UL32_HHV11
ID UL32_HHV11 Reviewed; 596 AA.
AC P10216;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Packaging protein UL32;
GN Name=UL32;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP FUNCTION.
RX PubMed=8648731; DOI=10.1128/jvi.70.6.3938-3946.1996;
RA Chang Y.E., Poon A.P., Roizman B.;
RT "Properties of the protein encoded by the UL32 open reading frame of herpes
RT simplex virus 1.";
RL J. Virol. 70:3938-3946(1996).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9499108; DOI=10.1128/jvi.72.3.2463-2473.1998;
RA Lamberti C., Weller S.K.;
RT "The herpes simplex virus type 1 cleavage/packaging protein, UL32, is
RT involved in efficient localization of capsids to replication
RT compartments.";
RL J. Virol. 72:2463-2473(1998).
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:8648731, ECO:0000269|PubMed:9499108}.
CC -!- INTERACTION:
CC P10216; F8RFH0: UL15; Xeno; NbExp=2; IntAct=EBI-9645871, EBI-9642200;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:9499108}. Host
CC nucleus {ECO:0000269|PubMed:9499108}. Note=Mainly cytoplasmic in
CC 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; X14112; CAA32307.1; -; Genomic_DNA.
DR PIR; E30085; WMBEH2.
DR RefSeq; YP_009137107.1; NC_001806.2.
DR SMR; P10216; -.
DR IntAct; P10216; 7.
DR MINT; P10216; -.
DR PRIDE; P10216; -.
DR DNASU; 2703352; -.
DR GeneID; 2703352; -.
DR KEGG; vg:2703352; -.
DR Proteomes; UP000009294; 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 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..596
FT /note="Packaging protein UL32"
FT /id="PRO_0000116014"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..214
FT /note="Zinc finger 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 308..581
FT /note="Zinc finger 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 423..502
FT /note="Zinc finger 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ SEQUENCE 596 AA; 63950 MW; 6E650D5EE9CB09B8 CRC64;
MATSPPGVLA SVAVCEESPG SSWKAGAFER AYVAFDPSLL ALNEALCAEL LTASHVIGVP
PVGTLDEDVA ADVVTAPSRA RGGAGDGGGS GGRGGPRNPP PDPCGEGLLD TGPFSAAAID
TFALDRPCLV CRTIELYKQT YRLSPQWVAD YAFLCAKCLG APHCAASIFV AAFEFVYVMD
RHFLRTKKAT LVGSFARFAL TINDIHRHFF LHCCFRTDGG VPGRHAQKQP KPSPSPGAAK
VQYSNYSFLA QSATRALIGT LASGGEEGAG SAAGSGTQPS LTTALMNWKD CARLLDCTEG
RRGGGDSCCT RAAARNGEFE TVAGDREPEE SPDTWAYADL VLLLLAGTPA VWESGPQLRA
AAEARRATVR QSWEAHRGAR TRDVAPRFAQ FTEPDAQPDL DLGPLMATVL KHGRGRGRTG
GECLLCNLLL VRAYWLALRR LRASVVRYSE NNTSLFDCIV PVVDQLEADP ETQPGDGGRF
VSLLRAAGPE AIFKHMFCDP MCAITEMEVD PWVLFGHPPA THPDELLLHK AKLACGNEFE
GRVCIALRAL IYTFKTYQVF VPKPTALATF VREAGALLRR HSISLLSLEH TLCTYV
