ID A0A080LW51_9PROT Unreviewed; 469 AA.
AC A0A080LW51;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
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:KFB71965.1};
GN ORFNames=AW09_002862 {ECO:0000313|EMBL:KFB71965.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB71965.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB71965.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:KFB71965.1}.
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DR EMBL; JDVG02000460; KFB71965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080LW51; -.
DR Proteomes; UP000020077; 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}.
FT DOMAIN 19..109
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 134..444
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 469 AA; 50950 MW; 1D5CE53A726DA652 CRC64;
MPDLLPNSAD LATPLPVIPV SLLNRLARER LEAAFPLCWV AGEVSNLSHA SSGHVYFSLK
DSAAQVRCVL FRSRAQLLGW RLENGQHIEA CVLVTLYEVR GDFQLTVEAA RRTGIGNLYD
QFLRLKDKLA REGLFDSTAK RPLPAFPRRV GIVTSLQAAA LHDVLSTLRR RAGQVGIVIY
PTQVQGDGAA SQIAAAIRCA GERRECELLI VCRGGGSIED LWAFNDEAVA RAIRACPLPV
ISGVGHETDF TIADFAADQR APTPTAAAEL AAPEQAALLA RLAACRFALR RQIEQNLNQR
GQQLDWLAHR LQRPAQYLAR HQDHLHKLQR RLGAGLLQAS AQARATLVSV TRRLLLSRPD
PVRQAGHLEA LAARLCSAWQ TTTQARYADL DRLAAGLAHL NPAAVLARGY CVVSNAQGQI
VRESKVLEPG QQIAVFFQRG RAEAAVLTVF EDDGIAFAAP AIASATSPE
//
