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Database: UniProt
Entry: A0A3B7DMM5_9ACTN
LinkDB: A0A3B7DMM5_9ACTN
Original site: A0A3B7DMM5_9ACTN 
ID   A0A3B7DMM5_9ACTN        Unreviewed;       416 AA.
AC   A0A3B7DMM5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=C6I20_11640 {ECO:0000313|EMBL:AXT86888.1};
OS   Aeromicrobium sp. A1-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2107713 {ECO:0000313|EMBL:AXT86888.1, ECO:0000313|Proteomes:UP000257855};
RN   [1] {ECO:0000313|EMBL:AXT86888.1, ECO:0000313|Proteomes:UP000257855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1-2 {ECO:0000313|EMBL:AXT86888.1,
RC   ECO:0000313|Proteomes:UP000257855};
RA   Liao L., Chen B.;
RT   "Complete genome of Aeromicrobium sp. A1-2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC         ECO:0000256|RuleBase:RU004355};
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}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
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DR   EMBL; CP027482; AXT86888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7DMM5; -.
DR   KEGG; aeb:C6I20_11640; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000257855; 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   NCBIfam; TIGR00237; xseA; 1.
DR   PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 2.
DR   Pfam; PF13742; tRNA_anti_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00378};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257855}.
FT   DOMAIN          14..104
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          127..340
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   DOMAIN          295..396
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   416 AA;  44575 MW;  0D4BF2C8ED193235 CRC64;
     MALETTADQP APLRQISQLI DGYVGRLGAV WVEAEIAQLT RRQGVCFLTL RDLIAKISIE
     ATCHVSVLDA SPGAITEGAR VIVHAKPSFY APRGTLALEL REIRPQGEGE LLAQLERRKQ
     LLAAEGLFDP RHKLSLPVLP HGIGLITGKN SAAERDVLQN ARLRWPDVRF VVRHALMQGN
     GSAADVMRGL AELASDDSIE VIVIARGGGS IEDLLPFSDE GLIRAVHACR TPVVSAIGHE
     PDTPILDLVA DLRASTPTDA AKRIVPDVGE ELAGLASIRA RSRLVIGAIV SRELHGLAAI
     RSRPVLATPS TLVDAQQAIV QEARDRARRS LGHRLDRAGD EIGHHLARVR ALSPLATLER
     GYAVAQLPDG TVVTSVGQVA DEVELSIRVV DGTIAARVLT TETTPHGKED DHGQDT
//
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