ID   A0A167CZP6_9PEZI        Unreviewed;       637 AA.
AC   A0A167CZP6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Fumarate reductase {ECO:0000313|EMBL:KZL83229.1};
DE   Flags: Fragment;
GN   ORFNames=CI238_07843 {ECO:0000313|EMBL:KZL83229.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83229.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL83229.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83229.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL83229.1}.
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DR   EMBL; LFIW01001190; KZL83229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167CZP6; -.
DR   STRING; 1573173.A0A167CZP6; -.
DR   Proteomes; UP000076584; 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:UP000076584}.
FT   DOMAIN          553..629
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          510..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL83229.1"
SQ   SEQUENCE   637 AA;  68620 MW;  7DC3A76120F312F4 CRC64;
     LSSGAHQYTS TKMAPRVIVV GGGLSGLSAA HTIYLAGGNV VVLDKQGFFG GNSTKATSGI
     NGALTRTQVD TGIADSVKQF YDDTLKSARD KARPDLIKVL TYKSAAAVEW LQDVFNLDLT
     LVSRLGGHSQ PRTHRGHDAK FPGMAITYAL MQRLEELAET EPGRVEIIKK ARVTGLNKDG
     NTITGVTYEF NGEEQKVDGP VILATGGYAA DFGETSLLKK HRPDTYGLAT TNGTHATGDG
     QKMVMAIGGN GIDMDKVQVH PTGLVDPKDP GSKWKFLAAE ALRGEGGLLL NADGDRFCDE
     LGHRDYVSGM MWKEKDKNKF PIRLVLNSKA SKVLDFHTRH YSGRGLMKKM TGAELAKEIG
     CKPEHLQKTF TTYNAIADGK QKDPWGKKFF HNLPLDINDD FHVALMEPVL HFTMGGIEIN
     DKAQVLNSEQ KPFDGLFACG ELAGGVHGAN RLGGSSLLGC VVYGRVAGDT ASNYLFQQAL
     SGAGGAASRL GQISLHLDPA QPGRVTIDWN NAGGAGGQGI PAQQTTSAAG PTPVKDGQKA
     SKPNNPKEFT IPEKEFTMEE VAKHNTKEDL WVVVKGVVMD LSNWLEEHPG GPQAIMNFMG
     RDATEEFEML HDDEVIPKYA PQQVIGRVKG QTPSLEI
//