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Q977V2 | MVLDNLGSSLRGSLDKLRGKSRLDEDDVQEIVKEIQRSLLSADVDVSLVMDLSDSIKTRALEEEPPGGTSARDHVLKIVYEELVDLIGESTEIPLESQTIMLAGLQGSGKTTTSAKMAWWFSKKGLRPAVIQTDTFRPGAYDQAKQMCERAEVDFYGDPDCDDPVQIAREGLEATEDADVHIVDTAGRHALEDDLIDEIEEIEGVVQPDLNLLVLDAAIGQGAKEQAQQFDESIGIGGVVITKLDGTAKGGGALTAVNETDSSIAFLGMGETVQDIERFEPNGFISRLLGMGDLKQLSERVERAMSETQAEDEDWDPEEMMKGNFTLKDMQKQMEAMDKMGPLDQVLDMIPGFGGGIKDQLPDDAMDVTKDRMRSFEVIMDSMTEEELENPRKVGASRVRRIAQGSGQDEETIQELLEQHRMMEQTIKQFQNMGDGDMQRMMKKLQNQGGGGGGGMGGLGGMGPF | 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 receptor FtsY.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50918
Sequence Length: 465
Domain: Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Subcellular Location: Cytoplasm
EC: 3.6.5.4
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P56005 | MFQALSDGFKNALNKIRFQDDEKALDRALDELKKTLLKNDVHHKVARELLKKVESQTKLNGIGKQQFLDALEKSLLEILSAKGSSGFTFAQTPPTVVLMAGLQGSGKTTTTAKLAHYLKTKNKKVLLCACDLQRLAAVEQLKVLGEQVGVEVFYEENKSVKEIASNALKRAKEAQFDVLLVDSAGRLAIDKELMQELKEVKEILNPHEVLYVADALSGQDGVKSANTFNEEIGVSGVVLSKFDSDSKGGIALGITYQLGLPLRFIGSGEKIPDLDVFVPERIVGRLMGAGDIVSLAEKTASVLNPNEAKDLSKKLKKGQFTFNDFLNQIEKVKKLGSMSSLISMIPGLGNMASALKDTDLESSLEVKKIKAMVNSMTKKEQENPEILNGSRRKRIALGSGLEVSEINRIIKRFDQASKMAKRLTNKKGISDLMNLMSQAKNQTPPKMR | 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 receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49175
Sequence Length: 448
Domain: Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Subcellular Location: Cytoplasm
EC: 3.6.5.4
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P61011 | MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM | 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 proteins to the endoplasmic reticulum membrane . Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes . Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA . Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA . SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER . Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 55705
Sequence Length: 504
Domain: The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit SRPRA . The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another . SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER .
Subcellular Location: Nucleus speckle
EC: 3.6.5.4
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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'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed.
Sequence Mass (Da): 27745
Sequence Length: 248
Domain: The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling.
Subcellular Location: Cytoplasm
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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 pre-mRNA. 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. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment.
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation.
Sequence Mass (Da): 25476
Sequence Length: 221
Subcellular Location: Nucleus
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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 pre-mRNA. 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. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity).
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation (By similarity).
Sequence Mass (Da): 25487
Sequence Length: 221
Subcellular Location: Nucleus
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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 pre-mRNA. 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. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity).
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation (By similarity).
Sequence Mass (Da): 25448
Sequence Length: 221
Subcellular Location: Nucleus
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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 during alternative splicing . Also functions as export adapter involved in mRNA nuclear export . Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity . Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export . RNA-binding is semi-sequence specific .
PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 19330
Sequence Length: 164
Subcellular Location: Nucleus
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Q08170 | MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHARGPRRDGSYGSGRSGYGYRRSGRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLDGTEVNGRKIRLVEDKPGSRRRRSYSRSRSHSRSRSRSRHSRKSRSRSGSSKSSHSKSRSRSRSGSRSRSKSRSRSQSRSRSKKEKSRSPSKEKSRSRSHSAGKSRSKSKDQAEEKIQNNDNVGKPKSRSPSRHKSKSKSRSRSQERRVEEEKRGSVSRGRSQEKSLRQSRSRSRSKGGSRSRSRSRSKSKDKRKGRKRSREESRSRSRSRSKSERSRKRGSKRDSKAGSSKKKKKEDTDRSQSRSPSRSVSKEREHAKSESSQREGRGESENAGTNQETRSRSRSNSKSKPNLPSESRSRSKSASKTRSRSKSRSRSASRSPSRSRSRSHSRS | 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 | MPRVYIGRLSYQARERDVERFFKGYGKILEVDLKNGYGFVEFDDLRDADDAVYELNGKDLCGERVIVEHARGPRRDGSYGSGRSGYGYRRSGRDKYGPPTRTEYRLIVENLSSRCSWQDLKDYMRQAGEVTYADAHKGRKNEGVIEFVSYSDMKRALEKLDGTEVNGRKIRLVEDKPGSRRRRSYSRSRSHSRSRSRSRHSRKSRSRSGSSKSSHSKSRSRSRSGSHSRSKSRSRSQSRSRSKKEKSRSPSKDNKSRSRSRSPDKSRSKSKDHAEDKLQNNDSAGKAKSHSPSRHDSKSRSRSQERRAEEERRRSVSRARSQEKSRSQEKSLLKSRSRSRSRSRSRSKDKRKGRKRSRDESRSRSRSKSERSRKHSSKRDSKVSSSSSSSKKKKDTDHSRSPSRSVSKEREHAKAESGQRGSRAEGESEAPNPEPRARSRSTSKSKPNVPAESRSRSKSASKTRSRSKSPSRSASRSPSRSRSRSHSRS | 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 | MTSLIQSIPRYIYESNSLPKLIRSGLDRKSPIGLSLLKRNCRNRSFAANMSTSSKLSTNIKDLSLFDLEEFPARSYIGGKWVTAASGKTFDVENPGLNETLAPVTDMSVEETRKAIKVAHEAFLSYRNSDIKERYAILRRWYDLIMENADDLATMMTLENGKALGDAKGEVVYAAKFIDWFAGEALRISGDSSMSSNPQNRIITIKQPVGVVGIITPWNFPAAMITRKVGAALAAGCTVVIRPAAETPFTALALAKLAERAGVPAGVLNMVTANSPSEHGIELTTNPLIRKVSFTGSTNVGKILAKQSSSTLKKLSLELGGNAPFIVFEDADLEKAADALMACKFRGSGQTCVCANRIYVHSSVYDAFVDLVTERVSKFKLGYGLDAGVTHGPLISEKAISKVKQHVEDAVQKGGVVVTGGKVASNLGPMYFEPTVIINAKQGMLISEEETFGPVGALFKFDTEDEVVAWANDSPVGLAGYLFSKDISRVFRVGEALQVGMVGCNTGLVSDVLSPFGGVKESGFGREGSKYGISEYLDIKSLTISTL | 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 | MAPQFKRPELFGFDKSHAQSFVQGKWISSPNNKTFEVDNPATGEIIGKVADVSVEETKKAISAANEAFKTYKNFTHVQRSQLLERWAELIMENKDDLVKMLTLENGKPLSQAEMEVTTCSGYLKWYAAEAVRTFGDVAPSSLQSQNFLISIKQPVGVSALITPWNFPAAMIARKGGAALAAGCTAIFLPAFRTPYVCLGLVRLAQEAGFPDGVLNVITSSDASAHGKELTTNPIVRKVSFTGSTNVGKILMGQSASTIKKVSMELGGNAPFIVFPDFPIDQAVESFCTIKFNSCGQVCVCPNRVYVHKNVYDEFVSKLTEKVKTIKVGDGFDSSSAVGPLISQDGCKKVSKHIEDAVSKGAKITVGGKEISSSKGYFFEPTVLSGVTQDMLVASEETFGPLASVFKFDDTEEVIEWANDSDVGLAGYVFTNNLSTMIHVAKELEVGLVGANIEMVDEPFISFGGIKQSGFGKEAGRLGVQEFMVVKEINLKTL | 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 | MVIGAAARVAIGGCRKLISSHTSLLLVSSQCRQMSMDAQSVSEKLRSSGLLRTQGLIGGKWLDSYDNKTIKVNNPATGEIIADVACMGTKETNDAIASSYEAFTSWSRLTAGERSKVLRRWYDLLIAHKEELGQLITLEQGKPLKEAIGEVAYGASFIEYYAEEAKRVYGDIIPPNLSDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALASGCTVVVKPSELTPLTALAAAELALQAGVPPGALNVVMGNAPEIGDALLTSPQVRKITFTGSTAVGKKLMAAAAPTVKKVSLELGGNAPSIVFDDADLDVAVKGTLAAKFRNSGQTCVCANRVLVQDGIYDKFAEAFSEAVQKLEVGDGFRDGTTQGPLINDAAVQKVETFVQDAVSKGAKIIIGGKRHSLGMTFYEPTVIRDVSDNMIMSKEEIFGPVAPLIRFKTEEDAIRIANDTIAGLAAYIFTNSVQRSWRVFEALEYGLVGVNEGLISTEVAPFGGVKQSGLGREGSKYGMDEYLEIKYVCLGDMNRH | 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 meristem (SAM) structure and subsequent adaxial-abaxial axis-dependent development of cotyledons and leaves .
