VPK2_SWPVK
ID VPK2_SWPVK Reviewed; 440 AA.
AC P32216;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein kinase 2;
DE EC=2.7.11.1;
GN ORFNames=C20L;
OS Swinepox virus (strain Kasza) (SWPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX NCBI_TaxID=10277;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA Massung R.F., Jayarama V., Moyer R.W.;
RT "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT identification of genetic elements supporting phenotypic observations
RT including a novel G protein-coupled receptor homologue.";
RL Virology 197:511-528(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:0000305}.
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DR EMBL; L22013; AAC37851.1; -; Genomic_DNA.
DR RefSeq; NP_570182.1; NC_003389.1.
DR GeneID; 932408; -.
DR KEGG; vg:932408; -.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF05445; Pox_ser-thr_kin; 1.
DR PIRSF; PIRSF015695; STPK_F10L; 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..440
FT /note="Serine/threonine-protein kinase 2"
FT /id="PRO_0000086794"
FT DOMAIN 85..440
FT /note="Protein kinase"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 91..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 52905 MW; 7A1676808849C119 CRC64;
MKEINSLECQ WESIDDNNDT TILGDDIYFD YIISQLDIHQ NWSPDIRLIR YFRKFNKESF
DKISDTEYIN PSFFQQRDKR FYPLNDDFYH ISTGGYGIVF KMDKYVVKFV YEPNKQYSPI
DTTAEYTIPK FLYNNLKGDE KKLIVCAWAM GLNYKLTFLH RLYKRVLYML LLIIQTIDNQ
RLNIHHFSHK YFLKSFNEKK SDIKFVKLLS YFYPIVVQSN INVINYFTHM FHFFEHEKRA
NYLYDRGNII IFPLARFSSD KVTEQMAIEL GFKSIVQYVK FIFLQISLLY IKIYELPCCD
NFLHVDLKPD NILIFNSDCP ITIKFKKYTY VFNEPIKACL NDFDFSQVAN ILNKKIKNSL
KIEHNWYYDF HFFIHTLLRT YPEIESDKEF SDSLEDFIMC CTKNTCEKFR LKVSILHPIS
FLENLITKNI FSNWINGESC