ID   ICP27_EHV1B             Reviewed;         470 AA.
AC   P28939; Q6DLK6;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=mRNA export factor ICP27 homolog;
DE   AltName: Full=Transcriptional regulator IE63 homolog;
GN   ORFNames=5;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
CC   -!- FUNCTION: Multifunctional regulator of the expression of viral genes
CC       that mediates nuclear export of viral intronless mRNAs. This immediate
CC       early (EI) protein promotes the nuclear export of viral intronless
CC       mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Homodimerization is required for transactivation.
CC       Associates in a complex with RNA, and host export factors NXF1/TAP and
CC       ALYREF; these interactions allow nuclear export of viral transcripts.
CC       Interacts with three host shuttling SR proteins SRSF1, SRSF3 and SRSF7.
CC       Interacts with host SRPK1. Interacts with IE62; this interaction
CC       enhances IE62 transactivation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC       {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm.
CC       {ECO:0000250}.
CC   -!- DOMAIN: Binds viral intronless RNAs and SR proteins through the Arg-
CC       rich region. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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DR   EMBL; AY665713; AAT67262.1; -; Genomic_DNA.
DR   PIR; F36795; WZBEA4.
DR   RefSeq; YP_053050.1; NC_001491.2.
DR   SMR; P28939; -.
DR   GeneID; 1487550; -.
DR   KEGG; vg:1487550; -.
DR   Proteomes; UP000001189; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR008648; ICP27-like.
DR   Pfam; PF05459; Herpes_UL69; 1.
PE   3: Inferred from homology;
KW   Activator; Early protein; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Metal-binding; Reference proteome; RNA-binding;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..470
FT                   /note="mRNA export factor ICP27 homolog"
FT                   /id="PRO_0000115826"
FT   ZN_FING         359..446
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
SQ   SEQUENCE   470 AA;  51321 MW;  99AC5258EFB74B0E CRC64;
     MALSSVSSCE PMEDEMSIMG SDTEDNFTGG DTCAEATRGL VNKSAFVPTQ TVGTVSALRN
     VVGDPPKSVV VSFSASPQRA QPSNPKSERP AFGHGRRNRR RPFRRNNWKQ QQRGWEKPEP
     ENVPARQSAG SWPKRSSLPV HMRLGQRGGD SSSADSGHGG AGPSDRWRFK TRTQSVARVH
     RNRRRGNANH GSNTPGRSAG DRLNAAAASS IADVCRRVTS SRIGEMFHGA RETLTTPVKN
     GGFRAENSSP WAPVLGFGSD QFNPEARRIT WDTLVEHGVN LYKLFEVRSH AAEAARSLRD
     AVMRGENLLE ALASADETLS WCKMIVTKNL PMRTRDPIIS SSVALLDNLR LKLEPFMRCY
     LSSSGSPTLA ELCDHQRLSD VACVPTFMFV MLARIARAVG SGAETVSRDA LGPDGRVLAD
     YVPGACLAGT LEAIDAHKRR CKADTCSLVS AYTLVPVYLH GKYFYCNQIF