US03_HHV2H
ID US03_HHV2H Reviewed; 481 AA.
AC P13287;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Serine/threonine-protein kinase US3;
DE EC=2.7.11.1;
GN Name=US3;
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 [GENOMIC DNA].
RX PubMed=3027242; DOI=10.1099/0022-1317-68-1-19;
RA McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT "DNA sequence and genetic content of the HindIII l region in the short
RT unique component of the herpes simplex virus type 2 genome: identification
RT of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL J. Gen. Virol. 68:19-38(1987).
RN [2]
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 [3]
RP REVIEW.
RX PubMed=2855680; DOI=10.1016/0968-0004(88)90157-0;
RA Leader D.P., Purves F.C.;
RT "The herpesvirus protein kinase: a new departure in protein
RT phosphorylation?";
RL Trends Biochem. Sci. 13:244-246(1988).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=19945726; DOI=10.1016/j.virol.2009.11.012;
RA Finnen R.L., Roy B.B., Zhang H., Banfield B.W.;
RT "Analysis of filamentous process induction and nuclear localization
RT properties of the HSV-2 serine/threonine kinase Us3.";
RL Virology 397:23-33(2010).
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 inhibition of apoptosis.
CC Phosphorylates UL31 and UL34, two critical regulators of capsid budding
CC from nucleus to endoplasmic reticulum, thereby facilitating virion
CC egress. Modulates and redistributes host components of the nuclear
CC envelope, including LMNA, emerin/EMD and the nuclear matrix protein
CC MATR3. Phosphorylates envelope glycoprotein B (gB), probably to direct
CC it to the cell surface. Promotes virus intracellular spread by
CC restructuring host cell cytoskeleton. Blocks host apoptosis to extend
CC cell survival and allow efficient viral replication. Promotes viral
CC gene expression by phosphorylating host HDAC2 to reduce viral genome
CC silencing (By similarity). {ECO:0000250}.
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: Host cytoplasm {ECO:0000269|PubMed:19945726}.
CC Host nucleus {ECO:0000269|PubMed:19945726}.
CC -!- PTM: Phosphorylated by UL13; this phosphorylation regulates subsequent
CC phosphorylation of UL31 and UL34 by US3. Autophosphorylated (By
CC similarity). {ECO:0000250}.
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; X04798; CAA28489.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06710.1; -; Genomic_DNA.
DR PIR; B43674; B43674.
DR SMR; P13287; -.
DR PRIDE; P13287; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; 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:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0039525; P:modulation by virus of host chromatin organization; 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 Pfam; PF00069; Pkinase; 1.
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 cytoplasm; Host nucleus; Host-virus interaction; Kinase;
KW Modulation of host cell apoptosis by virus;
KW Modulation of host chromatin by virus; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..481
FT /note="Serine/threonine-protein kinase US3"
FT /id="PRO_0000086181"
FT DOMAIN 191..478
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 12..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 481 AA; 52678 MW; F6C217BE331F3680 CRC64;
MACRKFCGVY RRPDKRQEAS VPPETNTAPA FPASTFYTPA EDAYLAPGPP ETIHPSRPPS
PGEAARLCQL QEILAQMHSD EDYPIVDAAG AEEEDEADDD APDDVAYPED YAEGRFLSMV
SAAPLPGASG HPPVPGRAAP PDVRTCDTGK VGATGFTPEE LDTMDREALR AISRGCKPPS
TLAKLVTGLG FAIHGALIPG SEGCVFDSSH PNYPHRVIVK AGWYASTSHE ARLLRRLNHP
AILPLLDLHV VSGVTCLVLP KYHCDLYTYL SKRPSPLGHL QITAVSRQLL SAIDYVHCKG
IIHRDIKTEN IFINTPENIC LGDFGAACFV RGCRSSPFHY GIAGTIDTNA PEVLAGDPYT
QVIDIWSAGL VIFETAVHTA SLFSAPRDPE RRPCDNQIAR IIRQAQVHVD EFPTHAESRL
TAHYRSRAAG NNRPAWTRPA WTRYYKIHTD VEYLICKALT FDAALRPSAA ELLRLPLFHP
K
