ID E1R4R4_SEDSS Unreviewed; 484 AA.
AC E1R4R4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Exodeoxyribonuclease I {ECO:0000256|ARBA:ARBA00019900};
DE EC=3.1.11.1 {ECO:0000256|ARBA:ARBA00012108};
DE AltName: Full=DNA deoxyribophosphodiesterase {ECO:0000256|ARBA:ARBA00031220};
GN OrderedLocusNames=Spirs_3051 {ECO:0000313|EMBL:ADK82152.1};
OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS (Spirochaeta smaragdinae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Sediminispirochaeta.
OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK82152.1, ECO:0000313|Proteomes:UP000002318};
RN [1] {ECO:0000313|EMBL:ADK82152.1, ECO:0000313|Proteomes:UP000002318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC {ECO:0000313|Proteomes:UP000002318};
RX PubMed=21304743; DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
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 -!- 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; CP002116; ADK82152.1; -; Genomic_DNA.
DR RefSeq; WP_013255611.1; NC_014364.1.
DR AlphaFoldDB; E1R4R4; -.
DR STRING; 573413.Spirs_3051; -.
DR KEGG; ssm:Spirs_3051; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_12; -.
DR OrthoDB; 9776650at2; -.
DR Proteomes; UP000002318; 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; 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 SMART; SM00479; EXOIII; 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};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADK82152.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000002318}.
FT DOMAIN 196..350
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51784"
FT DOMAIN 353..476
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 484 AA; 56056 MW; 1B1470EB39F12AB1 CRC64;
MARSIYWYDL ETFGTHPRLD RIAQFAGLRT DEALNELGEP LVLYCKITQD YVPDPKACLI
TGITPEETLR KGLSERRFIE RINEEFMQPG SCVAGFNSIA FDDEFIRATL YRNLMDPFRR
EWAGGNSRWD LLDVLRAARD LRPQGITWPE GENGRPTFRL EKLTEANALP HQNAHDALSD
VRATIAMARL LREKQPKIFS YLYRGRIKDH ARQLIDLHKR RPFLHTSAML SNEYGYTSIL
APVAPHPANQ NAILCFDLRQ DPEPLIERSV DELRRLIFAP SEELSLEESR IRLIPIHINR
SPVLAPLSTL DPDTAKRLGL DVTLCGKRAA KLAEASLLTQ KIMEVFRRDE AEIRRDPELE
IYSGGFFSDA DRQRMERFRE LSPEAMLKRR GDFYDRRLPE LAWRFVCRNH SEILDENERK
KWKSFCAGRL LFPPERLIND FAFFKRKVKE LSGDTNLPAG DKKIIKKLAE WATIIEVDVL
SYEG
//
