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Database: UniProt
Entry: A0A2K8UFB5_9GAMM
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ID   A0A2K8UFB5_9GAMM        Unreviewed;       483 AA.
AC   A0A2K8UFB5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Exodeoxyribonuclease I {ECO:0000256|ARBA:ARBA00019900, ECO:0000256|PIRNR:PIRNR000977};
DE            EC=3.1.11.1 {ECO:0000256|ARBA:ARBA00012108, ECO:0000256|PIRNR:PIRNR000977};
GN   ORFNames=THSYN_27100 {ECO:0000313|EMBL:AUB84242.1};
OS   Candidatus Thiodictyon syntrophicum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiodictyon.
OX   NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB84242.1, ECO:0000313|Proteomes:UP000232638};
RN   [1] {ECO:0000313|EMBL:AUB84242.1, ECO:0000313|Proteomes:UP000232638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cad16T {ECO:0000313|EMBL:AUB84242.1,
RC   ECO:0000313|Proteomes:UP000232638};
RA   Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT   "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT   strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT   an alpine meromictic lake.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000563,
CC         ECO:0000256|PIRNR:PIRNR000977};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000977-2};
CC       Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000256|PIRSR:PIRSR000977-
CC       2};
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DR   EMBL; CP020370; AUB84242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8UFB5; -.
DR   KEGG; tsy:THSYN_27100; -.
DR   OrthoDB; 9763470at2; -.
DR   Proteomes; UP000232638; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd06138; ExoI_N; 1.
DR   Gene3D; 1.10.287.1240; -; 1.
DR   Gene3D; 3.30.1520.20; Exonuclease ExoI, domain 2; 1.
DR   Gene3D; 1.20.1280.70; Exonuclease ExoI, domain 3; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF08411; Exonuc_X-T_C; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51785; EXOI_C; 1.
DR   PROSITE; PS51784; EXOI_SH3; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR000977};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR000977};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR000977};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000977};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000977-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000977-2};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000977};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232638}.
FT   DOMAIN          196..349
FT                   /note="ExoI SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51784"
FT   DOMAIN          356..479
FT                   /note="ExoI C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51785"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
SQ   SEQUENCE   483 AA;  53481 MW;  8EAFC3F602D53E9D CRC64;
     MAATFYWHDY ETWGVDPRRD RPCQFAGQRT DEDLNPVGEP LVLYCRPALD LLPQPEACLV
     TGITPQLADA KGLIEAEFTA AIADVLSVPG TCGTGYNSIR FDDEVTRHLL YRNLRDPYAR
     EWQHGNSRWD LIDILRLAQA LRPEGIVWPL RDDGTASFRL EDLTAANAIP HAGAHDALID
     VQATIALARL LRRAQPRLYD YALRLRDKRE VRTMLEKGEP LVHASARFPA ALGCIAPVVA
     VAQHPTNGNG VICLDLRADP DQLLDLSVEE LRRRLFTPSA QLPAGVERIP LKTVQVNHSP
     VLAPLKTLTA AAAARWSIDP AQVVRRAQTV RDKAAAIRAR VQAVHQPAPE GPNGQSATDP
     DLMLYSGGFL SDADRRTLER VRALAPADLA AANPRFADPR LPQMLFRYRA RNWPETLSPE
     EREEWDAWRL TRLTDPQAGG SIQLDQYEAQ LAALAQTHAA DPAKRQVLDQ LGAWAEALMD
     AGD
//
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