(data stored in ACNUC7421 zone)

SWISSPROT: Q47SR2_THEFY

ID   Q47SR2_THEFY            Unreviewed;        81 AA.
AC   Q47SR2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00337};
DE   AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE            Short=Exonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
GN   Name=xseB {ECO:0000256|HAMAP-Rule:MF_00337};
GN   OrderedLocusNames=Tfu_0467 {ECO:0000313|EMBL:AAZ54505.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54505.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides. {ECO:0000256|HAMAP-
CC       Rule:MF_00337, ECO:0000256|SAAS:SAAS00198688}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to
CC         5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00337,
CC         ECO:0000256|SAAS:SAAS01115318};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00337, ECO:0000256|SAAS:SAAS00198687}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00337,
CC       ECO:0000256|SAAS:SAAS00198693}.
CC   -!- SIMILARITY: Belongs to the XseB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00337, ECO:0000256|SAAS:SAAS00573442}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000088; AAZ54505.1; -; Genomic_DNA.
DR   RefSeq; WP_011290914.1; NC_007333.1.
DR   STRING; 269800.Tfu_0467; -.
DR   EnsemblBacteria; AAZ54505; AAZ54505; Tfu_0467.
DR   KEGG; tfu:Tfu_0467; -.
DR   eggNOG; ENOG4105YX8; Bacteria.
DR   eggNOG; COG1722; LUCA.
DR   HOGENOM; HOG000228798; -.
DR   KO; K03602; -.
DR   OMA; RCEQHLA; -.
DR   BioCyc; TFUS269800:G1G4Q-474-MONOMER; -.
DR   Proteomes; UP000000434; 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:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.1040; -; 1.
DR   HAMAP; MF_00337; Exonuc_7_S; 1.
DR   InterPro; IPR003761; Exonuc_VII_S.
DR   InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR   PANTHER; PTHR34137; PTHR34137; 1.
DR   Pfam; PF02609; Exonuc_VII_S; 1.
DR   PIRSF; PIRSF006488; Exonuc_VII_S; 1.
DR   ProDom; PD028235; Exonuc_VII_S; 1.
DR   TIGRFAMs; TIGR01280; xseB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SR2.
DR   SWISS-2DPAGE; Q47SR2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00337,
KW   ECO:0000256|SAAS:SAAS00198692};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00337,
KW   ECO:0000256|SAAS:SAAS00198691};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00337,
KW   ECO:0000256|SAAS:SAAS00198690, ECO:0000313|EMBL:AAZ54505.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00337,
KW   ECO:0000256|SAAS:SAAS00198689};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
SQ   SEQUENCE   81 AA;  8854 MW;  69E3EB16D1F86FFC CRC64;
     MTAEENPPAE PELSYEEARE ELVAVVRRLE SGGLTLKESL ALWERGEELA KTCEAWLEGA
     RAKLAAALAE DTPEPEEGAP F
//

If you have problems or comments...

PBIL Back to PBIL home page