ID A0A4U0X589_9PEZI Unreviewed; 399 AA.
AC A0A4U0X589;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=B0A49_10173 {ECO:0000313|EMBL:TKA71604.1};
OS Cryomyces minteri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Cryomyces.
OX NCBI_TaxID=331657 {ECO:0000313|EMBL:TKA71604.1, ECO:0000313|Proteomes:UP000308768};
RN [1] {ECO:0000313|EMBL:TKA71604.1, ECO:0000313|Proteomes:UP000308768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5187 {ECO:0000313|EMBL:TKA71604.1,
RC ECO:0000313|Proteomes:UP000308768};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:TKA71604.1}.
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DR EMBL; NAJN01000554; TKA71604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0X589; -.
DR STRING; 331657.A0A4U0X589; -.
DR Proteomes; UP000308768; 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:SF35; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G11160)-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:UP000308768}.
FT DOMAIN 224..328
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43895 MW; B9817D3C5B6BB412 CRC64;
MATASATQAQ EEKHVQWKGQ ESSEPTPSVT PLCTTDGELA FADLPPFPSD IPTAPLLRLS
LSKLLAGSQE EEERLWRACC DLGFFYLDLR DDKDGGKGDE RLLEDAARLF EVAKEVFDLP
VAEKVKYDFK EKGSYYGYKG YGDGVIDKEG TKDRNEFYNT SKDDILNQTD PLPAPQLLQP
HRPLFSSFIH HSHAIVTLVL SILNTQLGLP ARTLQSKHRL SAVSGDQVRF VKAPAQPAED
RQTALGEHTD FGSVTVLFNR LGGLQVRLPG SGAWTFVQPL RGHAVVNLGD AVAKFTAGLL
RSNIHRVVSP PGDQAAVARY SLVYFARPED DVVLKRLRGS RLVDEKVAGA GGVAEEEEEE
EVSSKEWILR RALGRRGVGA WEKSNGTEEL SMRRGGTKA
//