ID A1AWW9_RUTMC Unreviewed; 566 AA. AC A1AWW9; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 93. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082}; DE EC=3.1.3.16 {ECO:0000256|PROSITE-ProRule:PRU01082}; DE AltName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN OrderedLocusNames=Rmag_0686 {ECO:0000313|EMBL:ABL02426.1}; OS Ruthia magnifica subsp. Calyptogena magnifica. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Candidatus Pseudothioglobaceae; Candidatus Ruthturnera. OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL02426.1, ECO:0000313|Proteomes:UP000002587}; RN [1] {ECO:0000313|EMBL:ABL02426.1, ECO:0000313|Proteomes:UP000002587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cm {ECO:0000313|EMBL:ABL02426.1, RC ECO:0000313|Proteomes:UP000002587}; RX PubMed=17303757; DOI=10.1126/science.1138438; RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.; RT "The Calyptogena magnifica chemoautotrophic symbiont genome."; RL Science 315:998-1000(2007). 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 -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PROSITE-ProRule:PRU01082}; 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; CP000488; ABL02426.1; -; Genomic_DNA. DR RefSeq; WP_011738051.1; NC_008610.1. DR AlphaFoldDB; A1AWW9; -. DR STRING; 413404.Rmag_0686; -. DR KEGG; rma:Rmag_0686; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034273_0_0_6; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000002587; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51746; PPM_2; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Reference proteome {ECO:0000313|Proteomes:UP000002587}; 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 545..565 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 7..229 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT DOMAIN 262..558 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT ACT_SITE 385 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" SQ SEQUENCE 566 AA; 64137 MW; 3982EC6BD982194F CRC64; MKQLKVIVNS HCIAGVKEEN QDACAYYVPN PKALEYKGIV GAIADGVSAC ERAKEASGCC VKGFLSDYYS TPESWSVEHS AGQVISALNN WLYSQSMRFG EISSMLCTLS VVIIKSNIAH IFHVGDSRIY RYRKGVLIQL TKDHILSLNK EKTYLTRAMG FDLSINVDYQ TFNLELGDQF LMTTDGVHDY LQHTLLETLM NKASSVDKIV ERAIKQDSQD NASAMIITIK QLPKKNLDEV FDELTQKPVP PELTKGMKIN GFEIKSLIIS SAKMQLYLAK DISTEQLVAL KTPSINFEDE PEYLQHFMYE KWVGQRVQSP NVVKIYNSHK KANFLAYAMV YVKGQTLRAW MDKNKHSDIE VVVGFVKQII QGLRAFHRQE MLHCDLKPEN IMIDEIGQIK IIDFGSARIA GVAELVNPIN FIGNQGTQGY TAPEVILNES VSQASDQFSL GVIVYEMFSS HLPYQNKLDK SLSFKKLSKL IYEPVLIYNP NLPVWIDGAI RKACCLDYAE RYETLSEFLY DLEHPNSVFL SPQKNKQPKL KLTKYRLLSV LSFALNFILL LMLAIK //