UL32_HHV8P
ID UL32_HHV8P Reviewed; 467 AA.
AC F5HF47;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Packaging protein UL32 homolog;
GN Name=ORF68;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29875246; DOI=10.1128/jvi.00840-18;
RA Gardner M.R., Glaunsinger B.A.;
RT "Kaposi's Sarcoma-Associated Herpesvirus ORF68 Is a DNA Binding Protein
RT Required for Viral Genome Cleavage and Packaging.";
RL J. Virol. 92:0-0(2018).
RN [4]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-52; CYS-373; CYS-415 AND HIS-452, AND
RP ZINC-FINGER.
RX PubMed=33554858; DOI=10.7554/elife.62261;
RA Didychuk A.L., Gates S.N., Gardner M.R., Strong L.M., Martin A.,
RA Glaunsinger B.A.;
RT "A pentameric protein ring with novel architecture is required for
RT herpesviral packaging.";
RL Elife 10:0-0(2021).
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 (PubMed:29875246).
CC Facilitates thereby the transfer of newly replicated viral genomes to
CC the packaging motor (PubMed:33554858). {ECO:0000269|PubMed:29875246,
CC ECO:0000269|PubMed:33554858}.
CC -!- SUBUNIT: Forms an homopentameric ring. {ECO:0000269|PubMed:33554858}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus
CC {ECO:0000269|PubMed:29875246}. Note=Localizes to viral replication
CC compartments. {ECO:0000269|PubMed:29875246}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants maintain viral DNA replication
CC and late gene expression but does not produce infectious virions. In
CC addition, viral DNA is not cleaved after replication.
CC {ECO:0000269|PubMed:29875246}.
CC -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC {ECO:0000305}.
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DR EMBL; AF148805; AAD46496.2; -; Genomic_DNA.
DR RefSeq; YP_001129426.1; NC_009333.1.
DR SMR; F5HF47; -.
DR PRIDE; F5HF47; -.
DR DNASU; 4961470; -.
DR GeneID; 4961470; -.
DR KEGG; vg:4961470; -.
DR Proteomes; UP000000942; 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 Host cytoplasm; Host nucleus; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..467
FT /note="Packaging protein UL32 homolog"
FT /id="PRO_0000423766"
FT REGION 52..136
FT /note="Zinc finger 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 191..452
FT /note="Zinc finger 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 296..373
FT /note="Zinc finger 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT MUTAGEN 52
FT /note="C->A: Strong loss of stability."
FT /evidence="ECO:0000269|PubMed:33554858"
FT MUTAGEN 373
FT /note="C->A: Strong loss of stability."
FT /evidence="ECO:0000269|PubMed:33554858"
FT MUTAGEN 415
FT /note="C->A: Strong loss of stability."
FT /evidence="ECO:0000269|PubMed:33554858"
FT MUTAGEN 452
FT /note="H->A: Strong loss of stability."
FT /evidence="ECO:0000269|PubMed:33554858"
SQ SEQUENCE 467 AA; 51911 MW; 3B3C423978D2A52C CRC64;
MFVPWQLGTI TRHRDELQKL LAASLLPEHP EESLGNPIMT QIHQSLQPSS PCRVCQLLFS
LVRDSSTPMG FFEDYACLCF FCLYAPHCWT STMAAAADLC EIMHLHFPEE EATYGLFGPG
RLMGIDLQLH FFVQKCFKTT AAEKILGISN LQFLKSEFIR GMLTGTITCN FCFKTSWPRT
DKEEATGPTP CCQITDTTTA PASGIPELAR ATFCGASRPT KPSLLPALID IWSTSSELLD
EPRPRLIASD MSELKSVVAS HDPFFSPPLQ ADTSQGPCLM HPTLGLRYKN GTASVCLLCE
CLAAHPEAPK ALQTLQCEVM GHIENNVKLV DRIAFVLDNP FAMPYVSDPL LRELIRGCTP
QEIHKHLFCD PLCALNAKVV SEDVLFRLPR EQEYKKLRAS AAAGQLLDAN TLFDCEVVQT
LVFLFKGLQN ARVGKTTSLD IIRELTAQLK RHRLDLAHPS QTSHLYA