Catalytic Activity: H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
Sequence Mass (Da): 56559
Sequence Length: 528
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.24
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P51649 | MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL | 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.
Subcellular Location: Mitochondrion
EC: 1.2.1.24
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D0ZVG2 | MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQKLWAYNNRLTSLPEMSPGLQELDVSHNQLTRLPQSLTGLSSAARVYLDGNPLSVRTLQALRDIIGHSGIRIHFDMAGPSVPREARALHLAVADWLTSAREGEAAQADRWQAFGLEDNAAAFSLVLDRLRETENFKKDAGFKAQISSWLTQLAEDAALRAKTFAMATEATSTCEDRVTHALHQMNNVQLVHNAEKGEYDNNLQGLVSTGREMFRLATLEQIAREKAGTLALVDDVEVYLAFQNKLKESLELTSVTSEMRFFDVSGVTVSDLQAAELQVKTAENSGFSKWILQWGPLHSVLERKVPERFNALREKQISDYEDTYRKLYDEVLKSSGLVDDTDAERTIGVSAMDSAKKEFLDGLRALVDEVLGSYLTARWRLN | 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 polyubiquitin chains (in vitro) . Polyubiquitinates host PKN1, leading to its proteasomal degradation . Down-modulates production of host pro-inflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression; this depends only partially on its E3 ubiquitin-protein ligase activity .
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 77119
Sequence Length: 700
Domain: The LRR (leucine-rich repeat) domain mediates interaction with host PKN1 and inhibition of NF-kappa-B-dependent gene expression.
Subcellular Location: Secreted
EC: 2.3.2.27
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Q08945 | MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGMNPSYDEYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDRDEKKRKQLKKAKMAKDRKSRKKPVEVKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARRDYEKAMKEYEGGRGESSKRDKSKKKKKVKVKMEKKSTPSRGSSSKSSSRQLSESFKSKEFVSSDESSSGENKSKKKRRRSEDSEEEELASTPPSSEDSASGSDE | 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 that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.
PTM: Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity.
Sequence Mass (Da): 81075
Sequence Length: 709
Domain: The HMG box DNA-binding domain mediates DNA-binding. It has both affinity and specificity for DNA damaged globally with cisplatin.
Subcellular Location: Nucleus
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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 sulfonateSide 2 + [sulfonate-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28543
Sequence Length: 255
Subcellular Location: Cell membrane
EC: 7.6.2.14
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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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30139
Sequence Length: 278
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33978
Sequence Length: 319
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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Q62K56 | MTGTTLAATYGPISGADLEAELAQPRIADGDAQDAAVYERDGGARALPFASGGAPPDGDRADVRRAAGAGDASVRLTRVSKRYGERAVLADVDLSIGRGSFVSIVGRSGCGKSTLLRLVAELETPSAGTLVKRGDGGGALDTRIMYQEARLLPWKTVLQNVMLGLGRRAKDDARAVLDEVGLLARANDWPAQLSGGQRQRVALARALVHRPQLLLLDEPLGALDALTRIEMHALIERLWREHRFTALLVTHDVQEAVALADRVLLIEAGRIAFDQRVPLDRPRARASAAFAALEDRVLQRVLTGSDAAPAAPNAAGPEGASRGRAAPASGLRWAV | 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35427
Sequence Length: 335
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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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).
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25977
Sequence Length: 243
Subcellular Location: Cell membrane
EC: 7.6.2.14
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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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32458
Sequence Length: 303
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32884
Sequence Length: 299
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25984
Sequence Length: 241
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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Q9XX85 | MLLFQKTLSRVAAPISVAANLILILLIIFKSPAQMGNYKYLLIGLSIFEMSYAVLDVVSETTVLSIKKSFVVVVPYKDRSFGQETAMDINLIYCGFFGFSMGMFVVIFAYRSFLTTGNTILRKFEGFKIISWFAYPLFYAIVWILVAWGPLASFPEMDIVVRPFLLDELNMTVDEVAYTGRLFYSTIDNSLRYSAILTGVLQWVLTASSLFLVIFFGLRCYFHYGKLVQLTDVQSIRLRQLQNQLFLALVCQATVPLILMHIPVTILYTCCVLNIVFNPFSVATTIALFPAIDPLPTIFIVKNYRVALFEFVCPSCLCWSETLKHMGSNRITSYRSNTVNALSM | 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 and as well many xenobiotics that contain alcohol and phenol functional groups . Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis . Plays a key role in bile acid metabolism . In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).
PTM: The N-terminus is blocked.
Catalytic Activity: 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+)
Sequence Mass (Da): 33780
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 2.8.2.2
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O00204 | MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS | 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 sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA . Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation .
PTM: Phosphorylated.
Catalytic Activity: 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+)
Sequence Mass (Da): 41308
Sequence Length: 365
Domain: The C-terminus, which contains a proline/serine-rich region is involved in nuclear translocation and enzymatic thermostability.
Subcellular Location: Cytoplasm
EC: 2.8.2.2
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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
Sequence Length: 301
Subcellular Location: Cytoplasm
EC: 2.8.2.-
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Q8WU08 | MGANTSRKPPVFDENEDVNFDHFEILRAIGKGSFGKVCIVQKNDTKKMYAMKYMNKQKCVERNEVRNVFKELQIMQGLEHPFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVHFKEETVKLFICELVMALDYLQNQRIIHRDMKPDNILLDEHGHVHITDFNIAAMLPRETQITTMAGTKPYMAPEMFSSRKGAGYSFAVDWWSLGVTAYELLRGRRPYHIRSSTSSKEIVHTFETTVVTYPSAWSQEMVSLLKKLLEPNPDQRFSQLSDVQNFPYMNDINWDAVFQKRLIPGFIPNKGRLNCDPTFELEEMILESKPLHKKKKRLAKKEKDMRKCDSSQTCLLQEHLDSVQKEFIIFNREKVNRDFNKRQPNLALEQTKDPQGEDGQNNNL | 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 | MISQICNEVIGLVPKKEEPGWLSVTGHPGAVYCENSISSGPEATGADVSQAIRIAYFTPLKHIPGPWYASLTGLRLSWSVFANNRIHYVHSLHQKYGPIVRIGPQEIDVADPVAGREIHRMGSGFMKAPFYELLSPGPVDNIFNFRDPKLHAARRKLYARGFTLQSLRNEWEPKVRDIIKLTVEKIKCDAVKGEAEIMGWWTLMANEIVCQLTFGGGAGIVAKGVKEPFVLMLERRMGDLAHLLKHFAPPGYYLGRALAWFIPPLQDIFYSQERMFAAGGDVVSRAREAKKAQAEPRNLFNKALEAGNLTDTDIITDAGALLLAGSDPTAISLTFLLWCVLSRPEVQKQVEAEVATLEGELTDEACERLPILNAVIDESLRLYGAAPGCMPRSPPSGGVTIGGYFIPDDTIVATQNWSLQRNPSIWDDADTFDHTRWLSNSRITDQAKLAFNPFGYGARQCLGIHLGRMEMRLAAAMFFRECVGARLGRSVTDESMHVVDSFIAGVPRDRRCAITLT | 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 of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Sequence Mass (Da): 57140
Sequence Length: 517
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
EC: 1.14.-.-
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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 the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Sequence Mass (Da): 34576
Sequence Length: 305
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
EC: 1.11.1.-
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O87278 | MPNDPLLQPYQLKHLTLRNRIIVTAHEPAYPEDGMPKERYRAYTVERARGGVAMTMTAGSAAVSKDSPPVFNNLLAYRDEIVPWIREMTDAVHEEGAVIMIQLTHLGRRTRWDKGDWLPVVAPSHHREAAHRAFPKKIEDWDIDRIIKDFADAAERMKAGGMDGVELEAYGHLIDQFASPLTNELDGPYGGSLDNRMRFCFDVLKAIRARVGDEFILGVRYTADECLPGGTDKAEGLEISKRLKESGLIDYLNIIRGHIDTDPGLTDVIPIQGMANSPHLDFAGEIRAATNFPTFHAAKIPDVATARHAIASGKVDMVGMTRAHMTDPHIVRKIIEKREEDIRPCVGANYCLDRIYQGGAAYCIHNAATGRELTMPHSIAKAHCRRKVVVVGTGPAGLEAARVAGERGHEVIVFEAASDPGGQVRLTAQSPRRREMISIIDWRMSQCEKLGVTFHFNTWAEAEAIQAESPDVVIIATGGLPHTEVLSRGNELVVSAWDIISGDAKPGTNVLIFDDAGDHAALQAAEFLATAGARVEIMTPDRSFAPEVMAMNLVPYMRCLQKLDVTFTVTYRLEAVEKSGNELVAHVGSDYGGISKQRTFDQVVVNHGTIPLDELYFELKPFSSNLGEIAHDQMIAGEPQSVVRNAEGKFQLFRIGDAVAARNTHAAIYDALRLLKDI | 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 | MNTKMNERWRTPMKLKYLSCTILAPLAIGVFSATAADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAKDKEAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHEVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK | 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 glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes.
