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Database: UniProt
Entry: N2IY72_9PSED
LinkDB: N2IY72_9PSED
Original site: N2IY72_9PSED 
ID   N2IY72_9PSED            Unreviewed;       463 AA.
AC   N2IY72;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-MAR-2018, entry version 32.
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=HMPREF1487_07180 {ECO:0000313|EMBL:ENA31749.1};
OS   Pseudomonas sp. HPB0071.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA31749.1, ECO:0000313|Proteomes:UP000017050};
RN   [1] {ECO:0000313|EMBL:ENA31749.1, ECO:0000313|Proteomes:UP000017050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPB0071 {ECO:0000313|EMBL:ENA31749.1,
RC   ECO:0000313|Proteomes:UP000017050};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J.,
RA   Dai D., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Pseudomonas sp. HPB0071.";
RL   Submitted (MAR-2013) 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, ECO:0000256|SAAS:SAAS00984457}.
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:ENA31749.1}.
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DR   EMBL; AQFP01000010; ENA31749.1; -; Genomic_DNA.
DR   EnsemblBacteria; ENA31749; ENA31749; HMPREF1487_07180.
DR   PATRIC; fig|1203578.3.peg.2885; -.
DR   OrthoDB; POG091H02EK; -.
DR   Proteomes; UP000017050; 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; IPR012340; NA-bd_OB-fold.
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   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00237; xseA; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017050};
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:UP000017050}.
FT   DOMAIN       20    112       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      136    447       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   COILED      364    384       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   463 AA;  52010 MW;  E3FDD116E9D00D4D CRC64;
     MMPAMLNDPF QRLGLDREVL TVSQLNGRAR VLLEDVFSQV WVEGEISNLA RPASGHIYFT
     LKDKDAQVRC ALFRQNAVRV RNLLKDGMAV KVRGKVSLFE GRGDYQLILE TLEPAGDGLL
     RQAFEALKQK LLGEGLFAQE RKKPLPGHPC RIGIVTSPTG AVIRDIVSVF KRRAPQVELV
     LIPTAVQGRE ATAQIARALQ TADVQGFDAI ILARGGGSLE DLWCFNEEQV ARAVAAVQTP
     IVSAVGHETD VSIADFVADV RAPTPSAAAE LLAPHSGDLK NRLDALYRRL VVRMGERLSR
     EQLRLENMTR RLKHPGERLR QQAQRIDDLD MRLRRAFVID MNRRRDRLAH VETRLAGQHP
     GRQLALLRQR LDQLAQQLPR CMERQLKERR QRLAAQVQTL HIVSPLATLG RGYSILLDER
     GHAIRSADQT RNGQRLKARL AEGELDVRVE DNHREPTTLS LLD
//
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