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Database: UniProt
Entry: Q30Z95_DESAG
LinkDB: Q30Z95_DESAG
Original site: Q30Z95_DESAG 
ID   Q30Z95_DESAG            Unreviewed;       486 AA.
AC   Q30Z95;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   20-DEC-2017, entry version 94.
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   OrderedLocusNames=Dde_2204 {ECO:0000313|EMBL:ABB39001.1};
OS   Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans
OS   (strain G20)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB39001.1, ECO:0000313|Proteomes:UP000002710};
RN   [1] {ECO:0000313|EMBL:ABB39001.1, ECO:0000313|Proteomes:UP000002710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G20 {ECO:0000313|EMBL:ABB39001.1,
RC   ECO:0000313|Proteomes:UP000002710};
RX   PubMed=21685289; DOI=10.1128/JB.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C.,
RA   Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A.,
RA   Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(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. {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}.
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DR   EMBL; CP000112; ABB39001.1; -; Genomic_DNA.
DR   RefSeq; WP_011368096.1; NC_007519.1.
DR   STRING; 207559.Dde_2204; -.
DR   EnsemblBacteria; ABB39001; ABB39001; Dde_2204.
DR   KEGG; dde:Dde_2204; -.
DR   eggNOG; ENOG4105DVS; Bacteria.
DR   eggNOG; COG1570; LUCA.
DR   HOGENOM; HOG000229265; -.
DR   KO; K03601; -.
DR   OMA; NARRRWP; -.
DR   OrthoDB; POG091H02EK; -.
DR   Proteomes; UP000002710; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002710};
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:UP000002710}.
FT   DOMAIN        5    115       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      140    454       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   COILED      326    346       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   486 AA;  52911 MW;  E0D464FF0EB075CA CRC64;
     MTKIFSVGEV TRGIKNTLEA AYPFVWVRGQ VSNLSRPASG HVYFSLKDED ASLACVWFRH
     AQRGEETFDP LTGEVFDDGP RPGLAAVMRN GQEMLCAGRV TVYGPRGTYQ LVVELAQDVG
     LGELHLRFEE LKKKLAGMGW FDAARKRPLP RHPLRVAVVT AATGAAVRDF VRIAADRGSG
     CSIRIYPVPV QGDDAPPRIA AALELAAAHD WAQVVVLIRG GGSLEDLWAF NDERVAKAVF
     ESPLPVLTGI GHEVDTAIAD MVADVRAATP SHAAQLLWPE RQELVQRLDD ASQLLDRAWE
     LGMQEREKSV KECERALHWL SPQRSLERLD ERFAEAVRRL MAAAQALTER KERRLAAETA
     SLRHAFGPAA LDTGLLAVRQ LAARLVRAGE SFAERAAVRL ERETLRLKAA DPLLPLERGY
     SILQRPDGGF VRSVAGLEAG DNLRVLVRDG AADVAVTAVH AVSAAEAAGM PAGGKKIKGD
     RSDDES
//
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