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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
 
 
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