ID A0A317E8M5_9PROT Unreviewed; 470 AA.
AC A0A317E8M5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=DKG74_10875 {ECO:0000313|EMBL:PWR22912.1};
OS Zavarzinia aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=2211142 {ECO:0000313|EMBL:PWR22912.1, ECO:0000313|Proteomes:UP000245461};
RN [1] {ECO:0000313|EMBL:PWR22912.1, ECO:0000313|Proteomes:UP000245461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AS {ECO:0000313|EMBL:PWR22912.1,
RC ECO:0000313|Proteomes:UP000245461};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-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}.
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:PWR22912.1}.
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DR EMBL; QGLE01000005; PWR22912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317E8M5; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000245461; 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:UP000245461}.
FT DOMAIN 14..106
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 130..445
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 51009 MW; 3209D2A6D5F46B29 CRC64;
MSMEDAAAPN LPEMSVSELS GLLKRTVEDR FALVRVRGEL SGVKRHSSGH LYFALKDADA
VLDGVAWRNV AGRLKFRPED GLEVIATGRL TTYPGRSKYQ ILAESLEPAG AGALMALLEE
RKRKLAAEGL FAAERKRPLP FLPQVIGVVT SPTGAVIRDI LHRLADRFPR PVLVWPVAVQ
GEGAADQVAR AIRGFNAIAP GGAIPRPDLL IVARGGGSLE DLWAFNEEVV VRAAAESAIP
LISAVGHETD TTLIDFASDR RAPTPTAAAE MAVPVRADLL DRVEELGGRA RMATRRLLVE
HDTRLSGLAR GLRHPRSLIE AGEQRLDDLA ERLPRALRGL IADRRRQLAE VSGGLRPHVL
TGELRQKAER LAQVSERLAP AARRLFERAE RQLATPAQLL ESLSYHRVLS RGYAVVRRAG
KLETAAAALH PGDALEIEFA DGRVGAVAAG DPPRRRRKTD LPPPEQGTLI
//
