US03_EHV1V
ID US03_EHV1V Reviewed; 382 AA.
AC P84390; Q6S6W2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE EC=2.7.11.1;
GN OrderedLocusNames=69;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45957.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000250|UniProtKB:P28926};
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; Evidence={ECO:0000250|UniProtKB:P28926};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by protein 49; this phosphorylation regulates
CC subsequent phosphorylation of proteins 27 and 29 by US3 homolog.
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; AY464052; AAS45957.1; -; Genomic_DNA.
DR RefSeq; YP_053113.1; NC_001491.2.
DR SMR; P84390; -.
DR GeneID; 2948581; -.
DR KEGG; vg:2948581; -.
DR Proteomes; UP000008296; 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 Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..382
FT /note="Serine/threonine-protein kinase US3 homolog"
FT /id="PRO_0000086179"
FT DOMAIN 93..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28926,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28926,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28926,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 382 AA; 42543 MW; DFB3F4F1A75731C9 CRC64;
MENKQCDHLT DWFSTTSDAS ESMDTTPPLP PPTPSVDPSY SGAAADEDLY SDISEGDLEY
SDCDSASESD EDDDDCLIPS KEKAREVAAS FGYTVIKTLT PGSEGRVMVA TKDGQPEPVV
LKIGQKGTTL IEAMMLRNVN HPSVIQMKDT LVSGAITCMV LPHYSSDLYT FLTKESRRIP
IDQALIIEKQ ILEGLRYLHA QRIIHRDVKT ENIFINSVDQ VCIADFGAAQ FPVVEPADLG
LAGTVETNAP EVLARAKYNS KADIWSAGIV LFEMLAYPST LFEDPPSTPE EYVKSCHSQL
LKIISTLKIN PEEFPRDPGS RLVRGYIEYS RLERKPYTRY PCFQRVNLHI DGEFLVHKML
AFNAAMRPSA EELLSYPMFA QL
