ID A0A161WKI1_9PEZI Unreviewed; 429 AA.
AC A0A161WKI1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=CT0861_05004 {ECO:0000313|EMBL:KZL71516.1};
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:KZL71516.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL71516.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL71516.1,
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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:KZL71516.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIV01000070; KZL71516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161WKI1; -.
DR STRING; 708197.A0A161WKI1; -.
DR OrthoDB; 1786978at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 13..363
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 74..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 47081 MW; D5CE403382E962EA CRC64;
MTVKSQTPPQ PLKVAIIGGG PGGLGAAIEF GKLHYVDWTL YEKKPQISET GGGISLQRHT
WRLLELNGAA KNIHPSDYFR SPDGTSGQQR NGRTGKLLEQ SSHPKDTPPQ QLSCRMVRAK
LQAALLKDVD QSRIKTSKKL TDILVLPSGK VEIRFEDGLT DEVDLLVGAD GIRSFVRSFA
FPSHKIKYNG QSAYRTIIQK SAVEKIDGIP KSPVFWQNTG GKYVFTCPLG GDDFEVTARI
RRPIEGQEQV SWGRPFDFST IASEYDEFCE PVRKVIQLAA QGKTQEFALF SGARLESVIS
HGSLALIGDA SHPLSGAFGA GAGFALEDVF ALTRSIDWAH QNAKGLPAAL ELYDRIRSPH
YRDLYGVLDN FAALNSALLA ENLPVNEEIE ERVRRAGESK STWMYHYEID KAVDKLLGSA
GQLDQVAAA
//
