EX1_BUCAP
ID EX1_BUCAP Reviewed; 482 AA.
AC Q8K923;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Exodeoxyribonuclease I;
DE Short=ExoI;
DE Short=Exonuclease I;
DE EC=3.1.11.1 {ECO:0000250|UniProtKB:P04995};
DE AltName: Full=DNA deoxyribophosphodiesterase;
DE Short=dRPase;
GN Name=sbcB; OrderedLocusNames=BUsg_537;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive
CC manner. Also functions as a DNA deoxyribophosphodiesterase that
CC releases deoxyribose-phosphate moieties following the cleavage of DNA
CC at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or
CC AP lyase. {ECO:0000250|UniProtKB:P04995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:P04995};
CC -!- SUBUNIT: Monomer. Interacts with ssb (via C-terminus); this interaction
CC stimulates the exonuclease activity by recruiting the enzyme to its
CC substrate. {ECO:0000250|UniProtKB:P04995}.
CC -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
CC terminal domain form a central positively charged groove which binds
CC the DNA. {ECO:0000250|UniProtKB:P04995}.
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DR EMBL; AE013218; AAM68078.1; -; Genomic_DNA.
DR RefSeq; WP_011054044.1; NC_004061.1.
DR AlphaFoldDB; Q8K923; -.
DR SMR; Q8K923; -.
DR STRING; 198804.BUsg_537; -.
DR PRIDE; Q8K923; -.
DR EnsemblBacteria; AAM68078; AAM68078; BUsg_537.
DR KEGG; bas:BUsg_537; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_6; -.
DR OMA; RDRPAQF; -.
DR OrthoDB; 768812at2; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR023607; Exodeoxyribonuclease_I.
DR InterPro; IPR034748; EXOI_C.
DR InterPro; IPR034747; EXOI_SH3.
DR InterPro; IPR038649; EXOI_SH3_sf.
DR InterPro; IPR013620; Exonuc_1_C.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; PTHR11046; 1.
DR Pfam; PF08411; Exonuc_X-T_C; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51785; EXOI_C; 1.
DR PROSITE; PS51784; EXOI_SH3; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease.
FT CHAIN 1..482
FT /note="Exodeoxyribonuclease I"
FT /id="PRO_0000087108"
FT DOMAIN 13..194
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 203..351
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT DOMAIN 355..471
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 114
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 125
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 129
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 143
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 149
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 182
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 215
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 258
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 300
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 364
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 367
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
SQ SEQUENCE 482 AA; 57565 MW; B754EAAA4F7A84B2 CRC64;
MKNILKKNEV NFLFYDYETF GIHTSLDKPA QFSSIRTDKN FNIMEEPKCF YCFPSDDYLP
DPSSILITGI TPEYTEKHGF NEYKFSKKIH DVLLKPNTCI IGYNNINFDD EITRNIFYRN
FLDPYEWSWK NNNSRWDLLN VVRACYALRP SGIQWPKNEF GLPVFKLSDL TQKNNISHYN
AHDATSDVYA TIELAKLIKR KQPKLFDFFF KYRKKNELCR LIDIEKFTPI IYVSSYFGAL
RQNMSCILPL SWDLHNKNIL ISIDLFKDID KLIVFCKTVS ISNISIKDLF DLGIVLVYLN
RCPILAPIKV IRKEDTNRLN FKKYFYYKKI NLVKKNYFLI DLVKNVLLKK NENKNSLNVD
LQIYDSFFNF HDKNLIKKIS LTKSSDLKKM KLDFKDPRLK ELFFRYKARN FFNILKNDEK
KEWINYCLKT LNSFFLTGYI DKIESLLKIY SYDVKKNNLL SDLLKYVFKK YKKVFYKNIN
LS
