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Database: UniProt
Entry: A0A101HX61_9FIRM
LinkDB: A0A101HX61_9FIRM
Original site: A0A101HX61_9FIRM 
ID   A0A101HX61_9FIRM        Unreviewed;       206 AA.
AC   A0A101HX61;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|SAAS:SAAS00723543};
DE            EC=3.1.11.6 {ECO:0000256|SAAS:SAAS00723538};
DE   Flags: Fragment;
GN   ORFNames=XE00_0703 {ECO:0000313|EMBL:KUK84439.1};
OS   Desulfotomaculum kuznetsovii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=58135 {ECO:0000313|EMBL:KUK84439.1, ECO:0000313|Proteomes:UP000054111};
RN   [1] {ECO:0000313|EMBL:KUK84439.1, ECO:0000313|Proteomes:UP000054111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=45_62 {ECO:0000313|EMBL:KUK84439.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides.
CC       {ECO:0000256|SAAS:SAAS00723532}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to
CC       3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC       {ECO:0000256|SAAS:SAAS00723505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00723552}.
CC   -!- SIMILARITY: Belongs to the XseA family.
CC       {ECO:0000256|SAAS:SAAS00723548}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUK84439.1}.
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DR   EMBL; LGGU01000038; KUK84439.1; -; Genomic_DNA.
DR   PATRIC; fig|58135.3.peg.444; -.
DR   Proteomes; UP000054111; Unassembled WGS sequence.
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-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR   CDD; cd04489; ExoVII_LU_OBF; 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   Complete proteome {ECO:0000313|Proteomes:UP000054111};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00723549};
KW   Exonuclease {ECO:0000256|SAAS:SAAS00723511};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00723558};
KW   Nuclease {ECO:0000256|SAAS:SAAS00723518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054111}.
FT   DOMAIN        4     99       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      122    204       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   NON_TER     206    206       {ECO:0000313|EMBL:KUK84439.1}.
SQ   SEQUENCE   206 AA;  23165 MW;  0C094C6013CFBBA6 CRC64;
     MKILTVSEIT AHIKEIMDND LLLLNFWVKG EISNYKQAAS GHLYFTLKDE QCTIRSVMFR
     SRSKNLSFQP ENGLSVRARG YVTVYERDGI YQFYVEEMEP DGTGSLYQAF ELLKKKLQAE
     GLFDSEKKKK LPLLPRRVGI VTSPTGAVIR DMVDIIGRRW PGMYIVFAPA AVQGDNAGYE
     IAKSIELLNT IDLIDVIIIG RGGGPI
//
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