ID A0A0A0B6D5_9CELL Unreviewed; 407 AA.
AC A0A0A0B6D5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=Q760_01815 {ECO:0000313|EMBL:KGM01369.1};
OS Cellulomonas cellasea DSM 20118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM01369.1, ECO:0000313|Proteomes:UP000029833};
RN [1] {ECO:0000313|EMBL:KGM01369.1, ECO:0000313|Proteomes:UP000029833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM01369.1,
RC ECO:0000313|Proteomes:UP000029833};
RA Wang G., Zhuang W.;
RL Submitted (OCT-2013) 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:KGM01369.1}.
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DR EMBL; AXNT01000110; KGM01369.1; -; Genomic_DNA.
DR RefSeq; WP_052104300.1; NZ_AXNT01000110.1.
DR AlphaFoldDB; A0A0A0B6D5; -.
DR STRING; 1408250.Q760_01815; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000029833; 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; 2.
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:UP000029833}.
FT DOMAIN 15..108
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 132..345
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 316..401
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 407 AA; 43685 MW; 075D539396DC9720 CRC64;
MPLRALDTTA ERPWPVRLLS SKIAEYVARM APVWIEGQVV QLNRRPGAGV AFLTLRDTDV
DMSLPVSLKV GVLAASGAAV EEGARVVVHA KPEFWTKRGS LQMQADAVRA VGVGELLARI
EHLKGVLAAE GLFDARRKVP LPFLPRVVGL VCGRESKAEH DVVVNARARW PQVEFEIREV
AVQGVGAVAQ VSAAIAELDA DPRVEVIVVA RGGGAVEDLL PFSNEALVRA AAACRTPLVS
AIGHETDCPL LDLVADYRAS TPTDAAKHVV PDVGEERARL TQARSRMRGA LVHRLTREQH
GLDALRSRPV LAAPVRLVET REQDVHRLRD GARRALEQAV VRAGADTARL AAQVRALSPA
ATLARGYAVV QRADGAVVRD PQDVTQGEDL RVRVAHGEIH AAVTSGD
//