ID   Q1B026_RUBXD            Unreviewed;       666 AA.
AC   Q1B026;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABG03002.1};
GN   OrderedLocusNames=Rxyl_0021 {ECO:0000313|EMBL:ABG03002.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG03002.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG03002.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG03002.1; -; Genomic_DNA.
DR   RefSeq; WP_011563020.1; NC_008148.1.
DR   AlphaFoldDB; Q1B026; -.
DR   STRING; 266117.Rxyl_0021; -.
DR   KEGG; rxy:Rxyl_0021; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OrthoDB; 9762169at2; -.
DR   PhylomeDB; Q1B026; -.
DR   Proteomes; UP000006637; 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; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 4.
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:ABG03002.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006637};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABG03002.1};
KW   Transferase {ECO:0000313|EMBL:ABG03002.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          342..407
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          408..472
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          473..541
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          542..607
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          373..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   666 AA;  70686 MW;  9C647C57941D6A76 CRC64;
     MQQLVDNRYR IVRRLGSGGM ADVYLAHDDI LDRDVALKVL SSHYAADAEF VERFKREAQS
     AAALAHPNIV SIYDRGEAED GTYYIAMEYL PGGTLKDRIL RKGALPPKTA AAVALQIAEA
     LKAAHQRGVV HRDIKPHNIL ITESGDLKVT DFGIARAASS STMTRTGAVL GTAHYISPEQ
     AMGEPVGPPS DLYSLGVVLY EMLTGQLPYD ADTPIGIAMK HVNGHLRPPR EVNPAVPEGL
     DAITVRLLAK DPKERYQSAD ELMEDLERFL RGEDPAAAAP TAVMGRVGRD ETAPTRVQPA
     VGREGKRRRW PLVALLLAAL LALLGLGGYQ LLLEDQAGGR DAPPRMAVPD LQGMSLEEAQ
     RRYGDDFDIV EGERRDGPRE AGTILEQDPP PGERLERGSE ISVAVASGEN EVPAVVDSPA
     DEARSALSEA GFEVKVEERE SEEEQEGLVL EQSPEGGSTA EVGSTVTIAV GTGVPTVVVP
     DIPYGYTAEQ SRQVLEQAGL RLGSVGYAPN SQVAEGGIID QNPPPGTEVE EGTAVDIVLS
     SGPPQTEVPD VVGLDVNVAV QRLSGAGLGY ALIERQSGEP EGTVLSTSPP AGSTVDQGTQ
     VRVVYSVGRP EPRPEPTTAR PPEEQGGPQG GGGQGRDRGR DETQSRPAPA AGPGERRPPS
     GEDEGD
//