ID   A2372_ARTBC             Reviewed;         500 AA.
AC   D4B1P2;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase ARB_02372 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02372;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; ABSU01000027; EFE30674.1; -; Genomic_DNA.
DR   RefSeq; XP_003011314.1; XM_003011268.1.
DR   AlphaFoldDB; D4B1P2; -.
DR   SMR; D4B1P2; -.
DR   STRING; 63400.XP_003011314.1; -.
DR   EnsemblFungi; EFE30674; EFE30674; ARB_02372.
DR   GeneID; 9524215; -.
DR   KEGG; abe:ARB_02372; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_018354_1_0_1; -.
DR   OMA; THPQDHK; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
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   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..500
FT                   /note="Uncharacterized FAD-linked oxidoreductase ARB_02372"
FT                   /id="PRO_5003053847"
FT   DOMAIN          60..232
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         98
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P08159"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   500 AA;  54539 MW;  5831B60526AFBC39 CRC64;
     MHSIIFKAAV ALLGVSTAAG FSYQNSRLCL KLLAQGVEVD LPNSTDYETE QQNYWSTACT
     ALRPDCIIAP KNARDMSRAV AAIQESKTTR FAIKSGGHSP NQLFSSIHDG VLISTRNLKQ
     ITYNEHTQTA VLGPGLKWEE AVGGLKDKGQ TVVGGRLGGI GVGGLILGGG LSFLSGQYGW
     ATNNVVNFEV VLANGTIVNA NATSNPDLYA VMKGGSGNFG IVTAFTVKTH TQDPEIWGGS
     MFFDGNHTES LTRAIRDFAE YNTDDKASII GTVNRNPSLI WVVFLTYDGP SPPEDVFRNF
     TQIPNIRNTV KRQSYHSLML ANDEYIRHGN RFSIGAETSV NPSGTHGYDI FKSFIDHWND
     VTDDFIDIPG SASSLALQPL PRSISTKAKE SGGDVAGFDP RYDYLLLQIA VSWNSSTSDS
     VIEAATRKYY TVQGDMIKQF TNEGKLPKAY CPLYLNDLNA NQDFWGRVAP STREKALAVR
     RAVDPTLFFQ NRVTGGFRLG