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
//