EX7L_XYLF2
ID EX7L_XYLF2 Reviewed; 444 AA.
AC B2I9F0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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};
GN OrderedLocusNames=XfasM23_2006;
OS Xylella fastidiosa (strain M23).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB93405.1; -; Genomic_DNA.
DR RefSeq; WP_004090422.1; NC_010577.1.
DR AlphaFoldDB; B2I9F0; -.
DR EnsemblBacteria; ACB93405; ACB93405; XfasM23_2006.
DR GeneID; 58017421; -.
DR KEGG; xfn:XfasM23_2006; -.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000001698; 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.
FT CHAIN 1..444
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122103"
SQ SEQUENCE 444 AA; 49782 MW; DA4E4FD9C3F4106D CRC64;
MQHRDEILTP SQLNTLARDL LESAFPLVWI EGELGNVSRP SSGHLYVTLK DAQAQVRCAM
FKPKSQWLTF QPREGLRVLA RGRLTLYEAR GDYQIVLDHL EESGEGALRR AFEQLRIRLE
AEGLFDPARK QPLPVHPRRI AVITSPSGAV IRDILSVLMR RFPLVEIELL PSLVQGDTAA
AQITHLLGGA DSSGRYDAIL IARGGGSLED LWAFNNEQLA RTIAAAHTPV ISAIGHETDF
TLADFAADIR APTPSVAAEL LVPDQRALRQ HLGQLQQRLL HLQQHRLDQA IQRADQLGLR
LQARNPEMHL RLLAQRQAEA GRRLQQCLHH VLDRAQGQLR NHHTRLYALN PRQQIAGLQK
HLKHLNPQQP LQRRLQQEQL RLHGLVRALE AVNPLATVAR GYALVRRADN NTLVRDSAQV
CVGDVLDTKL AHGQLRVRVE ISST
