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Database: UniProt
Entry: A0A0R1W6P2_9LACO
LinkDB: A0A0R1W6P2_9LACO
Original site: A0A0R1W6P2_9LACO 
ID   A0A0R1W6P2_9LACO        Unreviewed;       449 AA.
AC   A0A0R1W6P2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
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=FD16_GL001314 {ECO:0000313|EMBL:KRM13170.1};
OS   Lactobacillus suebicus DSM 5007 = KCTC 3549.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM13170.1, ECO:0000313|Proteomes:UP000051820};
RN   [1] {ECO:0000313|EMBL:KRM13170.1, ECO:0000313|Proteomes:UP000051820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM13170.1,
RC   ECO:0000313|Proteomes:UP000051820};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRM13170.1}.
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DR   EMBL; AZGF01000003; KRM13170.1; -; Genomic_DNA.
DR   RefSeq; WP_010622081.1; NZ_BACO01000038.1.
DR   EnsemblBacteria; KRM13170; KRM13170; FD16_GL001314.
DR   PATRIC; fig|1423807.3.peg.1341; -.
DR   Proteomes; UP000051820; 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; 1.
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 {ECO:0000313|Proteomes:UP000051820};
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:UP000051820}.
FT   DOMAIN        7    102       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      128    437       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
SQ   SEQUENCE   449 AA;  50671 MW;  13378AD1EF1FC3BE CRC64;
     MDNSKYLSIS TITKYIKRKF DVDPYLGRVY LTGEISNFRL RTNAHQYFSL KDDHAKISAI
     MFKSAFQKVK FTPEDGMKVL VSGRIGLYES SGSYQIYVDS MQPDGVGALY QAYEQLKKKL
     ASEGLFDEFK KPLPKFPKKI AVVTSPSGAV IRDIITTTRR RFPIVQLVLF PAQVQGDAAA
     PDIAKQIKRA NDDGSFDTLI IGRGGGSIED LWPFNEEIVA RAISDSNLPV ISSVGHETDT
     TIADLVADVR AATPTAAAEL AVPVLTDEIL KITQQRQRLM AAIRNLIKLD QQRLDKLQKS
     YIFQQPTRLY EGYSQNVDIL KQRLNQQINA SFSNWQQSLS VMRNRLSFQA LQQQVNSAQQ
     SKVNVEQRLK RGIQLLLDNR KREFSSTIES LDFLSPLKIM SRGYTYVTKD DHVIRGVKQL
     KIGSNINLHF NDGNASAEIK SINEEHENE
//
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