ID   AN_ELHVK                Reviewed;         484 AA.
AC   Q18LC9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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; AF322977; ABG36590.1; -; Genomic_DNA.
DR   SMR; Q18LC9; -.
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..484
FT                   /note="Alkaline nuclease"
FT                   /id="PRO_0000408153"
FT   SITE            176
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            214
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            237
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            239
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   484 AA;  54945 MW;  54F4ACEB100E2C26 CRC64;
     MDFLSILPPQ RHCTSELCDN DESVQAIISA LEYTGLAKIL TETFSADEFV EALDARLLYI
     AHIILSCKET NVPINTDTFL CPLAERIKVD VDDLNAGSLK CMKVLLHHCT NRYFIKIVEK
     MTRGQSSNLL WFLVRNELVT GSSVVKQCSY KPGLNSVAHG IFRPASRFEV FGKVHEPIVR
     DVIATFVERR PIPVSETLGL LIDPFSGTFG ASIDLCYGIE EHDDGFVTVG ERAHVYEIKC
     MARYIYSAAD VEGFLDNPTL KGFASLIKGA TFPLIEHRLP GATPSSGAHI VSHDRMFETN
     RKRKSIYESN DYVRRLLNIN RGVKSTVYIF REKPQPDERD KLTLECLAKF TANIFLNARH
     KYFDQTSMQY FVVTQHYIND HPDPECIEPD TLPRVSVVTA LFKTRNIGTH HSLEVNHKTY
     PNSAIPFALI VTPVAFDAEI LSVFLRETFD NYAQQVYNKS KIRLWDPNFL RGFVASHREL
     EKTP