ID   A0A218Z308_9HELO        Unreviewed;       381 AA.
AC   A0A218Z308;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=B2J93_4763 {ECO:0000313|EMBL:OWP01913.1};
OS   Marssonina coronariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP01913.1, ECO:0000313|Proteomes:UP000242519};
RN   [1] {ECO:0000313|EMBL:OWP01913.1, ECO:0000313|Proteomes:UP000242519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:OWP01913.1,
RC   ECO:0000313|Proteomes:UP000242519};
RA   Cheng Q.;
RT   "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT   blotch.";
RL   Submitted (APR-2017) 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:OWP01913.1}.
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DR   EMBL; MZNU01000257; OWP01913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218Z308; -.
DR   STRING; 503106.A0A218Z308; -.
DR   InParanoid; A0A218Z308; -.
DR   OrthoDB; 2908779at2759; -.
DR   Proteomes; UP000242519; 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: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   PANTHER; PTHR47990:SF62; IRON_ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
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:UP000242519}.
FT   DOMAIN          215..322
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   381 AA;  43140 MW;  EA099E36882285F0 CRC64;
     MSTATTMPAA TLKLELRTAY GPVFRDVLNT PPRGCTAAEI PIIDLAPLYS ANFDDRKELS
     KQIRAAAVNT GFFYIKNHGI EDKTIADAKK QLLAFFKQSP DQKMRVSKER SKYFNGYVGP
     KSTNISPGES VDVKESFGWR YSPQYDPETK DLNAIPDEVK PWIRGEEFVW EETCHLPGFK
     DDVLHYWASC LTLARKLVRV FALSLDLEEN YFDSRVTYPG ADGVFNYYPP TTEEETKNDS
     VGLGSHTDLQ LFTLLWQDMT GGLQVLNREG QWIQATPVEG TIVVNIGDFM MRLCNDIYRS
     TVHRVYNRST AERVSMPFFF GLNFNCVVGV VPSCVSEDNP PKYEPISCGD WCQLRFKLEE
     NQFKKNYGRA SQAQSTVVIA A
//