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Database: UniProt
Entry: F4RYW1_MELLP
LinkDB: F4RYW1_MELLP
Original site: F4RYW1_MELLP 
ID   F4RYW1_MELLP            Unreviewed;       330 AA.
AC   F4RYW1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGG02317.1};
GN   ORFNames=MELLADRAFT_117566 {ECO:0000313|EMBL:EGG02317.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; GL883131; EGG02317.1; -; Genomic_DNA.
DR   RefSeq; XP_007414302.1; XM_007414240.1.
DR   AlphaFoldDB; F4RYW1; -.
DR   STRING; 747676.F4RYW1; -.
DR   EnsemblFungi; EGG02317; EGG02317; MELLADRAFT_117566.
DR   GeneID; 18926046; -.
DR   KEGG; mlr:MELLADRAFT_117566; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_117566; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_035825_0_0_1; -.
DR   InParanoid; F4RYW1; -.
DR   OrthoDB; 52212at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF82; PYRUVATE DEHYDROGENASE COMPLEX PROTEIN X COMPONENT, MITOCHONDRIAL; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT   DOMAIN          38..113
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          182..220
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          123..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  34715 MW;  2914425A9F39785B CRC64;
     MITPFVLRRA SCNVYGGILT RRSVAQKPFH SSTSPRAISP LRMPALSPTM ESGQISKWNL
     DPGTAFSAGD ILLTVETDKA EVDVEAQDDG YMGQHLVPAR TAVKVGEVIA VLGEEAEDVN
     KSVEVPEAWK STGDSSGSIK TEDSQNKIKS TGTSDGACAS SSSDNKKSAA EFGNLHPTAK
     MPLSPAVSRL LIENQISDAT EIKGTGLNGR LTKGDVLLHL GKVSSPVGSA QNMIDDDARS
     RALEKSSLSS ATSTSDLKPQ PPIDGPTLRR LITEGLALVS QSTETPIPSK PSASFSSILG
     DYHSMIPLST PTSSIPPPPT RDTYLDGLSS
//
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