ID I3ZW37_9EURY Unreviewed; 444 AA. AC I3ZW37; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 02-DEC-2020, entry version 38. DE SubName: Full=Putiative protein kinase 1 {ECO:0000313|EMBL:AFL95921.1}; GN ORFNames=CL1_1724 {ECO:0000313|EMBL:AFL95921.1}; OS Thermococcus cleftensis. 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 //