AN_VZVD
ID AN_VZVD Reviewed; 551 AA.
AC P09253;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 73.
DE RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN ORFNames=ORF48;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
CC -!- FUNCTION: Plays a role in processing non linear or branched viral DNA
CC intermediates in order to promote the production of mature packaged
CC unit-length linear progeny viral DNA molecules. Exhibits endonuclease
CC and exonuclease activities and accepts both double-stranded and single-
CC stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'->
CC 3' direction and the products are 5'-monophosphate nucleosides.
CC Additionally, forms a recombinase with the major DNA-binding protein,
CC which displays strand exchange activity. {ECO:0000255|HAMAP-
CC Rule:MF_04009}.
CC -!- SUBUNIT: Interacts with major DNA-binding protein; this interaction
CC increases the nuclease processivity of the alkaline exonuclease.
CC {ECO:0000255|HAMAP-Rule:MF_04009}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04009}.
CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04009}.
CC -!- SIMILARITY: Belongs to the herpesviridae alkaline nuclease family.
CC {ECO:0000255|HAMAP-Rule:MF_04009}.
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DR EMBL; X04370; CAA27931.1; -; Genomic_DNA.
DR PIR; D27344; NDBE48.
DR SMR; P09253; -.
DR PRIDE; P09253; -.
DR Proteomes; UP000002602; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_04009; HSV_AN; 1.
DR InterPro; IPR001616; Herpes_alk_exo.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR034720; Viral_alk_exo.
DR Pfam; PF01771; Viral_alk_exo; 1.
DR PRINTS; PR00924; ALKEXNUCLASE.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 3: Inferred from homology;
KW Endonuclease; Exonuclease; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..551
FT /note="Alkaline nuclease"
FT /id="PRO_0000115697"
FT SITE 188
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 260
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 286
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 288
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ SEQUENCE 551 AA; 61271 MW; 0BFA496E45C0D33D CRC64;
MARSGLDRID ISPQPAKKIA RVGGLQHPFV KTDINTINVE HHFIDTLQKT SPNMDCRGMT
AGIFIRLSHM YKILTTLESP NDVTYTTPGS TNALFFKTST QPQEPRPEEL ASKLTQDDIK
RILLTIESET RGQGDNAIWT LLRRNLITAS TLKWSVSGPV IPPQWFYHHN TTDTYGDAAA
MAFGKTNEPA ARAIVEALFI DPADIRTPDH LTPEATTKFF NFDMLNTKSP SLLVGTPRIG
TYECGLLIDV RTGLIGASLD VLVCDRDPLT GTLNPHPAET DISFFEIKCR AKYLFDPDDK
NNPLGRTYTT LINRPTMANL RDFLYTIKNP CVSFFGPSAN PSTREALITD HVEWKRLGFK
GGRALTELDA HHLGLNRTIS SRVWVFNDPD IQKGTITTIA WATGDTALQI PVFANPRHAN
FKQIAVQTYV LSGYFPALKL RPFLVTFIGR VRRPHEVGVP LRVDTQAAAI YEYNWPTIPP
HCAVPVIAVL TPIEVDVPRV TQILKDTGNN AITSALRSLR WDNLHPAVEE ESVDCANGTT
SLLRATEKPL L