ID A0A399T6D6_9BACT Unreviewed; 481 AA.
AC A0A399T6D6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=D1614_00390 {ECO:0000313|EMBL:RIJ50435.1};
OS Maribellus luteus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Maribellus.
OX NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ50435.1, ECO:0000313|Proteomes:UP000265926};
RN [1] {ECO:0000313|EMBL:RIJ50435.1, ECO:0000313|Proteomes:UP000265926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XSD2 {ECO:0000313|EMBL:RIJ50435.1,
RC ECO:0000313|Proteomes:UP000265926};
RA Zhou L.Y.;
RT "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT sediment.";
RL Submitted (AUG-2018) 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:RIJ50435.1}.
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DR EMBL; QWGR01000001; RIJ50435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399T6D6; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000265926; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000265926}.
FT DOMAIN 5..111
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 135..471
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT COILED 279..325
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 481 AA; 54757 MW; C84D9F0BFBFE74A7 CRC64;
MNQKLTLTEL NERIKDALLS AFPGTVWVVA EVSELKENRS GHCYLELVEK EGNTITARSR
ATIWSYTYRM LKPYFETTTG QLFTHGIKIL VQAAVEYHPA YGLSLNIRDI DPTYTVGDMA
LQRKQIIERL QQEGVFEMNK ELELPLVPQK IAVISSATAA GYQDFMNQLE SNEYGFRFYT
HLFEAYMQGA EAVPSIIRAL ERIFQYDDFF DAVVIIRGGG ATADLSSFDN YDLAINITQF
PLPVITGIGH EKDDTIIDLV AHTRLKTPTA VAEFLVNGVE RFYERLLELE NSIVQLSRET
LQFQKEKLED LAENLSDTVS EFIRDKQSSL SRTGTRLQQG VSSFSFGKQR ELIGQKHQLN
KVLSVWSVEA RNKLNRKHRI LRRVAGESLL KQQALLDRVQ RKVGTEARKR LSKEIERMRL
NENTVRLLTP ENVLKRGFTL TLKEGKIIKS AKGLKVGEEL ETRFADGNVK SKITNQSDNG
K
//
