ID A0A0G3V508_9ACTN Unreviewed; 615 AA.
AC A0A0G3V508;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=IMCC26256_111916 {ECO:0000313|EMBL:AKL74184.1};
OS Actinobacteria bacterium IMCC26256.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL74184.1, ECO:0000313|Proteomes:UP000035517};
RN [1] {ECO:0000313|EMBL:AKL74184.1, ECO:0000313|Proteomes:UP000035517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL74184.1,
RC ECO:0000313|Proteomes:UP000035517};
RA Kim S.;
RT "Genome sequencing of freshwater Actinobacteria.";
RL Submitted (MAY-2015) 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; CP011489; AKL74184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3V508; -.
DR STRING; 1650658.IMCC26256_111916; -.
DR KEGG; abai:IMCC26256_111916; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000035517; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
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:AKL74184.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000035517};
KW Transferase {ECO:0000313|EMBL:AKL74184.1}.
FT DOMAIN 18..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 357..421
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 422..486
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 487..553
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 554..615
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 305..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 615 AA; 63255 MW; 9225C85F40A25A34 CRC64;
MAVGGGGDLV GGVLADRYRL LSPIGAGGSG RVYIADDVKL KRRVAVKVLH PGLAEDAGFL
RRFRNEARLS AQLHHPNIMA VHDWGDEGEP FMVVELLTGG SLRGMLDAGA TLTPSQAAHV
GAQVASALEY AHGHGFVHRD IKPANLLFDE HGIVRVADFG LARALAEASW TEPSGTILGT
ARYASPEQVS GSPLDQRSDL YALALVLVEA VTGDLPFATD TTLATLAART QSPVAAPAAL
GPLVAVVERA GRVDPNDRYP DAATMRSALE DAVKMLPPPG PLRLAGLDEV LSDPNPTQVP
VSRGLLFDQE RPEQPPPVTA RRPAPPRRRP TAAIVVGAAI SAAVLTAAVL LSNANLGAAV
VTPNAVGSTL SNARDLIASG GLLVTENERF SDDPRGVVIS QSPAAGHDIT SGGRVQIVVS
RGPAPIAIPR VAGKTVADAR SELAAAGFAV IEDHRFDETA PSGTVIRTKP AQRAPRDSTV
AIMVSDGKAP VAIPALANST YDNAVNALTN AGFIPARSEA FSDTVAAGTV INTDPAGGGK
AQPGSTVKII VSKGPDVVTV PNVRGLTLDA ASAQLQAAGL TSAVSGVYRP GAKVRAQDPP
NGAVVKRGAT VTLFF
//
