UL13_VZVO
ID UL13_VZVO Reviewed; 510 AA.
AC Q6YP73;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Serine/threonine-protein kinase UL13 homolog;
DE AltName: Full=Protein kinase ORF47;
DE EC=2.7.11.1;
GN ORFNames=ORF47;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VZV-Oka;
RX PubMed=11162813; DOI=10.1006/viro.2000.0775;
RA Faga B., Maury W., Bruckner D.A., Grose C.;
RT "Identification and mapping of single nucleotide polymorphisms in the
RT varicella-zoster virus genome.";
RL Virology 280:1-6(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
RN [4]
RP FUNCTION.
RX PubMed=12368341; DOI=10.1128/jvi.76.21.10980-10993.2002;
RA Kenyon T.K., Cohen J.I., Grose C.;
RT "Phosphorylation by the varicella-zoster virus ORF47 protein serine kinase
RT determines whether endocytosed viral gE traffics to the trans-Golgi network
RT or recycles to the cell membrane.";
RL J. Virol. 76:10980-10993(2002).
CC -!- FUNCTION: Multifunctional serine/threonine kinase that plays a role in
CC several processes including egress of virus particles from the nucleus,
CC modulation of the actin cytoskeleton and regulation of viral and
CC cellular gene expression. Regulates the nuclear localization of viral
CC envelopment factor proteins 24 and 27, by phosphorylating the protein
CC kinase ORF66, indicating a role in nuclear egress. Disrupts host
CC nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc
CC receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation
CC of glycoprotein E (gE) by UL13 alters its subcellular localization,
CC from the host early endosome to the plasma membrane. Participates in
CC the transcriptional regulation of cellular and viral mRNAs mainly by
CC phosphorylating the viral transcriptional regulator IE63 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12368341}.
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 -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250}. Host nucleus
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Displays a substrate specificity similar to host CDC2.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY016447; AAK19940.1; -; Genomic_DNA.
DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57656.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57727.1; -; Genomic_DNA.
DR RefSeq; NP_040169.1; NC_001348.1.
DR GeneID; 1487678; -.
DR KEGG; vg:1487678; -.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; 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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host nucleus; Host-virus interaction; Kinase;
KW Nucleotide-binding; Serine/threonine-protein kinase; Transferase; Virion;
KW Virion tegument.
FT CHAIN 1..510
FT /note="Serine/threonine-protein kinase UL13 homolog"
FT /id="PRO_0000385456"
FT DOMAIN 132..458
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 138..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 510 AA; 57351 MW; 66D7FB3E8A1D340A CRC64;
MDADDTPPNL QISPTAGPLR SHHNTDGHEP NATAADQQER ESTNPTHGCV NHPWANPSTA
TCMESPERSQ QTSLFLLKHG LTRDPIHQRE RVDVFPQFNK PPWVFRISKL SRLIVPIFTL
NEQLCFSKLQ IRDRPRFAGR GTYGRVHIYP SSKIAVKTMD SRVFNRELIN AILASEGSIR
AGERLGISSI VCLLGFSLQT KQLLFPAYDM DMDEYIVRLS RRLTIPDHID RKIAHVFLDL
AQALTFLNRT CGLTHLDVKC GNIFLNVDNF ASLEITTAVI GDYSLVTLNT YSLCTRAIFE
VGNPSHPEHV LRVPRDASQM SFRLVLSHGT NQPPEILLDY INGTGLTKYT GTLPQRVGLA
IDLYALGQAL LEVILLGRLP GQLPISVHRT PHYHYYGHKL SPDLALDTLA YRCVLAPYIL
PSDIPGDLNY NPFIHAGELN TRISRNSLRR IFQCHAVRYG VTHSKLFEGI RIPASLYPAT
VVTSLLCHDN SEIRSDHPLL WHDRDWIGST
