EX7L_MYCSK
ID EX7L_MYCSK Reviewed; 411 AA.
AC A1UKL7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Mkms_4183;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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; CP000518; ABL93375.1; -; Genomic_DNA.
DR RefSeq; WP_011561485.1; NC_008705.1.
DR AlphaFoldDB; A1UKL7; -.
DR SMR; A1UKL7; -.
DR STRING; 189918.Mkms_4183; -.
DR EnsemblBacteria; ABL93375; ABL93375; Mkms_4183.
DR KEGG; mkm:Mkms_4183; -.
DR HOGENOM; CLU_023625_2_1_11; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
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; 2.
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..411
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303802"
SQ SEQUENCE 411 AA; 44739 MW; B8F0BDE201BAD169 CRC64;
MTTPADDQGK SPENPWPVRA VATRVAKYID RLGMVWIEGQ LTELKIRQTT AWMVLRDPAA
DMSLSVSCPR DLVANAPVPL SEGTQVIVLG KPQFYTRNGS FSLRISEIRA VGIGELLARI
DRLRRLLDAE GLFDPRLKRP IPFLPGTIGL ITGRASHAER DVMTVAANRW PAVRFAVRNT
IVQGPNAVPQ IVGALRELDR DPGVDVIVLA RGGGSVEDLL PFSDETLCRE IASCTTPVVS
AVGHEPDNPL CDLVADLRAA TPTDAAKRVV PDAAAEQAFV TDLRRRSARA LRQWVHREQH
HLDQLRSRPV LARPLQAIDA RADEVHRAVA AARRDVRRMV TVESERVGHL SARLTTLGPA
ATLARGYAVV QTMPDTNVLR TTADAPAGTH LRIRVADGAI TAVSEGTDEA H