ICP27_HHV7J
ID ICP27_HHV7J Reviewed; 526 AA.
AC P52355;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=mRNA export factor ICP27 homolog;
GN ORFNames=U42;
OS Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
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}.
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DR EMBL; U43400; AAC54704.1; -; Genomic_DNA.
DR PIR; T41944; T41944.
DR Proteomes; UP000009246; 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: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; Reference proteome;
KW Transcription; Transcription regulation; Virion; Virion tegument; Zinc;
KW Zinc-finger.
FT CHAIN 1..526
FT /note="mRNA export factor ICP27 homolog"
FT /id="PRO_0000115830"
FT ZN_FING 239..351
FT /note="CHC2-type"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10238"
SQ SEQUENCE 526 AA; 61754 MW; 693C4B33FCD34A24 CRC64;
MNKVLIFDRN MYPRGVKKNV LGRQRYGLKT IKRTLVHKPA NKYVSRFTKQ FHRRIIPIKQ
LDESKLDALS LRELEQLKLI IEEKQEEKRA QTHALTFFAN LPTAPFGSSY TAEALGLRKY
SGEARDPAHR IRDRFPRNHE KIYLEKEELM TTDLLLRYKN CLNSLNREQH QQILGDRVFS
LTNSPSLAFS LAIIEEACIY YKYHFVHNLP IDPQDLFMYT ITIMKFEYFN KLNMAKLCCV
FNDNGHGDIE YRIFRQLCGK PVYDRDMPNT EYEVQQQTPG SFQYPAQQAL SFIVTFARIL
RQIKERILQT KQPQFIRDFD QDRVSEQYQC GMISRLVGDQ FNNHQCDDIG CQTRIQRMMS
PWKPSLYFCT YLPKEFVEFG LHPNMPEEYN SFNVACSTTP SCSFASQQSK QTVQLNLQTK
KQAKCKKLLT ADKTNKGQKT NELRENRLKK DWSKEVDSID FETNTTLQED ETRFVFIEND
TSMKSAKIKE NNGEENSDNE MELDLDYEDV ETCETDINDT DSDDSD