ID   UL32_EHV1B              Reviewed;         620 AA.
AC   P69329; P28952; Q6S6P3;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Packaging protein UL32 homolog;
GN   OrderedLocusNames=28;
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: 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. Note=Mainly
CC       cytoplasmic in transfected cell culture. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be an envelope glycoprotein.
CC       {ECO:0000305}.
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DR   EMBL; AY665713; AAT67285.1; -; Genomic_DNA.
DR   PIR; B36798; WZBEC1.
DR   RefSeq; YP_053073.1; NC_001491.2.
DR   SMR; P69329; -.
DR   GeneID; 1487568; -.
DR   KEGG; vg:1487568; -.
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: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..620
FT                   /note="Packaging protein UL32 homolog"
FT                   /id="PRO_0000116016"
FT   REGION          100..186
FT                   /note="Zinc finger 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          306..605
FT                   /note="Zinc finger 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          433..525
FT                   /note="Zinc finger 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         518
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         525
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         605
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ   SEQUENCE   620 AA;  67301 MW;  C475E85B2EA1C667 CRC64;
     MAASCNLDVI GEDGGCALTG GWQPGAFERP YMGFDARLLS TNSSLCSELI FSAHLMQISP
     TPQPREQVDV CEDPDNDPPE PSCAQFVDAV ADSLALDKLC LICRTIDLYR RQFGLSPQWI
     ADYAMLCTKT LAAPPCAVAT VVAAFEFVYL MDKHYLRRGK TTLVGAFARR VLTLVDIQRH
     FFLHVCFRTD GGVPRCAASG TAPAATAMAG LGMADKVQYS NYSFLVQSST RAMLLTVADV
     PSGDDGALQA VPHGRHGAGR PADGGGGVFG PKQQSTVAAL MSWKECAKMI DCSGSERRRP
     GATMTCCERA RADDDEYERQ LLSTENTYLG SADNQAEGGN DTHLKWGYAD LTLLLLSQSS
     TWEASEKTSL ASQSRRACVE EYWASHRTVL ARDTAPRFAR FVDADAVPDT ATGPVLATTL
     KHVRSRGRTC AECVLCNLIL TREHWLALRR FKRDVISYSS NNANLFDCIS PVLSALSDAN
     SEPLAGDCGV GGGGTCPEDS GRFLELMHAA GTEAIYKHLF CDPMCALVEL QTNPSVLFSP
     IGPPPEPDEI ELQKARLASE NWFSGRVCAG LWALAFTFKT YQIFTPKPTA CAAFIKDAGL
     LLRRHNLPLI SLEHTLCNYV