPSLFVDALQALQPGQLSPVLRSPNGYHILKLLNRRGGSSPLVVDQTHVRHILIKLSEVVSELEAEQKINSIKE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q82W17 | MIQFSSDRQLKFRKYWLIYAVFATMLAADVFAQSSYSREDIKPIDRIVAVVNEEVITQQEINEVLQNTVQQLQRQNTQLPRMEILEKQLLERLILKRIQLQRAKEIGLTVSDNDLDQTLRRIIQDNHLTMDEFRQVLLQEGTDMNRFREEIRGEILMSRLKEQEVNSRVNVTENEIDNFLQNQANSPAGNEEYRIAHILVQISEQMDEAQIEARHKRAETAYESLRQGADFVRVSAEFSDAPDAMQGGELGWRPLGQLGSPFTEMLVNMQPGEVTPVVRSPVGFHILKLLERRQQEQKVTIIEQTHAQHILIKVSELVSE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
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