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Database: UniProt
Entry: R5D8Q2_9FIRM
LinkDB: R5D8Q2_9FIRM
Original site: R5D8Q2_9FIRM 
ID   R5D8Q2_9FIRM            Unreviewed;       401 AA.
AC   R5D8Q2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN   ORFNames=BN795_00655 {ECO:0000313|EMBL:CCX75204.1};
OS   Firmicutes bacterium CAG:83.
OC   Bacteria; Firmicutes; environmental samples.
OX   NCBI_TaxID=1262992 {ECO:0000313|EMBL:CCX75204.1, ECO:0000313|Proteomes:UP000018101};
RN   [1] {ECO:0000313|EMBL:CCX75204.1, ECO:0000313|Proteomes:UP000018101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:83 {ECO:0000313|Proteomes:UP000018101};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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_00378, 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|HAMAP-Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
CC       ECO:0000256|SAAS:SAAS00723505}.
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC       ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723552}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355,
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:CCX75204.1}.
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DR   EMBL; CAWX010000205; CCX75204.1; -; Genomic_DNA.
DR   Proteomes; UP000018101; 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-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; 2.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
DR   Pfam; PF13742; tRNA_anti_2; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018101};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|SAAS:SAAS00723549};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723511};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723558};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00378,
KW   ECO:0000256|RuleBase:RU004355, ECO:0000256|SAAS:SAAS00723518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018101}.
FT   DOMAIN        6    100       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      124    342       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   DOMAIN      331    393       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
SQ   SEQUENCE   401 AA;  44661 MW;  6A9FF83A337710C1 CRC64;
     MEGQIYTVSE VNGFIKNVID GIPQLSGIYI RGELSNYKIY PSGHHYFTLK DGEGALRCVM
     FKGSAMKLRF RPENGMQVIA YGRISVFPRD GAYQLYCSQL SPDGVGDLYV AFEQLKDKLY
     REGLFDEGHK KPLPRYPQRI AIVTSSAGAA IHDMIRILRR RYPIARVLLL PVRVQGVEAP
     PEIVGAIRYA NRWKLADVLI TGRGGGSMED LWAFNDERVA RAIYASEIPV ISAVGHEPDV
     TIADFVADRR ASTPSNAAEI AVPDMAELLQ RLDSFRSRMA QGTLNGLERQ ERRLKALAEK
     RVLTDPLAFV QDKRLQLDYV QQKLLTAANA QWQEEQRRFA ALAAKLDALS PLKVLGRGYA
     MARTEDGAVL RTAAQVQSGE TIHLQLAQGG LRCTVTEKEE A
//
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