UL32_EBVB9
ID UL32_EBVB9 Reviewed; 525 AA.
AC P03184; Q777G8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Packaging protein UL32 homolog;
GN ORFNames=BFLF1;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998075; DOI=10.1016/0042-6822(85)90230-2;
RA Hudson G.S., Gibson T.J., Barrell B.G.;
RT "The BamHI F region of the B95-8 Epstein-Barr virus genome.";
RL Virology 147:99-109(1985).
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 -!- SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. Note=Mainly
CC cytoplasmic in transfected cell culture.
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; V01555; CAA24878.1; -; Genomic_DNA.
DR EMBL; M11923; AAA45867.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53398.1; -; Genomic_DNA.
DR PIR; E93065; QQBE6.
DR RefSeq; YP_401648.1; NC_007605.1.
DR PDB; 6XFA; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J=42-525.
DR PDBsum; 6XFA; -.
DR SMR; P03184; -.
DR PRIDE; P03184; -.
DR DNASU; 3783697; -.
DR GeneID; 3783697; -.
DR KEGG; vg:3783697; -.
DR Proteomes; UP000153037; 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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host nucleus; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..525
FT /note="Packaging protein UL32 homolog"
FT /id="PRO_0000116021"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..179
FT /note="Zinc finger 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 255..510
FT /note="Zinc finger 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 357..434
FT /note="Zinc finger 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ SEQUENCE 525 AA; 57912 MW; BF3D24F548D8A128 CRC64;
MAHKVTSANE PNPLTGKRLS SCPLTRSGVT EVAQIAGRTP KMEDFVPWTV DNLKSQFEAV
GLLMAHSYLP ANAEEGIAYP PLVHTYESLS PASTCRVCDL LDTLVNHSDA PVAFFEDYAL
LCYYCLNAPR AWISSLITGM DFLHILIKYF PMAGGLDSLF MPSRILAIDI QLHFYICRCF
LPVSSSDMIR NANLGYYKLE FLKSILTGQS PANFCFKSMW PRTTPTFLTL PGPRTCKDSQ
DVPGDVGRGL YTALCCHLPT RNRVQHPFLR AEKGGLSPEI TTKADYCGLL LGTWQGTDLL
GGPGHHAIGL NAEYSGDELA ELALAITRPE AGDHSQGPCL LAPMFGLRHK NASRTICPLC
ESLGAHPDAK DTLDRFKSLI LDSFGNNIKI LDRIVFLIKT QNTLLDVPCP RLRAWLQMCT
PQDFHKHLFC DPLCAINHSI TNPSVLFGQI YPPSFQAFKA ALAAGQNLEQ GVCDSLITLV
YIFKSTQVAR VGKTILVDVT KELDVVLRIH GLDLVQSYQT SQVYV
