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Database: UniProt
Entry: A0A231HHY4_9BURK
LinkDB: A0A231HHY4_9BURK
Original site: A0A231HHY4_9BURK 
ID   A0A231HHY4_9BURK        Unreviewed;       455 AA.
AC   A0A231HHY4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=PuT2_12195 {ECO:0000313|EMBL:OXR48448.1};
OS   Pusillimonas sp. T2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1548123 {ECO:0000313|EMBL:OXR48448.1, ECO:0000313|Proteomes:UP000216496};
RN   [1] {ECO:0000313|EMBL:OXR48448.1, ECO:0000313|Proteomes:UP000216496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2 {ECO:0000313|EMBL:OXR48448.1,
RC   ECO:0000313|Proteomes:UP000216496};
RA   Yuan M., Qiu J.G., Ma Y.;
RT   "The genome sequence of Pusillimonas sp. T2.";
RL   Submitted (JUN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXR48448.1}.
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DR   EMBL; NIQA01000008; OXR48448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231HHY4; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000216496; 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; 1.
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:UP000216496}.
FT   DOMAIN          20..112
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          136..446
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   455 AA;  49776 MW;  3C5CBAB243A1AE4D CRC64;
     MTTNPSFSTD LPAAGADTVL TVAQLNRQVG NLLEGSFSRI WVRGEVSNFT QAASGHWYFT
     IKDERASVRA VMFRGRAQAV SFVPKAGERF EFRATVTLYE PRGDYQLQVE TLRRAGQGDL
     HEAFIRLKEK LTAEGLFDPS RKRALATMPR AVGVITSLAA AALHDVLTAM ARRAPHVPVI
     VYPAPVQGEG AAAQLRQALH AAIDRNEVDT LLLVRGGGSL EDLWSFNDEA LARAVAASPI
     PVICGVGHET DFTICDFVAD LRAPTPTAAA ELSCVARQEC LDQVEDLVVA LARQQRRILE
     RAALRLDRAM AQLVSPQQRL AQQRRQISTL QQQLWRAVCR HSELEGARLN LLKTRLGAAL
     PPVARRRREL DALQRRLLAA GARQLRAPQA RLDAAALTLQ ALSPRKILAR GYALVRDPRG
     ELVKNALDLS AGDRLTLELS QGSADVEVLK TTGLL
//
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