ID   ICP27_ELHVK             Reviewed;         659 AA.
AC   Q18LF8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=mRNA export factor ICP27 homolog;
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
CC   -!- FUNCTION: Immediate early (EI) protein that plays many roles during
CC       productive infection including regulation of viral gene expression and
CC       nuclear export of intronless viral RNAs. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250}. Virion
CC       {ECO:0000250}. Host nucleus. Host cytoplasm. Note=Shuttles between host
CC       nucleus and cytoplasm.
CC   -!- SIMILARITY: Belongs to the HHV-1 ICP27 protein family. {ECO:0000305}.
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; AF322977; ABG36561.1; -; Genomic_DNA.
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:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion 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   Host cytoplasm; Host nucleus; Metal-binding; Transcription;
KW   Transcription regulation; Virion; Virion tegument; Zinc; Zinc-finger.
FT   CHAIN           1..659
FT                   /note="mRNA export factor ICP27 homolog"
FT                   /id="PRO_0000408180"
FT   ZN_FING         130..273
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   REGION          317..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..659
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P10238"
SQ   SEQUENCE   659 AA;  71941 MW;  6566387C38EBC220 CRC64;
     MESGRRPIVP YTGPVPDVKK LLTENRFARL ADLVVPLEVL GETDFVRHIH AQFENLSRDE
     MDELVLARTV AINSAPSLFS ILLMAEETCS YFSAIDRLDI PVNPYDPYAS TLSALKHATF
     SKLNVAKLSC MMSNGERPPS ASSDYDFLKK IASGNGATVK SFSRSSESTV APFPAATKQV
     PDISDIREFD FETFRHPFQK VICFLATIEK VISEIKGHRA PGCIAGGPIN PKDRSRYIRD
     YDKQGIMRRY KDGCIIGLVK QGFCEHACND NACRRRCKFA LSVPYNLGMV FCPPTENSSV
     EDMDAYFERN RCPTRNGSFD DSRSATSGDG SSCSSAHKVT TPTDGVMMPE FPFSDQTDTS
     NNGTVRFSER RVSSSSKHRR RSNKHISPLD RPNDYHYQKN QPTPSDEKRY YHGSGSSSTE
     AVSTASAPLT GSAANQHPQH CGGQSGSDTG VISRGEGRHH GSHNGIPDFV SRSPVTTPPE
     VFSPERRSSE ERSSSDQRRK SPLSRSASAT SGGSKRRSFV DSPPRHESED EDEDSDSSSS
     EAQKDRFKKR SGSRSNTPPS SPSKPDSAPA ASASPGGDGG NDSDDGATEK GVTSNAKESV
     RVSERFETGD KSPTFIETED ESDDEDDQMS ITSYDHSESS SAESGSETDG EDGESDMTL