US03_EHV1B
ID US03_EHV1B Reviewed; 382 AA.
AC P28926; Q6S6W2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE EC=2.7.11.1;
GN OrderedLocusNames=69;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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 protein 26 and 29, two critical regulators of capsid
CC budding from nucleus to endoplasmic reticulum, thereby facilitating
CC virion egress. Modulates and redistributes host components of the
CC nuclear envelope, including LMNA, emerin/EMD and the nuclear matrix
CC protein MATR3. Phosphorylates envelope glycoprotein B (gB), probably to
CC direct 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:0000250}. Host nucleus
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by protein 49; this phosphorylation regulates
CC subsequent phosphorylation of proteins 26 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY665713; AAT67326.1; -; Genomic_DNA.
DR PIR; F36802; TVBEG1.
DR RefSeq; YP_053113.1; NC_001491.2.
DR SMR; P28926; -.
DR GeneID; 2948581; -.
DR KEGG; vg:2948581; -.
DR Proteomes; UP000001189; 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..382
FT /note="Serine/threonine-protein kinase US3 homolog"
FT /id="PRO_0000086177"
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:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
