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EX7L_STRMU
ID   EX7L_STRMU              Reviewed;         447 AA.
AC   Q8DVB5;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=SMU_580;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC       insoluble oligonucleotides, which are then degraded further into small
CC       acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC         direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00378}.
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DR   EMBL; AE014133; AAN58319.1; -; Genomic_DNA.
DR   RefSeq; NP_721013.1; NC_004350.2.
DR   RefSeq; WP_002262108.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVB5; -.
DR   STRING; 210007.SMU_580; -.
DR   PRIDE; Q8DVB5; -.
DR   EnsemblBacteria; AAN58319; AAN58319; SMU_580.
DR   KEGG; smu:SMU_580; -.
DR   PATRIC; fig|210007.7.peg.513; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OMA; WPAVRFE; -.
DR   PhylomeDB; Q8DVB5; -.
DR   Proteomes; UP000002512; 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   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_0000197890"
SQ   SEQUENCE   447 AA;  51147 MW;  560412CE7DAFA6A3 CRC64;
     MSDYLSVSSL TKYLKLKFDR DPYLERVYLT GQVSNFRRRP NHQYFSLKDE KAVIQATMWS
     GIYRKLGFEL EEGMKINVIG RVQLYEPSGS YSIIIEKAEP DGIGALAVQF EQLKKKLAEA
     GYFDDRHKQR LSQFVKKIGV VTSPSGAVIR DIITTVSRRF PGVDILLFPT KVQGEGAAQE
     VADNIRLANE RTDLDLLIVG RGGGSIEDLW AFNEEIVVQA IFESHLPIIS SVGHETDTTL
     ADFAADRRAA TPTAAAELAT PVTKADLLAF LKERQMRSYQ AVMRLIRQKD EQVKKLQRSV
     IFRQPERLYD AYVQKLDHLR THLLTKVRQV YDVYDSKEHL LRQRLLSFNL SGCIQRYQAQ
     LKQDQRLLLS HMSSQYDSKL ARFEKAQDAL LSLDTTRIVA RGYAIVQKDN HIIQSTQQIK
     KGDRLHLEMK DGQVQVEVEN VKQEENI
 
 
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