ID   PK1_NPVLD               Reviewed;         274 AA.
AC   P41720;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serine/threonine-protein kinase 1;
DE            EC=2.7.11.1;
GN   Name=PK1; Synonyms=PK-1; OrderedLocusNames=LdOrf-3;
OS   Lymantria dispar multicapsid nuclear polyhedrosis virus (LdMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=10449;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=5-6-1;
RX   PubMed=8107234; DOI=10.1128/jvi.68.3.1728-1736.1994;
RA   Bischoff D.S., Slavicek J.M.;
RT   "Identification and characterization of a protein kinase gene in the
RT   Lymantria dispar multinucleocapsid nuclear polyhedrosis virus.";
RL   J. Virol. 68:1728-1736(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Cl 5-6;
RX   PubMed=9887315; DOI=10.1006/viro.1998.9469;
RA   Kuzio J., Pearson M.N., Harwood S.H., Funk C.J., Evans J.T., Slavicek J.M.,
RA   Rohrmann G.F.;
RT   "Sequence and analysis of the genome of a baculovirus pathogenic for
RT   Lymantria dispar.";
RL   Virology 253:17-34(1999).
CC   -!- FUNCTION: In vitro, can phosphorylate histone H1.
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   -!- DEVELOPMENTAL STAGE: Expressed throughout the infection cycle beginning
CC       at 4 hours postinfection, first as a delayed-early gene and
CC       subsequently as a late gene.
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; U04322; AAC18617.1; -; Unassigned_DNA.
DR   EMBL; AF081810; AAC70188.1; -; Genomic_DNA.
DR   PIR; T30350; T30350.
DR   RefSeq; NP_047639.1; NC_001973.1.
DR   SMR; P41720; -.
DR   GeneID; 1488482; -.
DR   KEGG; vg:1488482; -.
DR   BRENDA; 2.7.11.1; 3111.
DR   Proteomes; UP000203997; 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   2: Evidence at transcript level;
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_0000086544"
FT   DOMAIN          17..265
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         23..31
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;  32438 MW;  DAEC7165D267F6DD CRC64;
     MDALIGDFAD FHKECSARTA LHLVNGKFGK VSVWKHGPTQ KSFFYKRIEH KHFNAIEPFV
     HHLMKFNKYF LRLFYSLHSL REHLLVMDYI PDGDLFDLMQ TEPRLREPEI SLIAYQLIDA
     LQALHKHNVV HNDVKLENVL YRRFEQIYVC DYGLCKIAGS PSTFEGTVDY FSPEKINKHA
     AAVHFDWWAV GVLLYEISTG KHPFKLDQDE SLDVETLHKR QIQLDVTFPA DFDNPFLEEF
     ICFLLGYCYD YRAHSYEVIQ KNTYWKSIVH WKQR