ID   ICP27_EBVA8             Reviewed;         479 AA.
AC   Q1HVH2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=mRNA export factor ICP27 homolog;
DE   AltName: Full=Mta;
DE   AltName: Full=ORF57 protein homolog;
DE   AltName: Full=Protein SM;
GN   ORFNames=BMLF1;
GN   and
GN   ORFNames=BSLF2;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA   Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT   "The genome of Epstein-Barr virus type 2 strain AG876.";
RL   Virology 350:164-170(2006).
CC   -!- FUNCTION: Promotes the nuclear export of a subset of early and late
CC       viral mRNAs by interacting with intronless mRNAs and cellular export
CC       proteins. Additionally may prevent the establishment of cellular
CC       antiviral state, by acting as an alternative splicing factor for
CC       cellular RNAs such as STAT1, resulting in a STAT1 mRNA incapable of
CC       producing the STAT1alpha isoform (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with host XPO1 and with the XPO1 export pathway
CC       components small GTPase RAN and nucleoporin NUP214. Interacts with host
CC       SPEN, OTT1 and OTT3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=shuttles
CC       between the nucleus and the cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: Binds viral intronless RNAs. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by cellular protein kinase CK2.
CC   -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR   EMBL; DQ279927; ABB89236.1; -; Genomic_DNA.
DR   RefSeq; YP_001129456.1; NC_009334.1.
DR   SMR; Q1HVH2; -.
DR   PRIDE; Q1HVH2; -.
DR   GeneID; 5176227; -.
DR   KEGG; vg:5176227; -.
DR   Proteomes; UP000007639; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR008648; ICP27-like.
DR   Pfam; PF05459; Herpes_UL69; 1.
PE   3: Inferred from homology;
KW   Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host PKR by virus; Metal-binding; mRNA transport;
KW   Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation; Transport; Viral immunoevasion; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..479
FT                   /note="mRNA export factor ICP27 homolog"
FT                   /id="PRO_0000375953"
FT   ZN_FING         354..454
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         445
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
SQ   SEQUENCE   479 AA;  53540 MW;  4DA16F8CC06BD53E CRC64;
     MVPSQRLSRT SSISSNEDPA ESHILELEAV SDTNTDCDMD PMEGSEEHST DGEISSSEEE
     DEDPTPAHTI PARPSSVVIT PTSASFVIPR KKWDLQDKTV TLHRSPLCRD EDEKEETGNS
     SYTRGHKRRR GEVHGCTDES YGKRRHLPPG ARAPRAPRAP RVPRAPRSPR APRSNRATRG
     PRSESRGAGR STRKQARQER SQRPLPNKPW FDMSLVKPVS KITFVTLPSP LASLTLEPIQ
     DPFLQSMLAV AAHPEIGAWQ KVQPRHELRR SYKTLREFFT KSTNKDTWLD ARMQAIQNAG
     LCTLVAMLEE TIFWLQEITY HGDLPLAPAE DILLACAMSL SKVILTKLKE LAPCFLPNTR
     DYNFVKQLFY ITCATARQNK VVETLSSSYV KQPLCLLAAY AAVAPAYINA NCRRRHDEVE
     FLGHYIKNYN PGTLSSLLTE AVETHTRDCR SASCSRLVRA ILSPGTGSLG LFFVPGLNQ