Sequence Mass (Da): 99548
Sequence Length: 898
Subcellular Location: Secreted
EC: 3.4.24.-
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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 fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Catalytic Activity: (2S,3S)-versiconal hemiacetal acetate + H2O = (2S-3S)-versiconal hemiacetal + acetate + H(+)
Sequence Mass (Da): 31456
Sequence Length: 286
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
EC: 3.1.1.94
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Q00707 | MAFLSLPILTALGAVVYVLFQLVYNLYFHPLRDYPGPLLWRASSLPWKLTLLRGTMHHDLMRHHQTYGDTVRIKPDEISYANGQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTRNHARFRSLFGHAFSDKGLRAQEPTIARYADLLVEVLREVADTGKSVEMVRYFNMAIFDSIGALSFGESFDSLRNRELHPWVDTIHKNLKSVAISHVLRSMGVEFLAPYLMPAELRGKRQENYTYAIEKLKKRMQKTGDQGDFWDRVIVKSADGNQSGDGMSYGEMINNAAVMVVAGSETTSSALCGCTYLLCKFDKMDKAVAEVRGAFAAADQIDLVSVSRLPYLTAVIDETLRMYPSVPGQPPRVVPEGGAIVCGRFVPAETRVGVSHLGAYYAPYNFSHADKFIPERHLAGAKLEEPFRHDNYAAYQPWSVGVRNCIGRNLAYAEVRLTLAKLLWHFDISLDEERTGNFLDQKIWSIWAKRELYLEIRTREF | 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 of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Catalytic Activity: H(+) + NADPH + O2 + versicolorin B = 2 H2O + NADP(+) + versicolorin A
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56129
Sequence Length: 496
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
Subcellular Location: Membrane
EC: 1.14.19.n5
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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 hexanoate by the fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Catalytic Activity: 6-demethylsterigmatocystin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + sterigmatocystin
Sequence Mass (Da): 23130
Sequence Length: 204
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
EC: 2.1.1.109
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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 the fatty acid synthase (FAS) units stcJ and stcK . The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF . 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG . The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme . The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone . The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone . The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) . The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) . The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin . The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin . The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP .
Sequence Mass (Da): 30255
Sequence Length: 274
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
EC: 1.-.-.-
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A1KM51 | MREYDIVVIGSGPGGQKAAIASAKLGKSVAIVERGRMLGGVCVNTGTIPSKTLREAVLYLTGMNQRELYGASYRVKDRITPADLLARTQHVIGKEVDVVRNQLMRNRVDLIVGHGRFIDPHTILVEDQARREKTTVTGDYIIIATGTRPARPSGVEFDEERVLDSDGILDLKSLPSSMVVVGAGVIGIEYASMFAALGTKVTVVEKRDNMLDFCDPEVVEALKFHLRDLAVTFRFGEEVTAVDVGSAGTVTTLASGKQIPAETVMYSAGRQGQTDHLDLHNAGLEVQGRGRIFVDDRFQTKVDHIYAVGDVIGFPALAATSMEQGRLAAYHAFGEPTDGITELQPIGIYSIPEVSYVGATEVELTKSSIPYEVGVARYRELARGQIAGDSYGMLKLLVSTEDLKLLGVHIFGTSATEMVHIGQAVMGCGGSVEYLVDAVFNYPTFSEAYKNAALDVMNKMRALNQFRR | 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: 1.6.1.1
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Q58CP9 | MDVCARLALWLLWGLLLHHGQSLSQSHSEKATGSGANSEESTAAEFCRIDKPLCHSEDEKLSFDAVRSIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRLAPKPPQMIRAADEALSAMTSNGSHRLIEGAHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSSPALPSGSPHLDSSRSHSPSPPDPDTPSPAGDSRALQASRNTRIPHLAGKKAAAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK | 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 activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch.
PTM: Glycosylation is required for cell surface expression.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 77151
Sequence Length: 683
Domain: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.
Subcellular Location: Cell membrane
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G5EF60 | MGRVSWIIALYLTINVVIVVNGDRVTRNVEVTAEEEKIRDKLGYEAIRDIHRDMDDDHSGSIDRNESTGFMKEDMQMRGSERTRRENKFHGDDDAITVDDLWEAWFESIERTWTNERLVEWLINDVNLPSIVEAVKAKKIDGKILPRFASPNSDFLNKELGIKSSVYRQKLRLNSLDVVLFGYKDNNNRTKDILLAFLALLLTSLIFLYVRQKQKAQQKVNELSNKLTELKCMETEFEDVQKMLNDERSKRSISDGVVNHTEMENLRVQLEEAERRLEANSNGSQAPLALQPLLRRTCENEMAFLEKQRQDCFKEMKEAIEMVDRLQKKQGSVLSSLKLATGAASTSDQVDSKIFALKSRMEKIHTLTRETQERWLQIESLCGFPLLYLNETEHINRSIASSHFYNKSHEGSSSSGSISNAHSNPNAVNSNFVKKVSPPIPPSQQTANLRFVPTEQSDSIHSEDTSPIVEDVAISRSLTQDLAEADMQSIVSGSTNGSGSVAALKKRKGIFPKLFRRNTSKSSSLGGTSN | 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 activity of gonad sheath cells and spermatheca. Essential for fertility. Does not play a role in posterior body wall muscle contraction (pBoc) rhythmicity, intestinal cell oscillatory Ca(2+) signaling or intestinal ER Ca(2+) hemostasis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60021
Sequence Length: 530
Subcellular Location: Membrane
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Q13586 | MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK | 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 activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1 . Involved in enamel formation . Activated following interaction with STIMATE, leading to promote STIM1 conformational switch .
PTM: Glycosylation is required for cell surface expression.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 77423
Sequence Length: 685
Domain: The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.
Subcellular Location: Cell membrane
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Q9P246 | MLVLGLLVAGAADGCELVPRHLRGRRATGSAATAASSPAAAAGDSPALMTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVEESDEFIREDMKYKDATNKHSHLHREDKHITIEDLWKRWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTVSIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTMAKPPGSLARSSSLCRSRRSIVPSSPQPQRAQLAPHAPHPSHPRHPHHPQHTPHSLPSPDPDILSVSSCPALYRNEEEEEAIYFSAEKQWEVPDTASECDSLNSSIGRKQSPPLSLEIYQTLSPRKISRDEVSLEDSSRGDSPVTVDVSWGSPDCVGLTETKSMIFSPASKVYNGILEKSCSMNQLSSGIPVPKPRHTSCSSAGNDSKPVQEAPSVARISSIPHDLCHNGEKSKKPSKIKSLFKKKSK | 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 endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83971
Sequence Length: 746
Subcellular Location: Endoplasmic reticulum membrane
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P83093 | MLLFGLLVAGVADGCDLVPRHLRGRRASGSAGAAASPSAAAAGERQALLTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVPQFPGTVAKPAGSLARSSSLCRSRRSIVPSSPQSQRAQLPAHAPLAAHPRHPHHPQHPQHSLPSPDPDILSVSSCPALYRNEEEEEAIYFTAEKQWEVPDTASECDSLNSSSGRKPSPPSSLEMYQTLSSRKISRDELSLEDSSRGESPVTADVSRGSPECVGLTETKSMIFSPASRVYNGILEKSCSMHQLSSGIPVPHPRHTSCSSAGNDSKPVQEASNVSRVSSIPHDLCHNGEKSKKPSKIKSLFKKKSK | 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 endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx (By similarity).
