KRB2_VACCW
ID KRB2_VACCW Reviewed; 283 AA.
AC P24362; Q76ZL1;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pseudokinase B12 {ECO:0000303|PubMed:31341052, ECO:0000303|PubMed:33177193};
GN Name=B12; OrderedLocusNames=VACWR194; ORFNames=B12R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2607336; DOI=10.1099/0022-1317-70-12-3187;
RA Howard S.T., Smith G.L.;
RT "Two early vaccinia virus genes encode polypeptides related to protein
RT kinases.";
RL J. Gen. Virol. 70:3187-3201(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION, AND LACK OF ACTIVITY.
RX PubMed=8277291; DOI=10.1099/0022-1317-74-12-2807;
RA Banham A.H., Smith G.L.;
RT "Characterization of vaccinia virus gene B12R.";
RL J. Gen. Virol. 74:2807-2812(1993).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30768651; DOI=10.1371/journal.ppat.1007608;
RA Olson A.T., Wang Z., Rico A.B., Wiebe M.S.;
RT "A poxvirus pseudokinase represses viral DNA replication via a pathway
RT antagonized by its paralog kinase.";
RL PLoS Pathog. 15:e1007608-e1007608(2019).
RN [6]
RP FUNCTION, AND INTERACTION WITH B1/VPK1 AND HOST VRK2.
RX PubMed=31341052; DOI=10.1128/jvi.00855-19;
RA Rico A.B., Wang Z., Olson A.T., Linville A.C., Bullard B.L., Weaver E.A.,
RA Jones C., Wiebe M.S.;
RT "The Vaccinia Virus (VACV) B1 and Cellular VRK2 Kinases Promote VACV
RT Replication Factory Formation through Phosphorylation-Dependent Inhibition
RT of VACV B12.";
RL J. Virol. 93:0-0(2019).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST VRK1 AND VRK2.
RX PubMed=33177193; DOI=10.1128/jvi.02114-20;
RA Rico A.B., Linville A.C., Olson A.T., Wang Z., Wiebe M.S.;
RT "The Vaccinia Virus B12 Pseudokinase Represses Viral Replication via
RT Interaction with the Cellular Kinase VRK1 and Activation of the Antiviral
RT Effector BAF.";
RL J. Virol. 95:0-0(2021).
CC -!- FUNCTION: Pseudokinase that plays a role in viral DNA replication
CC repression by activating the antiviral protein BANF1 and inhibiting the
CC activity of host VRK1, a cellular modulator of BANF1.
CC {ECO:0000269|PubMed:30768651, ECO:0000269|PubMed:31341052,
CC ECO:0000269|PubMed:33177193}.
CC -!- ACTIVITY REGULATION: Both catalytically active kinases B1/VPK1 and host
CC VRK2 repress B12 inhibitory activity in a B1/VPK1 deletion mutant
CC strain. {ECO:0000269|PubMed:30768651}.
CC -!- SUBUNIT: Interacts with B1/VPK1 (PubMed:31341052). Interacts with host
CC VRK1 (PubMed:33177193). Interacts with host VRK2 (PubMed:31341052,
CC PubMed:33177193). {ECO:0000269|PubMed:31341052,
CC ECO:0000269|PubMed:33177193}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:30768651}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:2045793, ECO:0000269|PubMed:8277291}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants exhibit rescued DNA replication
CC and viral yield in multiple cell lines when B1 kinase/VPK1 is deleted.
CC {ECO:0000269|PubMed:30768651}.
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; D11079; BAA01842.1; -; Genomic_DNA.
DR EMBL; D00629; BAA00520.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89473.1; -; Genomic_DNA.
DR PIR; A33610; TVVZBW.
DR RefSeq; YP_233076.1; NC_006998.1.
DR SMR; P24362; -.
DR DNASU; 3707665; -.
DR GeneID; 3707665; -.
DR KEGG; vg:3707665; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Early protein; Host nucleus; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..283
FT /note="Pseudokinase B12"
FT /id="PRO_0000086197"
FT DOMAIN 1..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 283 AA; 33310 MW; D2819B94F73F9C77 CRC64;
MESFKYCFDN DGKKWIIGNT LYSGNSILYK VRKNFTSSFY NYVMKIDHKS HKPLLSEIRF
YISVLDPLTI DNWTRERGIK YLAIPDLYGI GETDDYMFFV IKNLGRVFAP KDTESVFEAC
VTMINTLEFI HSQGFTHGKI EPRNILIRNK RLSLIDYSRT NKLYKSGNSH IDYNEDMITS
GNINYMCVDN HLGATVSRRG DLEMLGYCMI EWFGGKLPWK NESSIKVIKQ KKEYKKFIAT
FFEDCFPEGN EPLELVRYIE LVYTLDYSQT PNYDRLRKLF IQD