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Database: UniProt/SWISS-PROT
Entry: EX7L_THISH
LinkDB: EX7L_THISH
Original site: EX7L_THISH 
ID   EX7L_THISH              Reviewed;         447 AA.
AC   B8GP32;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   29-MAY-2013, entry version 33.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit;
DE            EC=3.1.11.6;
DE   AltName: Full=Exodeoxyribonuclease VII large subunit;
DE            Short=Exonuclease VII large subunit;
GN   Name=xseA; OrderedLocusNames=Tgr7_1034;
OS   Thioalkalivibrio sp. (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A.,
RA   Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-
RT   EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large
CC       acid-insoluble oligonucleotides, which are then degraded further
CC       into small acid-soluble oligonucleotides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'-
CC       or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the XseA family.
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DR   EMBL; CP001339; ACL72121.1; -; Genomic_DNA.
DR   RefSeq; YP_002513108.1; NC_011901.1.
DR   STRING; 396588.Tgr7_1034; -.
DR   EnsemblBacteria; ACL72121; ACL72121; Tgr7_1034.
DR   GeneID; 7316611; -.
DR   KEGG; tgr:Tgr7_1034; -.
DR   PATRIC; 23961586; VBIThiSp19295_1041.
DR   eggNOG; COG1570; -.
DR   KO; K03601; -.
DR   OMA; ENAQVRC; -.
DR   ProtClustDB; CLSK727215; -.
DR   BioCyc; TSUL396588:GH5B-1048-MONOMER; -.
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:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
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   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; Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN         1    447       Exodeoxyribonuclease 7 large subunit.
FT                                /FTId=PRO_1000205684.
SQ   SEQUENCE   447 AA;  50351 MW;  D00C0FEAA3DD2B27 CRC64;
     MAVTDRDIFT VTRLNQAVQG LLEGTFPLIW VEGELSSVSR PASGHLYFTL KDSGAQVRCA
     LFRNRAQLMR FRPADGMQVL VRARVGLYAP RGDYQLIVEH MEEAGDGALR RAFEELKQRL
     EREGLFDAER KRPLPRFPRR LGVITSPTGA AIRDILSVLR RRFPGLPALI YPVPVQGAAA
     APAIAEALRT ASARKDCDVL ILARGGGSLE DLWAFNEEIV ARAIHDCEIP VVSGVGHEVD
     VTIADLAADL RAATPSAAAE LVSPLRDEWL LHVERQRRLL VERMQRGLQH QALKLDNLER
     RLRQQHPERR LQNQAQRVDE LERRLALAMQ HRLRHRESRL ARLQDRLQHR SPARALERLE
     AREAQLRLRL DSALRRRLDR FEARLAAAGR ALHSVSPLAT LGRGYSILTT AEGQVIRDAS
     QVQVNDRVEA RLGKGRLSCT VVTRYEG
//
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