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Database: UniProt
Entry: C6HJ44_AJECH
LinkDB: C6HJ44_AJECH
Original site: C6HJ44_AJECH 
ID   C6HJ44_AJECH            Unreviewed;       383 AA.
AC   C6HJ44;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|ARBA:ARBA00012720};
DE            EC=4.2.99.18 {ECO:0000256|ARBA:ARBA00012720};
GN   ORFNames=HCDG_06078 {ECO:0000313|EMBL:EER39856.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER39856.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001668};
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409}.
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DR   EMBL; GG692428; EER39856.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HJ44; -.
DR   STRING; 544712.C6HJ44; -.
DR   VEuPathDB; FungiDB:HCDG_06078; -.
DR   eggNOG; ENOG502QVDB; Eukaryota.
DR   HOGENOM; CLU_038423_0_1_1; -.
DR   OMA; EKFPEHW; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd08972; PF_Nei_N; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.20.190.10; MutM-like, N-terminal; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1.
DR   PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EER39856.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT   DOMAIN          2..135
FT                   /note="Formamidopyrimidine-DNA glycosylase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51068"
FT   REGION          290..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   383 AA;  42707 MW;  A54105054DCFA82B CRC64;
     MPELAEVARI VHYICSNLVG KTITKVHAQH DPVVFGKAGT SATEFKKHME GKKIVGSGQQ
     GKYFWIIMSS PPHPVMHFGM TGWLKFTNVN THYSRTAPSP KNEEPVWPPK FWKFRLQLDD
     SSNSEAAFVD PRRFGRVRLV DCPGAEIRKH SPLKENGPDP ILDKDIMTLD WLKKKLTSKK
     VPIKALLLDQ ANISGIGNWM GDEILYHAKI HPEQYCNTIP EAQIEQLHSA INYICSMSVD
     LLGDSEKFPA DWLFKHRWGK GKQNRSQNLP NGDKIVFITV GGRTSAVVPS VQKKTGPVAA
     DAEDEVTEID ELPPPKKKKG ATAKENKGAE NPKEESSTKK AATKKSKVEP TVEGDEEAHG
     QKQKAVAQTE SSSRRGKSFR SRK
//
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