EX1_BUCAI
ID EX1_BUCAI Reviewed; 413 AA.
AC P57620;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=BU555;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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}.
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; BA000003; BAB13247.1; -; Genomic_DNA.
DR RefSeq; NP_240361.1; NC_002528.1.
DR AlphaFoldDB; P57620; -.
DR SMR; P57620; -.
DR STRING; 107806.10039213; -.
DR PRIDE; P57620; -.
DR EnsemblBacteria; BAB13247; BAB13247; BAB13247.
DR KEGG; buc:BU555; -.
DR PATRIC; fig|107806.10.peg.560; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_0_0_6; -.
DR OMA; FIYVNRC; -.
DR Proteomes; UP000001806; 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; 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 SMART; SM00479; EXOIII; 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; Reference proteome.
FT CHAIN 1..413
FT /note="Exodeoxyribonuclease I"
FT /id="PRO_0000087107"
FT DOMAIN 12..193
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 202..349
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT DOMAIN 350..413
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 113
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 124
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 128
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 142
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 148
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 181
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 214
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 257
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 299
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 363
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 366
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
SQ SEQUENCE 413 AA; 49151 MW; 52B4779AC3FA6188 CRC64;
MIQFQKKTPN FLFYDYETFG IHTALDKPAQ FACIRTDINL NIIDDPQYFY CFPSDDYLPD
PGSVLITHIT PQYTEKNGTN EYNFSQKIYD ILMQSNTCVV GYNNINFDDE ITRNIFYRNF
FDPYEWSWKN GNSRWDILNL LRACYALRPT GINWPKNELG LTSFKLSDLT KTNNIVHLNA
HNAVSDVYAT IEIAKLVKKK QPRLFDFFFK IRKKNELYKL IDLRNFQPII YISAYFGAIY
HNMSCILPIA WHENNSNILI AIDLFKDIKT LINMCKKICF DSIFIKNLLD SGVVLLHLNR
CPILAPIQVI RKEDYNRLNF HRFSLNKKIE LIKKNMFFIQ NIKIIFSKNN NTNQFFNVDL
EIYNGFFNSK DKKKIQIIRN TDPVFLKHIF CNFHDSRLKN LFFRYRARNF FIH
