US03_BHV1S
ID US03_BHV1S Reviewed; 467 AA.
AC Q08097;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE EC=2.7.11.1;
OS Bovine herpesvirus 1.2 (strain ST) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=45407;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8122370; DOI=10.1006/viro.1994.1139;
RA Leung-Tack P., Audonnet J.F., Riviere M.;
RT "The complete DNA sequence and the genetic organization of the short unique
RT region (US) of the bovine herpesvirus type 1 (ST strain).";
RL Virology 199:409-421(1994).
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; Z23068; CAA80602.1; -; Genomic_DNA.
DR PIR; S35782; S35782.
DR SMR; Q08097; -.
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..467
FT /note="Serine/threonine-protein kinase US3 homolog"
FT /id="PRO_0000086175"
FT DOMAIN 164..462
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 64..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 170..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 467 AA; 49886 MW; 57359A4C95A89904 CRC64;
MERAAERLAR QRARGLWRSR FACCVAAEPS GSRLGQSVRG AAAAPARCAA EGSADLYLAV
NNEGPEVAPP ARTGPPDADG IEGGAAVAGN EQGGVAAGNE RRAATGDEKE SASGGENESE
SESESESESE SGADDGDWDD DDDAGPAGGV TREEAEGAAR ALNFRIIRRL TPGSEGRVFE
ATGPAPAQEH VVLKIGASAS TLAEAMLLRT LDHANVVKLK AVLFHGELVC AVLARYREDL
HTHLWKIDRP MALPTALQVT RAVLQGLAYL HSRRIAHRDV KTENVFLNGP GDVCLGDFGA
AHGPVTEPRY YGLAGTLETN SPELLARARY DCRTDVWSAG VVAYEMLAYP RALFDSPAGP
QGEDAEASGP PTILGDRDCA RQLLRVIRRL AVHAEEFPPS PTDRLTRNFK RHAATGREPH
SPYRCLAVLR LPCDADRLLH QMLTFDFRAR PTAAELLEHP VFGAASG