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83925
Sequence Length: 746
Subcellular Location: Endoplasmic reticulum membrane
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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 STIM1, promoting STIM1 conformational switch . Involved in STIM1 relocalization to ER-PM junctions . Contributes to the maintenance and reorganization of store-dependent ER-PM junctions .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33187
Sequence Length: 294
Domain: The GXXXG motif may mediate oligomerization . The C-terminus is necessary for its localization at ER-plasma membrane (ER-PM) junctions as well as for the store-dependent rearrangement of ER-PM junctions .
Subcellular Location: Endoplasmic reticulum membrane
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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 STIM1, promoting STIM1 conformational switch. Involved in STIM1 relocalization to ER-PM junctions. Contributes to the maintenance and reorganization of store-dependent ER-PM junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32500
Sequence Length: 288
Domain: The GXXXG motif may mediate oligomerization. The C-terminus is necessary for its localization at ER-plasma membrane (ER-PM) junctions as well as for the store-dependent rearrangement of ER-PM junctions.
Subcellular Location: Endoplasmic reticulum membrane
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P83094 | MRKNTIWNYSLIFFCCVLKSISTLDHGPHTVSVDSNRHNTQHQYKQNPNVASQRHSSHESGQSLHNSQSEHVTHIAASHAGSGGEHSTHLAQNLHRSSYNLLSEAMSQAVSNEFSSMGSGSADGACAADDFDCYSGSVQDRFGMEAIASLHRQLDDDDNGNIDLSESDDFLREELKYDSGYEKRQKAFHFNDDMHISVKELWEAWLRSEVHNWTIEQTTDWLAQSVQLPQYVDLFKLHKVTGAALPRLAVNNLQYVGNVLGIKDPIHKQKISLKAMDVVLFGPPRETGTRWKDYILVTLLLSAIIGCWYAYQQNKNAKRHLRRMAQDMEGLQRAEQSLQEMQKELERARMEQENVATEKLDLERRLKEAPTLSSSNSDLEVQQLKKEIEMLRNELSRAEFELVDNCWSPPPQLQSWLQYTYELESKNHQKKRTSAEKQLQSAREACEKLRKKRSSLVGAFVSTHGKSIDDVDRSIVEARNALGDVTNELQERLHRWKQIETCLGLNIVNNNGLPYLENVLYGRNGGLQSSMGMSSTKGSRARITNSTEDLDDESIQGKLNFENFSLLATE | 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 | MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP | 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 to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol . Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state . In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity).
PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (Probable). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (Probable). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42596
Sequence Length: 379
Domain: In absence of cGAMP, the transmembrane and cytoplasmic regions interact to form an integrated, domain-swapped dimeric assembly . In absence of cyclic nucleotide (c-di-GMP or cGAMP), the protein is autoinhibited by an intramolecular interaction between the cyclic dinucleotide-binding domain (CBD) and the C-terminal tail (CTT) (By similarity). Following cGAMP-binding, the cyclic dinucleotide-binding domain (CBD) is closed, leading to a 180 degrees rotation of the CBD domain relative to the transmembrane domain . This rotation is coupled to a conformational change in a loop on the side of the CBD dimer, which leads to the formation of the STING1 tetramer and higher-order oligomers through side-by-side packing . The N-terminal part of the CBD region was initially though to contain a fifth transmembrane region (TM5) but is part of the folded, soluble CBD (By similarity).
Subcellular Location: Endoplasmic reticulum membrane
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P0DUE1 | MEKNGAHSFLSDTPVTSLTMSVPVLRHPHVYHAFISYCADADTSHARTILDSVESRGFTCCFAERDFLPGECTSDVVVDAIHCSKNVILVISPASLQSEWSKFEMLMAVDDSHQRNNVCLVPVLLGGVKVDDLPPPLRPLTCIELMDDFRNTDDIIQAISKPEDTWESLLPVGNLAHGFAWGYYYGYLKIILPDLDKTVRQWRRVNNAEGRMSEKLFLFFPQSCRCRDSIADESSLIKHRGHLPIITKDRAGIIERQYKNTIYSVTDDNGEDYFFAGEYIGVIHTMFEMEQNATTGLQTREKYVQSMRFYLTLKRILDTDPECSKKCKIVFYKDVNNSSDAMPKLICNEIKNQLRKESSDDTTVCMTPFNSPFPSISSPDFARCSLKSPSSTNMVKSEPNIYREESGKTKSVERG | 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
Sequence Mass (Da): 47031
Sequence Length: 415
Domain: Homodimerizes by swapping the N-terminal TIR and C-terminal nucleotide-binding domains. Ligand binding induces lid closure and repositions the TIR domain . The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity (By similarity).
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Q39228 | MAGGFVSQTPGVRNYNYKLTPKVFVTCFIGAFGGLIFGYDLGISGGVTSMEPFLEEFFPYVYKKMKSAHENEYCRFDSQLLTLFTSSLYVAALVSSLFASTITRVFGRKWSMFLGGFTFFIGSAFNGFAQNIAMLLIGRILLGFGVGFANQSVPVYLSEMAPPNLRGAFNNGFQVAIIFGIVVATIINYFTAQMKGNIGWRISLGLACVPAVMIMIGALILPDTPNSLIERGYTEEAKEMLQSIRGTNEVDEEFQDLIDASEESKQVKHPWKNIMLPRYRPQLIMTCFIPFFQQLTGINVITFYAPVLFQTLGFGSKASLLSAMVTGIIELLCTFVSVFTVDRFGRRILFLQGGIQMLVSQIAIGAMIGVKFGVAGTGNIGKSDANLIVALICIYVAGFAWSWGPLGWLVPSEISPLEIRSAAQAINVSVNMFFTFLVAQLFLTMLCHMKFGLFFFFAFFVVIMTIFIYLMLPETKNVPIEEMNRVWKAHWFWGKFIPDEAVNMGAAEMQQKSV | 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 | MAGGGLALDVSSAGNIDAKITAAVVMSCIVAASCGLIFGYDIGISGGVTTMKPFLEKFFPSVLKKASEAKTNVYCVYDSQLLTAFTSSLYVAGLVASLVASRLTAAYGRRTTMILGGFTFLFGALINGLAANIAMLISGRILLGFGVGFTNQAAPVYLSEVAPPRWRGAFNIGFSCFISMGVVAANLINYGTDSHRNGWRISLGLAAVPAAIMTVGCLFISDTPSSLLARGKHDEAHTSLLKLRGVENIADVETELAELVRSSQLAIEARAELFMKTILQRRYRPHLVVAVVIPCFQQLTGITVNAFYAPVLFRSVGFGSGPALIATFILGFVNLGSLLLSTMVIDRFGRRFLFIAGGILMLLCQIAVAVLLAVTVGATGDGEMKKGYAVTVVVLLCIYAAGFGWSWGPLSWLVPSEIFPLKIRPAGQSLSVAVNFAATFALSQTFLATLCDFKYGAFLFYGGWIFTMTIFVIMFLPETKGIPVDSMYQVWEKHWYWQRFTKPTST | 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 | MAVVVSNANAPAFEAKMTVYVFICVMIAAVGGLIFGYDIGISGGVSAMDDFLKEFFPAVWERKKHVHENNYCKYDNQFLQLFTSSLYLAALVASFVASATCSKLGRRPTMQFASIFFLIGVGLTAGAVNLVMLIIGRLFLGFGVGFGNQAVPLFLSEIAPAQLRGGLNIVFQLMVTIGILIANIVNYFTATVHPYGWRIALGGAGIPAVILLFGSLLIIETPTSLIERNKNEEGKEALRKIRGVDDINDEYESIVHACDIASQVKDPYRKLLKPASRPPFIIGMLLQLFQQFTGINAIMFYAPVLFQTVGFGSDAALLSAVITGSINVLATFVGIYLVDRTGRRFLLLQSSVHMLICQLIIGIILAKDLGVTGTLGRPQALVVVIFVCVYVMGFAWSWGPLGWLIPSETFPLETRSAGFAVAVSCNMFFTFVIAQAFLSMLCGMRSGIFFFFSGWIIVMGLFAFFFIPETKGIAIDDMRESVWKPHWFWKRYMLPEDDHHDIEKRNA | 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: Membrane
