ID   VPK2_VAR67              Reviewed;         439 AA.
AC   P33801;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
GN   ORFNames=C14L, F10L;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=India-1967 / Isolate Ind3;
RX   PubMed=8109158; DOI=10.1016/0168-1702(93)90093-3;
RA   Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V.,
RA   Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of a 43 kbp segment of the genome of
RT   variola virus India-1967 strain.";
RL   Virus Res. 30:239-258(1993).
RN   [2]
RP   COMPLETE GENOME.
RC   STRAIN=India-1967 / Isolate Ind3;
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
CC   -!- FUNCTION: Essential serine-protein kinase. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. Poxviruses subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; X69198; CAA48975.1; -; Genomic_DNA.
DR   PIR; E36840; E36840.
DR   RefSeq; NP_042078.1; NC_001611.1.
DR   GeneID; 1486570; -.
DR   KEGG; vg:1486570; -.
DR   Proteomes; UP000002060; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..439
FT                   /note="Serine/threonine-protein kinase 2"
FT                   /id="PRO_0000086800"
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;  52215 MW;  9C461CE74A278632 CRC64;
     MGVANDSSPE YQWMSPHRLS DTVILGDCLY FNNIMSQLDL HQNWAPSVRL LNYFKNFNRE
     TLLKIEENDY INSSFFQQKD KRFYPINDDF YHISTGGYGI VFKIDNYVVK FVFEATKLYS
     PMETTAEFTV PKFLYNNLKG DEKKLIVCAL AMGLNYKLTF LHTLYKRVLN MLLLLIQTMD
     GQELSLRYSS KVFLKAFNER KDSIKFVKLL SHFYPAVINS NINVINYFNR MFHFFEHEKR
     TNYEYERGNI IIFPLALYSA DKVDTELAIK LGFKSLVQYI KFIFLQMALL YIKIYELPRC
     DNFLHADLKP DNILLFDSNE PIIIHLKDKK FVFNERIKSA LNDFDFSQVA GIINKKIKNN
     FKVEHNWYYD FHFFVHTLLK TYPEIEKDIE FSTALEEFIM CTKTDCDKYR LKVSILHPIS
     FLEKFIMRDI FSDWINGRN