US03_SUHVN
ID US03_SUHVN Reviewed; 390 AA.
AC P24381; Q69397;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Serine/threonine-protein kinase US3 homolog;
DE EC=2.7.11.1;
GN Name=PK;
OS Suid herpesvirus 1 (strain NIA-3) (SuHV-1) (Pseudorabies virus (strain
OS NIA-3)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10349;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167928; DOI=10.1099/0022-1317-71-8-1747;
RA van Zijl M., van der Gulden H., de Wind N., Gielkens A., Berns A.;
RT "Identification of two genes in the unique short region of pseudorabies
RT virus; comparison with herpes simplex virus and varicella-zoster virus.";
RL J. Gen. Virol. 71:1747-1755(1990).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P24381-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P24381-2; Sequence=VSP_018838;
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 -!- MISCELLANEOUS: [Isoform Short]: Major isoform (95%). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01243.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D10451; BAA01242.1; -; Genomic_DNA.
DR EMBL; D10451; BAA01243.1; ALT_INIT; Genomic_DNA.
DR SMR; P24381; -.
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 Alternative initiation; ATP-binding; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Kinase; 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..390
FT /note="Serine/threonine-protein kinase US3 homolog"
FT /id="PRO_0000024340"
FT DOMAIN 109..389
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018838"
SQ SEQUENCE 390 AA; 43023 MW; 50FB66E50F45EDA4 CRC64;
MLAMWRWVTK RSRLRRGHAH LGGNKGVRGI CSLYLAGLSR GLSRVHAQRS HAATMADAGI
PDEILYSDIS DDEIIIDGDG DGDSSGDEDD DDGGLTRQAA SRIATDLGFE VLQPLQSGSE
GRVFVARRPG EADTVVLKVG QKPSTLMEGM LLKRLAHDNV MSLKQMLARG PVTCLVLPHF
RCDLYSYLTM RDGPLDMRDA GRVIRSVLRG LAYLHGMRIM HRDVKAENIF LEDVDTVCLG
DLGAARCNVA APNFYGLAGT IETNAPEVLA RDRYDTKVDV WGAGVVLFET LAYPKTIAGG
DEPAINGEMH LIDLIRALGV HPEEFPPDTR LRSEFVRYAG THRQPYTQYA RVARLGLPET
GAFLIYKMLT FDPVRRPSAD EILNFGMWTV
