ID   A1SQA8_NOCSJ            Unreviewed;       488 AA.
AC   A1SQA8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=Noca_4496 {ECO:0000313|EMBL:ABL83993.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL83993.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL83993.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA   Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA   Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA   Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA   Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT   Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
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};
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DR   EMBL; CP000509; ABL83993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1SQA8; -.
DR   STRING; 196162.Noca_4496; -.
DR   KEGG; nca:Noca_4496; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; 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; 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:ABL83993.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Transferase {ECO:0000313|EMBL:ABL83993.1}.
FT   DOMAIN          8..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          277..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   488 AA;  51913 MW;  99951DCAAF73CAA8 CRC64;
     MPSRLGRYAV RRRIGSGGFA TVWLAYDEQL DSPVAIKVLA DNWTEDQAVR QRFLEEGRFL
     RKVESPYVVS VYDAGELEDG RPYLVMSYAD QGTLADRLEV LGLTPGQALE VVRQVGAGLQ
     ALHVRGVLHR DVKPANVLFR TVEEGGRSEV RAMVADLGLG KALDMSSRLT MIAGTPSFVA
     PEQAQGEPLD ARADQYSLAA LTYLMLCGRA PYSHASLAAA AAPCAPPALS TPERPFPDAV
     EAVVRRGLAA DREDRWPDVA AYVEALAAAL GADADADPSG PWLPLDPDLT RPGARPSPLP
     PSRPLADPVP PRRTGRRVLA AIVGLVALAA GAGVGYAVEQ HGDAEVSLTD RTGTLSVIVP
     SDWDRARSTR MWQAPGGGGE FPALSVGSSA DWTDAGSTAQ GVFLGILPGD ELPEQVPQHP
     ECGTADDPVD DTIDDNPTRT VVYTRCPGGV TVERVVQLAS NRLLWVQVRS ADRATATAVL
     DDVEAHGY
//