ID   Q6MC95_PARUW            Unreviewed;       655 AA.
AC   Q6MC95;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=PC_RS05205 {ECO:0000313|EMBL:CAF23804.1};
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Protochlamydia.
OX   NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23804.1, ECO:0000313|Proteomes:UP000000529};
RN   [1] {ECO:0000313|EMBL:CAF23804.1, ECO:0000313|Proteomes:UP000000529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25 {ECO:0000313|EMBL:CAF23804.1,
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; CAF23804.1; -; Genomic_DNA.
DR   RefSeq; WP_011175630.1; NC_005861.2.
DR   AlphaFoldDB; Q6MC95; -.
DR   STRING; 264201.pc1080; -.
DR   KEGG; pcu:PC_RS05205; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_408763_0_0_0; -.
DR   OrthoDB; 9768004at2; -.
DR   Proteomes; UP000000529; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   PANTHER; PTHR23150:SF19; FORMYLGLYCINE-GENERATING ENZYME; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000529};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..328
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   655 AA;  74740 MW;  48EF016FD1251EE4 CRC64;
     MEQRILGDYI IIKSIGHGTL GEVYLAEHRF MKTQYILKIL PEELSTDRSF IQRFQEDISF
     LSTLDHPNIV KTHNISFAQG VYFLVTDCVV DQMGEMTNLA QYLMELDRRL EEDEIINILM
     QIAEALDYAH SKKMGNRELI HRGLKPNNIL IGKRRQNLEV HLSDFGLSWI IGPGAVLTRT
     YKNVAEALEI GSQNLWQKMG QDRYPSPSID SQKLIPLHAS FLQTHAFFAP EQKRLDFPHS
     VSMKTDVFAF GVLVYYLLMN ELPEGIFEMP SNSSRYRYQW DTLLEKCLQN QPAKRTDSLV
     TALKETLQEP KSKNAKIEEL TLGKEEFFFN NEASIIFEEG KCNVQKGVSE SLVTLKIEEA
     PPVIEEAVST LRPVLQNPLL ERPQTDHDPA AIFQISSAVK VYNPERKDVT NVKPILTDMV
     IIEGGNFYRG SQDGNRDEMP RHQITLSSFA LDVHPVTNEQ FVRFLEVMGG EKDSNHNDII
     RLRDSRIKRS GGKLSIESGY AKHPVVGVTW YGAIAYAKWI GKRLPTEAEW EIAARGGQEN
     VLYPTGEEIE KTQANFFSSD TTTVMSYAPN NCGLYDMAGN VYEWCHDWYG YNYYELSMQE
     PDFPQGPLQG VYRVLRGGCW KSLKEDLRCS RRHRNNPGTV NGTYGFRCAA DVQIS
//