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Database: UniProt
Entry: A0A1G9XBA7_9ACTO
LinkDB: A0A1G9XBA7_9ACTO
Original site: A0A1G9XBA7_9ACTO 
ID   A0A1G9XBA7_9ACTO        Unreviewed;       456 AA.
AC   A0A1G9XBA7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN04487766_10953 {ECO:0000313|EMBL:SDM93595.1};
OS   Actinomyces ruminicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=332524 {ECO:0000313|EMBL:SDM93595.1, ECO:0000313|Proteomes:UP000199671};
RN   [1] {ECO:0000313|EMBL:SDM93595.1, ECO:0000313|Proteomes:UP000199671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPR-7B {ECO:0000313|EMBL:SDM93595.1,
RC   ECO:0000313|Proteomes:UP000199671};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNHU01000009; SDM93595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9XBA7; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000199671; Unassembled WGS sequence.
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}.
FT   DOMAIN          56..151
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          174..396
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   DOMAIN          365..443
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  49474 MW;  2667CC957324AA83 CRC64;
     MGPVTDYPPN RRTSPGPPAL TPASAPGDTP AGNGASRPLA RLARETTPDN PWPLRLLSTK
     IDEYINKMTF VWVEGQIVQF NRRPGSGVQY LTLRDADADM SMSVSVFTRE LAAIEQATGT
     QVTEGARVVV HAKPRFWTKR GSLELRADDI RPVGIGDLLA RIEQLRRILA AEGLFDAERK
     HPLPFLPRKV GLVCGRNAKA KDDVIVNARL RWPGLPFEIR EVAVQGAQAV REVTAAIREL
     DADPEVDVIV VARGGGAVED LLPFSDEGLV RAAAAARTPI VSAIGHETDC PLLDLVADYR
     ASTPTDAARR IVPDLAEEMM GLDQARERLR TVLRSRLDAE QRGLDQVLAR PVMADPTLIV
     RDRIAELDQA RERMRRALSA TLSLATADLR ADHARLRALS PQGVLDRGYA ILRAPGVGII
     TSAQQLKKGD LIEGVLASGR LVAQVVGTTK PATPEP
//
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