ID F2SMA8_TRIRC Unreviewed; 472 AA.
AC F2SMA8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=TERG_03829 {ECO:0000313|EMBL:EGD87582.1};
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:EGD87582.1, 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};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; GG700650; EGD87582.1; -; Genomic_DNA.
DR RefSeq; XP_003236787.1; XM_003236739.1.
DR AlphaFoldDB; F2SMA8; -.
DR STRING; 559305.F2SMA8; -.
DR GeneID; 10378051; -.
DR VEuPathDB; FungiDB:TERG_03829; -.
DR eggNOG; ENOG502RGYQ; Eukaryota.
DR HOGENOM; CLU_018354_0_2_1; -.
DR InParanoid; F2SMA8; -.
DR OMA; TYINFAH; -.
DR OrthoDB; 1608525at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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:UP000008864}.
FT DOMAIN 48..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 50656 MW; 7714F51E5AC2B2F0 CRC64;
MASSGYAASD AALSSLNKEL RPKLSSSALI TASTDPDWEE YARWSAYNSP IPGAVVSPAS
EQDVAVIVQH CISNGVPFLA QSGGHGWSST LNLGPDGIII SLRKLNTVTF NHDGTEVIIE
GGALTSEVME AASQKGSLVI TGNCNSVGAL GAALGGGYGF LTGLRPHRRG HILSLTVVSG
TGALKTVTAE SDPDLFWGLR GAAPNLGIVT SVVMKAYPVE ASGQYAWLGA LVYPADKVEP
VLRAVSELTL TPKMTVFFYF LTSGAPDYSP LIAVAPWYYG TEAEGRVAFA SVIDIGPIAD
TTQVLYYPRW NEKAAAFCTR GGYKPSFGVG LSSIVLETWI KVWDEFVSWT ALSGTGSSVV
LMEAYCLDMV RSVPDHSSSF PWRSNITINA IVIPWFTDKK LAEEALSLGR RIRRLLQSTD
DLKSPAVYVN FAHGDEDPAE IYGSNLPRLR DIKAREDPNN FFCHWFGIGS TP
//
