AN_GAHVM
ID AN_GAHVM Reviewed; 524 AA.
AC Q9E6Q5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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 Name=MDV024;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14204.1; -; Genomic_DNA.
DR RefSeq; YP_001033940.1; NC_002229.3.
DR SMR; Q9E6Q5; -.
DR GeneID; 4811485; -.
DR KEGG; vg:4811485; -.
DR Proteomes; UP000008072; 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..524
FT /note="Alkaline nuclease"
FT /id="PRO_0000406500"
FT SITE 197
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 257
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 282
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 284
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ SEQUENCE 524 AA; 60194 MW; C3D1EBB67A55494D CRC64;
MELGTKFPLS KSCKDESRKR KRGITIDCDS QILVGDEQSN STKTKPYDEI CENIVPNYTF
GNYILQKIDP NDCRHSLHPL YHRLFYIADV IKQGISEGSL LENKYSYILE TEHILLDESR
INNLSPSIHA SRWCKMVESL TRLQANSELW HIFRQCLLTA SSVKWSPNGT INTAGLITND
LPSRGQTESI LFGTRNESLA KSLIAALCVS QSSVRTIDNS DKKNEFDNTT TGILDIEKYS
CGLMIDIRTG MLGASLDMVM CNRNRHGILA PCLTDNNIET YEIKCRFKYA FCPEMRSELS
QCYERLMATK TVQWFRRFLY TIDCPCVDYF RPDNYPRAKE ALITSDDDWK VGHSAYHAAQ
SRIKCNEFEM HHLTLNKNMS SRVWLFGEPD LQTNSIYPLL WNTGERVLSI PIFANPRHQN
FKQIFLQSYV ASGYFGNRKI VPFLATFIGR HRRQTELGRC FSLFVDDTEA SEVVYEITPE
QAIPVILIIT PVIIDNTFYV GIEESGYRAF GELVDHLWAK QCRI