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Database: UniProt
Entry: A0A0L0T0I9_ALLM3
LinkDB: A0A0L0T0I9_ALLM3
Original site: A0A0L0T0I9_ALLM3 
ID   A0A0L0T0I9_ALLM3        Unreviewed;       837 AA.
AC   A0A0L0T0I9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   03-MAY-2023, entry version 27.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN   ORFNames=AMAG_12971 {ECO:0000313|EMBL:KNE68303.1};
OS   Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS   macrogynus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE68303.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE68303.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE68303.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-2009) 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|RuleBase:RU910737}.
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DR   EMBL; GG745356; KNE68303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0T0I9; -.
DR   EnsemblFungi; KNE68303; KNE68303; AMAG_12971.
DR   VEuPathDB; FungiDB:AMAG_12971; -.
DR   OrthoDB; 126305at2759; -.
DR   Proteomes; UP000054350; 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; 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; 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; 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.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU910737};
KW   DNA excision {ECO:0000256|RuleBase:RU910737};
KW   DNA repair {ECO:0000256|RuleBase:RU910737};
KW   DNA-binding {ECO:0000256|RuleBase:RU910737};
KW   Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW   Exonuclease {ECO:0000256|RuleBase:RU910737};
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:UP000054350}.
FT   DOMAIN          1..99
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          138..206
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          425..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  89784 MW;  14D0FCEFB32D052D CRC64;
     MGIPGLLPLL ADIHEPVHLA QFRGRAIAVD AFAWLHRAAH ACAPDLALGR PTTKYLSFCR
     NRLLLLRQHG ITPVVVFDGA PLPLKAGTNA DRSARRADAR QRAHALVAAG KHADAEPLFK
     QCISVTPAMV QALISLCEEL DVPHIVAPYE ADAQLAYLER SGYVDAVLTE DSDLLVFGAR
     RVLVKLGPDG HATLLDRARL TTDVKQPVSL VRWPTVRFLD WCILGGCDYL PSLPRVGLKT
     AAKLLQRATG MNREYSPSTV LRSVLRIAAT EYKPIPTDYA ARFDMARRTF LHQRVFCPRS
     QKLVHLRPWN GTTETAPDYL GADIDPNMAV AIAVGAIDPV TRVAHRAVRP LHRFFLERRR
     DAGAWEVPVL AVSVPRTVQR TRSMPLAFQP ATTAAAAPHA KPAPAPAVSA AATNRVLARP
     LSRSHSFQVA PAPPVPRGGS AVPATAFGGF RDTVSSSSSS SSSSGGTSTA SPSPQYAVDD
     DDMYAVDVFQ EFEDELVIQP PPQPKVQKKK ASPYFAGKQK QQHEREKEPE VRAVLVPTVF
     ARPLSPQARP QQHQEQNPRA VLVPTVRVRP ISPSPPPPPM RTVIVGTALA FSVAPSSPCL
     DVPSTSSPVP AATRRVTVDL GPPSSPCFGV PGAAEWIDED GSDEDAWSGG MGDADEGDGS
     DSTPAPTTTR RFEVCVETKS GMSSSQWFPP YNRTAQTTSA VGPPVPVCAP GYEEARAHGR
     AAPPAYRAPA HEPNRTITSF FARASAPPST ASTPGPARKY ASPTLTPAPA PALVPRDNRA
     ATGFPGYSRD RRPTFSDAVP PPAKRVALDA QWPAKTPARP VDRPSPPAGT RLTDVLS
//
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