ID C1G5Y7_PARBD Unreviewed; 628 AA.
AC C1G5Y7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=PADG_02592 {ECO:0000313|EMBL:EEH46494.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46494.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH46494.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH46494.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275959; EEH46494.1; -; Genomic_DNA.
DR RefSeq; XP_010758525.1; XM_010760223.1.
DR AlphaFoldDB; C1G5Y7; -.
DR STRING; 502780.C1G5Y7; -.
DR GeneID; 22582046; -.
DR KEGG; pbn:PADG_02592; -.
DR VEuPathDB; FungiDB:PADG_02592; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG2404; Eukaryota.
DR HOGENOM; CLU_011398_4_5_1; -.
DR InParanoid; C1G5Y7; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; 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 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; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 544..620
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 67784 MW; 8560FA996F1B3773 CRC64;
MPSRVIVVGG GLSGLSAAHT VYLNGGNVLV LDKQNFFGGN STKATSGING ALTRTQTELG
IADSVKQFYE DTLKSARDKA RPDLIKVLTY NSASAIHWLQ EIFNLDLTLV SRLGGHSFPR
THRGHDAKFP GMAITYALMQ RLEELTESEP HRVQVLKKAR VTAVNKEGNT ITGVTYEHNG
ETHIADGVVI LATGGYAADF TEDSLLKKWR PDTYNLPSTN GVHATGDGQK MLMAIGANGI
DMDKVQVHPT GLVDPKDSDS KWKFLAAEAL RGEGGLLLNS DGQRFADELG HRDYVSGEMW
KEKEKGKWPI RLILNSKASN VLDFHTRHYA GRGLMKKMTG KELAKEIGCG EAALKKTFDD
YNQIADGKMQ DPFGKKFFHN GPVKIDDTFY VALMQPVLHF TMGGIEINDK AQVLNSEKKP
FEGLFACGEL AGGVHGANRL GGSSLLGCVV YGRVAGDSAS QYLLQQVLSN PSAAASSRLN
QISLHIDPSQ PGKVSVEWTS PSGGSSGAKS IQAAPVPTAA AGKSAAPAKA ADNVADVANF
KVPDKEFTME EVAKHNKKDD LWIVVKGVVM DVTNWLEEHP GGAQALFSHM GKDASEEFEM
LHDDEVIPKY AAGIVIGRVK GQTPSLEY
//