US03_GAHVG
ID US03_GAHVG Reviewed; 402 AA.
AC Q05101;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE EC=2.7.11.1;
GN Name=US1206; Synonyms=US3;
OS Gallid herpesvirus 2 (strain GA) (GaHV-2) (Marek's disease herpesvirus type
OS 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10388;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1282282; DOI=10.1007/bf01703085;
RA Sakaguchi M., Urakawa T., Hirayama Y., Miki N., Yamamoto M., Hirai K.;
RT "Sequence determination and genetic content of an 8.9-kb restriction
RT fragment in the short unique region and the internal inverted repeat of
RT Marek's disease virus type 1 DNA.";
RL Virus Genes 6:365-378(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7831788; DOI=10.1016/s0042-6822(95)80048-4;
RA Brunovskis P., Velicer L.F.;
RT "The Marek's disease virus (MDV) unique short region: alphaherpesvirus-
RT homologous, fowlpox virus-homologous, and MDV-specific genes.";
RL Virology 206:324-338(1995).
RN [3]
RP FUNCTION.
RX PubMed=15767401; DOI=10.1128/jvi.79.7.3987-3997.2005;
RA Schumacher D., Tischer B.K., Trapp S., Osterrieder N.;
RT "The protein encoded by the US3 orthologue of Marek's disease virus is
RT required for efficient de-envelopment of perinuclear virions and involved
RT in actin stress fiber breakdown.";
RL J. Virol. 79:3987-3997(2005).
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 ECO:0000269|PubMed:15767401}.
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; M80595; AAB59895.1; -; Genomic_DNA.
DR EMBL; L22174; AAA64965.1; -; Genomic_DNA.
DR SMR; Q05101; -.
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..402
FT /note="Serine/threonine-protein kinase US3 homolog"
FT /id="PRO_0000086776"
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 110..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 402 AA; 44715 MW; 93E29494B3572C7B CRC64;
MSSTPEAETM ECGISSSKVH DSKTNTTYGI IHNSINGTDT TLFDTFPDST DNAEVTGDVD
DVKTESSPES QSEDLSPFGN DGNESPETVT DIDAVSAVRM QYNIVSSLPP 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
