ID A0A1Q8ZHD1_9CYAN Unreviewed; 422 AA.
AC A0A1Q8ZHD1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BST81_03915 {ECO:0000313|EMBL:OLP19696.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP19696.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP19696.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
RL Submitted (NOV-2016) 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:OLP19696.1}.
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DR EMBL; MQTZ01000011; OLP19696.1; -; Genomic_DNA.
DR RefSeq; WP_075597234.1; NZ_MQTZ01000011.1.
DR AlphaFoldDB; A0A1Q8ZHD1; -.
DR STRING; 1922337.BST81_03915; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000186296; 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:UP000186296}.
FT DOMAIN 15..109
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 134..303
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 289..403
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 422 AA; 47390 MW; 70F13D564133C154 CRC64;
MSSPFPNLLV PDTALSVGSL TTYIQTVLEQ DDRLQQIWVI GEVSSATQYR SGLFFTLQDP
DIKASINCVV WNSQLHKLAT LPVQGAQLIL LGRIHLHPQR GQYQLIIWQA LPAGEGLRAL
RYRQLRDRLE IEGLFDPARK RPIPSHPQTI AVVTSPQAAA WGDIQRTLKR RYSGLHVLLS
PALVQGEQAP ASIVTAIRRV EQDGRAEALI LARGGGATED MACFNDERVV RAVATCSIPV
IAGIGHQRDE SLADLAADIC AHTPTAAAEQ SVPLLADLYL EHRNRVAWLQ DASSHYLNML
RTHEQRLRDR LQRLHPERQL QREMQFMRWQ RQRLLRATTQ HLRQADQHCQ MLKQKLATLD
PQAVLRRGYA VVRQTDGTIA RSSQTLHLNE ELLVQLGQGQ IKVKVTDMMN LDASTNADVN
LP
//
