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Database: UniProt
Entry: Q4WYW5_ASPFU
LinkDB: Q4WYW5_ASPFU
Original site: Q4WYW5_ASPFU 
ID   Q4WYW5_ASPFU            Unreviewed;       828 AA.
AC   Q4WYW5;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Isochorismatase family protein family {ECO:0000313|EMBL:EAL92138.1};
GN   ORFNames=AFUA_3G14500 {ECO:0000313|EMBL:EAL92138.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL92138.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL92138.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the isochorismatase family.
CC       {ECO:0000256|ARBA:ARBA00006336}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL92138.1}.
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DR   EMBL; AAHF01000002; EAL92138.1; -; Genomic_DNA.
DR   RefSeq; XP_754176.1; XM_749083.1.
DR   AlphaFoldDB; Q4WYW5; -.
DR   STRING; 330879.Q4WYW5; -.
DR   EnsemblFungi; EAL92138; EAL92138; AFUA_3G14500.
DR   GeneID; 3512184; -.
DR   KEGG; afm:AFUA_3G14500; -.
DR   VEuPathDB; FungiDB:Afu3g14500; -.
DR   eggNOG; ENOG502QRZN; Eukaryota.
DR   HOGENOM; CLU_005335_0_0_1; -.
DR   InParanoid; Q4WYW5; -.
DR   OMA; KMYHLSG; -.
DR   OrthoDB; 1644896at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   CDD; cd00299; GST_C_family; 1.
DR   Gene3D; 1.20.1050.10; -; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; PF13410; GST_C_2; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          466..580
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          700..828
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          313..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  92270 MW;  87BF2C02D6AB116A CRC64;
     MSLLSAFSAL PTVQTRKALL LLDFQNDFVR PSGALHVPNA AEILENIAQL VTAFRRTGDV
     IWVRSHYESH RPLIDSDFQD RIVLGRETDE QRKRAERPSS KTPVDEEAFL SSESSQCCRP
     QSSGFQFPAP VLAAIDAEND TLMDKSDYSA LQDEGMILSL RTRFITELYL CGSLSNVSVY
     ATALDAVRHG FSVTLIEDCL GFRDFVRHEE AMRRMADIFG ASGITTQELF EELDWQETDA
     IARQSTHRPV RAVTPAGIEG VMDELDVKTI RGPTANEGTP ESLGSRRRRL DALLAEQTDG
     EDDDPLDLTS LARSRSRYGP SGSPGSSSQA HGAGEKKARV RVRRTRRQDH KVDASNRTEE
     RRSGKTKKSR DIRGPGDKIG EGDSRIIYDL DLPEDAFASI RSEVAWQKMY HMSGQVPRLV
     AVQGQTRDDG SIPIYRHPAD ESPPLRPFTP TVNQIRIIVE RILGHPLNHV LIQLYRDGQD
     SISEHSDKTL DIVRGSFICN VSLGAQRVMT LRNKVKAADE DQRPTQRISM PHESLFILGE
     KTNMRWLHGI RPDKRQAAEK STEELAYGGE RISLTFRHIG TFLNEAGDAI WGQGAVSKDQ
     SQANTVIHGD PAETERLVRA FGQENQATEF DWDAVYGGGF DVVNFVTTST AKLVEDSDPV
     TNLRVRLALS ENGIRYEVSA SSEDENSTEG KARPVLITAD GTEVAGELDI MNFLAKHAPE
     LTRAGVEVLR GGSQLLKINE LLQDWRTSHS NGEKINPESL DLWEKALDGQ YYLGGAALGL
     DDCFLWPVLR DIVQTCGPFS IDEYPNLAQY YRRVEKRGIV KATLEELK
//
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