ID   UL32_HHV6U              Reviewed;         484 AA.
AC   P52463; Q69059;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Packaging protein UL32;
GN   Name=U36; Synonyms=XIRF1;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8289364; DOI=10.1128/jvi.68.2.597-610.1994;
RA   Nicholas J., Martin M.E.D.;
RT   "Nucleotide sequence analysis of a 38.5-kilobase-pair region of the genome
RT   of human herpesvirus 6 encoding human cytomegalovirus immediate-early gene
RT   homologs and transactivating functions.";
RL   J. Virol. 68:597-610(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA16743.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L25528; AAA16743.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X83413; CAA58416.1; -; Genomic_DNA.
DR   PIR; T09330; T09330.
DR   RefSeq; NP_042929.1; NC_001664.2.
DR   SMR; P52463; -.
DR   PRIDE; P52463; -.
DR   DNASU; 1487914; -.
DR   GeneID; 1487914; -.
DR   KEGG; vg:1487914; -.
DR   Proteomes; UP000009295; 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; 2.
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..484
FT                   /note="Packaging protein UL32"
FT                   /id="PRO_0000116017"
FT   REGION          74..154
FT                   /note="Zinc finger 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          286..390
FT                   /note="Zinc finger 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ   SEQUENCE   484 AA;  56407 MW;  A4D43C75A3DEF4DA CRC64;
     MYKGWDSEAL PIQSEILNEI LLYCYLTPQP PIPSETTTAT SPTNIENEIS NLDNSENLEE
     LKQLSVALNI DRRCNICSIV NLCLKQNKSW IYDYSLLCYK CNYAPKTPLS LLIVSTEFLM
     LIRERFPNIN FDGLFLNNIV SIFDFHVHFF IHRCFANTVN DHIQSENITL NHMAIIRSTL
     LKEDTIPHIK IKKFLTKKMN PKKTQSSELN KKLTVPMKTR FTTLLFYMWS GTNVFDRVPF
     TDLTIRKHRF IKNLYSNKTD IELTAGPILL AQIPFSITKN KTTSVCLLCE LMAASKQDYL
     FLKYLHQSIM DYCQNNLKMI DRVQFVIADI FEKTKIHTHV KNLSDYSKAI FDNEFSFSDD
     NFTLDTHVYL ILRQTGTVGV YKHFFCDPLC LANCKTINPE VLFNTTDAGE IQDLKVTICY
     RNEYLSIVEK HVWLAIHLFK AFQIIKPNHK NKTQITEFLK DFTNLLALHH FDIVDPIFTV
     NYYV