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Database: UniProt
Entry: A0A161WIY7_9PEZI
LinkDB: A0A161WIY7_9PEZI
Original site: A0A161WIY7_9PEZI 
ID   A0A161WIY7_9PEZI        Unreviewed;       630 AA.
AC   A0A161WIY7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=FAD binding domain-containing protein (Isoamyl alcohol oxidase) {ECO:0000313|EMBL:KZL70916.1};
GN   ORFNames=CT0861_01297 {ECO:0000313|EMBL:KZL70916.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL70916.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL70916.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL70916.1,
RC   ECO:0000313|Proteomes:UP000076552};
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   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:KZL70916.1}.
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DR   EMBL; LFIV01000082; KZL70916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161WIY7; -.
DR   STRING; 708197.A0A161WIY7; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          166..348
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  68626 MW;  19272EB20D08A17E CRC64;
     MSKRSTVLQQ PACQATRSQV HSRDQPDSQR PSGKMTRASL TNLLLLACLS LIATAVSTPK
     LVPYQENGKK YECKCSPADD CWPKANAWDK LNKTVGGNLV RHIPPAAVCY NQYRGIATYD
     AAKCAEATAK WTDERWQISQ PASQLWTWGS NNTCELTTDP TKTCTLGNYP EFVIMARTKD
     HVKAGVKFAK SNNLRLVLRN TGHDFQGRSA GAGSLAINTH NFKDISFVDR YKGPGDYQGP
     VITIGAGVQG FEISAAARAR NPPQNVVTGE CETVGVAGGY IGGGGHGPLS GNYGFGADQA
     LSFEVLTASG DFITANSKSN ADLYYALKGG GPGNYAVVLS VTLKTYPDTI PGAALFLNVN
     ATTGANFEQV TKTVNKLHEL GNYMVDNGLY GIYELYPPVI GGALHVQPIM GMNMTARELT
     AVVQPLLSYL DTEQIPYDFG VKEYPDYYTL FHDIFEPEAA AQNGLTGGWV FTHDDMANNQ
     PAIAEAIQLA LSPAPNQFGI VISHFFDPGN KAKKAESATH PRWRGATMRT MAILPQALDA
     TWATKLALND LMVNTITEKF KQAGPKGLAY VNENYAFMNN WQDAFWGPVY PKLVSTKKKW
     DPNGVFFSWS TPGSEEWTVV DYANRLCKAK
//
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