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Database: UniProt
Entry: A0A126Z1B0_9MICO
LinkDB: A0A126Z1B0_9MICO
Original site: A0A126Z1B0_9MICO 
ID   A0A126Z1B0_9MICO        Unreviewed;       422 AA.
AC   A0A126Z1B0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AX769_08810 {ECO:0000313|EMBL:AMM20244.1};
OS   Frondihabitans sp. PAMC 28766.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM20244.1, ECO:0000313|Proteomes:UP000070552};
RN   [1] {ECO:0000313|EMBL:AMM20244.1, ECO:0000313|Proteomes:UP000070552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA   Park H.;
RT   "Complete genome of Frondihabitans sp.";
RL   Submitted (FEB-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; CP014513; AMM20244.1; -; Genomic_DNA.
DR   RefSeq; WP_066278299.1; NZ_CP014513.1.
DR   AlphaFoldDB; A0A126Z1B0; -.
DR   STRING; 1795630.AX769_08810; -.
DR   KEGG; frp:AX769_08810; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000070552; 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:UP000070552}.
FT   DOMAIN          16..107
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          130..349
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   DOMAIN          311..399
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   REGION          401..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  45685 MW;  59C3B48341FE064F CRC64;
     MTIVTPPPTP ENPWPVGLLA GKVRDWIDRL GTAWVEGEIT QWNVAGGNVY GKLKDLEMDA
     TVSFSIWSSV KSRVPADLKQ GDRVIAAIKP NFWVKGGSLT MQVFEMRHVG LGDLLERLER
     LRRQLASEGL FGADRKRPLP FLPQCIGLVT GKDSDAEKDV LRNAQLRWPS VRFRVVHAAV
     QGDRMVGEVT AAIQTLDADP EVDVIIVARG GGDFQNLLGF SDEVLVRAAA AAHTPIVSAI
     GHEADRPLLD DVADLRASTP TDAAKRVVPD VGEELQAVRQ ARARLGQRLT HLINTEIDRL
     GQIRSRPVLA NPQTLIEVRA DELVRYVARS EELLHRTIER ASTRLSELTA GLRALSPEST
     LRRGYAIAQL PSGAVLRDVA DAPAETPLVL TLAAGTLGVT SSGPLTIPSE SATGSRGPDT
     AR
//
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