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B1 kinase (Serine/threonine-protein kinase 1) (EC 2.7.11.1)

 B1_VACCA                Reviewed;         300 AA.
O57252;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
07-NOV-2018, entry version 76.
RecName: Full=B1 kinase;
AltName: Full=Serine/threonine-protein kinase 1;
EC=2.7.11.1;
Name=VPK1; OrderedLocusNames=MVA167R, ACAM3000_MVA_167; ORFNames=B1R;
Vaccinia virus (strain Ankara) (VACV).
Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
Orthopoxvirus; Vaccinia virus.
NCBI_TaxID=126794;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9601507; DOI=10.1006/viro.1998.9123;
Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
"The complete genomic sequence of the modified vaccinia Ankara strain:
comparison with other orthopoxviruses.";
Virology 244:365-396(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Isolate Acambis 3000;
Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
Osborne J., Khristova M., Wohlhueter R.M.;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Essential serine/threonine-protein kinase that plays
different role in the viral life cycle. Phosphorylates the host
small ribosomal protein RACK1 thereby customizing the ribosomes to
a state optimal for viral mRNAs (which contain poly-A leaders) but
not for host mRNAs. Facilitates viral DNA replication by
inhibiting host BANF1, a cellular host defense responsive to
foreign DNA. Phosphorylates host BANF1 on serine and threonine
residues; this leads to BANF1 relocalization to the cytoplasm,
loss of dimerization and impaired DNA binding activity. Indeed,
BANF1 activity depends on its DNA-binding property which is
blocked by VPK1-mediated phosphorylation. Required for viral
intermediate genes expression, probably by inhibiting host BANF1.
Modulates cellular responses via host JUN by two different
mechanisms, either by direct phosphorylation or by modulation of
upstream JIP1-MAPK complexes. Seems to participate in the
accumulation/processing of late proteins and thus in virion
maturation. {ECO:0000250|UniProtKB:P16913}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P16913}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P16913};
-!- SUBUNIT: Interacts with host JIP1; this interaction increases the
amount of MAPK bound to JIP1 and subsequently increases the
activity of transcription factors, such as JUN, that respond to
these complexes. {ECO:0000250|UniProtKB:P16913}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P16913}. Host
cytoplasm {ECO:0000250|UniProtKB:P16913}. Note=Localizes in
cytoplasmic viral factories and is a minor component of the
virion. {ECO:0000250|UniProtKB:P16913}.
-!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P16913}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Poxviruses subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U94848; AAB96545.1; -; Genomic_DNA.
EMBL; AY603355; AAT10565.1; -; Genomic_DNA.
PIR; T37440; T37440.
ProteinModelPortal; O57252; -.
Proteomes; UP000159908; Genome.
Proteomes; UP000172909; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Host cytoplasm; Kinase; Magnesium;
Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
Transferase; Virion.
CHAIN 1 300 B1 kinase.
/FTId=PRO_0000086790.
DOMAIN 16 282 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 22 30 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 147 147 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 45 45 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SEQUENCE 300 AA; 34273 MW; 04C9D7FD3BC0F7C6 CRC64;
MNFQGLVLTD NCKNQWVVGP LIGKGGFGSI YTTNDNNYVV KIEPKANGSL FTEQAFYTRV
LKPSVIEEWK KSHNIKHVGL ITCKAFGLYK SINVEYRFLV INRLGADLDA VIRANNNRLP
KRSVMLIGIE ILNTIQFMHE QGYSHGDIKA SNIVLDQIDK NKLYLVDYGL VSKFMSNGEH
VPFIRNPNKM DNGTLEFTPI DSHKGYVVSR RGDLETLGYC MIRWLGGILP WTKISETKNC
ALVSATKQKY VNNTATLLMT SLQYAPRELL QYITMVNSLT YFEEPNYDKF RHILMQGVYY


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