ID   Q6MC51_PARUW            Unreviewed;       464 AA.
AC   Q6MC51;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=PC_RS05430 {ECO:0000313|EMBL:CAF23848.1};
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Protochlamydia.
OX   NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23848.1, ECO:0000313|Proteomes:UP000000529};
RN   [1] {ECO:0000313|EMBL:CAF23848.1, ECO:0000313|Proteomes:UP000000529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25 {ECO:0000313|EMBL:CAF23848.1,
RC   ECO:0000313|Proteomes:UP000000529};
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(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; BX908798; CAF23848.1; -; Genomic_DNA.
DR   RefSeq; WP_011175674.1; NC_005861.2.
DR   AlphaFoldDB; Q6MC51; -.
DR   STRING; 264201.pc1124; -.
DR   KEGG; pcu:PC_RS05430; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_589050_0_0_0; -.
DR   OrthoDB; 22013at2; -.
DR   Proteomes; UP000000529; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   PANTHER; PTHR44167:SF18; SERINE_THREONINE-PROTEIN KINASE RAD53; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000529}.
FT   DOMAIN          178..455
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   464 AA;  53979 MW;  B7A883C8442F57BD CRC64;
     MQMRNCLSMP LMNHRNNCTS SSYTDLSSES STFSFCSIDS NDSSSDLETL TKIKDLAPVI
     VNEFSVTQST WKSSRNHIIQ VITSAITVKN VQLQASKTLT PFLKFSNIDL LLQLQIPLTK
     TQLTSTFEFL SENLPLLKPA TITGPIWHQI ALTALNSYFD TNFCLEIHNH AIFILFLSHP
     STVISQGRHK NVYKIFQLTG IPKLYAAAIT TILKRDPEAK KLKEMQINEE RFLTNLASNP
     QVVKTYSIHY YPANLSFDER QVIIMEYCPK DLRGLLNNLI DKREKLTSNQ KYNCMFQLLQ
     FLNDFHSNGY LHRDIKPDNI LIKNLQLKFI DFGYSCHITE KEKLMRRCGT FQYLPIEIFE
     DLERPFGQEK DMWGAACIIW LLFYESLYPW YKAISSDEKY LDFLKKEICD FRQTITSLKS
     PTPLDHLLFN LLNPDPRTRW TASQAFKYIL KHKKAFCEEE IIYI
//