ID   VPK2_VACCW              Reviewed;         439 AA.
AC   Q89121;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Vaccinia protein kinase 2;
GN   Name=VPK2; OrderedLocusNames=VACWR049; ORFNames=F10L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7666539; DOI=10.1128/jvi.69.10.6376-6388.1995;
RA   Wang S., Shuman S.;
RT   "Vaccinia virus morphogenesis is blocked by temperature-sensitive mutations
RT   in the F10 gene, which encodes protein kinase 2.";
RL   J. Virol. 69:6376-6388(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=8052637; DOI=10.1073/pnas.91.16.7653;
RA   Lin S., Broyles S.S.;
RT   "Vaccinia protein kinase 2: a second essential serine/threonine protein
RT   kinase encoded by vaccinia virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7653-7657(1994).
CC   -!- FUNCTION: Essential serine-protein kinase.
CC       {ECO:0000269|PubMed:8052637}.
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   -!- PTM: Autophosphorylated.
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; U32589; AAA83263.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89328.1; -; Genomic_DNA.
DR   RefSeq; YP_232931.1; NC_006998.1.
DR   DNASU; 3707506; -.
DR   GeneID; 3707506; -.
DR   KEGG; vg:3707506; -.
DR   Proteomes; UP000000344; 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; IPR008790; Poxvirus_ser/thr_kinase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF05445; Pox_ser-thr_kin; 1.
DR   PIRSF; PIRSF015695; STPK_F10L; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..439
FT                   /note="Serine/threonine-protein kinase 2"
FT                   /id="PRO_0000086799"
FT   DOMAIN          87..439
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         93..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   439 AA;  52131 MW;  5ECA321680FC9A96 CRC64;
     MGVANDSSPE YQWMSPHRLS DTVILGDCLY FNNIMSQLDL HQNWAPSVRL LNYFKNFNKE
     TLLKIEENDY INSSFFQQKD KRFYPINDDF YHISTGGYGI VFKIDNYVVK FVFEATKLYS
     PMETTAEFTV PKFLYNNLKG DEKKLIVCAW AMGLNYKLTF LHTLYKRVLH MLLLLIQTMD
     GQELSLRYSS KVFLKAFNER KDSIKFVKLL SHFYPAVINS NINVINYFNR MFHFFEHEKR
     TNYEYERGNI IIFPLALYSA DKVDTELAIK LGFKSLVQYI KFIFLQMALL YIKIYELPCC
     DNFLHADLKP DNILLFDSNE PIIIHLKDKK FVFNERIKSA LNDFDFSQVA GIINKKIKNN
     FKVEHNWYYD FHFFVHTLLK TYPEIEKDIE FSTALEEFIM CTKTDCDKYR LKVSILHPIS
     FLEKFIMRDI FSDWINGGN