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Database: UniProt
Entry: A0A1V6QHG8_9EURO
LinkDB: A0A1V6QHG8_9EURO
Original site: A0A1V6QHG8_9EURO 
ID   A0A1V6QHG8_9EURO        Unreviewed;       625 AA.
AC   A0A1V6QHG8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN   ORFNames=PENANT_c003G00965 {ECO:0000313|EMBL:OQD88645.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88645.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OQD88645.1}.
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DR   EMBL; MDYN01000003; OQD88645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QHG8; -.
DR   STRING; 416450.A0A1V6QHG8; -.
DR   OrthoDB; 1605658at2759; -.
DR   Proteomes; UP000191672; 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:UP000191672}.
FT   DOMAIN          541..617
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   625 AA;  67113 MW;  EBD5E9847B749C58 CRC64;
     MAPQVIVVGG GLSGLSAAHT VYLNGGNVVV LDKQAFFGGN STKATSGING ALTRTQTDLG
     IQDSVKQFYD DTLKSARDKA RPDLIKVLTY KSAAAVEWLQ DVFNLDLTLV SRLGGHSQPR
     THRGHDAKFP GMAITYALMQ RLEELADKEP GRVQIIKKAN VTSINKSGNN VTGVSYTLNG
     EPKSVDGIVV LATGGYAADF GDTSLLKQHR PDTFGLSSTN GTHATGDGQK MLMAIGANGI
     DMDKVQVHPT GLVDPKDPQA KFKFLAAEAL RGEGGLLLNS DGQRFSDELG HRDYVSGQMW
     KEKEKGKWPI RLILNSKASN VLDFHTRHYS GRGLMKKMSG KQLVEEIGCG EAALKKTFDD
     YNQIADGKKK DPWNKRFFHN FPFTLDDEFH VALMEPVLHF TMGGIEINEH AQVLNGEQKP
     FEGLYACGEL AGGVHGANRL GGSSLLGCVV YGRVAGDSAC QHLFQKLITS GGSASSRLGQ
     ISLHIDPNTP GKVSVEWGAA AGGNLPTLAA APADASATTA AAAAPEQKAA KPDPANFKIP
     ETEYTMEEVA KHNTKEDLWI AVKGIVLDVT NWLDEHPGGA NALFNFMGRD ATEEFAMLHD
     DEVIPKYAGH TVIGRIKGQT PSLDI
//
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