ID A0A1N7S3A1_9BURK Unreviewed; 459 AA.
AC A0A1N7S3A1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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 ECO:0000313|EMBL:SIT41847.1};
GN ORFNames=BN2475_320058 {ECO:0000313|EMBL:SIT41847.1};
OS Paraburkholderia ribeironis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT41847.1, ECO:0000313|Proteomes:UP000187012};
RN [1] {ECO:0000313|EMBL:SIT41847.1, ECO:0000313|Proteomes:UP000187012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM7296 {ECO:0000313|EMBL:SIT41847.1,
RC ECO:0000313|Proteomes:UP000187012};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYGX02000032; SIT41847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7S3A1; -.
DR STRING; 1247936.BN2475_320058; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000187012; 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 Gene3D; 2.40.50.1010; -; 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:UP000187012}.
FT DOMAIN 20..111
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 135..445
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 459 AA; 50569 MW; 571E57EB2A05E852 CRC64;
MNSDNPFASP ATPGGEVVVP VSALNRAIGA MLERSFPLVW VAGEVSNFTR AASGHWYFSI
KDAQAQMRCV MFRGRAQYAE FTPREGDRIE VRALVTMYEP RGELQLNVEA VRRTGQGRLY
EAFLRLKAQL EAEGLFAAER KRALPAHPRA IGIVTSLQAA ALRDVLTTLS RRAPHIPVIV
YPAPVQGAGV SSKLAAMVDA ASARREVDVL IVCRGGGSIE DLWAFNEEVL ARAIAQSAIP
VVSGVGHETD FTIADFAADM RAPTPTGAAE LVSPQRVLLL RELDHRHATL ARGFGRMMER
RAQQLDWLAR RLVSPTERLA RQRIHLQQLS VRLASAGARP LRDARARFVL LQMRWQRWRP
DLAAHRARLG NLAQRLDAAL LRQHERQVAR IGTLAARLEV LSPQRTLERG YAAMLDAQSG
RAVRAPSSLK PGRRFTVHLA EGSADIALAD VQTRLADGF
//