ID A0A0S4L3P3_9BACT Unreviewed; 465 AA.
AC A0A0S4L3P3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:CUS32316.1};
GN ORFNames=COMA1_10566 {ECO:0000313|EMBL:CUS32316.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS32316.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS32316.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS32316.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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; CZQA01000001; CUS32316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4L3P3; -.
DR STRING; 1742972.COMA1_10566; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000199032; 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:UP000199032}.
FT DOMAIN 25..117
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 141..455
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 465 AA; 50913 MW; 65B586BB0241198F CRC64;
MRRGLTHTKP SSSLFPLDSP SRQVLTVSEL TAMVRASLET SFSEVWLEGE ISNLRAPGSG
HLYCTLKDQT SQIRAVIFRS TALRLRFGLE DGLHVIVRGR VSVYEPRGEY QLILDHVEPR
GLGALQLALE QLKRRLEDEG LFDVTRKRSL PALPRTVGLV TSATGAAVRD MMAVLHRRCP
IVRIILVPVS VQGDGSAEQI VAAIDALNQL EAVDVIIVGR GGGSLEDLWS FNEEIVVRAV
ACSAVPIVSA VGHETDVTLT DFAADVRAPT PSAAAELVVP VLAELVERLE LLVTRARQAI
TAQCVEQHQR LDLVLAEMGH IRLRILKEAQ RVDEAVADLR EATQATLRSA MVDAQAWTQA
LMSQNPVFRV HRDLGIIPQL RSRLAAAMDH VVTQKMQLTR GTLWRLNGLS PLAILERGYA
ILEMVPSRQV IRGVEQVAVG DEVVARLTNG QVRCTVNDVT SNPSV
//
