ID A0A0B7FJX7_THACB Unreviewed; 730 AA.
AC A0A0B7FJX7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=RSOLAG1IB_02715 {ECO:0000313|EMBL:CEL57970.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL57970.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL57970.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL57970.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC DNA mismatch repair. {ECO:0000256|RuleBase:RU910737}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU910737};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000256|RuleBase:RU910737};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000256|ARBA:ARBA00010563,
CC ECO:0000256|RuleBase:RU910737}.
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DR EMBL; LN679102; CEL57970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7FJX7; -.
DR STRING; 1108050.A0A0B7FJX7; -.
DR Proteomes; UP000059188; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd09908; H3TH_EXO1; 1.
DR CDD; cd09857; PIN_EXO1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR037315; EXO1_H3TH.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00841; XPG_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU910737};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737, ECO:0000313|EMBL:CEL57970.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU910737};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU910737};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU910737};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU910737};
KW Nucleus {ECO:0000256|RuleBase:RU910737};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188}.
FT DOMAIN 79..149
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 80759 MW; 9F50DAC3F34D1868 CRC64;
MKQVRMLRHH GITPYIVFDG GPLPAKRGTE KDREEKRSKS LAQAQSLEAQ GRANGAYEYY
KKCIDITPQM AYQLIKALRA EGVSYVVAPY EADAQMTYLE REGIVDGIIT EDSDLVIFGC
RNLLFKLGQD GSCVNLRRDD LGAVSDLNLL GWSDKELRWM AMLSGCDYID SLPGIGLKKA
HKLLRKWKTV EKVIQAIRVE GSFKMPKEYP ESFKIAELAF LYQRVYDPVS QRLTHLGPPP
DEEWDESKDA FVGEDLPPDV AKKIAEGDFC PILRDAMVDI MPGFQPISRK GKTVSKDLPS
NPSVKDPHKS ISSYFGAATI SSQPKKYTPL PKFVSVKGSG RSTLSAQTME KTLSDEDWEV
MEIEGPTQPK PRPSTASRFF GDQSTPQKSR SSSRELAERK RKRADSLEEI ATPRASRTLV
PRWSGSLVDL TVDEENNKFI AESSNATSRS TSPDTFSLLQ DLSSPARPDR NSRSKSPESI
SGDLSSPEST RRLAPHPPLQ SRSSVGSAEL EGSPDQDPPM PTPMLTYNIL GTPLQASSSK
HTLQAKTTRR QSVVVDLREV FSQESVSEIS TSEEGPWTPS DPPIISQVPV NEGIPDLDDA
EYLSDDEKHQ AEATERQSRV AQGWIAQYGF KVVKGRKSLP SLSGTQPTAS PSPPRLSAPR
PTPVFQPLGM PKSRPKARGR KSEPALRAEI VIDDDDEDFL LGPGVVAEND IIVSSPERAA
ERFSRFKCPE
//
