ID A0A1Q5BI41_9ACTN Unreviewed; 530 AA.
AC A0A1Q5BI41;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A6A27_20520 {ECO:0000313|EMBL:OKI71006.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI71006.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI71006.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI71006.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI71006.1}.
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DR EMBL; LWLS01000059; OKI71006.1; -; Genomic_DNA.
DR RefSeq; WP_073834388.1; NZ_LWLS01000059.1.
DR AlphaFoldDB; A0A1Q5BI41; -.
DR STRING; 1718947.A6A27_20520; -.
DR OrthoDB; 4408092at2; -.
DR Proteomes; UP000186700; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:OKI71006.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000186700};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OKI71006.1};
KW Transferase {ECO:0000313|EMBL:OKI71006.1}.
FT DOMAIN 16..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 369..478
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 488..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 530 AA; 55278 MW; 7375DF1F882049D8 CRC64;
MGAAVRGGAQ LLGERYRLVE QLGAGGMSVV WRGYDEVLGR QVAVKVLASR LASDKAFRHR
IRIEAQAAAR LCHPNITNVY DYGESDQAGL TVPYVVMELV DGAPLSARLG RGGQLPWREA
VTIGAEVASA LATAHARGVV HRDVTPGNVM LTSTGVKVVD FGISALAGES EHGPDGALLG
TPAYLAPERL NNGQVSPATD VYAVGLLLYR MLTGGLPWQA STTTQMLRAH MYHDPEPMPP
VLGLPDEVAQ LVRQCLAKRC ADRPATAEVA RTLAEAAGIS AIVPVSPAVG QVDPTLAENA
GTTILPWSAE TDALPFSAVR TRTRAATRRR RVEAGVAAAG LVAVTATMWG MTSKSSASGG
VEPAQARMAL PQPIPCAVDY TLRRDSGKDF TADLTLTNTG DRELRGWTMS FTFPGRQTVT
SAQPAVHQQG RTVQLQAPAT DPALAPGASR KISLTGRYTG GNLLPVEFKV GDSTCGVQVS
GVAGSVPTTA PARTAAPKPP QKASTGKSSG SRANPEKHGK GKGDGKGKGD
//
