UL13_VZVD
ID UL13_VZVD Reviewed; 510 AA.
AC P09296;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP FUNCTION IN PHOSPHORYLATION OF ORF62 AND ORF63.
RC STRAIN=VZV-32;
RX PubMed=2535748; DOI=10.1128/jvi.63.1.450-455.1989;
RA Smith R.F., Smith T.F.;
RT "Identification of new protein kinase-related genes in three herpesviruses,
RT herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus.";
RL J. Virol. 63:450-455(1989).
RN [3]
RP FUNCTION.
RX PubMed=11507231; DOI=10.1128/jvi.75.18.8854-8858.2001;
RA Kenyon T.K., Lynch J.M., Hay J., Ruyechan W.T., Grose C.;
RT "Varicella-zoster virus ORF47 protein serine kinase: characterization of a
RT cloned, biologically active phosphotransferase and two viral substrates,
RT ORF62 and ORF63.";
RL J. Virol. 75:8854-8858(2001).
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) (By similarity).
CC Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular
CC localization, from the host early endosome to the plasma membrane.
CC Participates in the transcriptional regulation of cellular and viral
CC mRNAs mainly by phosphorylating the viral transcriptional regulator
CC IE63. {ECO:0000250, ECO:0000269|PubMed:11507231,
CC ECO:0000269|PubMed:2535748}.
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; X04370; CAA27930.1; -; Genomic_DNA.
DR PIR; C27344; WZBE47.
DR PRIDE; P09296; -.
DR Proteomes; UP000002602; 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 1: Evidence at protein level;
KW ATP-binding; Host nucleus; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Virion; Virion tegument.
FT CHAIN 1..510
FT /note="Serine/threonine-protein kinase UL13 homolog"
FT /id="PRO_0000086189"
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