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O04249 | MAGGSFGPTGVAKERAEQYQGKVTSYVIIACLVAAIGGSIFGYDIGISGGVTSMDEFLEEFFHTVYEKKKQAHESNYCKYDNQGLAAFTSSLYLAGLVSTLVASPITRNYGRRASIVCGGISFLIGSGLNAGAVNLAMLLAGRIMLGVGIGFGNQAVPLYLSEVAPTHLRGGLNMMFQLATTIGIFTANMVNYGTQQLKPWGWRLSLGLAAFPALLMTLGGYFLPETPNSLVERGLTERGRRVLVKLRGTENVNAELQDMVDASELANSIKHPFRNILQKRHRPQLVMAICMPMFQILTGINSILFYAPVLFQTMGFGGNASLYSSALTGAVLVLSTFISIGLVDRLGRRALLITGGIQMIICQVIVAVILGVKFGDNQELSKGYSVIVVIFICLFVVAFGWSWGPLGWTIPSEIFPLETRSAGQSITVAVNLLFTFIIAQAFLGLLCAFKFGIFLFFAGWVTVMTIFVYFLLPETKGVPIEEMTLLWSKHWFWKKVLPDATNLEDESKNVSV | 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 | MELDKDIQTTQKGFHCNLCHVNIPNRPSLEDHVKGKKHLHLLRLRAQRKTQEENSVFVSGFKADTSQTELKEYFQQFGLVTDVIMDKQKGVYAIVEFSESQDVQTTLAQPQHQLNGLKLRVKPREKKEFKLASRGKQDCKNTLISLDKLNFELCKAMSVNEQIQKVVESLELKDNEKKVRDLLVQLLQEVFTEFFPDCQIVPFGSSVNTFGLHSCDLDLFLDLENTKVFQARAKSSEQTGENQSEDCRSEDSILSDIDLSTASPAEILELVAVILRKCVPGVHKVQALSTARLPVVKFSHKELNLQGDITINNRLAVRNTKFLQLCSGIDSRLRPLVYTIRLWAKQKQLAGNLSGPGPLLNNYALTLLVIFFLQNRDPPVLPSVNQLKNMACEEEECAIEEWDCTFPSQPFSVPPSKNTEDLCTLLFGFFTFYSKFDFPASVVSLRDGHVLPITDFLKSDMEALKTADASSPKPKRSSAPRLGPMNVLDPFELNHNVAGNLNERTQKNFKRECCEAEKYCRSLQYQRKSAKGKSWGLVRLFAPQSEAAASSQPRAEKVLEVSVPFKPASLPESLRAQLASAGKDFRGLWFAEVCSAVQKVFNEILQCSPTEETQSLDKTDKSGSEMEVNNNRSLEDTNIQVKGEAGKKRPLSVEEGPSTFTITQAKRQRLDVDLEHPEPLHWTWTQRSRVWAGRRKVRRDLLKTSDEASKPEGGCVDMESRVTQSIVEKEEKLHDALEFKVDAEVVGGNESTKVVLRFHPSIDTAGVFQDFFHFLESFLPKMAETIMGRAEDITDMS | 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 complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase.
Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
Sequence Mass (Da): 89937
Sequence Length: 797
Domain: The zinc-finger domain is required for terminal uridylyltransferase activity. Together with the RRM domain, binds the 5'-area of U6 snRNA.
Subcellular Location: Nucleus
EC: 2.7.7.19
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Q9H6E5 | MAAVDSDVESLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRAARKAQGLRSVFVSGFPRDVDSAQLSEYFLAFGPVASVVMDKDKGVFAIVEMGDVGAREAVLSQSQHSLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLAKALAEAADVGAQMIKLVGLRELSEAERQLRSLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEEPQPVPKAPESPSLDSALASPLDPQALACTPASPPDSQPPASPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLLEDREEGDLGKASELAETPKEEKAEGAAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASRLEPSINVEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGGLPSNLWEGLRLGPLNLQDPFDLSHNVAANVTSRVAGRLQNCCRAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPLAPFTQLTAALVQVFREALGCHIEQATKRTRSEGGGTGESSQGGTSKRLKVDGQKNCCEEGKEEQQGCAGDGGEDRVEEMVIEVGEMVQDWAMQSPGQPGDLPLTTGKHGAPGEEGQPSHAALAERGPKGHEAAQEWSQGEAGKGASLPSSASWRCALWHRVWQGRRRARRRLQQQTKEGAGGGAGTRAGWLATEAQVTQELKGLSGGEERPETEPLLSFVASVSPADRMLTVTPLQDPQGLFPDLHHFLQVFLPQAIRHLK | 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'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs . In addition to adenylyltransferase activity, also has uridylyltransferase activity . However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase . Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA . Not involved in replication-dependent histone mRNA degradation.
PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
Sequence Mass (Da): 93847
Sequence Length: 874
Domain: The zinc-finger domain is required for terminal uridylyltransferase activity . Together with the RRM domain, binds the 5'-area of U6 snRNA .
Subcellular Location: Nucleus
EC: 2.7.7.19
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A9JTS5 | MEAEESSSSVVPLPQDVQSVVRGGFRCLLCGVNIPNRPSLTDHLSGRRHVRLHEERDKRNQQQERSVYVSNFPRETSEEQLRDVFQKISPVRNIVMDKDRGLYAIVEFESKDGMCAALEEPQIKLSGKRLRVKPREKKEFQRKKGGSPRTLQPPDPEALSKELLNCADVEQQIKKLVSLCSPSHHESHLRELLLSLLQETFTEFFPGCQLLPFGSSVNGFEISGCDLDLYLDLGDDEAENVEGKAEKEIQNREESSTDMEVSMEDPETERKEEEMEIGNSKNDEDEDVTPGLSLKGLSSEEILEVVGKVLRHCVPGVHGVQSVPTARRPVIHFQHKTSGLRGDVTLNNRLALRNSSFLRLCSDLDARVPQLVYTVRYWARVNQLAGNPFGGGPLLNNYALTLLVFFFLQTRNPPVLPTLVHLREETANEVPQVIDGWDCSFPSDPAQVKESGNQQSLSSLLSEFFSFYASLDLHLLILCPCNGLTIPLPFSSPPPAWSEGFRLGPLNIQDPFELSHNVCGNVSSRAARRFISHCAAAARICRTPNYNLHSTSHPWGITPILLPPPTERECVGRGGTEISIPLGGVSPEKTYAAVSKVFVDVLLCTLEEGREDSCQEGKALELSTKHAKAQCKVEKNEVGGELGEQEVPCKAEQNNTKEASKQKSIFKTEEGMTESARRKREMTEPCMSDMTNGKKRRLEFTRGIWDHHLATSAMEEEMCGEAHKDSKTKIDYSNNGTAQWELLVWHRVWEGRRKERRRKQKGEADGVELEIAVSQALALEKEDKCDGPLMKLILTAQLTVKESLQLYLTPKFDPQGLSSTFFHFLESYLPRMVAQIQGCGDPV | 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 complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase.
Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
Sequence Mass (Da): 94496
Sequence Length: 843
Domain: The zinc-finger domain is required for terminal uridylyltransferase activity. Together with the RRM domain, binds the 5'-area of U6 snRNA.
Subcellular Location: Nucleus
EC: 2.7.7.19
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A0A348B793 | MSPTSDFVNTTSTAKGHEIIAGLTAKPVEGSTITLCKDIIREFFDKVQVPSPNFTRDPELEARVADIVRTWGNEEHLRPYVVTSLILTVTAYSHIANFETRVQITLFTIIIIAMDDPVVFDSLATREFHQRMCTGVIQDEAGMLGAFTKILESMWDHYSGFSANTIYASALRFVNASIIENETDVTTLRSHALPFVEYKRSMTATTEAYACFIWDKARFPDVKVYMQAIPDAMLYVSYVNDILSFYKEELAGETANYIHERAYVTGKSIPDTLRNLINETASAVERVRDILGEGEARAAFENFAAGYIRVHTGNPRYHLKDVIGGDYIIDRV | 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 | MSAVTQVVETAIGCVIPSCIEFGSSMRIATSLGSPSVTQSPCVNRDVEDIARTARESIRFFLAELSIECVPYTQDPALEAQVASATRCWPDRERLAPHIRTGIVIAATAYAHNSLATRTLIALYTAIGVALDEPDILESANAIGFHHSLCTETSERPSAILDEWRRILARMWDHFPRFGASCILTSTLQFLNMTMLENETKGKVLNRTAMPFVEYRRMTDGFPEVYTAFIWEKGRFPDVQVYMQAIPNAMRFINFGNDILSFYKEEAAGETGTYIHDRARLTGLSSVETLREVVEETVSAWRQVCEILGEGIARDAWNSFVRGYVTFHVHNPRYRLSELL | 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 binding to Mg(2+).
