EX7L_HAMD5
ID EX7L_HAMD5 Reviewed; 448 AA.
AC C4K5U1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=HDEF_1282;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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; CP001277; ACQ67934.1; -; Genomic_DNA.
DR RefSeq; WP_015873725.1; NC_012751.1.
DR AlphaFoldDB; C4K5U1; -.
DR SMR; C4K5U1; -.
DR STRING; 572265.HDEF_1282; -.
DR EnsemblBacteria; ACQ67934; ACQ67934; HDEF_1282.
DR GeneID; 66260982; -.
DR KEGG; hde:HDEF_1282; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000002334; 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..448
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000205677"
SQ SEQUENCE 448 AA; 51226 MW; 8A78264D62E707F6 CRC64;
MPLSHFSDLL TVSQLNIRVR DILEKNIGQI WLMAEISNFS QPSSGHWYFT LKDERTQVRC
TMFRNNNRHI FFKVQNGLQV LVRACVSLYE PRGEYQLIVE SMEPAGEGIL RQKFEQLKKK
LAAEGLFAEK YKKPLPDSVK QLGVITSISG AALFDILKVL QHRDPSLPVV IYPTKVQGEY
APSQIVKALS IANRRAECDL VILARGGGSL EDLSCFNDER VARAIFDSDL PIVSAIGHET
DVSIADLVAD LRASTPSAAA ERVTRDRRDI IQKLGSHQQR MAMAMDYYFS KLRQRFVHLS
HCIEQQHPQL ELERQKMQLI HFKISMEKII QAKLKGLIHQ EAHLKKNVLR RAPQIQIYQY
QKQIQEEFHQ LKAAMERKIH HYVQRFAVVS SRLETVSPLA TLARGYSVTC FSSGSMLKKI
EQVQIGDELN TRLQGGWIKS QVLEIKKN
