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EX7L_HAHCH
ID   EX7L_HAHCH              Reviewed;         444 AA.
AC   Q2SCJ1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=HCH_04944;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC31633.1; -; Genomic_DNA.
DR   RefSeq; WP_011398698.1; NC_007645.1.
DR   AlphaFoldDB; Q2SCJ1; -.
DR   STRING; 349521.HCH_04944; -.
DR   EnsemblBacteria; ABC31633; ABC31633; HCH_04944.
DR   KEGG; hch:HCH_04944; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OMA; WPAVRFE; -.
DR   OrthoDB; 1371775at2; -.
DR   Proteomes; UP000000238; 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..444
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000303789"
SQ   SEQUENCE   444 AA;  49534 MW;  96D57E97F2A9CBDD CRC64;
     MSELSPHSPF SVTELNRQVR RLLEVSFMQV WVTGEISNFS CPSSGHWYFS LKDDKAQVRC
     AMFRNRNMFV KQRPRDGEAV TLRAKVSLYE GRGEFQLIAE SMELAGEGEL RRAFEELKLK
     LSREGLFEES RKRPLPAMPK QVGVITSPTG AAVRDILTVL ERRFPAIPVL LFPVPVQGKE
     AGPAIVAAIA SANRLNCCDV LIVGRGGGSL EDLWAFNEEP VARAIAASAI PVVSAVGHET
     DITIADLVAD LRAPTPSAAA EKVSPDQAEW KHRFLIYEQR LDAAAQRLLR QEGLRLNQLR
     GRLKHPGRRL QESAQRLDDL EVRLHRQAQN LLSVRRNQLT HLRDRLLASS PRQSLKNRYA
     TVDALNHRLQ TAVLSVLRHK SQHFAKLCGH MEAVSPIATL ARGYAIVSDE NGQIIRSEKE
     VRTGQKVKAR LSDGEIHCEV VASV
 
 
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