EC: 4.2.3.-
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K4LMW2 | MAVYVNSTTGPPSSVVRNSAGFHPSIWGDTFIPSGNSAVQKTDVDRKEEENLQLLKQEVKKMLTAGDTCQQDLICLIDDIQRLGLSYHFEAEIDTLLQHVKDSYLEYYGTKNHDNLHDVALSFRLLRQEGHNISSDVFSKFQDSDGKFNEKLVKDVRGMLSLFEAAHLSVHGENILEDALEFTTSHLNSYLNSNPNAPLADLVRRALKYPLRKSFNRMVARHYISIYHKYYWHKQVLLDLAKCDFNLVQKVHQKELGYITRWWKDLDFTNKLPFARDRVVECYFWITGVYFEPRYAAPRKFLTKVISLTSIIDDIYDVYGTPEELVQLTDAIDKWDINILDQLPEYMRHAYKPLLDVFAEGEEEMAKEGLPTYGVDYAKEAFKRLTVTYLHEAKWLQAQYFPTFEEYMSVALVSGAVKMLSVSSFVRMGNIATREAFEWLSKDPLIVNGLSVICRLSDDIVGHEFENQRPHIPSAVECYMKSHHVTKETAYAELRKPIINAWKDMNEECLQPEAPPKPLLERVFNLARVINFLYDGHDGYTHSSTRTKDMITSVLINPIPA | 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-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.3.143
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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) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34400
Sequence Length: 297
Subcellular Location: Cell membrane
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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 | MGKDRLPELLQRSLSTNSSNSSSNGSLLLNVYSGTTEFIIGNTGGNNNSYSVVSQNSHSCSNNNSSTEPKDRSSSKMTQYGSNVDDILNPYTEIRQQLAQIAANLETMNRMAQTVNLRTFNENEMDELHNKNLRLGNQLMTRFNDFKANLPAENDYSLEARMKRTLFYGLHQTFINLWHKNELFLQNYETKVKKNLRLHTKIINSEASEQEIELLIENKTTKLFVDNFLQETEKERQTLREMMDRFNELRRLEKSIEEVHALFMRIQTLVMEQSEVIQRVEFHAQQATLHVDKGADELDQAEQHQKKARKKKIMLIVILAAVLLVLLLVGIYL | 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) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity). Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34180
Sequence Length: 297
Subcellular Location: Cell membrane
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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) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane . Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34195
Sequence Length: 298
Subcellular Location: Cell membrane
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Q20797 | MSDFHNIRSRRRIPEASSYSTVDFDYDPDQKNHTSAVAPTSFAYSSLTTVFNASASQLWNSAQEALVSSYDTAEGTESIDADRSKVVETLESLSIFGNPLDHIIITMPSRDRTSEFRATAKSYEMKAAANGIRPQPKHEMLSESVQFNQLAKRIGKELSQTCAKMEKLAEYAKKKSCYEERSQIDHLSSIVKSDITGLNKQIGQLQEFSKRRAGNMKNQNSGHIQLVVVGLQSKLANVGKDYQSVLEISTETMKAEKNRRDKFSSGAAVPMGLPSSSSGANVRSKLLQDDEQHGSSSIALDMGALSNMQSQQTMQQRDSSLEYAQARSNTMATIEGSISELGQIFSQLASLVSEQGEMITRIDSNVEDTALNIDMAHSELVRYLQNISKNRWLMIQVFGVLMVFFVVFVLFLT | 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 | MQTRRRLHQTDQQDYSSSSTYTIQEDQQGGAGAGSVGTGTAGGSVGLLAQSLVPPPTGHEAAIHIGDNYQSGDSISTPDYSDDKYGKAARQWNLRAFSGHALRTLSAAAAVVTGNQPGINNDSQSNYSYPASIPTSSQFYQSKEEPQETEPEPEIFVMAARDRTGEFANAIRSLQARNITRAVNIRDPRKAKQVQSYSEFMMVARFIGKNIASTYAKLEKLTMLAKKKSLFDDRPQEIQELTYIIKGDLNALNQQIARLQDISKDQRRHTNGKHLVSHSSNMVLALQSKLASMSTDFKQILEVRTENLKQQKTRRDQFSQGPGPLAAHTVSPSTAKQGSLLLSEENQAVSIDMGSSDTTPLLSTQTQMAIYDDSDNYVQQRAETMQNIESTIVELGGIFQQLAHMVKEQEEIVERIDTNVADAELNIEAAHGEILKYFQSVSKNRWLMIKIFGVLIFFFLFFVVFMS | 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 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAGSSSSDIAPLPPPVTLVPPPPDTMSCRDRTQEFLSACKSLQTRQNGIQTNKPALRAVRQRSEFTLMAKRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRSRREQFSRAPVSALPLAPNHLGGGAVVLGAESHASKDVAIDMMDSRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHSEILKYFQSVTSNRWLMVKIFLILIVFFIIFVVFLA | 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 (Da): 39673
Sequence Length: 355
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q8K1E0 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAISSSSDSTPLPTPVALVPSPPDTMSCRDRTQEFQSACKSLQSRQNGIQTSKPALHAARQCSEFTLMARRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRNRREQFSRAPVSALPLAPNNLGGGPIILGAESRASRDVAIDMMDPRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHSEILKYFQSVTSNRWLMVKIFLILIVFFIIFVVFLA | 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 (Da): 39713
Sequence Length: 355
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q08851 | MIPRKRYGSKNTDQGVYLGLSKTQVLSPATAINSSSDIAPLPTPVALVPSPPDTMSCRDRTQEFLSACKSLQSRQNGIQTNKPALHATRQCSEFTLMARRIGKDLSNTFAKLEKLTILAKRKSLFDDKAVEIEELTYIIKQDINSLNKQIAQLQDFVRAKGSQSGRHLQTHSNTIVVSLQSKLASMSNDFKSVLEVRTENLKQQRNRREQFSRAPVSALPLAPNNLGGGPIVLGGESRASRDVAIDMMDPRTSQQLQLIDEQDSYIQSRADTMQNIESTIVELGSIFQQLAHMVKEQEETIQRIDENVLGAQLDVEAAHSEILKYFQSVTSNRWLMVKIFLILIVFFIIFVVFLA | 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 (Da): 39751
Sequence Length: 355
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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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 Location: Membrane
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C5P6D1 | MRLFQSTCVLVGTVLPLFTAFPISSPREIEIIPDKYIITFKKGIDQAAIEAHTAWVSSVQARNTARGFTTAETPGLERMFSIHNFNAYSGSFDRETIEEIRSHPNVESVEPDSMAYVTELIEQRNATYGPRRISHREIPTGDNSYWYDSKAGEGSFVYIMDTGINKAHVDFEGRAIPGVNLHDVAFDDTHGHGSHCAGIAGSKTYGVAKKATIVDVKVFTRGGGAWSLLMGGLDWSVKNITGEDRQAKSAVSISISGPTNQAMNNAVKAAVEAGVTVVVASGNDGRDAGRNSPGSAPESITVGSINSRRGMDTRSSFSNYGSSVAIHAPGEGIISTYKGSRDATANMSGTSMAAPHVAGLIAYLQSIHDLPDPAAARRKLLELATSDKIQDVRGSANKLAYNGSGK | 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 | MQLLNFGLLLLPFVAGDLAPQPEPLLAGPSDVVPGQYIVTLKEGLTSAQIRDHKKWVSSVHRANLDSFAAGASGVETEGIMKHFHIHDLNMYSGGFDEKTVEDLSRNPYVKSVHPDQHVYLAKTVTQRQARWGLGYMSSKGKPVPLHSTLVDYSYDDKAGEGVWAYVLDTGINVNHVEFEGRGILGHNAIPNKPHTDEFGHGTYVAGIIAGKTYGVAKKANVVSAKAFDTGSSTYNYILETYDWIVRNITDSNRKNKAVINLSISGAKYQPFDDAVEKAFKAGITTVVAAGNDGKDAKNNTPASSPNAITVGAVRWENTRPSFSNYGKLVDIWAPGELIKSCWKGGNNATSTQSGTSAASPHVAGLVAYLMSIENLPSPSAVTARVLNLTIPNLVKDAKDSPNRVAYNGIQERKFTLPKYY | 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 | MSHEEDLIDYSDEELQTTDAAATTAAPAANGAQDKKGDLTVSGGRPDKKGSYVGIHSTGFRDFLLKGELLRAITDCGFEHPSEVQQVCIPTAILNVDVLCQAKSGLGKTAVFVLTTLHQLEPVPGECSVLVMCHTRELAYQIKNEYARFSKYLPDVKTAVFYGGTPIQKDVEVLSNKESYPNIVVGTPGRLNALVRDKKLSLRNVKAFVLDECDKMLDQIDMRRDVQEIFRATPADKQVMMFSATLSQEIRPICKKFMRNPLEVYVDDDTKLTLHGLQQYYIKLSESEKNRKLNELLDSLEFNQVIIFVKSTLRANELDKLLRECNFPSIAVHSGVSQEERIKRYKEFKEFNKRICVATDVFGRGIDIERINLAINYDLPADADSYLHRVGRAGRFGTKGLSISFVSNEDDEKVLKEIEKRFEVALPEYPEGGVDSSTYMA | 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: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49587
Sequence Length: 441
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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O13750 | MFKTQTTLLTSLRRFSSSSQLKNSKSLYEQTIPNLMINSDTKVIFQGFTGKQGTFHAQHAMDYGTKVVGGTNPKKAGTTHLGKPVFGTIEEAMKETKADASAVFVPPPLAAGAIEEAIAAEVPLIVAITEGIPQHDMLRVSDILKTQSKSRLVGPNCPGIIRPGQCKIGIMPSHIHKPGCIGIVSRSGTLTYEAVNQTTQTDLGQSLVIGIGGDPFPGTNFIDALKLFLDDPNTQGIILIGEIGGSAEEDAAEFIRAANASRSTPKPVVSFIAGATAPKGRRMGHAGAIVAGGKGTAAAKFEALEAAGVRISRSPATLGSLIVEELNKLKH | 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 binding and nucleotide specificity is provided by the beta subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 34706
Sequence Length: 331
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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P53598 | MLRSTVSKASLKICRHFHRESIPYDKTIKNLLLPKDTKVIFQGFTGKQGTFHASISQEYGTNVVGGTNPKKAGQTHLGQPVFASVKDAIKETGATASAIFVPPPIAAAAIKESIEAEIPLAVCITEGIPQHDMLYIAEMLQTQDKTRLVGPNCPGIINPATKVRIGIQPPKIFQAGKIGIISRSGTLTYEAVQQTTKTDLGQSLVIGMGGDAFPGTDFIDALKLFLEDETTEGIIMLGEIGGKAEIEAAQFLKEYNFSRSKPMPVASFIAGTVAGQMKGVRMGHSGAIVEGSGTDAESKKQALRDVGVAVVESPGYLGQALLDQFAKFK | 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 binding and nucleotide specificity is provided by the beta subunit (By similarity).
