ID A0A380BPX7_SPOPA Unreviewed; 451 AA.
AC A0A380BPX7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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:SUJ04763.1};
GN ORFNames=NCTC4822_01587 {ECO:0000313|EMBL:SUJ04763.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ04763.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ04763.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UGYZ01000002; SUJ04763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380BPX7; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000254519; 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:UP000254519}.
FT DOMAIN 7..102
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 125..438
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 451 AA; 51274 MW; 3C9AAF5340315E95 CRC64;
MTKNPYLTVQ ALTKYVKRKF DADPHLRQVY VKGELSNVTL HPSGHIYFTL KDDKSRIRAV
MFKMNALKLK FRPENGMNVL IIGDVSVYEA SGQYQLYVQT MQPDGIGALY LAFEQLKEKL
EQEGLFNEKW KVPLPTYPAT VGVVTAQTGA AIQDICSTIS RRYPLAEILL FPAVVQGSQA
APSIVEAIEQ ANRYSGIDVL IVGRGGGSIE DLWAFNEEIV ARAIFSSRIP VISAVGHETD
TTIADFVADK RAPTPTAAAE LAVPSREELI DRTLDRKRAL YRAFSYKIKH EQKRLTTLQT
SYPLQFPERL YRPFIEKHIH LDERLRRSPK SIIERDEVQL ERLTNRLKTM SPMYRVNEAA
REISVLTNRL MTTSTHDLKQ RQNRFSSTVR MLTSLNPLHV IERGYSIVYQ DEKVQKSVEK
LEVGSTVDIK MQDGTAKAMI KSIHKDDLEE S
//
