ID   Q60B87_METCA            Unreviewed;       595 AA.
AC   Q60B87;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, 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=MCA0593 {ECO:0000313|EMBL:AAU93154.1};
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU93154.1, ECO:0000313|Proteomes:UP000006821};
RN   [1] {ECO:0000313|EMBL:AAU93154.1, ECO:0000313|Proteomes:UP000006821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC   {ECO:0000313|Proteomes:UP000006821};
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU93154.1; -; Genomic_DNA.
DR   RefSeq; WP_010959938.1; NC_002977.6.
DR   AlphaFoldDB; Q60B87; -.
DR   STRING; 243233.MCA0593; -.
DR   KEGG; mca:MCA0593; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   Proteomes; UP000006821; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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:AAU93154.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006821};
KW   Transferase {ECO:0000313|EMBL:AAU93154.1}.
FT   DOMAIN          10..236
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          269..525
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          575..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  65137 MW;  095B4F519F3C1203 CRC64;
     MSVSGQPVLR AAVVTLQGRR EDNQDFAAIA EPSPRDAAAR GFVAAVADGI GGARGGRVAA
     EVSVRSFMEA YYGLSETLGM QQLLDRCLGS ANRWVHAMGR LDPELAHMGT TFSGLIFRGR
     RAYLVHVGDS RIYRLRGDEP ELLTSDHTLS GPGLDHVLYR AVGLDPGLRI DYSVYPLEPH
     DRFLLCSDGL HGSLQQEQIR EILQERATPE TTAEALARLA FEQGSQDNIT ALVVDVIALP
     PAEKQSLRLA IESLPLLDLP EVGDEVDGFR LERLLSSGRY SALFLAADTL GQDKPVVVKF
     PHPRVASERE YYDAFVREAW IGARVKSPWV GEILEQTPGR QSRLYSVMPF YPGASLEHEL
     ARRPRIGLEA GIDLALKLCK AVHALHRQQI VHRDIKPDNV LLDPEGGLKL LDLGIARLPA
     WDEDQADPIP GTPSYMAPEM FQGERGSIAT DVFALGVTLY RTFAGGAYPY GEVEPFSTPR
     FGSPRPLTAH RPDLPAWLDA VLARAIAADP AQRPADAVEL AYELEAGLEK GGGRRPPRRP
     LPLYERNPLQ FWKAVAALLL ALLAMAGLRL SLSCRPPSEA ASRNNPLIHD NGDSR
//