ID Q0AXM0_SYNWW Unreviewed; 612 AA. AC Q0AXM0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 04-NOV-2026, entry version 104. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=Swol_1225 {ECO:0000313|EMBL:ABI68534.1}; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; OC Syntrophomonadaceae; Syntrophomonas. OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI68534.1, ECO:0000313|Proteomes:UP000001968}; RN [1] {ECO:0000313|Proteomes:UP000001968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968}; RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x; RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.; RT "The genome of Syntrophomonas wolfei: new insights into syntrophic RT metabolism and biohydrogen production."; RL Environ. Microbiol. 12:2289-2301(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000448; ABI68534.1; -; Genomic_DNA. DR RefSeq; WP_011640637.1; NC_008346.1. DR STRING; 335541.Swol_1225; -. DR KEGG; swo:Swol_1225; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OMA; AAFQYYV; -. DR OrthoDB; 9788659at2; -. DR CDD; cd06577; PASTA_pknB; 3. DR CDD; cd14014; STKc_PknB_like; 1. DR FunFam; 1.10.510.10:FF:000021; Serine/threonine protein kinase; 1. DR FunFam; 3.30.200.20:FF:000035; Serine/threonine protein kinase Stk1; 1. DR Gene3D; 3.30.10.20; -; 3. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF34; SERINE_THREONINE-PROTEIN KINASE YBDM-RELATED; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule. DR Proteomes; UP000001968; Chromosome. DR AlphaFoldDB; Q0AXM0; -. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001968}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310..334 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 10..267 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 334..400 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 401..468 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 471..538 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT ACT_SITE 133 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 612 AA; 67698 MW; 6ACD4758C0EE8C75 CRC64; MKTTVLGDRY ELMDKIGEGG MASVYRARCR TLDRIVAVKI LKEELLNDKS FVEKFNTEAL SAAQLSHPNI VNVFDVGQQD QLYYIVMEYV EGKSLKELLD TEAPLTVEMA VDIAIGICDG IHHAHSKGII HRDIKPHNIL ITSDGIVKVA DFGIAQAISQ KTITFGGNIV GSVHYISPEQ AKGEAVGPAS DIYSLGCVLY EMLTARLPFD ADSPITVALK HMYDEPASPR NINPKIPPAL EGIIMKAMEK LPAERFTSAE AMRNALLDLE GNSLAGYKRS NRNGKTLILP PWKEQEMDGV LKKKKIRTPF LVGIIIAVLG LLGGFLSTMG GQLFPDEVAV PNIVGMDIKE AERELSKVNL SMSVIQEFND EYDKNIIFFQ NPGPEQKVKE GREIKVKMSK GSELQKTPSL RGLKLIDAEI KLRNEGLELG RTEKIYDDKY EADIVISQNP EAGSRIKKGS KVDLMVSKGK TPEKVAMPKL LGLSLKEASN KLQENKLLPG EVKYQPSSEY YSDQVCSQEI ETGVLVDENS SIALTVSQGP GPLAKVKDIE FSLPLEQDYY KVLISIKDSQ GKRQVYEELH RAGDTVYAAV RYYGSGELEI LLNGKSYKTM KL //