US03_PSHV1
ID US03_PSHV1 Reviewed; 492 AA.
AC Q6UDG0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein kinase US3 homolog;
DE EC=2.7.11.1;
GN Name=US3;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
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; AY372243; AAQ73750.1; -; Genomic_DNA.
DR RefSeq; NP_944444.1; NC_005264.1.
DR SMR; Q6UDG0; -.
DR GeneID; 2656972; -.
DR KEGG; vg:2656972; -.
DR Proteomes; UP000006840; 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..492
FT /note="Protein kinase US3 homolog"
FT /id="PRO_0000406801"
FT DOMAIN 147..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 99..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 153..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 492 AA; 55381 MW; 619AD48D2507EF32 CRC64;
MTRKRFLCPS VCRSRAARTG ESKRRRLHSH DRRRCAITPD FDEDGRMAHI ANPRPNPLEC
AEASQKVIMA PSRSDTTGAH RCLEDAAPVG ELLVPRSSAD LHESQRGQPS GATDSQASTL
ETESAPPSAD SSSSAKLQRD DEFLAKYRVI GTLPAGSFGK ILVCALRASV GEAEASRVPR
SERRVAKRVR ATSRLAIYLE NEILALQYMN HENILKVEEV LRSEAYTYMI TRKYDYDLYS
FMYDGDLQWK DRPLLWQTRA IMKQLLCAVE YMHDKLLMHR DIKLENVFLN GDGTIVLGDL
GTAMTFEKPR VARDYGWVGT VTTNSPEMLA GDGYCEITDL WSCGLIMLDM LSKDLLPLNG
NTKKPGKQLR RIIRSLSVCD EEFPDPPCKL FDYIDSAEYT HTPMSVPPLI RRMGLPADFE
YPLVKMLTFD WHRRPGASEL LALPLFSSTI TEERLFVWGL KSGAAHFSSW KPACRIESDT
AALSLTMSDD DE
