ID   PK2_NPVAC               Reviewed;         215 AA.
AC   P41676;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
GN   Name=PK2; Synonyms=PK-2;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=46015;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6;
RX   PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA   Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT   "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT   virus.";
RL   Virology 202:586-605(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1;
RX   PubMed=8178427; DOI=10.1006/viro.1994.1200;
RA   Morris T.D., Todd J.W., Fisher B., Miller L.K.;
RT   "Identification of lef-7: a baculovirus gene affecting late gene
RT   expression.";
RL   Virology 200:360-369(1994).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST EIF2AK2.
RX   PubMed=9539707; DOI=10.1073/pnas.95.8.4164;
RA   Dever T.E., Sripriya R., McLachlin J.R., Lu J., Fabian J.R., Kimball S.R.,
RA   Miller L.K.;
RT   "Disruption of cellular translational control by a viral truncated
RT   eukaryotic translation initiation factor 2alpha kinase homolog.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:4164-4169(1998).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HOST EIF2AK2.
RX   PubMed=26216977; DOI=10.1073/pnas.1505481112;
RA   Li J.J., Cao C., Fixsen S.M., Young J.M., Ono C., Bando H., Elde N.C.,
RA   Katsuma S., Dever T.E., Sicheri F.;
RT   "Baculovirus protein PK2 subverts eIF2alpha kinase function by mimicry of
RT   its kinase domain C-lobe.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E4364-4373(2015).
CC   -!- FUNCTION: Plays a role in the inhibition of host eIF2alpha/EIF2S1
CC       phosphorylation, thereby increasing viral fitness. In the insect host,
CC       targets the endogenous insect heme-regulated inhibitor (HRI)-like
CC       eIF2alpha kinase. {ECO:0000269|PubMed:26216977,
CC       ECO:0000269|PubMed:9539707}.
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   -!- SUBUNIT: Interacts with the kinase domain of host EIF2AK2.
CC       {ECO:0000269|PubMed:26216977, ECO:0000269|PubMed:9539707}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: Asn-76 is present instead of the conserved Asp which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; L22858; AAA66753.1; -; Genomic_DNA.
DR   EMBL; U01142; AAA19444.1; -; Unassigned_DNA.
DR   PIR; D72865; D72865.
DR   RefSeq; NP_054153.1; NC_001623.1.
DR   SMR; P41676; -.
DR   GeneID; 1403956; -.
DR   KEGG; vg:1403956; -.
DR   Proteomes; UP000008292; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Host cytoplasm; Host-virus interaction; Kinase;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..215
FT                   /note="Probable serine/threonine-protein kinase 2"
FT                   /id="PRO_0000086547"
FT   DOMAIN          1..205
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        18
FT                   /note="I -> F (in Ref. 2; AAA19444)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  24944 MW;  A0F64E4976FE9B6C CRC64;
     MKPEQLVYLN PRQHRIYIAS PLNEYMLSDY LKQRNLQTFA KTNIKVPADF GFYISKFVDL
     VSAVKAIHSV NIVHHNINPE DIFMTGPDFD LYVGGMFGSL YKTFIKNNPQ NITLYAAPEQ
     IKKVYTPKND MYSLGIVLFE LIMPFKTALE RETTLTNFRN NVQQMPASLS QGHPKLTEIV
     CKLIQHDYSQ RPDAEWLLKE MEQLLLEYTT CSKKL