ID A0A179UMT3_BLAGS Unreviewed; 857 AA.
AC A0A179UMT3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=BDBG_05091 {ECO:0000313|EMBL:OAT09284.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT09284.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657457; OAT09284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179UMT3; -.
DR STRING; 559298.A0A179UMT3; -.
DR VEuPathDB; FungiDB:BDBG_05091; -.
DR OrthoDB; 126305at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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 SMART; SM00485; XPGN; 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:OAT09284.1};
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:UP000002038}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 138..208
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 93169 MW; F1AE4D1140D67FE4 CRC64;
MGITGLHGLL KSIQKPCNLR KFKGQTFGVD AYGWLHRGTV ACAIDLALDK HNTKYVDFAM
NRVRMLLYFG VTPYLVFDGD HLPSKAGTET ARAQRREESK KLGLELYRSG RVTEAHQELQ
KAVDVTPYMA RLMIEELKKL KIQYVVAPYE ADAQLVYLEK QGMINGIISE DSDLLVFGAK
RLLSKLDKHG DCVEINRGDF TACRDISLIG WTDADFRLMC ILSGCDYLAN LPKMGLKTAY
RNVRKYKTVE KILKMLQFEG NGARVPPQYL EDFKRAELTF LHQLVFCPLA RKLVTLSPLP
EHTSLDSMPF VGAYIEPDTA IGVACGDLDP ITKEPINLQP SYPERSRLLV SRRQTLPSTT
DLKQSKPIDS FFTPKRVPLG ELDPNSLTPS PSQQRLIEAN ARRSWVASSV PTRGNVRRAT
SSFFPPNTAS PSTSSTRVFP PRTTKTPLSS DREKFLASAS TVSKFQPVKR QRLCSDADEA
GAEAAAAVLG TEKRSRFFAG AGKGTGMGTT VGAKSSGSAG ISNADKARTK KAKRADFGVF
SDNVVEDIML QLPDGVSQAE TRDADGVNNM SEDGLSITQS KIEEGGESIE DIGSSIADAL
LNRNFPEEEP TATTTGLTQA MTGISTGGSD SQLSARMLEY EDEGLDDGDA CVNSSSCSLG
LRDKFGYVES NRRSEADHGT AAGNEHVYQN QHCEGEVGGE GGKIEKSPAP HTAQGQQRQP
SRMTALQRLG QSALYRSKSM GSLRTAKTSL MGGDEKDNNK GESEGVDAVD DDGGVTPSRS
GSCYSRPGGG RERCLSAAMM KHQSRGSEDL IIPDSEGESE VELEVDVLNE GEEKGRQTEK
GAAVDFKQFL FTGSGSG
//
