ID A0A1H5L3D4_9ACTN Unreviewed; 586 AA.
AC A0A1H5L3D4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SEE71582.1};
GN ORFNames=SAMN05216533_3377 {ECO:0000313|EMBL:SEE71582.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE71582.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEE71582.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE71582.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
RL Submitted (OCT-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; FNTQ01000001; SEE71582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5L3D4; -.
DR STRING; 1855349.SAMN05216533_3377; -.
DR Proteomes; UP000198812; 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; 1.10.510.10; 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; 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}; Kinase {ECO:0000313|EMBL:SEE71582.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198812};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SEE71582.1};
KW Transferase {ECO:0000313|EMBL:SEE71582.1}.
FT DOMAIN 33..287
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 274..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 586 AA; 63059 MW; AA22289DA0B50C0E CRC64;
MFPDRGAVLS LTLTRPLRGN VNQMQGLLIA GRYRLADIIG SGGMGRVWRA HDEVLHRAVA
IKELTAALYV SESDQAVLLA RTRAEARAAA RINHSAVVTV HDVLEHDGRP WIVMELVEGH
SLADAVKEQG RIEPREAARI GLWVLRALRA AHSAGVLHRD VKPGNVLIGR DGRVLLTDFG
IAQIEGDTTI TRTGEVVGSV DYLAPERVRG HDPGPSSDLW ALGATLYTAV EGRSPFRRTS
PLTTMQAVVE DEAGEPHGAG PLGPVITALL RKEPAERPSP EETEQMLAEA AEGRRPSGAQ
KYVPTQSHAG GIWRDSGGSH GETYDGSRGG EYGSSYGGQR PPGGSTTSPT AVAAPSAPVA
AQPRRRRLRT LALVVTLAAL LGGGAAVVLQ KWDFGQQQDG TGSVITPATS GSTSSGGATV
APGGTIPAGW KKYDDPVGFT LYLPAGWKRS VSIKKTNGLE QIDYSPDGGT HLVRVAVDTS
PDYSNAYDHM RNLERLLRQR LVDYKTVSLK EDTYRDLPSS RWEYTWTALP KDAKVPGAYR
AVDLGYFTGD GVEYAIYTAS PIDDWATTSK RFTFVLQGWR EGEVKP
//