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 35032
Sequence Length: 329
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q148D5 | MAASVFYSRLLAAATLRSHRPRTALPAAAQVLGSSGLFNNHGVQIQHQQQRNLSLHEYLSMELLQEAGVSIPKGHVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERRYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAETPEAIVKEPIDIVEGIKKEQAVRLAQKMGFPASIVDSAAENMIKLYDPFLKYDATMVEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLSILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPIVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKQAQVDVKFQLPI | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 50130
Sequence Length: 463
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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P53588 | MIGRISQPLLNTSQKFMAPAARTLMLHEHHGMKILQNYEIKVPPFGVAQDAETAFSEAKRIGGKDYVVKAQVLAGGRGKGRFSSGLQGGVQIVFTPDEVKQKAGMMIGANLITKQTDHRGKKCEEVMVCKRLFTRREYYFSITLDRNTNGPIVIASSQGGVNIEEVAATNPDAIVKMPIDVNVGITKELAHEIAVKMGFSKDCEQQASEIIEKLYQMFKGSDATLVEINPMAEDVNGDVYCMDCKLLLDSNAEFRQAKLFDLKDKKQEDELEIRAAAANLNYIRLDGTIGCMVNGAGLAMATMDIIKLHGGEPANFLDVGGGATVEQVTEAFKIITADKDKVSAILVNIFGGIMRCDVIAQGIIQAARELDLKIPIVVRLQGTKVEDAKALIATSQLRILPCDNLDEAAKMVVKLSNIVDLARATNVDVKFELSI | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 47419
Sequence Length: 435
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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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 succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 2248
Sequence Length: 20
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q9YI37 | RRLSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGTFEGGLKGGVKIVFSPEEAKAVSSRMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGIKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDWTQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSEIVTLAKQAHLDVKFQLPI | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 44975
Sequence Length: 413
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q55AI5 | MLSNIVKKTIQSSKNLKSLVLNKSTSSLVYQKRFLNVHEYQAQKMMKSYGINCPVGNVAETPEEAEKIAEVMNTQDLVVKAQVLAGGRGKGIFTSGLKGGVQLCSSAEDVKKFASKMLGHTLVTKQTGEDGKVVHQVYVTERHFLRKEMYFAILMDRKAGGPVMVASPEGGVDIEGVARDNPSAIFKEPIDIMIGVQPEQTKRLAEKLGFSKKNISMAQDQMKKLYDFFIKNDCTLVEINPLAETASGDVLCMDAKLNFDDNAAFRHPDIFKLRDKSQEDPREVKAAEFDLNYIGLDGNIGCLVNGAGLAMASMDIIKLYGGSPANFLDVGGGATQKQVTEAIKLISSDKKVKSILVNIFGGIMKCDVIALGIIAALKELSIATPLVVRLQGTNVEAAKKIMEDSGLRLIAADNLDDAAQKSVRIAEIVSLAEKSDLEISFKLPL | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 48350
Sequence Length: 445
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q9P2R7 | MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 50317
Sequence Length: 463
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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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 succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 24249
Sequence Length: 221
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q9Z2I9 | MAASMFYGRQLAAAALRSHRPQTTLRAAAQVLGNSGLFNKHGLQVQQQQQRTLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDWSQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAILVNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 50114
Sequence Length: 463
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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P53589 | MLRAAGNLSKSMMKSQRRFLNLQEFQSKEILEKHGCSVQNFVVASNRKEAEEKWMSFGDHEYVVKAQILAGGRGKGKFINGTKGIGGVFITKEKDAALEAIDEMIGKRLVTKQTTSEGVRVDKVMIAEGVDIKRETYLAVLMDRESNGPVVVASPDGGMDIEAVAEKTPERIFKTPIDIQMGMTEGQSLKIAKDLQFEGKLIGVAAQEIKRLYDLFIAVDATQVEINPLVETADGRVFCVDAKMNFDDSAAYRQKEIFAYETFEEHDPREVDAHQFNLNYIGMDGNIACLVNGAGLAMATMDLIKLHGGEPANFLDVGGAVTEDAVFNAVRIITSDPRVKCVLINIFGGIVNCATIANGVVSAVNKIGLNVPMVVRLEGTNVDAAKQIMKKSGLKILTANNLDEAAAKAVSSLPK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: CoA + GTP + succinate = GDP + phosphate + succinyl-CoA
Sequence Mass (Da): 45092
Sequence Length: 415
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.4
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Q9YI36 | EYQSKKIMADHGVTVQRFFVADSANDALEAAQRLKAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPKIVEQLAKQMIGYNLSTKQTPKDGVTVKKVMVAEALNISRETYFAILMDRACNGPVMVGSPQGGVDIEEVAVTSPELIFKEEIDIFEGIKDHQALQMAKNLGFKGPLQQQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKEIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIISLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITRACRELELKVPLVVRLEGTNVHEAQRILNESGLPIMSANDLEDAAKKAVASVAKK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: CoA + GTP + succinate = GDP + phosphate + succinyl-CoA
Sequence Mass (Da): 42343
Sequence Length: 391
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.4
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Q96I99 | MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: CoA + GTP + succinate = GDP + phosphate + succinyl-CoA
Sequence Mass (Da): 46511
Sequence Length: 432
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.4
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P53590 | IPAAPVAAQARKLLRDLAFRPPLLAARSQVVQLTPRRWLNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFSSGLKGGVHLTKDPEVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIEGIKDSQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVHEAQNILTNSGLPITSAVDLEDAAKKAVASVTKK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: CoA + GTP + succinate = GDP + phosphate + succinyl-CoA
Sequence Mass (Da): 46803
Sequence Length: 433
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.4
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O82662 | MRGLVNKLVSRSLSISGKWQNQQLRRLNIHEYQGAELMGKYGVNVPKGVAASSLEEVKKAIQDVFPNESELVVKSQILAGGRGLGTFKSGLKGGVHIVKRDEAEEIAGKMLGQVLVTKQTGPQGKVVSKVYLCEKLSLVNEMYFSIILDRKSAGPLIIACKKGGTSIEDLAEKFPDMIIKVPIDVFAGITDEDAAKVVDGLAPKAADRKDSIEQVKKLYELFRKTDCTMLEINPLAETSTNQLVAADAKLNFDDNAAFRQKEVFAMRDPTQEDPREVAAAKVDLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANFLDVGGNASEHQVVEAFKILTSDDKVKAILVNIFGGIMKCDVIASGIVNAAKEVALKVPVVVRLEGTNVEQGKRILKESGMKLITADDLDDAAEKAVKALAH | 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 enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 45346
Sequence Length: 421
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Subcellular Location: Mitochondrion
EC: 6.2.1.5
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Q8EFN8 | MNLHEYQAKSLFAEYGLPVSEGFACDTAQEAVEAAGRIGGNLWVVKCQVHAGGRGKAGGVKVTGDKEEIRAFAEYWLGKNLVTYQTDEKGQPVAKILVESCTDIANELYLGAVVDRATRRVVFMASTEGGVEIEKVAEETPELIHKAIIDPLTGPQPFQARDLGFKLGLNPTQMKQFTKIFMGLATMFVDHDFALLEINPLVITTEGNLHCLDGKIGIDGNALFRQPKIKAMHDPSQDDAREAHAAMFELNYVALDGNVGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVAEAFKIILSDSNVKAVLVNIFGGIVRCDMIAEGIIGAVKEVGVKVPVVVRLEGTNAELGREVLAKSGLDIIAANSLTDAAELVVKAAEGK | 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 specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Mass (Da): 41362
Sequence Length: 388
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
EC: 6.2.1.5
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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 direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process.
