ID   A7056_ARTBC             Reviewed;         588 AA.
AC   D4AS41;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase ARB_02478 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_07056;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE34105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000007; EFE34105.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003014494.1; XM_003014448.1.
DR   AlphaFoldDB; D4AS41; -.
DR   SMR; D4AS41; -.
DR   STRING; 663331.D4AS41; -.
DR   EnsemblFungi; EFE34105; EFE34105; ARB_07056.
DR   GeneID; 9520546; -.
DR   KEGG; abe:ARB_07056; -.
DR   eggNOG; ENOG502QQWK; Eukaryota.
DR   HOGENOM; CLU_018354_4_2_1; -.
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; -; 2.
DR   InterPro; IPR012951; BBE.
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; PF08031; BBE; 1.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..588
FT                   /note="Uncharacterized FAD-linked oxidoreductase ARB_02478"
FT                   /id="PRO_0000434915"
FT   DOMAIN          118..303
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         156
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P08159"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   588 AA;  63347 MW;  E362F511BA469A79 CRC64;
     MRSTAYLTAL LSFLGATHAA PEGPRCRCTP DQSCWPSPGL WQTLNKTLSG NLVAVKPVGT
     VCHDPTYNGG LCDSVKGMQT DSSWRSAQPG AVQSINWETW PEKNESCYID GPRQVPCGQG
     RIPLYSAVVQ SPLDIQKTVR FASKYNLRLV IKNTGHDFLG RSTGPQSLQI LTHNMKSINF
     TDNFVPEGKP DGRGIGQAVT IGAGVQLNEL YEAAGKRGLT QVIGLSTTVG AAGGYIQGGG
     HSPLGPWKGM STDHVLEYKV VTAGAKFVTA NEYQNSDLFW ALRGGGGGTF GVVTSVTLRT
     FKDPPTIVSQ VNVTMDGKAN ESYWAAVEKF QAYLPTLSDG GCSGYYYMLP NVTLGPQSAA
     VIIAAFYYAN KTDKAHVDNL YRPLFASLSS IPGINVASVS VPVSSSTEAF RSAFDQKPPR
     DGGGVNILGS RLFSRKLLEA PGGAANLTAA LSKLDFKNLQ PAIGHLVAGG QVAKNTHIQS
     ALNPSWRKAL VHLVISRDWS IDSTFAEQEK ISTKLTAEEI PLLAAVEPDM GAYTNEADVN
     EPRFQQTFWG TNYNTLLRVK NRWDPRGLFF VRSGVGSEAW DKQGLCRA