ID A0A1C6R9I3_9ACTN Unreviewed; 530 AA.
AC A0A1C6R9I3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=GA0070624_0227 {ECO:0000313|EMBL:SCL13769.1};
OS Micromonospora rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=568872 {ECO:0000313|EMBL:SCL13769.1, ECO:0000313|Proteomes:UP000199413};
RN [1] {ECO:0000313|Proteomes:UP000199413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45431 {ECO:0000313|Proteomes:UP000199413};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-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};
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DR EMBL; FMHV01000002; SCL13769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6R9I3; -.
DR STRING; 568872.GA0070624_0227; -.
DR OrthoDB; 4408092at2; -.
DR Proteomes; UP000199413; 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:SCL13769.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000199413};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SCL13769.1};
KW Transferase {ECO:0000313|EMBL:SCL13769.1}.
FT DOMAIN 16..289
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 370..479
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 482..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Polar 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; 55658 MW; FD9C958B82ABC56B CRC64;
MGGAVRNGTQ LLGERYRLVE QLGAGGMSVV WRGYDEVLGR QVAIKVLASR LASDKAFRHR
IRIEAQAAAR LCHPNITNVY DYGESEQVGL TVPYVVMELV DGGSLSSRLA REGQLPWREA
LIIGAEVASA LAAAHARGVV HRDVTPGNVM LTSTGVKVVD FGISALVGES EKGPDGALLG
TPAYLAPERL DNGQVSPATD VYAVGLLLYR MLTGRLPWRA STTTEMLRAH MYNDPDPMPS
VTGLPAEVGE LVRRCLAKRP GDRPPTADVA RTLADAAGIA AIVPVSPAVG QVDPGLVENA
STTILPWRSD TDALPLSGIR TRTRLATIRR RKVEAGVAAA GLVAVTATMW GVTSRSPASG
GIEPTEARMG MAEPVPCEVD YVLRRDTGRD FAAELTLRNT GTRELRDWTM SFTFPGQQTV
TKAQPAVQQQ GRTVLLRPPA TDPSLAPGAA KKVALSGRYT GSNPLPVQFR VGDTTCGVQV
AGVAGSTPAP TTKAPTKKTT AKGGGGSHSS DDGGGRDRSG NGKGGGKGKR
//