Sequence Mass (Da): 15868
Sequence Length: 138
Pathway: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular Location: Cytoplasm
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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, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure (By similarity).
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 29158
Sequence Length: 267
Subcellular Location: Cytoplasm
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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 to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure.
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 29088
Sequence Length: 267
Subcellular Location: Cytoplasm
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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 to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure.
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 30234
Sequence Length: 275
Subcellular Location: Cytoplasm
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P15715 | MARTPAKYCDLVMKGGITSGIVYPNAALALARDYRFKNIGGTSAGAIAAAACAAAAVGDRRKQMKAAIAQPEERVGFEGLAKASANLASPGFIKDLLQPAAGAGQAFRLLVTLAGNTGVLRKGVALLGSVVRIAPVETLLLLAALAGLAYAVGGQTGMIAAALPAAICAYLGGVVFAVLRIARVLRRNLMGLCTGTAPDQPARRPRMVLTDWLHETLQALSGKASGQPLTFGDLWTAERYPGEPGSDRAVTLKMITTGISHQEPRSLPFESALFWFRRKEFEALFPKVVVDWMVEKAGEPVTVAGEDYYLLPHGADMPVLVATRMSLSFPLLISAVPLHEPARRESLPGSDGENEAEDTTSDEDEQKTVLDSTEALTTGGKKRRARPAAFRICWFSDGGISSNFPIHLFDRALPRWPTFAINLVYPETSDTGSRPEVFLPENNRQGWQRHYQPIARKSAVHELCAFVFAIVATMQNWRDLLQSRAPGHRERIVHVSLSPQEGGLNLAMSKEVLAAVSKKGTAAGEAFARFSFENHYWIRWRNLASALQRYTIDIAASDAYRPKIPDYEPAYALAHDATSKPPSYRFASKAEREEAARLLEKLIGEGEKWSGEGPDLTKTAPRPLPQLQIAPTY | 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 | MFKRIALVCALFSGVCFAEGKQLLDKVVAIVNDNVITSSELNAQVELSKKQIIAQNMQMPDESVLRKQVLQHLIDVDLEMQMAKQNGITIENAEIDEAIEKIAASNHLNLSQMRDEITKQGISWQEYRQNIRKEMLISRVQQKAVGKDIIVTNEQVEQYLKTSGRIENSNLTYHLKNIVIPLSEEPTTKQLQRAKIEAENLLNKIKKGEDFSRLAIEESSGEFALEGGDLGERHLAELPEVFAKEVVHMKVGQVAGPIRAGNGFHLIKLVAVGGENQRHVITQTHVRHILLKPDASMVPSEAIKQVNNIYRQIQSGKDFALMAKQYSLDAASAVKGGDLGWVNPGELVPEFEKTMNSLPLHKVSKPVKTQYGWHLIEVIARRQKDDSEAFKKQQVRQFLQQRKFVEAVQNWQQHLRSQAYINIVDKDLA | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48492
Sequence Length: 429
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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Q60B78 | MKISSFRKGRWLGALALFAVVCWSMADAAVDRIVAVVDDGVILESELVRKVDEIKRSLRASRASLPPDSVLVRQVLERMIVDKIQIQMAEKMGIQVDDDTLRMAVSQIAQRNNLTPDQFRRSLAREGIDYGDFLDQVRSEIAMGRLRASQINNQIKISDREVEHYLEAQGGSGAVADREYRLGHILIATPREASPDEVKKARERADRVVKELKAGLDFKDASIRYSDDPQALEGGDLGWRKLSEIPSHIAEVVGGMKDGEVSDPIRSPGGYHIVKMLAMRGVGEAKLTKTHVRHILIRPNEVLSDEDAKNKLLALKTRIENGDDFAELARGHSDDKGSAIKGGDLGWVKPGALVPPFEEAMNALDENQLSDPVQTQFGWHLIQVLERQESSDTNEVLKNRARDELFKRKVDEETELWLRKIRDEAYVEIRLDETPASPGEDAPAGEDSPETFMR | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50789
Sequence Length: 454
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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Q1GZC0 | MHNHVFKTIARHGLIALFFFFSISAMAAEVAKMDRIVAIVDQGVITEKELEDRIQTVIAQLEKQGTQLPPRDVLQKQILERLINDRLQLQYAAQTGLRVDDAQLDKTIERIAEQNKLSTGEFRKALEAEGIPYRKFREDIRNEIILARLREREVDNRVNVTESEIDNFLTTQSSRNDIQDEFEVAHILIRAPEESTPEELQKLKAKAEAALKELQSGADFAQVSAGYSDAPNALEGGILGWKASSQLPSLFVDALQALQPGQLSPVLRSPNGYHILKLLNRRGGSSPLVVDQTHVRHILIKLSEVVSELEAEQKINSIKERLDHGADFAELARQYSEDASANNGGDLGWTNAGDTVPAFEKAMNALDINEISAPVRTPFGWHIIQVLERRKQDMTQESARLKARQEIRARKADDAFQDWLSELRDRAYVEYRLEDKY | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49426
Sequence Length: 437
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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Q82W17 | MIQFSSDRQLKFRKYWLIYAVFATMLAADVFAQSSYSREDIKPIDRIVAVVNEEVITQQEINEVLQNTVQQLQRQNTQLPRMEILEKQLLERLILKRIQLQRAKEIGLTVSDNDLDQTLRRIIQDNHLTMDEFRQVLLQEGTDMNRFREEIRGEILMSRLKEQEVNSRVNVTENEIDNFLQNQANSPAGNEEYRIAHILVQISEQMDEAQIEARHKRAETAYESLRQGADFVRVSAEFSDAPDAMQGGELGWRPLGQLGSPFTEMLVNMQPGEVTPVVRSPVGFHILKLLERRQQEQKVTIIEQTHAQHILIKVSELVSEEDAHQLINQLMERIHNGADFMDVAKAHSEDASASAGGDLGWVSPGDTVPEFEQAMNALLPGQVSPPVRTPFGWHLIKVIERRSQDVSERQQREAARHTIHARKADAIVQEWLQQLRDQAYVEYKVEDN | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51556
Sequence Length: 448
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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