ID A0A1W1V5N0_9DEIO Unreviewed; 402 AA.
AC A0A1W1V5N0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|RuleBase:RU004355};
DE EC=3.1.11.6 {ECO:0000256|RuleBase:RU004355};
GN ORFNames=SAMN00790413_00128 {ECO:0000313|EMBL:SMB88658.1};
OS Deinococcus hopiensis KR-140.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=695939 {ECO:0000313|EMBL:SMB88658.1, ECO:0000313|Proteomes:UP000192582};
RN [1] {ECO:0000313|EMBL:SMB88658.1, ECO:0000313|Proteomes:UP000192582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KR-140 {ECO:0000313|EMBL:SMB88658.1,
RC ECO:0000313|Proteomes:UP000192582};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004355};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family.
CC {ECO:0000256|RuleBase:RU004355}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWWU01000009; SMB88658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1V5N0; -.
DR STRING; 695939.SAMN00790413_00128; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000192582; 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-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR CDD; cd04489; ExoVII_LU_OBF; 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};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|RuleBase:RU004355};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004355};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU004355};
KW Reference proteome {ECO:0000313|Proteomes:UP000192582}.
FT DOMAIN 22..123
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 155..316
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 328..399
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 402 AA; 42889 MW; A9DC8303D6523BFF CRC64;
MTGRKRGKKA ETTRPPEQFL DLADVLAYVG QVIARGMPGA VWVRAEVASL TDRRHLYLDL
VQLEDGTEIA KCRATVWARE RYALEGKFRQ ATGGTLTAGL KVLLFCTAEF HPQYGFSLNV
LDVAPEFTVG DVALRLEALR ETLVREGVYG LNRLMTAPSD YARVAVISPS EAAGLGDFRR
EVDALARAGV TQFVYLEATF QGREASRSLT GAISGAREAH GKEPLDALVL IRGGGAVTDL
AWLNDLEVAR ALATFPAPVI TGLGHARDDT LPDEVACIRT DTPSKAAGLI VRTVAGAAAQ
AQQHVRAIRA QASEVLVSAD AAALWAVDRA RNAARRQVDA AQADTDALMR QALGLTPART
LARGYALVRD ADGQPVTRAA QVQPGEALTL EFADGAVGVR GE
//
