ID   US03_CHV9D              Reviewed;         345 AA.
AC   Q04543;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE            EC=2.7.11.1;
GN   Name=US2;
OS   Cercopithecine herpesvirus 9 (strain DHV) (CeHV-9) (Simian varicella
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=36348;
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8384754; DOI=10.1006/viro.1993.1185;
RA   Fletcher T.M. III, Gray W.L.;
RT   "DNA sequence and genetic organization of the unique short (US) region of
RT   the simian varicella virus genome.";
RL   Virology 193:762-773(1993).
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 homologs, two critical regulators of
CC       capsid budding from nucleus to endoplasmic reticulum, thereby
CC       facilitating virion egress. Modulates and redistributes host components
CC       of the nuclear envelope, including LMNA, emerin/EMD and the nuclear
CC       matrix protein MATR3. Phosphorylates envelope glycoprotein B (gB),
CC       probably to direct it to the cell surface. Promotes virus intracellular
CC       spread by restructuring host cell cytoskeleton. Blocks host apoptosis
CC       to extend cell survival and allow efficient viral replication. Promotes
CC       viral gene expression by phosphorylating host HDAC2 to reduce viral
CC       genome 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:0000250}. Host nucleus
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by UL13 homolog; this phosphorylation regulates
CC       subsequent phosphorylation of UL31 and UL34 homologs by US3.
CC       Autophosphorylated (By 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; L07067; AAA47887.1; -; Genomic_DNA.
DR   PIR; B46113; B46113.
DR   SMR; Q04543; -.
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   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..345
FT                   /note="Serine/threonine-protein kinase US3 homolog"
FT                   /id="PRO_0000086176"
FT   DOMAIN          49..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         55..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   345 AA;  38954 MW;  5379B30FC13781ED CRC64;
     MNYDDDCLYE DKHMDTDIYD MLADEDTSDV DNTLAVCATA RAGIEKAGFS VLETFTPGAE
     GFTFACIENK TRENVVIKAG QRGGTVTEAH ILRNINHPVI IRLMGTFTYN SFTCLVLPRY
     KTDLYCYLSD RRRIAICDML SIERSVLRAI QYLHENRIIH RDVKAENIFI NHPGDVCLGD
     FGAACYPVDI TQNKYYGWAG TIATNAPELL ARDPYGPAVD IWSAGIVLFE MATCHDSLFE
     KDGLDGDCDS DRQIKLIIRR TGVHPSEFPI DAQATLDEIY RTCQKTSRKP GTRPTWTNLY
     ELPLELEYLI CKMLAFDAHK RPSAKALLDF AAFYDIPDPY PNPTN