EX7L_MOOTA
ID EX7L_MOOTA Reviewed; 402 AA.
AC Q2RIB5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=Moth_1515;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(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; CP000232; ABC19824.1; -; Genomic_DNA.
DR RefSeq; WP_011393024.1; NC_007644.1.
DR RefSeq; YP_430367.1; NC_007644.1.
DR AlphaFoldDB; Q2RIB5; -.
DR SMR; Q2RIB5; -.
DR STRING; 264732.Moth_1515; -.
DR PRIDE; Q2RIB5; -.
DR EnsemblBacteria; ABC19824; ABC19824; Moth_1515.
DR KEGG; mta:Moth_1515; -.
DR PATRIC; fig|264732.11.peg.1641; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
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.
FT CHAIN 1..402
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122073"
SQ SEQUENCE 402 AA; 44118 MW; 0F3B30F797EC4CD3 CRC64;
MPEVKVLAVR ELTAYLQRLL ANDGRLANVW VKGEISNLRS PTSGHLYFSL KDQAATLRCV
MFQGRSRGLS LGLRDGLEVI ARGQVAIYPR DGVYQLYVAE IFPAGTGLAS LALQELTARL
EREGLFAADR KRPLPLLPRR VGLVTSPTGA ALRDMITISR RRFPGIELIL APARVQGEVA
PRQLALALEL LAKRGGVDVI IIGRGGGSAE DLSAFNTELV ARAIYACPVP VIAAVGHETD
LTLADRVADR RAPTPSAAAE MAVPVRAELE QRLKSLAERA RRGMEHRLEL ARARLERLTK
SSGLDRPRQE LYYRQQYVDG LEQRLLASWE RRSREREQGL NLLAARLEAA SPLAILARGY
AVCRRPGDGA PLKSSREVLP GEKVEVILKE GLLRCQVEEV GG
