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Database: UniProt
Entry: A5E1R5_LODEL
LinkDB: A5E1R5_LODEL
Original site: A5E1R5_LODEL 
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};
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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
//
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