UL13_HHV2H
ID UL13_HHV2H Reviewed; 518 AA.
AC P89436;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein kinase UL13;
DE EC=2.7.11.1;
GN ORFNames=UL13;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
RN [2]
RP AUTOPHOSPHORYLATION.
RX PubMed=18207213; DOI=10.1016/j.virol.2007.11.023;
RA Cano-Monreal G.L., Tavis J.E., Morrison L.A.;
RT "Substrate specificity of the herpes simplex virus type 2 UL13 protein
RT kinase.";
RL Virology 374:1-10(2008).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19640559; DOI=10.1016/j.virol.2009.06.051;
RA Cano-Monreal G.L., Wylie K.M., Cao F., Tavis J.E., Morrison L.A.;
RT "Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins.";
RL Virology 392:137-147(2009).
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 factors UL34 and UL31, by phosphorylating the US3 kinase,
CC indicating a role in nuclear egress. Disrupts host nuclear lamins,
CC including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed
CC of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E
CC (gE) by UL13 alters its subcellular localization, from the host early
CC endosome to the plasma membrane. Participates in the transcriptional
CC regulation of cellular and viral mRNAs mainly by phosphorylating the
CC viral transcriptional regulator ICP22. Additional substrates have been
CC identified, including UL41, UL49 or host EF1D (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19640559}.
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:0000269|PubMed:19640559}.
CC -!- PTM: Autophosphorylated.
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; Z86099; CAB06773.1; -; Genomic_DNA.
DR PRIDE; P89436; -.
DR Proteomes; UP000001874; 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; Host-virus interaction; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Virion; Virion tegument.
FT CHAIN 1..518
FT /note="Serine/threonine-protein kinase UL13"
FT /id="PRO_0000385455"
FT DOMAIN 151..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 157..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 518 AA; 57000 MW; C1FBA121CF07A21B CRC64;
MDESGRQRPA SHVAADISPQ GAHRRSFKAW LASYIHSLSR RASGRPSGPS PRDGAVSGAR
PGSRRRSSFR ERLRAGLSRW RVSRSSRRRS SPEAPGPAAK LRRPPLRRSE TAMTSPPSPP
SHILSLARIH KLCIPVFAVN PALRYTTLEI PGARSFGGSG GYGEVQLIRE HKLAVKTIRE
KEWFAVELVA TLLVGECALR GGRTHDIRGF ITPLGFSLQQ RQIVFPAYDM DLGKYIGQLA
SLRATTPSVA TALHHCFTDL ARAVVFLNTR CGISHLDIKC ANVLVMLRSD AVSLRPAVLA
DFSLVTLNSN STISRGQFCL QEPDLESPRG FGMPAALTTA NFHTLVGHGY NQPPELSVKY
LNNERAEFNN RPLKHDVGLA VDLYALGQTL LELLVSVYVA PSLGVPVTRV PGYQYFNNQL
SPDFAVALLA YRCVLHPALF VNSAETNTHG LAYDVPEGIR RHLRNPKIRR AFTEQCINYQ
RTHKAVLSSV SLPPELRPLL VLVSRLCHAN PAARHSLS
