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Database: UniProt
Entry: A0A1Q5SXH8_9EURO
LinkDB: A0A1Q5SXH8_9EURO
Original site: A0A1Q5SXH8_9EURO 
ID   A0A1Q5SXH8_9EURO        Unreviewed;       373 AA.
AC   A0A1Q5SXH8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=PENSUB_12714 {ECO:0000313|EMBL:OKO92729.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO92729.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKO92729.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO92729.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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:OKO92729.1}.
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DR   EMBL; MNBE01000740; OKO92729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5SXH8; -.
DR   STRING; 1316194.A0A1Q5SXH8; -.
DR   OrthoDB; 1380829at2759; -.
DR   Proteomes; UP000186955; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186955}.
FT   DOMAIN          174..285
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          100..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  41784 MW;  900235CD80F42F98 CRC64;
     MAASSIPTVD YSLSTSPVTR PQFLSQLRDA LVKVGFFYLK NHPISKFQQK DLLAQARELF
     QLSPEKKREI GMTRSKHFVG YVGLDDGLTL TKKDHRESYT LGYESPAPHP DEPVYRNLRG
     PNPWPDSSAL PGFRSTTETY MIEMKRLADD FNVLVAEALD MKPTALAHLF DGTPFDRLML
     AKYPLPDEDQ EIQGKGKHKD ASFLTFLLPG TSHGGLEALS QTNDWIPVPP VPGALIVNVG
     MQLEALTDGV CYAAFHRVLI RREDFVDSDG HDLGPRFSFP LFHTISLDAN QSEPLEMSPH
     ICVMARDDMA RRNARVSLRR LFQAGCAGYG VFGTRLKVYP KVTQRWWPQY LDFLTPDKVP
     QLTAALCSGS SNP
//
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