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Shutoff alkaline exonuclease (SOX) (EC 3.1.-.-)

 G1EUJ3_BHV4             Unreviewed;       489 AA.
G1EUJ3;
19-OCT-2011, integrated into UniProtKB/TrEMBL.
19-OCT-2011, sequence version 1.
28-FEB-2018, entry version 12.
RecName: Full=Shutoff alkaline exonuclease {ECO:0000256|HAMAP-Rule:MF_04009};
Short=SOX {ECO:0000256|HAMAP-Rule:MF_04009};
EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04009};
Name=ORF 37 {ECO:0000313|EMBL:AEL29781.1};
Bovine herpesvirus 4 (BoHV-4) (Movar virus).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Rhadinovirus.
NCBI_TaxID=10385 {ECO:0000313|EMBL:AEL29781.1};
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
NCBI_TaxID=9689; Panthera leo (Lion).
[1] {ECO:0000313|EMBL:AEL29781.1}
NUCLEOTIDE SEQUENCE.
STRAIN=V.test {ECO:0000313|EMBL:AEL29781.1};
PubMed=21846388;
Palmeira L., Machiels B., Lete C., Vanderplasschen A., Gillet L.;
"Sequencing of Bovine herpesvirus 4 V.test strain reveals important
genome features.";
Virol. J. 8:406-406(2011).
-!- FUNCTION: Plays a role in processing non linear or branched viral
DNA intermediates in order to promote the production of mature
packaged unit-length linear progeny viral DNA molecules. Exhibits
endonuclease and exonuclease activities and accepts both double-
stranded and single-stranded DNA as substrate. Exonuclease
digestion of DNA is in the 5'-> 3' direction and the products are
5'-monophosphate nucleosides. Additionally, forms a recombinase
with the major DNA-binding protein, which displays strand exchange
activity. Also acts as a cytoplasmic RNA endonuclease that induces
degradation of the majority of the cellular messenger RNAs during
early lytic infection. The resulting inhibition of cellular
protein synthesis serves to ensure maximal viral gene expression
and evasion from host immune response. Internally cleaves host
mRNAs which are then degraded by the cellular exonuclease XRN1.
Bypasses therefore the regulatory steps of deadenylation and
decapping normally required for XRN1 activation.
{ECO:0000256|HAMAP-Rule:MF_04009}.
-!- SUBUNIT: Forms a complex with the DNA polymerase, the DNA
polymerase processivity factor, and the major DNA binding protein.
{ECO:0000256|HAMAP-Rule:MF_04009}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-
Rule:MF_04009}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04009}.
-!- SIMILARITY: Belongs to the herpesviridae alkaline nuclease family.
{ECO:0000256|HAMAP-Rule:MF_04009}.
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EMBL; JN133502; AEL29781.1; -; Genomic_DNA.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-UniRule.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-UniRule.
HAMAP; MF_04009; HSV_AN; 1.
InterPro; IPR001616; Herpes_alk_exo.
InterPro; IPR011335; Restrct_endonuc-II-like.
InterPro; IPR034720; Viral_alk_exo.
Pfam; PF01771; Herpes_alk_exo; 1.
PRINTS; PR00924; ALKEXNUCLASE.
SUPFAM; SSF52980; SSF52980; 1.
3: Inferred from homology;
Endonuclease {ECO:0000256|HAMAP-Rule:MF_04009};
Exonuclease {ECO:0000256|HAMAP-Rule:MF_04009};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04009};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04009};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04009};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04009};
Nuclease {ECO:0000256|HAMAP-Rule:MF_04009}.
SITE 184 184 Required for function.
{ECO:0000256|HAMAP-Rule:MF_04009}.
SITE 221 221 Required for function.
{ECO:0000256|HAMAP-Rule:MF_04009}.
SITE 244 244 Required for function.
{ECO:0000256|HAMAP-Rule:MF_04009}.
SITE 246 246 Required for function.
{ECO:0000256|HAMAP-Rule:MF_04009}.
SEQUENCE 489 AA; 56788 MW; 127679287D586DBD CRC64;
MTMASPVDFF DSQPLLDEMD TIDLDAQSRK ITEFTFSSFM GHSRIQQFMS TCNVIPRMPA
MRYMYFYYLF KKIGEFIGNN DIVKFYEDKV FDKYNPPGSI YEVYMACHHM DFYKQYAICL
LLESITREQH LSTLWDTLRN GIISSSKMHW VIKQRKTSKK IFEPWPIKNN YYIASPLAFG
LRCEGIVKSI LINIIYPNTP NCIDYGFMQS PLDGIFGVSL DFCTNISHDE NGMLIFEPDC
CVYEIKCRFK YMFSKSECDP LYGKYVSLYQ NPNKKNLINF ILSVSRPAVE FVAPGGIPSE
HDFLLTHGLE WRWEPPKRKR TVKSTNWIIE CIKYNSCVES DVFILSDPSI TNGNITIKSH
FKADLFVNPK HTYFFQVLLQ YKVVESYIQF SPSTKTLGSQ KNFIVSAFFR KRNFKDPLTC
TLGDTGEVLK ETVEIPVMII ITQVRIPKFI LKENMRKATT YWADCSEKTF THSPWVTGLH
LAVGKSMTP


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