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Database: UniProt
Entry: S7TWC4_DESML
LinkDB: S7TWC4_DESML
Original site: S7TWC4_DESML 
ID   S7TWC4_DESML            Unreviewed;       493 AA.
AC   S7TWC4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=dsmv_2143 {ECO:0000313|EMBL:EPR41362.1};
OS   Desulfococcus multivorans DSM 2059.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfococcaceae; Desulfococcus.
OX   NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR41362.1, ECO:0000313|Proteomes:UP000014977};
RN   [1] {ECO:0000313|EMBL:EPR41362.1, ECO:0000313|Proteomes:UP000014977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR41362.1,
RC   ECO:0000313|Proteomes:UP000014977};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT   bacteria.";
RL   Genome Announc. 1:e00618-e00613(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPR41362.1}.
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DR   EMBL; ATHJ01000076; EPR41362.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7TWC4; -.
DR   STRING; 897.B2D07_06360; -.
DR   PATRIC; fig|1121405.3.peg.1681; -.
DR   eggNOG; COG0515; Bacteria.
DR   Proteomes; UP000014977; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011460; DUF1566.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF07603; DUF1566; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EPR41362.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:EPR41362.1};
KW   Transferase {ECO:0000313|EMBL:EPR41362.1}.
FT   DOMAIN          30..339
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   493 AA;  56110 MW;  D2974C59CB89544C CRC64;
     MIDEIEITIA KFIYTGILAE DTLMKKIGRY IVRGQLGRGG MGRVYKVEMP VTGKIVALKL
     LKPDPLLTDL LGLENIRGMF VREAVTMANL KHPNLLDVWD FDEAEGMPFY IMDYHCNNLG
     TMIGESHMIE KPSRRIPAEK AVRYIRQILE GLACLHYAGV VHRDIKPFNV LITDYDTVKI
     CDFGLSKMRG YPFRGPSNLK VGTPGYASPE QQKDPDAVDF SADLFSVGVM FYRMLTGILP
     MKDPASPQAH NPDLDVFWDR FLLKAIEPSP LRRYRRARSM LAALDDVYAV WRGKQEKICR
     YPYPTGLEDL ASDAPATVEY EKPRSRPLNV DLKKARRLFG LDELFRPQVY TENDFNVDVD
     DVVADRATGL LWERSGSEYP MTWDRARHYV RGLNDQGFSG RTDWRLPTVA ELTTLLMKTY
     PQETLCISSV FDETQRGLWS SDRRSPAAAW YVSLDLGFVA WHDHTARCYV RAVCDRSGST
     DEFNAAQATG ERS
//
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