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Database: UniProt
Entry: A0A127MGD1_9SPHN
LinkDB: A0A127MGD1_9SPHN
Original site: A0A127MGD1_9SPHN 
ID   A0A127MGD1_9SPHN        Unreviewed;       488 AA.
AC   A0A127MGD1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-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=AZE99_11315 {ECO:0000313|EMBL:AMO72363.1};
OS   Sphingorhabdus sp. M41.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO72363.1, ECO:0000313|Proteomes:UP000073959};
RN   [1] {ECO:0000313|EMBL:AMO72363.1, ECO:0000313|Proteomes:UP000073959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M41 {ECO:0000313|EMBL:AMO72363.1,
RC   ECO:0000313|Proteomes:UP000073959};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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}.
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; CP014545; AMO72363.1; -; Genomic_DNA.
DR   RefSeq; WP_067201119.1; NZ_CP014545.1.
DR   EnsemblBacteria; AMO72363; AMO72363; AZE99_11315.
DR   KEGG; sphg:AZE99_11315; -.
DR   KO; K03601; -.
DR   Proteomes; UP000073959; 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   Complete proteome {ECO:0000313|Proteomes:UP000073959};
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:UP000073959}.
FT   DOMAIN       24    117       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      140    455       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
SQ   SEQUENCE   488 AA;  53046 MW;  0225265AE098213D CRC64;
     MDDSLSLDAK LLAESGQGDN APPLSVSEIS GALKRVVEDR FGYVRIRGEI SGFKRAASGH
     VYLALKDDKA VIDGVMWKGN AGRLPFRPED GIEVVVSGKL TTYPGRSKYQ VVIDKMELAG
     EGALMALFEK LKAKLLAEGL FDQDRKKPIP FLPKTIGVVT SPTGSVIRDI LHRLADRCPS
     HVIVWPVLVQ GEGAAKQISH AIRGFSEMAP DGPVARPDLV IVARGGGSIE DLWSFNEEIV
     VRAVADCSIP IISAVGHETD TTLCDFAADL RAPTPTAAAE MAVPVRAEWL ATLAEGKARM
     ARSVQRSLST AQERLEAQRR LMPALTDLLR PHQQRVDETS ERMKYGMSQN IAHARSRFAS
     SAGALRPSIL KQRLARSQEQ YKRLDLPVSL VQRPLDEARQ RLDALWRLAQ QVSPDGPLKR
     GYARVSGPDG SLIANRAAAI KAGDLDLHFQ DGVVGAIVTD EAPAKPKPAP PSPSRVKKAP
     DDRQQDLF
//
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