ID A0A3P1SYM3_9BACT Unreviewed; 438 AA.
AC A0A3P1SYM3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN ORFNames=EII32_02875 {ECO:0000313|EMBL:RRD02367.1};
OS Prevotella sp. OH937_COT-195.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2491051 {ECO:0000313|EMBL:RRD02367.1, ECO:0000313|Proteomes:UP000267043};
RN [1] {ECO:0000313|EMBL:RRD02367.1, ECO:0000313|Proteomes:UP000267043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH937_COT-195 {ECO:0000313|EMBL:RRD02367.1,
RC ECO:0000313|Proteomes:UP000267043};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004355};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family.
CC {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:RRD02367.1}.
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DR EMBL; RQZH01000004; RRD02367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1SYM3; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000267043; 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-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR CDD; cd04489; ExoVII_LU_OBF; 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; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU004355};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004355};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU004355}.
FT DOMAIN 6..113
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 137..434
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 438 AA; 48898 MW; 17B7221B4D8B7146 CRC64;
MMRNTLSLYE LNQLLAEVID IGMPREYWVE AEISELRVVR GHCHIDLVEK SDDSNTPVAR
ASAKCWQTTW SVVSPHFEKV TGQRLHAGMK VLLLVGANFH PAYGFSWIIS DIDPTYTLGD
MARKRQEIIA RLKEEGVFEL QKELTLPLFC RNIAVISSAN AAGYGDFVNQ LEGNEYGFRF
QVRLFPAIMQ GEGVEQSIIS ALDAIYETSA TEGETAPDCV VIIRGGGATS DLSGFDTLAL
AENVAQFPIP IITGIGHERD ESILDMVSHI RVKTPTAAAA LLTDNLKRIW DYLQYAQGVL
TAGAKQRMDM EQLRLQRVSQ KIPSMFSLVK ERQENRIGQM FREMIAAAKL TISNLKHEIE
VISVNLHSVP EHKIAGEKHR LQMLEQRAMS LNPDLLLKKG YSITMHDGKV VRDASKLKPG
DKLETRVENG SIHSTVDA
//
