EX7L_ERYLH
ID EX7L_ERYLH Reviewed; 477 AA.
AC Q2N6Q7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=ELI_12710;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC64634.1; -; Genomic_DNA.
DR RefSeq; WP_011415456.1; NC_007722.1.
DR AlphaFoldDB; Q2N6Q7; -.
DR STRING; 314225.ELI_12710; -.
DR EnsemblBacteria; ABC64634; ABC64634; ELI_12710.
DR KEGG; eli:ELI_12710; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000008808; 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..477
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303786"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 51620 MW; B552CD0CA3C3E6AF CRC64;
MSDLIAQSRA GDNAEPLSVS ALSQMLKRTV EDRFGYVRLR GELSGVKRAA SGHMYCSLKD
EKAVIDGVMW KGTTARLAFQ PEDGLEVIAT GKLTTYPGRS KYQIVLESLE MAGEGALLAL
LEKTRQRLEA EGLFARDRKR PLPFLPRTIG VVTSPTGAVI RDILHRLADR FPSHVLVWPV
LVQGQGAAEQ VSAAIRGFGA IKAGGEVPRP DLLIVARGGG SIEDLWSFNE EMVVRAIADS
PIPVISAVGH ETDTTLADYA ADRRAPTPTA AAEIAVPVKG ELAATLNDYA ARQQRGVLRP
LSLGRERLEA RVQRLPTIET LLQPQAQKLD ERVERLRGAL RDRAAKGREA LATQRLSPTM
LQRAEREARR KLDQVRLAPA LVERRAARDG ERLAGLSRVL ATLNPRAPLE RGYALVRDAD
GKLVRAKGEA TKQARLAVEF ADGSLDVVPA GKAAAAPKRV KKSPPPGTSG AQEDLFG
