AN_EBVB9
ID AN_EBVB9 Reviewed; 470 AA.
AC P03217; Q777D2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 92.
DE RecName: Full=Shutoff alkaline exonuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE Short=SOX {ECO:0000255|HAMAP-Rule:MF_04009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN ORFNames=BGLF5;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP INTERACTION WITH BALF5; BMRF1 AND BALF2.
RX PubMed=9434720; DOI=10.1006/viro.1997.8891;
RA Zeng Y., Middeldorp J., Madjar J.J., Ooka T.;
RT "A major DNA binding protein encoded by BALF2 open reading frame of
RT Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding
RT proteins: DNAase, EA-D, and DNA polymerase.";
RL Virology 239:285-295(1997).
RN [3]
RP MUTAGENESIS OF PHE-452 AND VAL-458.
RX PubMed=9501034; DOI=10.1006/viro.1997.8974;
RA Liu M.T., Hsu T.Y., Lin S.F., Seow S.V., Liu M.Y., Chen J.Y., Yang C.S.;
RT "Distinct regions of EBV DNase are required for nuclease and DNA binding
RT activities.";
RL Virology 242:6-13(1998).
RN [4]
RP FUNCTION.
RX PubMed=19264771; DOI=10.1128/jvi.00170-09;
RA Feederle R., Bannert H., Lips H., Muller-Lantzsch N., Delecluse H.J.;
RT "The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic
RT functions in virus replication.";
RL J. Virol. 83:4952-4962(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=19538972; DOI=10.1016/j.jmb.2009.06.034;
RA Buisson M., Geoui T., Flot D., Tarbouriech N., Ressing M.E., Wiertz E.J.,
RA Burmeister W.P.;
RT "A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease
RT with DNase and RNase activities.";
RL J. Mol. Biol. 391:717-728(2009).
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. Also acts as a cytoplasmic RNA
CC endonuclease that induces degradation of the majority of the cellular
CC messenger RNAs during early lytic infection. The resulting inhibition
CC of cellular protein synthesis serves to ensure maximal viral gene
CC expression and evasion from host immune response. Internally cleaves
CC host mRNAs which are then degraded by the cellular exonuclease XRN1.
CC Bypasses therefore the regulatory steps of deadenylation and decapping
CC normally required for XRN1 activation. {ECO:0000255|HAMAP-
CC Rule:MF_04009, ECO:0000269|PubMed:19264771}.
CC -!- SUBUNIT: Forms a complex with the DNA polymerase BALF5, the DNA
CC polymerase processivity factor BMRF1, and the major DNA binding protein
CC BALF2. {ECO:0000255|HAMAP-Rule:MF_04009, ECO:0000269|PubMed:9434720}.
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; V01555; CAA24827.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53437.1; -; Genomic_DNA.
DR PIR; A03779; QQBE37.
DR RefSeq; YP_401687.1; NC_007605.1.
DR PDB; 2W45; X-ray; 3.00 A; A/B=1-470.
DR PDB; 2W4B; X-ray; 3.50 A; A/B=1-470.
DR PDBsum; 2W45; -.
DR PDBsum; 2W4B; -.
DR SMR; P03217; -.
DR BioGRID; 971815; 1.
DR PRIDE; P03217; -.
DR DNASU; 3783773; -.
DR GeneID; 3783773; -.
DR KEGG; vg:3783773; -.
DR SIGNOR; P03217; -.
DR EvolutionaryTrace; P03217; -.
DR Proteomes; UP000153037; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0039657; P:suppression by virus of host gene expression; 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 1: Evidence at protein level;
KW 3D-structure; Decay of host mRNAs by virus; Early protein; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus; Exonuclease;
KW Host cytoplasm; Host gene expression shutoff by virus;
KW Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
KW Hydrolase; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..470
FT /note="Shutoff alkaline exonuclease"
FT /id="PRO_0000115700"
FT SITE 166
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 203
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 225
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 227
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT MUTAGEN 452
FT /note="F->A: 98% loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:9501034"
FT MUTAGEN 458
FT /note="V->A: 80% loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:9501034"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:2W45"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:2W45"
FT TURN 176..180
FT /evidence="ECO:0007829|PDB:2W45"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 214..228
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2W45"
FT TURN 329..334
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:2W45"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 384..393
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:2W4B"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2W45"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2W4B"
FT STRAND 417..425
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 430..449
FT /evidence="ECO:0007829|PDB:2W45"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2W45"
SQ SEQUENCE 470 AA; 52667 MW; 81C2048E8A65CE80 CRC64;
MADVDELEDP MEEMTSYTFA RFLRSPETEA FVRNLDRPPQ MPAMRFVYLY CLCKQIQEFS
GETGFCDFVS SLVQENDSKD GPSLKSIYWG LQEATDEQRT VLCSYVESMT RGQSENLMWD
ILRNGIISSS KLLSTIKNGP TKVFEPAPIS TNHYFGGPVA FGLRCEDTVK DIVCKLICGD
ASANRQFGFM ISPTDGIFGV SLDLCVNVES QGDFILFTDR SCIYEIKCRF KYLFSKSEFD
PIYPSYTALY KRPCKRSFIR FINSIARPTV EYVPDGRLPS EGDYLLTQDE AWNLKDVRKR
KLGPGHDLVA DSLAANRGVE SMLYVMTDPS ENAGRIGIKD RVPVNIFINP RHNYFYQVLL
QYKIVGDYVR HSGGGKPGRD CSPRVNIVTA FFRKRSPLDP ATCTLGSDLL LDASVEIPVA
VLVTPVVLPD SVIRKTLSTA AGSWKAYADN TFDTAPWVPS GLFADDESTP
