AN_HHV7J
ID AN_HHV7J Reviewed; 480 AA.
AC P52346;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN Name=U70;
OS Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
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; U43400; AAC54731.1; -; Genomic_DNA.
DR PIR; T41971; T41971.
DR RefSeq; YP_073810.1; NC_001716.2.
DR SMR; P52346; -.
DR PRIDE; P52346; -.
DR DNASU; 3289528; -.
DR GeneID; 3289528; -.
DR KEGG; vg:3289528; -.
DR Proteomes; UP000009246; 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 HAMAP; MF_04009; HSV_AN; 1.
DR InterPro; IPR001616; Herpes_alk_exo.
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..480
FT /note="Alkaline nuclease"
FT /id="PRO_0000115696"
FT SITE 168
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 205
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 228
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 230
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ SEQUENCE 480 AA; 56000 MW; CA3EAAF48B5113E2 CRC64;
MAIDYAQISC NLASIIEEDS VFLFLIDKLN NLDISRRKIS FNFIRLCYTY YILIKFNSRF
KDTFLARSFI DYMHQNISDF IDENVELSDL YSNIYVRLQD ASPKVVKNLF KILERETRGQ
STNPLWHAMR KNCITATKIY DIYISKSFSG IQEHSYLGDA VLYGIKHERI IEHLLKTFFV
KKPWISKTLG LLLDPSSGVF GASIDSYYGI SFNDNNLIEV GDKVVIFELK FRYKYLREKN
DLFVSELLQN PSEIALAKFI LSHPIPAIEY RENGKMPSAR EYLITNNPLY DSGKKRRACL
TPKNLTFDIT RLIPMNEKNV STAIIFDVVK DCILNTLVAY QKAIFTIDAF INPRHRYYFQ
SILQQYVMTQ FYIQDHDNPE NIEKENLPSV YIVSAIFRKR EDDEKNCRLL IEDTEYLEEE
IPLILLITPI TIDAEFTSRV IKDICCIWEN KIAQQTNLKI WAQSAVRQYM AASSARPKTP