AN_EHV1V
ID AN_EHV1V Reviewed; 565 AA.
AC Q6S6S2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 50.
DE RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN OrderedLocusNames=50;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N.J., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45934.1; -; Genomic_DNA.
DR SMR; Q6S6S2; -.
DR Proteomes; UP000008296; 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.
FT CHAIN 1..565
FT /note="Alkaline nuclease"
FT /id="PRO_0000115693"
FT SITE 229
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 292
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 317
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 319
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ SEQUENCE 565 AA; 62438 MW; C51F9CC633D6AEF9 CRC64;
MDSSPVTYSG EPPYKLRRLS PSYPYVSKLR ERCASKIETL SEGSARDSLE EEDVSEAMAT
GAFLATRLYL PSVLPQRITT LTFLDHFKKS RPLPNSDKRL NPIFYRLAYI RDLVGEMELE
GIVERGTASR LLGASSPAGF VAGTYTHARD LSKTMSLASV RDAVLAIEAQ TRDQSESQLW
ALLRRGLATA STMKWGALGP QYHPQWCEVS TNAKGIPNNP ALQFGQTNER TARSLISALY
VARSEAATPD LLVDPGCGQC FVFDESASVP GDAYACGLLM DARTGVVGAS LDMLVCDRDP
SGVLSPHSTQ TTLDFFEIKC RAKYLFDPDL FSPVATAYAN LLKHRTAVCL RKFLRSIKNP
AVEYFASTSV PGATEALITC NSSWKPREVN ETNRRCGDFD RDHIALNLDA SSDVWLFSEP
DLESETITPA RWDTGELALS VPVFANPRHP NFKQILVQAY VLSGHFPDHQ LRPFLVTFIG
RHRKRCEEGK TFTICDRPEG SPYNLNEVVH SSCAIPILLF VTPVIVDREG CWEDIEIESL
TAFNKTADAI WDSDSPADVS EPTSS