PK1_NPVOP
ID PK1_NPVOP Reviewed; 274 AA.
AC O10269;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN Name=PK1; ORFNames=ORF1;
OS Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=262177;
OH NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT polyhedrosis virus genome.";
RL Virology 229:381-399(1997).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U75930; AAC59000.1; -; Genomic_DNA.
DR RefSeq; NP_046157.1; NC_001875.2.
DR SMR; O10269; -.
DR PRIDE; O10269; -.
DR GeneID; 912025; -.
DR KEGG; vg:912025; -.
DR BRENDA; 2.7.11.1; 4430.
DR Proteomes; UP000009248; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..274
FT /note="Serine/threonine-protein kinase 1"
FT /id="PRO_0000086545"
FT DOMAIN 16..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 274 AA; 31502 MW; F260B6CC6051BCA2 CRC64;
MDAALQSLSR FVADCAVLAP KVVNGRFGKM DVLHHRPTTS KLFLRKTIAA HSFSADEINV
HDLMSDHPSF VDMYFCYSSP TAWAIVMDYV PCPDLFETLQ TQGALDNALV VNIVRQLCDA
LNDLHNATGY IHNDVKLENV LYFGARDRVY LCDYGLCKRE HSPVHDGTLE YFSPEKIRRH
NYARSFDWYA VGVLAYKLLT GGRHPFERSA DEVLDLASMR RRQQYNDPAA LKNVRNLMAR
DFVFCLTRFN FECRSTDYKQ IAKHSFLASR HDYI
