ID A0A0P9EP72_RHOGW Unreviewed; 630 AA.
AC A0A0P9EP72;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=RHOBADRAFT_48688 {ECO:0000313|EMBL:KPV74027.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV74027.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV74027.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV74027.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KQ474081; KPV74027.1; -; Genomic_DNA.
DR RefSeq; XP_018270076.1; XM_018415173.1.
DR AlphaFoldDB; A0A0P9EP72; -.
DR STRING; 578459.A0A0P9EP72; -.
DR GeneID; 28975621; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme 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 Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR PANTHER; PTHR43400:SF1; FUMARATE REDUCTASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT DOMAIN 553..629
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 67299 MW; A4E0E26ACD6FA37D CRC64;
MSGPQVIVVG AGLSGLSAAH TLYEKGANVL VLEKNAFAGG NSTKATSGIN GAGTKAQEKL
GIKDSAAAFF ADTKKSARDL ARDDLIEVLT GKSGDAVNWL VERFNLDLTK VSRLGGHSFE
RTHRGSKLFP GMMITYALME GLEELAEQDP KRMRFLKKAD VKKLVKEGDE VVGLEFEFQG
KTHTAHGPVI LATGGYAADF AKDGLLAKFR PELLDLPTTN GDHCTGAGTK MAMAVGANGI
DLEKVQVHPT GLVDPNDPDA KVKFLAAEAL RGVGGLLLNK EGDRFADELG HRDYVTGRIW
EDNKLPVRLI LNGEASKEIE WHCKHYVARG LMKKIDTVDD LAKEMGLPLS KIQGTFDDYM
AICKDPKKDP FGKKYFSATN WGKNAGPFHV AIMSPVLHYT MGGLEIDPLS QVLNTEKKPI
KGLFASGEIA GGVHGANRLG GSSLLGCVVF GRVAADTAAS YLLKSLSSGS GAVARLGQVN
NHLQPPSTTI SIDPSTQQVH LTLNWSGQGA SSSSSGGVKP TGPSTAEQPA NEVDAAVKHD
EETKAGEKKG VEQKEYSLEE VAKHNTKDDI WIAVNGQVLN VTNFLQDHPG GAKALMLYAG
QEASEAFNML HEKTVVAKYA PDTIIGTYKQ
//
