EX7L_MESFL
ID EX7L_MESFL Reviewed; 404 AA.
AC Q6F1D5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=Mfl331;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) 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: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; AE017263; AAT75688.1; -; Genomic_DNA.
DR RefSeq; WP_011183228.1; NC_006055.1.
DR RefSeq; YP_053572.1; NC_006055.1.
DR AlphaFoldDB; Q6F1D5; -.
DR SMR; Q6F1D5; -.
DR STRING; 265311.Mfl331; -.
DR EnsemblBacteria; AAT75688; AAT75688; Mfl331.
DR GeneID; 2898002; -.
DR KEGG; mfl:Mfl331; -.
DR PATRIC; fig|265311.5.peg.331; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_14; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000006647; Chromosome.
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; 2.
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; Reference proteome.
FT CHAIN 1..404
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303798"
SQ SEQUENCE 404 AA; 45683 MW; D78CA8020F6963B0 CRC64;
MENKIFSVAE ISQIFKEAIE GSNYFKNIYV RGEVGNLTFN KSGHVYFSLK DNQSTIAAMI
WKSNAHKLTN LNVKEGMEIT CYGRLTYYVP SGRVSFEAVD VSVEGKGDLQ EIFEERLKEI
TALGWTDESR KKPINRFAKN IGLITTDSGA AIKDLITTLK RRMPSVNIYL FPTMVQGETA
KFDIANKIQQ ANLFEPKLDI LIVGRGGGSY EDLWTFNEMK VLKAIVDSSI PVISAVGHEP
DITLSDYVAD LRAATPTAAA ELASISTEEL LKELAYNYEN QIRLFKNVYN NQQLKIEEFK
KQNILKINNK YDLQSLDLNY IEKSFINNIN NIISRNEMFI ENIESKTALL DPKKPLDKGF
GLIMSKDKQI INSVDKVDIN QEIKLVLKDG EIETIIKGVK KHGK
