ID C7PYX2_CATAD Unreviewed; 837 AA.
AC C7PYX2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ACU69528.1};
GN OrderedLocusNames=Caci_0591 {ECO:0000313|EMBL:ACU69528.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69528.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU69528.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU69528.1; -; Genomic_DNA.
DR RefSeq; WP_012784823.1; NC_013131.1.
DR AlphaFoldDB; C7PYX2; -.
DR STRING; 479433.Caci_0591; -.
DR KEGG; cai:Caci_0591; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_000288_135_1_11; -.
DR InParanoid; C7PYX2; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000000851; Chromosome.
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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-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:ACU69528.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ACU69528.1};
KW Transferase {ECO:0000313|EMBL:ACU69528.1}.
FT DOMAIN 15..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 301..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 837 AA; 86273 MW; 600E1D0DAF3CFFF7 CRC64;
MDALKPEDPS RVGPFTPLAR IGAGGMGRVY LARSRGGRPV AVKVIRAEYA EDERFRTRFR
REVQAARTVD GMYTAPVLDA GPDDAEPWLA TAYIPGPSLQ RAVHEHGPLP ERTARVMGAG
IAEALGAIHS AGLIHRDLKP SNVILGPDGP RVIDFGISAS EGGSSLTTTG IVVGSPRYSS
PEQCRADPAL GPASDVFALG GVMVYATTGV PPFGDGPDHV QLYLVVHETP DLTGVPMGLR
PIVSACLEKD PANRPTTDEL LDTLLPPEEA GATNAVDWLP DAVYRDLREY SAAPIVALAA
GTTHERGEDS ARTPAPGEAT PTGAGFDGGG VTGIGSGVGT TAAPSSAGSD GPSNPGRRRM
LAGIAGAVVV AAGGGGAWYA ATRDSGRKSA TQSAGATFPP STGSQNPSTP AAPSTTPTPS
TTPSTTPTPT PSHVLGPWQE DWSSKTDLGG ASGGAVISGS KLVGVYTATS VSNPIPPQDL
IAIDTVSGGS AFPARSIPAV DNVGGAGIAA DDTHAYSYGA GTVYAWNLSD GSAAWNAKSG
LQTSTSTNNM PTTGILGMVG TLLMVGSGNY DPGFPPCLAA FDVTLKKAVW TLKPEDMQIV
ASPPTGLVLN QTSIAVSIPK LGNLFYVMLC DENSLRVLKA MDMATGKEVW HVFFEAYSDN
GAGTVTPTVT GTEQHVYLTD MHSGSVHAYS AAGKWMWTYP SAVGKTAPSS DRRFTGQVLE
SGDAVYAADA NRVYALQVST KAVGGTPVWK NPATFNGIAN VPALVGDKIW VEVHTPTEKN
PLAMIVVDTA DGQVVHSYPM PEGPTASSAE LTVPDPSGQA AYVLTASGQV LGYRRNQ
//
