ID   VPK2_VACCP              Reviewed;         405 AA.
AC   P29884;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Vaccinia protein kinase 2;
GN   Name=VPK2; ORFNames=F8;
OS   Vaccinia virus (strain L-IVP) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=31531;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mikryukov N.N., Chizhikov V.E., Prikhod'Ko G.G., Urmmanov I.M.,
RA   Serpinskii O.I., Blinov V.M., Nikulin A.E., Vasilenko S.K.;
RT   "Structural-functional organization of segment of vaccinia virus genome.";
RL   Biotekhnologiya 4:442-449(1988).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M57977; AAA48288.1; -; Genomic_DNA.
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   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..405
FT                   /note="Serine/threonine-protein kinase 2"
FT                   /id="PRO_0000086797"
FT   DOMAIN          54..405
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         60..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   405 AA;  48133 MW;  FC3A279E770035CA CRC64;
     MGVANDSSPE YQWMSPHLNY FKNFNKETLL KIEENDYINS SFFQQKDKRF YPINDDFYHI
     STGGYGIVFK IDNYVVKFVL EAIKLYSPME IMAELTVPKF LYNNLKGDEK KLIVCVWAMG
     LNYKLTFLHT LYKRVLHMLL LLIQTMDGQE LSLRYSSKVF LKAFNERKDS IKFVKLLSHF
     YPAVINSNIN VINYFNRMFH FFEHEKGTNY EYERGNIIIF PLTLYSADKV DTELAIKLGF
     KSLVQYIKFI FLQMALLYIK IYELPCCDNF LHADLKPDNI LLFDSNEPII IHLDKKFVFN
     ERIKSALNDF DFSQVAGIIN KKIKNNFKVE HNWYYDFHFF VHTLLKTYPE IEKDIEFSTA
     LEEFIMCTKT DCDKYRLKVS ILHPISFLEK FIMRDIFSDW INGGN