ID   UL52_HCMVM              Reviewed;         668 AA.
AC   Q6SW79; D2K3M0;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Packaging protein UL32 homolog;
GN   Name=UL52;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
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 {ECO:0000250}. Host nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC       {ECO:0000305}.
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DR   EMBL; AY446894; AAR31618.1; -; Genomic_DNA.
DR   RefSeq; YP_081511.1; NC_006273.2.
DR   SMR; Q6SW79; -.
DR   PRIDE; Q6SW79; -.
DR   DNASU; 3077432; -.
DR   GeneID; 3077432; -.
DR   KEGG; vg:3077432; -.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; 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..668
FT                   /note="Packaging protein UL32 homolog"
FT                   /id="PRO_0000418287"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..282
FT                   /note="Zinc finger 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   REGION          392..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..574
FT                   /note="Zinc finger 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         282
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ   SEQUENCE   668 AA;  74119 MW;  FB12353FE11C0E31 CRC64;
     MNPSTHVSSN GPTTPPHGPH TTFLPPTSPA PSTSSVAAAT LCSPQRQAVS RYSGWSTEYT
     QWHSDLTTEL LWHAHPRQVP MDEALAAAAA ASYQVNPQHP ANRYRHYEFQ TLSLGTSEVD
     ELLNCCAEET TCGGTQSTVL TNATNTTSCG GAVAGSSNAG PAGASAACDL DAELAGLETS
     AADFEQLRRL CAPLAIDTRC NLCAIISICL KQDCDQSWLL EYSLLCFKCS YAPRAALSTL
     IIMSEFTHLL QQHFSDLRID DLFRHHVLTV FDFHLHFFIN RCFEKQVGDA VDNENVTLNH
     LAVVRAMVMG EDTVPYNKPR RHPQQKQKNN PYHVEVPQEL IDNFLEHSSP SRDRFVQLLF
     YMWAGTGVMS TTPLTELTHT KFARLDALST ASEREDARMM MEEEEDEEGG EKGGDDPGRH
     NGGGTSGGFS ESTLKKNVGP IYLCPVPAFF TKNQTSTVCL LCELMACSYY DNVVLRELYR
     RVVSYCQNNV KMVDRIQLVL ADLLRECTSP LGAAHEDVAR CGLEAPTSPG GDSDYHGLSG
     VDGALARPDP VFCHVLRQAG VTGIYKHFFC DPQCAGNIRV TNEAVLFGHL HPHHVQEVKL
     AICHDNYYIS RLPRRVWLCI TLFKAFQITK RTYKGKVHLA DFMRDFTQLL ENCDIKLVDP
     TYVIDKYV