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Database: UniProt
Entry: A0A0J6YNV2_COCIT
LinkDB: A0A0J6YNV2_COCIT
Original site: A0A0J6YNV2_COCIT 
ID   A0A0J6YNV2_COCIT        Unreviewed;       353 AA.
AC   A0A0J6YNV2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=CIRG_08535 {ECO:0000313|EMBL:KMP08854.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP08854.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; DS028098; KMP08854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YNV2; -.
DR   STRING; 404692.A0A0J6YNV2; -.
DR   Proteomes; UP000054565; 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   PANTHER; PTHR47990:SF277; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 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}.
FT   DOMAIN          172..299
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   353 AA;  39155 MW;  3687A2CAB54A7698 CRC64;
     MANPSRYSPL TKLPIQLPII DISNTRPETG KAMIDAATKY GFLYVDSVTS DFSDEDVESA
     FAMARKFFAS PHEEKVQVKI GSNNRGWTGM HVETLDPNHQ KRGDFKEAFN FGEFKNDKAQ
     QPLPSSLVPH EAEISRFMNL CRKTCDRILT LLALGLGIPS DWFTTRHDSS KGPSGVTFRF
     LYYPSIQSPS TSTFQQNIDV RAGAHSDYGS ITLLFQRDGQ PGLEIQTPTG GWAPVPIRPQ
     QESTTTSFPP ILVNIGDLLS YWTNGLLKST VHRVVFPVEQ QSGSSHGDDR YSMAYFCHPL
     DDTELVPVPS KLVEQHRDAI AGDGPNADKI MTARDHLASR LAATYGGNPN EYK
//
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