US03_GAHVM
ID US03_GAHVM Reviewed; 402 AA.
AC Q9E6L8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein kinase US3 homolog;
DE EC=2.7.11.1;
GN Name=MDV092;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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}.
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; AF243438; AAG14266.1; -; Genomic_DNA.
DR RefSeq; YP_001034009.1; NC_002229.3.
DR SMR; Q9E6L8; -.
DR GeneID; 4811451; -.
DR KEGG; vg:4811451; -.
DR Proteomes; UP000008072; 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..402
FT /note="Protein kinase US3 homolog"
FT /id="PRO_0000406504"
FT DOMAIN 102..386
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 108..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 402 AA; 44691 MW; 94EB0A672EF6A8D3 CRC64;
MSSSPEAETM ECGISSSKVH DSKTNTTYGI IHNSINGTDT TLFDTFPDST DNAEVTGDVD
DVKTESSPES QSEDLSPFGN DGNESPETVT DIDAVSAVRM QYNIVSSLSP GSEGYIYVCT
KRGDNTKRKV IVKAVTGGKT LGSEIDILKK MSHRSIIRLV HAYRWKSTVC MVMPKYKCDL
FTYIDIMGPL PLNQIITIER GLLGALAYIH EKGIIHRDVK TENIFLDKPE NVVLGDFGAA
CKLDEHTDKP KCYGWSGTLE TNSPELLALD PYCTKTDIWS AGLVLFEMSV KNITFFGKQV
NGSGSQLRSI IRCLQVHPLE FPQNNSTNLC KHFKQYAIQL RHPYAIPQII RKSGMTMDLE
YAIAKMLTFD QEFRPSAQDI LMLPLFTKEP ADALYTITAA HM
