EX7L_VIBCM
ID EX7L_VIBCM Reviewed; 446 AA.
AC C3LT19;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=VCM66_0724;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; CP001233; ACP05045.1; -; Genomic_DNA.
DR RefSeq; WP_000099131.1; NC_012578.1.
DR AlphaFoldDB; C3LT19; -.
DR SMR; C3LT19; -.
DR EnsemblBacteria; ACP05045; ACP05045; VCM66_0724.
DR GeneID; 57739476; -.
DR KEGG; vcm:VCM66_0724; -.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000001217; Chromosome I.
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 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 PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..446
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200688"
SQ SEQUENCE 446 AA; 50543 MW; AAE17369636A4BC9 CRC64;
MSSSLANRNI YTVSRLNSEV RLLLENEMGI VWLVGEISNF SAPVSGHWYL TLKDSQAQVK
CAMFKGNNRL VNFKPQNGQQ VLVKARLSLY EPRGDYQIIL ESMQPEGDGR LQQQFEQLKM
QLAAEGLFAQ TRKKPLPENP RCVGIITSRT GAALHDILHV LKRRDPNLPV VIYPTLVQGE
EAAIQIAQAI GRANTRAECD VLIVGRGGGS LEDLWCFNHE IVARTIAASE IPIISAVGHE
IDVTIADFVA DVRAPTPSAA AELVSRDHRH KQQALHQWQA KLASTMRHYL AQQETQFARL
QHKLDKQHPQ ARLERQQQQL DELSLRLEQK MQQRLATQQQ RWDRLSHKIE LHSPIHLIRQ
QRFNLIQQEQ RINQSIQRYL IQSRHQLALL SEKLDAVSPL ATLARGYSVT RTTQGELVRQ
SAQVKPGDTL VTQLMDGEIL STVNSR
