ID   A1AWW9_RUTMC            Unreviewed;       566 AA.
AC   A1AWW9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABL02426.1};
GN   OrderedLocusNames=Rmag_0686 {ECO:0000313|EMBL:ABL02426.1};
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   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};
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=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; 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:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00143; PP2Cc; 1.
DR   CDD; cd14014; STKc_PknB_like; 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; PTHR48011; CCR4-NOT TRANSCRIPTIONAL COMPLEX SUBUNIT CAF120-RELATED; 1.
DR   PANTHER; PTHR48011:SF84; KINASE, PUTATIVE-RELATED; 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   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABL02426.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABL02426.1};
KW   Transferase {ECO:0000313|EMBL:ABL02426.1};
KW   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"
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
//