ID   K1WZL8_MARBU            Unreviewed;       629 AA.
AC   K1WZL8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Flavocytochrome c {ECO:0000313|EMBL:EKD18446.1};
GN   ORFNames=MBM_03439 {ECO:0000313|EMBL:EKD18446.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18446.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD18446.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18446.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; JH921433; EKD18446.1; -; Genomic_DNA.
DR   RefSeq; XP_007291328.1; XM_007291266.1.
DR   AlphaFoldDB; K1WZL8; -.
DR   STRING; 1072389.K1WZL8; -.
DR   GeneID; 18759374; -.
DR   KEGG; mbe:MBM_03439; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG2404; Eukaryota.
DR   HOGENOM; CLU_011398_4_5_1; -.
DR   InParanoid; K1WZL8; -.
DR   OMA; EDLWVVV; -.
DR   OrthoDB; 1605658at2759; -.
DR   Proteomes; UP000006753; 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:UP000006753}.
FT   DOMAIN          545..621
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          493..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  67932 MW;  690C9D25D7A6CA6A CRC64;
     MAPRVIVVGG GLSGLSAAHT IYLAGGNVVV LDKQGFFGGN STKATSGING ALTRTQVDSN
     ISDSVKQFYD DTLKSARDKA RPDLIKVLTY KSAAAVEWLQ DVFNLDLTLV SRLGGHSQPR
     THRGHDAKFP GMAITYALMQ RLEELAENEP ERVQIIKKAR VTAVNKDGNK ITGVSYEFEG
     EPYTVEGPVV LATGGYAADF TETSLLKKWR PDTFDLASTN GVHATGDGQK MVMAIGGNGI
     DMDKVQVHPT GLVDPKDPGS KWKFLAAEAL RGEGGLLLNG DGDRFCDELG HRDYVSGEMW
     KEKDKGKFPV RLLLNSKASN VLDFHTRHYS GRGLMKKMTG KELAKEIGCT EEHLQSTFTA
     YNEIADGKKK DPYGKKFFHN GPVDINDDFH VAVMEPVLHF TMGGIEINDK AEILNSEGKP
     FEGLYACGEL AGGVHGANRL GGSSLLGCVV YGRVAGDTAS NYLFRNALSG AGGVAASRLG
     QISLHIDPNQ PGKISVEWDS AGSSSDSQIS SQSQTSAAPV LKQGADSADP GKVSKPNKAA
     FKIPEKEFTM EEVAKHNTKE DLWVVVKGVV MDVSDWLDEH PGGPQAIMNF MGRDATEEFE
     MLHDDEVIRK YAPSQVIGRV KGQEITLEA
//