ID T0LRW0_COLGC Unreviewed; 485 AA.
AC T0LRW0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Thiol-specific monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_09553 {ECO:0000313|EMBL:EQB50950.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB50950.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:EQB50950.1}.
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; AMYD01001925; EQB50950.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LRW0; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_3_1; -.
DR OMA; FRHREVM; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 3.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:UP000015530}.
SQ SEQUENCE 485 AA; 55046 MW; 1CE3B35DD0C6E470 CRC64;
MAKEIRRVAV IGAGPAGAIA TDALVKEQAF DVVRVFERRD LAGGTWVYTP ELPSRIPSLR
DLVEQRANPP VDLPKTFPTW TPKTEKINSH QLRYADTGVH ETLHSNITPE IMAFTQEPIP
KILSERTIAQ YGPGAPFRHR ELIREWVEAI FTRGGHDKLV EFSTTVELAE KKGDEWILTL
RKVVPGKSKD YWWQETFDAI VVGSGHFYLP YIPDISGLIK YDEKFPGRVK HTKHFRSPEE
FRGKKVVVVG GSVSAFDALH DIRLVSQTPV IASLREPLPA FGWAPFTHPD ITIKPQITHF
CHKTGRITFS DKSTVDDVDV VLFATGYDFS FPFLPKLKVE NRRIPRLYQH VFHTDDPSLA
FVGMVTGGFT FRVFEWQAVA AARVFAGRGQ LPSTTEMERW EADRLVKRGD GVPFFTLSPD
FEEYFEALRA IAGEPAPGST GRILPKFDPK WLEAFADVIN ARVDWWKKET EKAEKQQKTL
YKSKL
//