ID A0A426GEZ2_9CAUL Unreviewed; 508 AA.
AC A0A426GEZ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=EIK80_19425 {ECO:0000313|EMBL:RRN62731.1};
OS Caulobacter sp. 602-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN62731.1, ECO:0000313|Proteomes:UP000268773};
RN [1] {ECO:0000313|EMBL:RRN62731.1, ECO:0000313|Proteomes:UP000268773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=602-1 {ECO:0000313|EMBL:RRN62731.1,
RC ECO:0000313|Proteomes:UP000268773};
RA Gao J., Sun J.;
RT "The genome of Caulobacter sp 602-1.";
RL Submitted (NOV-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:RRN62731.1}.
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DR EMBL; RRYI01000007; RRN62731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426GEZ2; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000268773; 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 14..107
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 130..470
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT REGION 469..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 54899 MW; 0CEEBFF641D91802 CRC64;
MSDLPPSDSN APPYSVSELA FALKRTLEDR YGFVRLRGEL SKVTHHSNGH VYLTIKDDKS
AIDGVVWKGN VRALSVRPEH GLEVIVTGKI TTYPAGSRYQ IVIDSMEAAG VGALLAQLER
LKAKLAAEGL FAPERKKPLP SMPAVVGVIT SPTGAVIRDI LHRIRDRWPC QVLVWPCVVQ
GDAAAVQVSA AIRGFNAIAP GGPVPRPDIL IVARGGGSVE DLWAFNDEAL ARTVAEGTIP
LISAVGHETD TTLIDFVSDR RAPTPTAAAE MATPVLAELR ALISDFDRRL NRSGARLIED
RRTRLVSAAR GLPRPDDILA LAQQRFDIAS GRLDAALHRN TTVHAQALLK VTARLTPEVL
TRQRAIKAER VGDLGRRLDL AARRAPDRVA QHARLPALWQ RLNAAGDRRL QRDAERLAGL
EKLRQSLNPE RPLELGFALV RKGDGTLARS ASDLVSGERV SLKFKSGDRD AVIDGEGGFV
PPPAPTSVPA PRPRPKPAAP PVDQGDLF
//
