ID A0A8K0J0D2_9HYPO Unreviewed; 182 AA.
AC A0A8K0J0D2;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=E4U42_002208 {ECO:0000313|EMBL:KAG5912544.1};
OS Claviceps africana.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=83212 {ECO:0000313|EMBL:KAG5912544.1, ECO:0000313|Proteomes:UP000811619};
RN [1] {ECO:0000313|EMBL:KAG5912544.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCC 489 {ECO:0000313|EMBL:KAG5912544.1};
RA Wyka S.A., Mondo S.J., Liu M., Dettman J., Nalam V., Broders K.D.;
RT "Whole genome comparisons of ergot fungi reveals the divergence and
RT evolution of species within the genus Claviceps are the result of varying
RT mechanisms driving genome evolution and host range expansion.";
RL bioRxiv 0:0-0(2020).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC {ECO:0000256|ARBA:ARBA00038168, ECO:0000256|RuleBase:RU362121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG5912544.1}.
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DR EMBL; SRPY01001780; KAG5912544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8K0J0D2; -.
DR OrthoDB; 1925334at2759; -.
DR Proteomes; UP000811619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR050668; Cytochrome_b5.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR PANTHER; PTHR19359; CYTOCHROME B5; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121};
KW Reference proteome {ECO:0000313|Proteomes:UP000811619}.
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 110..182
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 80..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG5912544.1"
SQ SEQUENCE 182 AA; 19499 MW; 50B8057436222F85 CRC64;
MAQLFDAAEV AKHKTRESCW VVLYGQVYDV TDFLAAHPGG PGVILRLAGG DATAEYDPVH
PPGTLEDNLP PEARLGSLRA ETTGSGADST PTPTTTTTTT TPMPTTDHGP PLASLVNLDE
IEAEAKRRLS KKAWAYYFSA SDDLVSKTRN STVYRDILLR PRLLVDCTLC DTSTTLLGHG
VG
//
