ID   I3ZW37_THECF            Unreviewed;       444 AA.
AC   I3ZW37;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   07-APR-2021, entry version 39.
DE   SubName: Full=Putiative protein kinase 1 {ECO:0000313|EMBL:AFL95921.1};
GN   ORFNames=CL1_1724 {ECO:0000313|EMBL:AFL95921.1};
OS   Thermococcus cleftensis (strain DSM 27260 / KACC 17922 / CL1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=163003 {ECO:0000313|EMBL:AFL95921.1, ECO:0000313|Proteomes:UP000006064};
RN   [1] {ECO:0000313|EMBL:AFL95921.1, ECO:0000313|Proteomes:UP000006064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL1 {ECO:0000313|EMBL:AFL95921.1,
RC   ECO:0000313|Proteomes:UP000006064};
RX   PubMed=22887670; DOI=10.1128/JB.01016-12;
RA   Jung J.H., Holden J.F., Seo D.H., Park K.H., Shin H., Ryu S., Lee J.H.,
RA   Park C.S.;
RT   "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT   sp. Strain CL1, Isolated from a Paralvinella sp. Polychaete Worm Collected
RT   from a Hydrothermal Vent.";
RL   J. Bacteriol. 194:4769-4770(2012).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003651; AFL95921.1; -; Genomic_DNA.
DR   RefSeq; WP_014789552.1; NC_018015.1.
DR   EnsemblBacteria; AFL95921; AFL95921; CL1_1724.
DR   GeneID; 13037032; -.
DR   KEGG; thm:CL1_1724; -.
DR   HOGENOM; CLU_035393_0_0_2; -.
DR   OrthoDB; 32984at2157; -.
DR   BioCyc; TSP163003:G1H5T-1802-MONOMER; -.
DR   Proteomes; UP000006064; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFL95921.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:AFL95921.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..331
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          311..351
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   444 AA;  50896 MW;  8F15F2D97D493422 CRC64;
     MWRDDIGRLR KIVWSFLALN PIGIAGYWAS KKMNVIPKTR TEHKKNRKTN QLYIRSILPG
     FPPELLDKYE PLEFLGEGGF AKVFKVRRKS DGKVMALKVS RLDEKAKKFF LKEVRAWRLL
     DHPNIVKLYN TFDEPLPYLE IEFVDGIQLN GEVIRDLGKY PKPVDEEKAL HFIRGIAEGL
     KHAHAKQVFH RDLKPQNVLI TSNLTPKITD WGLAKVGAIS TTATTTKGLT LLYAAPEQLD
     DETYGHTDAR TDIYQLGLIF YELLTGKLPY QGTSPAVVMA KVINPAVKPK PPSHFNKALA
     KYDGIFEKLL AKRKEERYQS VEEFLRDLEL MKKLDGERNK LAKEIEKTKT TMSMTIDSRE
     LKKLMRQLVE QLSRNALLHA QLNDKAGLIN ALEDLKAFSR NHREELEGAI GQFELMMRES
     VPISKSTLDE LKILLHKVQR EVEG
//