ID C7PX38_CATAD Unreviewed; 1104 AA.
AC C7PX38;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ACU77295.1};
GN OrderedLocusNames=Caci_8472 {ECO:0000313|EMBL:ACU77295.1};
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:ACU77295.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU77295.1, 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; ACU77295.1; -; Genomic_DNA.
DR RefSeq; WP_015797020.1; NC_013131.1.
DR AlphaFoldDB; C7PX38; -.
DR STRING; 479433.Caci_8472; -.
DR KEGG; cai:Caci_8472; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_282652_0_0_11; -.
DR InParanoid; C7PX38; -.
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; cd00161; RICIN; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.80.10.50; -; 1.
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 InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ACU77295.1};
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:ACU77295.1};
KW Transferase {ECO:0000313|EMBL:ACU77295.1}.
FT DOMAIN 12..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 329..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1104 AA; 108460 MW; 253E569383818B45 CRC64;
MWGEGTVLAG RYQLRQRIGG GSMGDVWRAL DTVLGREVAV KILLPALLDD AGFAARFHTE
ARVLAALSHP GIVSVFDYGE ADDPRTAFLV MELITGRPLS ELLDESAPLS EVTTLTLVAQ
TLEALQAAHD RGIVHRDVKP ANLMLRGGSV VVTDFGVART ADARRLTAAD VVLGTAVYAA
PEQARHTAVT AAADQYAVGV IAYECLTGAP PFDSGTPLGI MMKHLQEPVP PLPDTISPAV
RELVMRALAK DPAERFASAR EMAETARRLA LRGESVTRIG TPQDSFQTGV DVAAMEAAAA
ALAEAGAGAG ARGDGDFLSF TVLPREAEGE GAGAGLRSTG GGDVGAGAGA GDVAEEAGPE
IAPAWASYAV RPQAEGTDWA SFTVRSSGDE TAPLPDGEAA DEDSDAEAAG AEAGVGDAAR
ADVARWRSRT VPQDSFTSGV VAEESAAAAE VEVEVGRAAR GGFGARWRKR KPEPQEVSTA
DSGDQAGASA SGVVEPSAEH KGSGAEPSSA GQSVTSQSAT GHGATGQGAA NPSAADPSTT
GQSTAEQSIR GQSAADQSAD QSAADQSAAE LSTAGQSVAN QGTAEAGAAE SAAAGPGAAD
QSTEQAADTP SNAALPEADL SAAAGMPSDS ALPEAGLSAA AGTPIDAALP EAGLSAAAGT
PIDAALPEAG LSAAAATPID AALPEADLPA ADDTSSDSAL PEADLPAAVA ANTAAAANAS
ASAADAGAAG LDVGSGAAGV AAAGVDSGEA ASDPLPPTAE VPALRIAPGH AMPLDSFNAG
VELDPVDEEG VVAARVVPQD SFTVGVPEAV TGVGADGSGG GSSGRRRAIV VAAVGVAVVV
AVAVAYPLSH GGSRAAAQAG VPVGLASGSS ASGGVSSSGV SVTSVVSETS TIVVSASVPS
APGKPSATSA VPPASGAGKT APTSSAGSAL TSRPPVSPVS SAASSSAGVP PVPATSSAPA
VPHKSGYITS VGDGDAIDVF GNSSGAPIYS DGAQLTVEPQ SGRTGQSFQA TALTSNGQAV
YEFGDGLNTN QLIDATGGKV TLSHCACGSA FQMWWLSQDS TTPSGAFYIN NQGAGQCLTD
NGQTNALSLK PCVAGDKAQQ WYLP
//
