ID A0A1K0FQJ9_9ACTN Unreviewed; 558 AA.
AC A0A1K0FQJ9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=BG844_06340 {ECO:0000313|EMBL:OJF15101.1};
OS Couchioplanes caeruleus subsp. caeruleus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Couchioplanes.
OX NCBI_TaxID=56427 {ECO:0000313|EMBL:OJF15101.1, ECO:0000313|Proteomes:UP000182486};
RN [1] {ECO:0000313|EMBL:OJF15101.1, ECO:0000313|Proteomes:UP000182486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43634 {ECO:0000313|EMBL:OJF15101.1,
RC ECO:0000313|Proteomes:UP000182486};
RA Sheehan J., Caffrey P.;
RT "Couchioplanes caeruleus draft genome sequence.";
RL Submitted (SEP-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJF15101.1}.
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DR EMBL; MEIA01000069; OJF15101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K0FQJ9; -.
DR Proteomes; UP000182486; Unassembled WGS sequence.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000182486}.
FT DOMAIN 12..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 275..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
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 558 AA; 58708 MW; E8ED440E8F2A6359 CRC64;
MDLSGRCVGS TYILICPVGQ GATGTVWRGM ERTSGEHVAV KLLHEGMLRQ PKLVTRFVQE
RTILKMLRHE YIVGVRDLLS AGESLGLVMD FVAGGSLREH LRREGTLPPG EAARLLAQVA
AALAEAHGIN VVHRDVKPDN ILLREADGRL DVRLTDFGIA RILDTPGLTT PQAIIGTPHY
MAPETISGGE PTPPADVYAL GVVLHELVAG RPPYAGDPMT VLRSHLDDEP VRPAGIAEEL
WSVIRSCMDK DRDRRPSAVE LAEILSGLAR NLTGVPALPG PATEADAGDD GPPRPAPSPL
RPARHPSAPG DPRPRSPRNR PGTRRWRRPG AMAALVGAVL LSSAAAGYGV WQSRLLQAAG
ASIAAAPPPR PDGYLPGGRS TANPSGPPAP VLAQTVVAGA GSGTADGRRQ DTGGAQAQAS
AGPANVGVSI GPGQVSGLAR FGPYQCGEAY TWDIGHPVLA KPCHAVGSAI RAVGYIEATP
GVQTDVSLSV QDVKTDEVVA GPYVCKGLMF TDFALKHTCG PVDLDAPRGR RYRVVESWQY
TGRSLLPGGT VRGPEFIW
//
