UL32_HHV6Z
ID UL32_HHV6Z Reviewed; 484 AA.
AC Q9QJ33;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Packaging protein UL32 homolog;
GN Name=U36;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z29;
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
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}.
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DR EMBL; AF157706; AAD49650.1; -; Genomic_DNA.
DR RefSeq; NP_050217.1; NC_000898.1.
DR SMR; Q9QJ33; -.
DR PRIDE; Q9QJ33; -.
DR DNASU; 1497038; -.
DR GeneID; 1497038; -.
DR KEGG; vg:1497038; -.
DR Proteomes; UP000006930; 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 homolog"
FT /id="PRO_0000408436"
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; 56379 MW; 24C06E5251A3FF55 CRC64;
MYKGWDSEAL SIQSEIVNEI LLYCYLTPQP PIPSETTTAT SPTNIENEIS NLESSENLEE
LKRLSVALNI DRRCNICSIV NLCLKQNKSW IYDYSLLCYK CNYAPKTPLS LLIVSAEFIM
LIRERFPNIN FDGLFQNNIV SIFDFHVHFF IHRCFANTVN DHIQSENITL NHMAIIRSTL
LKEDSIPHIK IKKFLTKKMN PKKTQSPELN KKLTVPMKTR FTTLLFYMWS GTNVFDRVPF
TDLTIRKHRF IKNLYSNKTD IELTAGPILL AQIPFSITKN KTTSVCLLCE LMAASKQDYL
FLKYLHQSIM DYCQNNLKMI DRVQFVIADI FEKTKIHMHV KNLSDYSKAI FDNEFSFSDD
NFTLDTHVYL ILRQTGTVGV YKHFFCDPLC LANCKTINPE VLFNTTDAGE IQDLKVTICY
RNEYLSIVEK HVWLAIHLFK AFQIIKPNHK NKTQIAEFLK DFTNLLALHH FDIVDPIFTV
NYYV