EX7L_RUTMC
ID EX7L_RUTMC Reviewed; 466 AA.
AC A1AX20;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Rmag_0750;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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; CP000488; ABL02477.1; -; Genomic_DNA.
DR RefSeq; WP_011738102.1; NC_008610.1.
DR AlphaFoldDB; A1AX20; -.
DR SMR; A1AX20; -.
DR STRING; 413404.Rmag_0750; -.
DR EnsemblBacteria; ABL02477; ABL02477; Rmag_0750.
DR KEGG; rma:Rmag_0750; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000002587; 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; 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; Reference proteome.
FT CHAIN 1..466
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048783"
SQ SEQUENCE 466 AA; 52205 MW; 4FE839F20071E9E8 CRC64;
MFNIDEIYTI SNFLFLCNKT IEDKIPTCWL QGEISNLTRP ESGHWYFSLK DSKAQVYCVL
FRFNQRHIKF NPKNGMEVLV HVTPTLYKAR GNFQLIIQHL EPVGIGNLNL AFEQLKNKLV
NEGLFDNIHK KPLPNIINTI GVISSSTGAV IQDIIKVLNN RYPFSDILLF DSMVQGQGSV
KKLTNALNAA DQSGKCDVII IARGGGSLED LWAFNEETLA RAIFKASTPI ISAIGHETDT
TISDFVCDIC APTPSAAAML VTPDRLELLA NTDKLYMRLH QSYQQTLHDY QSVLNQLKLR
IPISNKQIAF FSQKLDHVSI NLNNHVKSTL VLNNAKLNSI FSALKQHSPI EAIKHIKILN
QVSFAQLKHQ IKQIININNS ALYLANEKLK KAIATLTDKH KTTLSIQANS LHHLSPLNTL
SRGFSITTNA KNQILSSITD IKINQAITTQ LADGKLYSNI KKIEKN
