ID Q2S486_SALRD Unreviewed; 609 AA. AC Q2S486; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:ABC45600.1}; GN OrderedLocusNames=SRU_0861 {ECO:0000313|EMBL:ABC45600.1}; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45600.1, ECO:0000313|Proteomes:UP000008674}; RN [1] {ECO:0000313|EMBL:ABC45600.1, ECO:0000313|Proteomes:UP000008674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31 RC {ECO:0000313|Proteomes:UP000008674}; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). 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; CP000159; ABC45600.1; -; Genomic_DNA. DR RefSeq; WP_011403623.1; NC_007677.1. DR RefSeq; YP_444995.1; NC_007677.1. DR AlphaFoldDB; Q2S486; -. DR STRING; 309807.SRU_0861; -. DR EnsemblBacteria; ABC45600; ABC45600; SRU_0861. DR KEGG; sru:SRU_0861; -. DR PATRIC; fig|309807.25.peg.888; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG1196; Bacteria. DR HOGENOM; CLU_448253_0_0_10; -. DR OrthoDB; 2485468at2; -. DR Proteomes; UP000008674; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008674}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 323..345 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 351..370 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 35..304 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 569..609 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 379..420 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 521..548 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 575..591 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..609 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 609 AA; 68444 MW; 36D717E7928480F8 CRC64; MSSYPTPSEY QEALQAPAVA FADPELQDST PRTNALGLPQ PITGSFAAVF PVTTDPGGRY AVKCFLSERP AQHARYEAVA EALDAVDHDA FVEFAYQPEG ISVRGDAYPL LKMEWTGGTT LNRFVEDHLD RPDVVDRLVE AWARLMADLE DMDLAHGDLQ HGNVLVETAG EALRLRLVDY DTMYVPALEG RASAEVGHRN YQHPDRTDAD FGPALDRFSG LVVYAALRAC AVRPELWDEY DTGENLLFRD ADFYAPEESP LFDALAETES LRALTDALRT ACYVEPADVP PLADVREGRL EPSQVSVSRS RARQGRDAAE RSTVARAFLP ATIGGGGVAL GLAAAGGGLT AAAVLLVGIG VGAGIVATRY RRLSLVRRRR RLEQEADRFA STIRELDREL ESLQKKRAEL RTSMDERRQE RLREIQAKAL HDRLKHHFVR EVRDIDGLTH KHVVRLKAAN LRTASEVTPE AVEDVRRISD RARARLKMWR AALEEKYADE IPDALSPAQE RRLQRYIEHR IDDLDDQIGR TREKIQTQRT ERERIEDRLD EMPDLSIGRY VRYLLRIDTL PDRTEEPPAP APRPGPESST DRVPVPEPVD EDRSWWERA //