ID A5E1R5_LODEL Unreviewed; 655 AA.
AC A5E1R5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=LELG_03552 {ECO:0000313|EMBL:EDK45373.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK45373.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK45373.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CH981527; EDK45373.1; -; Genomic_DNA.
DR RefSeq; XP_001525624.1; XM_001525574.1.
DR AlphaFoldDB; A5E1R5; -.
DR STRING; 379508.A5E1R5; -.
DR GeneID; 5232861; -.
DR KEGG; lel:LELG_03552; -.
DR VEuPathDB; FungiDB:LELG_03552; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; A5E1R5; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000001996; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF8; HYPOTHETICAL FUMARATE REDUCTASE (EUROFUNG); 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
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:UP000001996}.
FT DOMAIN 571..647
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 533..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 71265 MW; 490CC930F5A38BC6 CRC64;
MSELPQNPII IVGGGLAGLS AAHQAYLRGA NVVLIDKQGF LSGNSGKATS GINGALTRTQ
VNLNIKDSVE QFYQDTLKTA KDRANPDLIK VLTYQSADAV HWLQEVFGLD LSVVSRLGGH
SQPRTHRGHD SKFPGMAITY KLLEKLESLS EDEPERVAIL KNCQVVDLIK ADGEDTKVVG
VKYKNLQDKT KSDVYGPVIM ATGGYAADFT KNSLLRKYRP DIIDLPTTNG NHATGDGQKI
IMKNHGVGID MDKVQVHPTG LIDYHDKDVI AGKKQPRFLF LGAEALRGEG GIMLNGKGER
FVDELGTRDW VSGEMEKQNK AGNGPIRLVL SEESEKNLAF HIKHYTQRNL MRTVTGRQLC
EEIGCSEDDL KSQLDTYNKA AKGEIEDPFG KKYFPATPFE YKSDGKYHVS FITRVLHFTM
GGVKINDKAQ VLTDKEDGEP FEGLYAAGEV AGGVHGHNRL GGSSLLACVV YGRLSADQAS
SYALHKLSTS GGIGGNGVSQ SSANNRLNMI NLHIDPQNGK IIIDMNNEGS GDKLALSEAK
SDSKTTSKDS NSNQKKESSK KGSASAFAIP DKEFTPEEVA KHNKPDDCWC IIQNVVVDLS
SFLESHPGGA QSILNFAGRD ATESFEMLHE DNFIPKYVPK SVLGVIKGTK SKLDL
//