ID   Q3ACF7_CARHZ            Unreviewed;       764 AA.
AC   Q3ACF7;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:ABB15387.1};
GN   OrderedLocusNames=CHY_1343 {ECO:0000313|EMBL:ABB15387.1};
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB15387.1, ECO:0000313|Proteomes:UP000002706};
RN   [1] {ECO:0000313|EMBL:ABB15387.1, ECO:0000313|Proteomes:UP000002706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC   {ECO:0000313|Proteomes:UP000002706};
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA   Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA   Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB15387.1; -; Genomic_DNA.
DR   RefSeq; WP_011344253.1; NC_007503.1.
DR   AlphaFoldDB; Q3ACF7; -.
DR   STRING; 246194.CHY_1343; -.
DR   KEGG; chy:CHY_1343; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_357119_0_0_9; -.
DR   InParanoid; Q3ACF7; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000002706; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011528; NERD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR   Pfam; PF08378; NERD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50965; NERD; 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:ABB15387.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002706};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABB15387.1};
KW   Transferase {ECO:0000313|EMBL:ABB15387.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        487..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..134
FT                   /note="NERD"
FT                   /evidence="ECO:0000259|PROSITE:PS50965"
FT   DOMAIN          216..471
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   764 AA;  88207 MW;  9DFEB83A5E3B3443 CRC64;
     MGITIKEVSR ISGVFGQQGE EKVAEVLKEH LPDGYKIINS YRLNYQGDSW DIDHIVIGPN
     GIFVIETKNM RGRVFGGAMG NWWQEKWAGG QKEKIKIGNP AAQVNHYAKL VKEFLRLYFP
     EEETRILVYP VVVFAHEEAD FSKLRFTRPG RIGKTKILSL YELPAFILSR EEVSYDSDFI
     DKAINFLIPE DEREKTGMFK TGLYYQNLQE QFSRRYRLED LIGEGNFSKV YWAYDNKLDR
     EVAVKEINLT DLPGDIKDKI YNEAQLMAKI NHENIVKLYD TFYFDDKIYL IIELVQGKTL
     VEYLEEKGGM LSVKKAVNIM IQIAKALSYI HQHNIIHRDL KPENILISTD DIVKITDFGI
     AQLNEEEKEE GFILGTPVVM APEQILKTGI DQRTDIFALG CIFYYLLTGH YPFSGTNFSE
     LSYNILHFDP EPIRTYNSHC SLEIEKIILK CLEKNPENRY QKVSELLQDL IKYQEQKNLG
     LFFNKKTFLK IALVVLGIAF LYLFTLGTSM QNQGSAPISL NEILNKEQIT LTNDNFNQVF
     ANNYLAGAKV KITGRILDII GAQNGRTLCY FLLEPASLKD NKLTIALNLD PFSIFNGTKY
     YQLEGFLAYS PLVENGAAKP VVIVERYKPL EPWHLFDPPI KTVEVKQTLK RKDKEIIFEK
     IEFGKNETRL FITLRNLSNH PVNFNLLEPR ASQKDRFYVE ALYQNRDYPK LKDQLGPKEI
     VRGIIVLEKM DYQIKEAVFF LGLTMAGEEP YIFHVRWGDE NTGN
//