B1_VAR67
ID B1_VAR67 Reviewed; 300 AA.
AC P33800;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=B1 kinase;
DE AltName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Vaccinia protein kinase 1;
GN Name=VPK1; ORFNames=B1R;
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=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/threonine-protein kinase that plays
CC different role in the viral life cycle. Phosphorylates the host small
CC ribosomal protein RACK1 thereby customizing the ribosomes to a state
CC optimal for viral mRNAs (which contain poly-A leaders) but not for host
CC mRNAs. Facilitates viral DNA replication by inhibiting host BANF1, a
CC cellular host defense responsive to foreign DNA. Phosphorylates host
CC BANF1 on serine and threonine residues; this leads to BANF1
CC relocalization to the cytoplasm, loss of dimerization and impaired DNA
CC binding activity. Indeed, BANF1 activity depends on its DNA-binding
CC property which is blocked by VPK1-mediated phosphorylation. Required
CC for viral intermediate genes expression, probably by inhibiting host
CC BANF1. Modulates cellular responses via host JUN by two different
CC mechanisms, either by direct phosphorylation or by modulation of
CC upstream JIP1-MAPK complexes. Seems to participate in the
CC accumulation/processing of late proteins and thus in virion maturation.
CC In addition, inhibits B12 repressive activity on viral DNA replication
CC via a phosphorylation-dependent mechanism.
CC {ECO:0000250|UniProtKB:P16913}.
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 Evidence={ECO:0000250|UniProtKB:P16913};
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; Evidence={ECO:0000250|UniProtKB:P16913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P16913};
CC -!- SUBUNIT: Interacts with host JIP1; this interaction increases the
CC amount of MAPK bound to JIP1 and subsequently increases the activity of
CC transcription factors, such as JUN, that respond to these complexes.
CC Interacts with protein B12; this interaction inhibits the repressive
CC activity of B12 pseudokinase on viral replication factory formation.
CC {ECO:0000250|UniProtKB:P16913}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P16913}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P16913}. Note=Localizes in cytoplasmic
CC viral factories and is a minor component of the virion.
CC {ECO:0000250|UniProtKB:P16913}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P16913}.
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; CAA49110.1; -; Genomic_DNA.
DR PIR; A36855; A36855.
DR RefSeq; NP_042213.1; NC_001611.1.
DR SMR; P33800; -.
DR PRIDE; P33800; -.
DR GeneID; 1486550; -.
DR KEGG; vg:1486550; -.
DR BRENDA; 2.7.11.1; 6603.
DR Proteomes; UP000002060; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Host-virus interaction; Kinase; Magnesium;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Virion.
FT CHAIN 1..300
FT /note="B1 kinase"
FT /id="PRO_0000086793"
FT DOMAIN 16..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 300 AA; 34260 MW; 40CD8ABC00D3CBF0 CRC64;
MNFQGLVLTD NCKNQWVVGP LIGKGGFGSI YTTNDNNYVV KIEPKANGSL FTEQAFYTRV
LKPSVIEEWK KSHHISHVGV ITCKAFGLYK SINTEYRFLV INRLGVDLDA VIRANNNRLP
KRSVMLVGIE ILNTIQFMHE QGYSHGNIKA SNIVLDQMDK NKLYLVDYGL VSKFMSNGEH
VPFIRNPNKM DNGTLEFTPI DSHKGYVVSR RGDLETLGYC MIRWLGGILP WTKIAETKNC
ALVSATKQKY VNNTTTLLMT SLQYAPRELL QYITMVNSLT YFEEPNYDKF RHILMQGAYY
