EX7L_PSEU5
ID EX7L_PSEU5 Reviewed; 458 AA.
AC A4VNV0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=PST_3010;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP80651.1; -; Genomic_DNA.
DR RefSeq; WP_011914105.1; NC_009434.1.
DR AlphaFoldDB; A4VNV0; -.
DR SMR; A4VNV0; -.
DR STRING; 379731.PST_3010; -.
DR EnsemblBacteria; ABP80651; ABP80651; PST_3010.
DR KEGG; psa:PST_3010; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000000233; 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..458
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303811"
SQ SEQUENCE 458 AA; 50814 MW; FE555EBDCBDE266D CRC64;
MLKDPFQRLN LDREVLTVSQ LNGRARLLLE DVFAQVWVEG EISNLARPAS GHVYFTLKDR
NAQVRCALFR QNAARVRQAL RDGLAVRVRG KVSLFEGRGD YQLILDMLEP AGDGALRLAF
EALKEKLAAE GLFSAERKAA LPAHPRRIGI VSSPTGAVIR DIISVFRRRA PQVELTLIPT
AVQGREATGQ IVRALQLADA QGFDALILAR GGGSLEDLWC FNEEAVARAV DACVTPIVCA
VGHETDVSIA DFVADVRAPT PSAAAELLAP SSADLQQRLN GLQQRLVLRM RDRLHRDAMR
LDGLTRRLRH PGERLQQQAQ RIDDLEQRLL RALDRRLCSG QERLARLETR LAAQHPGRTL
NLLRQRLDHL SSRLPRAMQA NIKGRRQQLQ GLAQTLNVVS PLATLSRGYS ILLDDRGQAI
RSASQTQPGQ RLKARLGDGE LDVRVEDNHL QPVTLPLL