ID A0A086H0D6_STRSC Unreviewed; 764 AA.
AC A0A086H0D6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KFG01104.1};
GN ORFNames=IQ62_09355 {ECO:0000313|EMBL:KFG01104.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG01104.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG01104.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG01104.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KFG01104.1}.
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DR EMBL; JPPX01000076; KFG01104.1; -; Genomic_DNA.
DR RefSeq; WP_037692048.1; NZ_KL997412.1.
DR AlphaFoldDB; A0A086H0D6; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000028722; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 3.
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}; Kinase {ECO:0000313|EMBL:KFG01104.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KFG01104.1};
KW Transferase {ECO:0000313|EMBL:KFG01104.1}.
FT DOMAIN 11..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 262..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 764 AA; 84071 MW; 45E003E87182BF46 CRC64;
MADTRLIQGR YRLLDQIGRG GMGEVWRARD ESLGRLVAVK CLKPVNTQPD QSFTRVLRER
FRREARVAAA LQHRGVTVVH DFGEFDGVLF LVMELLEGRN LSQLLEDNKH HPLAVPVVVE
IADQVAAALA YTHQQGIVHR DLKPANIMLL TDGTVKICDF GIARLGRDVT FTSRLTGTGI
AMGTPHYMSP EQISGDQVDR RSDLYSFGCV LYEIATGAPP FDLDDAWAVL MGHRDTAPRP
PRSHRDEVPE YLDRIILDLL AKEPEERPHD AREVGRRVGE GRAVTAAAQA RSHVPTVLSR
PAPPESAPGT HRPRTRPEQP SSREARLPSW TRGMTTGHKA TGTGAGLGLT PPDASAGLTG
EWIARPATGG VEQPVHTERP TPSPELITTL AGRHNAGLSL GRLGRWTEAG EVHRAVAAER
EHALGPDHPD TLSSRYEVGF TLSRTGRPAD ALREFAHVAR AREHALGPDH PDTLAARQEM
AYVLGQLGRH LEAHQAYVSV LAVRERIAGP DHPDTLRCRH NLAFNLSRLG RLEDSYRMAS
EVAAARTRVL GANHPDTLVT RYEVAYALGQ LGRWPEALRT YQEVAESRAQ ALGPDHPDTL
AARHEVGISL GRLGRSTDAL TLYRALAGDR ARVHGPAHIE TLRARHGLGV NLGRLSRWEE
ALAESRDVCA LRERVLGPDH PDTLVSRREV AVGLGWLGRW PDALTEYRRV ADARERVLGP
DHPDALASRN DEAHCLEQLG RGQEAAELYR RVAASRQRRA TGGR
//
