UL52_HCMVA
ID UL52_HCMVA Reviewed; 668 AA.
AC P16793; Q7M6N1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Packaging protein UL32 homolog;
DE AltName: Full=Protein HFRF1;
GN Name=UL52;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029980; DOI=10.1016/0042-6822(87)90282-0;
RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P.,
RA Barrell B.G.;
RT "Large-scale rearrangement of homologous regions in the genomes of HCMV and
RT EBV.";
RL Virology 157:397-413(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18077717; DOI=10.1128/jvi.01967-07;
RA Borst E.M., Wagner K., Binz A., Sodeik B., Messerle M.;
RT "The essential human cytomegalovirus gene UL52 is required for cleavage-
RT packaging of the viral genome.";
RL J. Virol. 82:2065-2078(2008).
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.
CC {ECO:0000269|PubMed:18077717}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:18077717}.
CC Host nucleus {ECO:0000269|PubMed:18077717}.
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; M17209; AAA46006.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35411.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00157.1; -; Genomic_DNA.
DR PIR; S09815; QQBEW1.
DR SMR; P16793; -.
DR PRIDE; P16793; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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_0000116022"
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 401..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; 74121 MW; 29F675F40F3ED818 CRC64;
MNPSTHVSSN GPTTPPHGPH TTFLPPTSPA PSTSSVAAAT LCSPQRQAVS RYSGWSTEYT
QWHSDLTTEL LWHAHPRQVP MDEALAAAAA ASYQVNPQHP ANRYRHYEFQ TLSLGTSEVD
ELLNCCAEET TCGGTQSTVL TNATNTTSCG GAVAGSSNVG PAGASAACDL DAELAGLETS
AADFEQLRRL CAPLAIDTRC NLCAIISICL KQDCDQSWLL EYSLLCFKCS YAPRAALSTL
IIMSEFTHLL QQHFSDLRID DLFRHHVLTV FDFHLHFFIN RCFEKQVGDA VDNENVTLNH
LAVVRAMVMG EDTVPYNKPR RHPQQKQKNN PYHVEVPQEL IDNFLEHSSP SRDRFVQLLF
YMWAGTGVMS TTPLTELTHT KFARLDALST ASEREDARMM IEEEEDEEGG EKGGDDPGRH
NGGGTSGGFS ESTLKKNVGP IYLCPVPAFF TKNQTSTVCL LCELMACSYY DNVVLRELYR
RVVSYCQNNV KMVDRIQLVL ADLLRECTSP LGAAHEDVAR CGLEAPTSPG GDSDYHGLSG
VDGALARPDP VFCHVLRQAG VTGIYKHFFC DPQCAGNIRV TNEAVLFGRL HPHHVQEVKL
AICHDNYYIS RLPRRVWLCI TLFKAFQITK RTYKGKVHLA DFMRDFTQLL ESCDIKLVDP
TYVIDKYV
