ID   C6HPI4_AJECH            Unreviewed;       895 AA.
AC   C6HPI4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Isochorismatase family {ECO:0000313|EMBL:EER37856.1};
GN   ORFNames=HCDG_08115 {ECO:0000313|EMBL:EER37856.1};
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:EER37856.1, 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   -!- SIMILARITY: Belongs to the isochorismatase family.
CC       {ECO:0000256|ARBA:ARBA00006336}.
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DR   EMBL; GG692433; EER37856.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HPI4; -.
DR   STRING; 544712.C6HPI4; -.
DR   VEuPathDB; FungiDB:HCDG_08115; -.
DR   eggNOG; ENOG502QRZN; Eukaryota.
DR   HOGENOM; CLU_005335_0_0_1; -.
DR   OMA; KMYHLSG; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   CDD; cd00431; cysteine_hydrolases; 1.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032854; ALKBH3.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF5; ISOCHORISMATASE FAMILY PROTEIN FAMILY (AFU_ORTHOLOGUE AFUA_3G14500); 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT   DOMAIN          565..702
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          91..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  98551 MW;  71E8D0D0F41F6DA8 CRC64;
     MFPANLLSQS FPNVPCRKAL LILDLQNDFV KPDGALFVRN VPEFLDTVAA LAQRFRETGE
     VVWVQTQFEH RRPIFSPESG GEVIVVDKLL ASGNNNDDDN DNDNDNDNTT SKSANDKAKG
     ANIRSHLSSH SARHRSENTG NTNSSSNGGA KDGSGRPNSS QRRQKRISGG ESRREQFSVY
     SDDPEAFLSV LPKGDGARRC CLQKTVGCQF PAPILSAIDH ERDTILVKSD YSAFQSESLL
     LSFRTQFVRE LYICGSLSNV SVYATALDAV SHGLDVILVE DCLGFRSFAR HEEAMRRMAD
     MMGANGITSK ELAEEQDWEE AAVPSSEWPE HSAASTPVGI EDDMGVLAVK SPPKQPSPQK
     SDDAPLDVED QEPEGDELAD DLLEPSLRST APQPREAPLT SASATATTPS SDLKGKSNRA
     RMRKPRRTVS RDDTSQAERT QSQRQSVDMQ QLCGATSGTR RSRKSKHNQT DLGPDDSIGE
     GDSRIIYDLA LPPKSFQLLR EEVNWQKMYH LSGQVPRLVA VQGAVQPDNS VPIYRHPADE
     SPPLFPFSKI VNNVRHVVEK HIGHPLNHVL IQLYRDGQDR ISEHSDKTLD IVRGSYICNV
     SFGAQRTMTL RTKSSAAKAA ASTGDTSDAA DGGDEETPKE SSTERQTQRI PLPHNSLFIL
     GEKTNMRWLH AIRADKRPES EKSPEELAYG GQRISLTFRH IGTFIHPESD TIWGQGAISK
     TKQTAGQVIH GDCTETTQMI RAFGQENQQS DFNWEANYGQ GFNVVNFVTT SAGKLRLSGD
     DVADLRVQIC FAEYGVRYDI VAIDDFPAAL KGTLSLPHKS GNLEPRPVYM DVDGSTCFTG
     DDYDGLLRGA ATSQAVSRWP ALWHRGLCAV ARRARYHSRG RPPGRDALSV LDSLL
//