ID F2SEV6_TRIRC Unreviewed; 467 AA.
AC F2SEV6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=TERG_00275 {ECO:0000313|EMBL:EGD83995.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD83995.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; GG700648; EGD83995.1; -; Genomic_DNA.
DR RefSeq; XP_003238286.1; XM_003238238.1.
DR AlphaFoldDB; F2SEV6; -.
DR STRING; 559305.F2SEV6; -.
DR GeneID; 10377694; -.
DR VEuPathDB; FungiDB:TERG_00275; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_0_1_1; -.
DR InParanoid; F2SEV6; -.
DR OMA; WRKQGDD; -.
DR OrthoDB; 1952715at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961:SF48; AMINO ACID OXIDASESARCOSINE OXIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10130)-RELATED; 1.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 9..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 437..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50244 MW; 6443924D543DE7BC CRC64;
MSPDLPNHIL IVGGGVFGLS TALALSRRHK GSITLLEAAP AIPNPHGSSV DSSRILRADY
ANPAYARLAQ QALTQWRSTP WGHDGRYNRN GLVLVASSSS SGDHTYVRKS YENIKCLSPD
AVELLPTASD VRRVVPGYGV AAHVSGGYVN WDSAWSDAES AIRHAKHLLD ETGRVTFLSG
QAERLIIDHS NNNQNQVTGV ELSDGNRISA DLVVLATGAW TGKLVDLRGR AEATGHPLAY
LPLTDEEQRQ LNDMPTVLNL STGMFIIPPR NNELKIGRHG YGYRNPVRIN HPTASSAPVE
VSLPLHGTSV PLEGQLAARA ALREMLPALA DRPFSKTRVC WYTDTPKGDF IISYHPEIKS
LFIATGGSGH GYKFLPVLGD KIVDAMQGIL DSDLARLWAW TDNPVTTPAG GLGVVWTEDG
SRSGARGMLL VDELEKSTNT SPSNCPSNCP SNSTNDNSGD AKVISKL
//
