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Database: UniProt
Entry: N9Y2B7_9CLOT
LinkDB: N9Y2B7_9CLOT
Original site: N9Y2B7_9CLOT 
ID   N9Y2B7_9CLOT            Unreviewed;       406 AA.
AC   N9Y2B7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-MAR-2018, entry version 31.
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=HMPREF1092_01222 {ECO:0000313|EMBL:ENZ01987.1};
OS   Clostridium colicanis 209318.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=999411 {ECO:0000313|EMBL:ENZ01987.1, ECO:0000313|Proteomes:UP000013097};
RN   [1] {ECO:0000313|EMBL:ENZ01987.1, ECO:0000313|Proteomes:UP000013097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=209318 {ECO:0000313|EMBL:ENZ01987.1,
RC   ECO:0000313|Proteomes:UP000013097};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium colicanis 209318.";
RL   Submitted (JAN-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:ENZ01987.1}.
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DR   EMBL; AGYT01000008; ENZ01987.1; -; Genomic_DNA.
DR   RefSeq; WP_002597723.1; NZ_KB850956.1.
DR   EnsemblBacteria; ENZ01987; ENZ01987; HMPREF1092_01222.
DR   PATRIC; fig|999411.4.peg.1195; -.
DR   OrthoDB; POG091H02EK; -.
DR   Proteomes; UP000013097; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013097};
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:UP000013097}.
FT   DOMAIN        7    101       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      124    343       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   DOMAIN      331    391       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   COILED      317    345       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   406 AA;  45848 MW;  7A12EFD5A04560FF CRC64;
     MKIKVLAVSE VNNYIKKITE NDFILNNLSV KGEISNLKYH SSGHIYFSLK DDFSKINCIM
     FKSDAIELDF KLKEGLDVII KGRVSIYPQN GSLQLYCREI EEVGLGDLHV KFEKLKKKLY
     DEGLFDEKYK KDIPVNPSRI GVVTAETGAA IRDIINVTRR RNKGCDIVLY PAKVQGEGGF
     NTIIEGIEYF NKKKSVEVII IGRGGGSLEE LWNFNEEKLA YAIFNSKLPI ISAVGHEVDF
     TISDFVADVR AATPSQGAEI AVINTKEIEM ELKSINTLLN KKIESIIENE KRDLKGKFKL
     ISLNSPKVRI SNSFLEIDSL KEELNRRIRE KLEKEKMKIS EYNNLLNANN PLNILDKGFS
     LIKRNGITIK ETKELLKSEN IEIVLKDGSV SGKFKANGGE DYGKKS
//
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