ID   UL32_HHV2H              Reviewed;         598 AA.
AC   P89455;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Packaging protein UL32;
GN   Name=UL32;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
CC   -!- FUNCTION: Plays a role in efficient localization of neo-synthesized
CC       capsids to nuclear replication compartments, thereby controlling
CC       cleavage and packaging of virus genomic DNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC       {ECO:0000305}.
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DR   EMBL; Z86099; CAB06757.1; -; Genomic_DNA.
DR   SMR; P89455; -.
DR   PRIDE; P89455; -.
DR   Proteomes; UP000001874; 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:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002597; Herpes_env.
DR   Pfam; PF01673; Herpes_env; 1.
DR   PROSITE; PS51988; HERPESVIRUS_UL32; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host nucleus; Metal-binding; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..598
FT                   /note="Packaging protein UL32"
FT                   /id="PRO_0000406180"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..214
FT                   /note="Zinc finger 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          310..583
FT                   /note="Zinc finger 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          425..504
FT                   /note="Zinc finger 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         546
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         583
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ   SEQUENCE   598 AA;  64020 MW;  89BBAD9B65216669 CRC64;
     MATSAPGVPS SAAVREESPG SSWKEGAFER PYVAFDPDLL ALNEALCAEL LAACHVVGVP
     PASALDEDVE SDVAPAPPRP RGAAREASGG RGPGSARGPP ADPTAEGLLD TGPFAAASVD
     TFALDRPCLV CRTIELYKQA YRLSPQWVAD YAFLCAKCLG APHCAASIFV AAFEFVYVMD
     HHFLRTKKAT LVGSFARFAL TINDIHRHFF LHCCFRTDGG VPGRHAQKQP RPTPSPGAAK
     VQYSNYSFLA QSATRALIGT LASGGDDGAG AGAGGGSGTQ PSLTTALMNW KDCARLLDCT
     EGKRGGGDSC CTRAAARNGE FEAAAGALAQ GGEPETWAYA DLILLLLAGT PAVWESGPRL
     RAAADARRAA VSESWEAHRG ARMRDAAPRF AQFAEPQPQP DLDLGPLMAT VLKHGRGRGR
     TGGECLLCNL LLVRAYWLAM RRLRASVVRY SENNTSLFDC IVPVVDQLEA DPEAQPGDGG
     RFVSLLRAAG PEAIFKHMFC DPMCAITEME VDPWVLFGHP RADHRDELQL HKAKLACGNE
     FEGRVCIALR ALIYTFKTYQ VFVPKPTALA TFVREAGALL RRHSISLLSL EHTLCTYV