ID   Q2S2K2_SALRD            Unreviewed;       649 AA.
AC   Q2S2K2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Protein kinase domain {ECO:0000313|EMBL:ABC45436.1};
GN   OrderedLocusNames=SRU_1455 {ECO:0000313|EMBL:ABC45436.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45436.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC45436.1, 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   -!- 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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP000159; ABC45436.1; -; Genomic_DNA.
DR   RefSeq; WP_011404205.1; NC_007677.1.
DR   RefSeq; YP_445579.1; NC_007677.1.
DR   AlphaFoldDB; Q2S2K2; -.
DR   STRING; 309807.SRU_1455; -.
DR   EnsemblBacteria; ABC45436; ABC45436; SRU_1455.
DR   KEGG; sru:SRU_1455; -.
DR   PATRIC; fig|309807.25.peg.1510; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_020300_0_0_10; -.
DR   OrthoDB; 9813021at2; -.
DR   Proteomes; UP000008674; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013229; PEGA.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF08308; PEGA; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABC45436.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW   Transferase {ECO:0000313|EMBL:ABC45436.1}.
FT   DOMAIN          11..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          331..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   649 AA;  67917 MW;  E815EB3E8A11AC1F CRC64;
     MPDAGDILDG YRLDAVIGRG GMGTVYRATD QALEKTVALK VIAPHLADDD TFVRRFREEA
     KALARLDADG IVDVYTLRET EEALFFVMEH VEGPSLETVL RRRGQLEPPQ ALSLLRQVLT
     AVGHAHASGV LHRDLKPSNI LIDADGQAVI TDFGLAKILA SDADLTATHD QLGTVAYMSP
     EQVKGLQNVD AASDLFAVGL LAYEVLTGRL PFDRSGSDFV VQRAIVDASF PPPSTHAPEV
     PPAVEQVVLD LLSKDPAARP PDARAALDRL PAPEAADEEP LLTPDAPVSP DAGFTPWQWA
     GLAAGTLLVL MGTYAGVRAT LGLPVLSAAG PAPPETTRTA AAPAGPSAQE QTSPPVADDA
     GLSSREEKGS PAEASPPADA SPGDEAPSDE PPPSADASSE DSPPPAASSD GTSRTASSAA
     SAPDEPSPSS EPATGAVTVR SDPGGATVRL NERPIGRTPL TIGDLKPGTY RLLLDRDDHR
     AREATVSVAG ADTAVVSPTL LPRPAVVRLG ARPDGEVHID GASRSPTADG LVVDSLSPGS
     HTVVFTSALG RWEMEMTLDP GETYERTIDF TERVESAVTA RAPDGTPLPN ATVTVDDDTV
     GYTPQRLTLQ VGERTIRVAK EDHAPAERTV RVEPGMDTPL VFELAPEPD
//