ID   A2478_ARTBC             Reviewed;         565 AA.
AC   D4B1Z7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase ARB_02478 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02478;
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; ABSU01000028; EFE30558.1; -; Genomic_DNA.
DR   RefSeq; XP_003011198.1; XM_003011152.1.
DR   AlphaFoldDB; D4B1Z7; -.
DR   SMR; D4B1Z7; -.
DR   STRING; 663331.D4B1Z7; -.
DR   EnsemblFungi; EFE30558; EFE30558; ARB_02478.
DR   GeneID; 9523853; -.
DR   KEGG; abe:ARB_02478; -.
DR   eggNOG; ENOG502QQWK; Eukaryota.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OMA; FVCNRCV; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..565
FT                   /note="Uncharacterized FAD-linked oxidoreductase ARB_02478"
FT                   /id="PRO_0000434672"
FT   DOMAIN          118..302
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         155
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P08159"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   565 AA;  61795 MW;  9C3FAFBEAE627E86 CRC64;
     MKIPSQQVLL ALPLLASPAQ SYPGKHPRCS AGDACWPKEH VWQDFNSTIS GRLIRTFPAA
     AVCHTAQYDA AACSVAKERW TDSFWRTNQT GAYSAILWEL GEKGQCFINT PKEDRCDQGI
     VPYYSVSASG VKDIEKAVKF ADKHDLYLVV KNTGHDHLGR SSGSGAFSIW THNLKGKEWH
     KSFKPKGAPS NVSGIPAVTL QAGEQLLDVY KAAAAEGVTF AGGSAQTVGA AGGFMTGGGV
     SPFSHFYGLA VDNVLEVNLV TAQGKAKTIN QYTDPDYFYA LRGGGGSAWG VITSVTYKTH
     PKPTHIRVGI AQLNITTEDS RRVVIEKTLQ ALPDITEAGW VGYGVYATEK SNPTAFQVIF
     LQPNATMENF NKTFEPMNEI ATLPGVTGGA VSYVFPDFLE YSKNFLRDPN IATNVIDASR
     LVSRQVLTER ARDLVDLMFE YPTTGPGFNS IVKVNSDERD NTAVHSSFKN SRALISFSVD
     WADNASEKEK KAAKKTSAEV SKRLAEIVGK ETGTYLNEAS PYEPDWQNAF WGDKYARLLS
     IKRRIDPKNL FVCNRCVGTD IILEP