UL32_ALHV1
ID UL32_ALHV1 Reviewed; 468 AA.
AC O36419;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Packaging protein UL32 homolog;
GN Name=68;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(1997).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family.
CC {ECO:0000305}.
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DR EMBL; AF005370; AAC58116.1; -; Genomic_DNA.
DR PIR; T03164; T03164.
DR RefSeq; NP_065568.1; NC_002531.1.
DR SMR; O36419; -.
DR GeneID; 911771; -.
DR KEGG; vg:911771; -.
DR Proteomes; UP000000941; 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..468
FT /note="Packaging protein UL32 homolog"
FT /id="PRO_0000405766"
FT REGION 59..138
FT /note="Zinc finger 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT REGION 296..374
FT /note="Zinc finger 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01332"
SQ SEQUENCE 468 AA; 51981 MW; BD6CD3248745650B CRC64;
MSSNKTSSFV PWKVATILKH QKTLEAVIQK AFLPGDPAEA LNSSQFCETT AALDSTAPCK
ICQCLHQLCT HHSPDLSFYG DYAIICYYAL HAPKTMASNL MLLADCLELI QLYFPDAPSP
PPNINGLDIY LHFFVNRCFR LANTEKIMEW SNLDMLKTEF LRATLSGSLS GAFCFKTLWP
SLTRAPVRMA DECTCTPITN PGCGLDGGKL FHPACIGKDN FLDLILIFWK NTDAMTPANS
LLADTLSRHQ VYFQNLTPVE TNASLDPSPA LDTTQGPCLL SPALCLQKKN HTSSLCLLCE
CLASHSEAAS VFQTFKHLVL NSINNKVKLL DRILFLQQDA DSLSFIQDRE LLKSVLVNCS
PQEIHKHLFC DPLCALNSSL TDSVVLFGEV PDFEFTAFKA TLATGNSLVH RSFQSCEILE
TLILLFKSLQ TVKANKTTVS EIIKEVDASL KKHKFSLLSC YYTFNIYT