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Database: UniProt
Entry: R5X275_9FIRM
LinkDB: R5X275_9FIRM
Original site: R5X275_9FIRM 
ID   R5X275_9FIRM            Unreviewed;       403 AA.
AC   R5X275;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN   ORFNames=BN568_00594 {ECO:0000313|EMBL:CDA06419.1};
OS   Blautia sp. CAG:257.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1262756 {ECO:0000313|EMBL:CDA06419.1, ECO:0000313|Proteomes:UP000018056};
RN   [1] {ECO:0000313|EMBL:CDA06419.1, ECO:0000313|Proteomes:UP000018056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:257 {ECO:0000313|Proteomes:UP000018056};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC       insoluble oligonucleotides, which are then degraded further into small
CC       acid-soluble oligonucleotides. {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC         direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00378,
CC         ECO:0000256|RuleBase:RU004355};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC       ECO:0000256|RuleBase:RU004355}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA06419.1}.
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DR   EMBL; CBBB010000271; CDA06419.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5X275; -.
DR   STRING; 1262756.BN568_00594; -.
DR   Proteomes; UP000018056; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR   GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04489; ExoVII_LU_OBF; 1.
DR   Gene3D; 2.40.50.1010; -; 1.
DR   HAMAP; MF_00378; Exonuc_7_L; 1.
DR   InterPro; IPR003753; Exonuc_VII_L.
DR   InterPro; IPR020579; Exonuc_VII_lsu_C.
DR   InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR   NCBIfam; TIGR00237; xseA; 1.
DR   PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
DR   Pfam; PF13742; tRNA_anti_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00378};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018056}.
FT   DOMAIN          5..99
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          123..339
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   DOMAIN          304..391
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   403 AA;  45477 MW;  52763ACF2DF4CCA4 CRC64;
     MKRVYSVGQV NRYVKNMFLQ DFVLKKVYVK GEVSNCKYHP SGHIYFSLKD ETGVLSCVMF
     AGHRRGLAFR MKDGDQVVVG GAVDVYERDG RYQLYAKEIT QEGEGVLYER FLALKRELEE
     MGMFAQEYKQ PIPKFIRRLG VVTAPAGAAI QDIRNISLRR NPYVQIILYP ALVQGEGAAD
     SIVKGIRMLD EAGVDVMIVG RGGGSIEDLW AFNEEKVARA IFDCRTPVIS AVGHETDFTI
     ADFVADLRAP TPSAAAELAV AQYGKLVENT AGFRERLNRG MNAKLNLERL RLDQLQMRFQ
     YLSPESRLRE RRQLLLDYED ALRDGMKWKL QEKRHVLGLY LERYKGLSPL GKLSQGYAFV
     ADSRGRAVKT TAGIKPGDRM EISVTDGVIE AEVTGIRKET WET
//
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