ID U5GZ54_USTV1 Unreviewed; 574 AA.
AC U5GZ54;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN ORFNames=MVLG_00458 {ECO:0000313|EMBL:KDE09563.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE09563.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE09563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE09563.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE09563.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC Lamole {ECO:0000313|EMBL:KDE09563.1};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_00458T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; AEIJ01000032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541644; KDE09563.1; -; Genomic_DNA.
DR AlphaFoldDB; U5GZ54; -.
DR STRING; 683840.U5GZ54; -.
DR EnsemblFungi; MVLG_00458T0; MVLG_00458T0; MVLG_00458.
DR HOGENOM; CLU_003291_4_2_1; -.
DR InParanoid; U5GZ54; -.
DR OMA; RCTHYGA; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000017200; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd03478; Rieske_AIFL_N; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000017200}.
FT DOMAIN 38..138
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 138..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 61202 MW; FE3A55F31D075A39 CRC64;
MLTALLRTIP PSRPLITSFT RPFARSFLTT RYNMAPQRVE INIEPLADGT MKEVPFPKTD
SESKILISKV QGCYYATSAK CTHYGAPLAK GVLTSDGRII CPWHGAAMSC KTGDIEDAPG
LDNLATFKIE SEGDKLFVTP PENGDVTATR QPPSNSGSKS QTGVVIVGGG AGAAHAVEAL
RQNGYEGSIK VISKEPYLPI DRTKLSKALL ADPSKVALRS QDFYDKLGVE FQLNTEVESI
DFDKSSVKVS GGNSVSYEKL ILATGSNPNR IPVDGSKLGN IFVLRTIEDT KQINDALGGE
DGPKKNVVVI GSSFIGMEAA LAAAGKANVT VVGMENAPFE AILGKAIGNG IRKFHESKGT
KFYLPGALSH FSASSSDSSK VGSVELKDGT SIPADLVVLG VGVKPATAFL KASGVELEKD
GSVVVDEYLK LHGKENVFAV GDIATYKDVK TGKNTRVEHW NVASNHARNV AATIAGKSPT
PYEKISVFWS AQGQQLRYAG TSRAKTWEDV IVQGSPEDLK FVAYYTAGED VVAVASMQND
PIAAHCSELM RLNKMLSVKE IKDGKSPLDV KLVA
//