ID   A0A0W0F1G8_9AGAR        Unreviewed;       865 AA.
AC   A0A0W0F1G8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN   ORFNames=WG66_17256 {ECO:0000313|EMBL:KTB30165.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB30165.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB30165.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB30165.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00005896}.
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:KTB30165.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LATX01002394; KTB30165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0F1G8; -.
DR   eggNOG; ENOG502QTFW; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00657; Ferritin_like; 1.
DR   CDD; cd03467; Rieske; 1.
DR   Gene3D; 3.60.130.10; Clavaminate synthase-like; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR007402; DUF455.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   PANTHER; PTHR30468; ALPHA-KETOGLUTARATE-DEPENDENT SULFONATE DIOXYGENASE; 1.
DR   PANTHER; PTHR30468:SF10; TAUD_TFDA-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF04305; DUF455; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF02668; TauD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT   DOMAIN          429..499
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          402..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  97142 MW;  20C23364D27425A3 CRC64;
     MILARGIQVI RGAAKPFNIL PSTRHFALPR SSTLASLNVY ESYDNTTHIG TSFTGVQLSE
     IMKHRNSDVL LRDLAHLVSH RGVVFFRDQD ININQQIEFG DRLGRLSGKP ATSTLHKHPI
     SEDTPEFGPE VSVISSMDGI AVLGDHTTLR ASQGWHADIT FEKVPSDYAV LKIHTLPETG
     GDTLWASGYE AYDRLSPAFQ RFLEGLTAVH NADFFNVYAQ TRGLKIQDPR GSPENTGSNL
     TAVHPVIRTN PVTGFKSLFV NKTFTKRILE LTPDESNNVL DYLAKHISEN HDLQVRFKWQ
     KNDVAIWDNR VAFHTATNDY EGNRQGNRVV SVGEKPYFDP NSKSRRAALG MKPAVIAPLQ
     NLFTHSRFLL TLRSQEGKYH GLILFRLSTG VHPCFDGKHK VADDTDEARQ NGHSKEESKS
     AAPLDPRARA AQHQLYVMES TCPHLGAEMS HADIEEYEDT MVAVCPWHRY DFDLKTGKSE
     TGLRTCTYPV EVIDDNGVEK VYMGAPAEGT KWRLVEFRPV SEEFADPPPV KTTENDTNPN
     TNNIAVSQTE EPVVPLNDPP KTLMEWAVLI LNTPNPTLKV ERTKHAVHAF RTGKLNSIGH
     KSSKGPRPPD VPPREELFTR NIVDPLKVKK RRNRAVMLHA LANIEQWAID LAWDIMARFG
     PMHKDLPPAF FSDFAKMALD ESKHFSLLVS RLNALGTPYG TFPTHASLWD SARHTSKSFR
     SRLAIIHLVH EARGLDVSPT TIDKFRRAGD IDSVKVMEII HADEVTHVTA GHRWFCWACE
     QNEGGMDPVK AFREEVRTCW RGDIKGPFNV EDREKAGLAP EFYEDLKGEM GFEDESEEPK
     RPRIPGMTEI TQGLAKVEVG YDSKV
//