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Database: UniProt
Entry: A0A143HAW1_9BACL
LinkDB: A0A143HAW1_9BACL
Original site: A0A143HAW1_9BACL 
ID   A0A143HAW1_9BACL        Unreviewed;       449 AA.
AC   A0A143HAW1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-MAR-2018, entry version 16.
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=ATY39_04930 {ECO:0000313|EMBL:AMW98848.1};
OS   Rummeliibacillus stabekisii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Rummeliibacillus.
OX   NCBI_TaxID=241244 {ECO:0000313|EMBL:AMW98848.1, ECO:0000313|Proteomes:UP000076021};
RN   [1] {ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; CP014806; AMW98848.1; -; Genomic_DNA.
DR   RefSeq; WP_066786671.1; NZ_CP014806.1.
DR   KEGG; rst:ATY39_04930; -.
DR   KO; K03601; -.
DR   Proteomes; UP000076021; 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:UP000076021};
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:UP000076021}.
FT   DOMAIN        7    103       tRNA_anti_2. {ECO:0000259|Pfam:PF13742}.
FT   DOMAIN      126    438       Exonuc_VII_L. {ECO:0000259|Pfam:PF02601}.
FT   COILED      282    302       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   449 AA;  50228 MW;  006C03DB31BD362B CRC64;
     MLAMPYLSVQ ALTKYIKKKF DADPHLRNVY VKGELSNVKH HIGSGHIYFT LKDEKSQVKA
     VMFAMRAKKL KFKPENGMKV LIKGDVTVYE GGGQYQLYAE EMEPDGIGSL YLAFEQLKEK
     LQQEGLFSES HKKQIPVFPQ RIAVVTAPTG AAIRDICTTI KQHYKLVDIV IFPALVQGEN
     AAKSIAKAIE QANNTPNIDT LIVGRGGGSI EDLWAFNEEI VARAIFNSKL PIISGVGHET
     DTTIADFVAD ARAATPTAAA KLAVPSSQEL LKYLLTKKAQ LIQLTQSKIR SERSRLDRLQ
     KSYPLSLPDR LYRPFTEQLM RLDDRLQQGT VRYVKDQKQL IQRLDQALAM RTPVTQIKQE
     KKNIINLESA LQKAIVGQIN QKKEEFRSAI RTLEALNPLS IMTRGYSIAY QNGTVVKSVD
     DLQTQDQIEV HLHDGKALAS IVSVTKKGD
//
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