ID A4BV62_9GAMM Unreviewed; 477 AA.
AC A4BV62;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 72.
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=NB231_00455 {ECO:0000313|EMBL:EAR20404.1};
OS Nitrococcus mobilis Nb-231.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Nitrococcus.
OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR20404.1, ECO:0000313|Proteomes:UP000003374};
RN [1] {ECO:0000313|EMBL:EAR20404.1, ECO:0000313|Proteomes:UP000003374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR20404.1,
RC ECO:0000313|Proteomes:UP000003374};
RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR20404.1}.
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DR EMBL; AAOF01000023; EAR20404.1; -; Genomic_DNA.
DR AlphaFoldDB; A4BV62; -.
DR STRING; 314278.NB231_00455; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR Proteomes; UP000003374; 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:UP000003374}.
FT DOMAIN 23..116
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 139..454
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT COILED 325..352
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 477 AA; 54025 MW; 8D8A2CDED7AD91A8 CRC64;
MSCYHLGMSE PHPLSHETRR DVYTVSRLNQ EVRLLLEHAL PLLWVEGEIS NLSQPRSGHL
YFTLKDEAAQ VRCAMFRNRS LYLRFRPKDS LHVLARARIS LYAPRGDFQL IIEHMEEAGD
GALRRAFEAL KNRLAQEGLF AAEHKKPLPA LPRRIGVVTS PSGAALRDVL SVLRRRFPAI
RVLIYPVAVQ GANAPGEITA TIRLAARRRE VDALLLTRGG GSLEDLWAFN EEAVARAIHE
CPLPIVSAVG HETDTTIADF VADQRAPTPS AAAELLSPDG PGWLTRIDHL AERLRQGLRR
GLERQRHGLG RLERRLANQH PGRRLQERAQ RLDELEQRMT RAERGRRREL TTRHGHLADR
LHRQDPRCRV RERLEQIAAL RRRLHAALGQ DLGSRRQLLA ATVRALEAVS PLKTLGRGYA
IVRRQRDDHI VRRPSEVTPG ERVSARLYSG ELVCRVEALR ETSDAHTLPG RSHETDE
//