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Database: UniProt
Entry: A0A094FP63_9PEZI
LinkDB: A0A094FP63_9PEZI
Original site: A0A094FP63_9PEZI 
ID   A0A094FP63_9PEZI        Unreviewed;       646 AA.
AC   A0A094FP63;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V500_08222 {ECO:0000313|EMBL:KFY85655.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY85655.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY85655.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007801}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY85655.1}.
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DR   EMBL; JPKC01002455; KFY85655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094FP63; -.
DR   STRING; 1420913.A0A094FP63; -.
DR   HOGENOM; CLU_009665_9_3_1; -.
DR   Proteomes; UP000029284; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02979; PHOX_C; 1.
DR   Gene3D; 3.40.30.20; -; 1.
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; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR   InterPro; IPR038220; PHOX_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43004:SF7; P-HYDROXYBENZOATE-M-HYDROXYLASE; 1.
DR   PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF07976; Phe_hydrox_dim; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029284}.
FT   DOMAIN          20..378
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          423..600
FT                   /note="Phenol hydroxylase C-terminal dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07976"
SQ   SEQUENCE   646 AA;  71767 MW;  866B910FA21C9CCA CRC64;
     MADNTSPNEL VPAPAVELYD IVIVGAGPVG LLLSTCLARW GYKIKHIDNR PEPTKTGRAD
     GIQPRSLDLL KNMGLKPQIM AHKPAKVFEV AFWDPTSAQD GIHRTGTWAS CPSFIDARYP
     FTTLLHQGHI ERAFITDLEK NGVAIQRPWT ITGFKTDADV DPTYPVEVNI AHIDGTAKET
     VRAKYLFGGE GARSFIRDQL KIQITHKDPI AHVWGVMDGV VQTDFPDIKM KCTIHSEHGS
     IMVIPREENM VRLYIQIASS TDKDWTPRRT ATEEEVQAAA KKIMAPYNIT WERVEWFSVY
     PIGQGIASKY TLDHRVFLGG DSCHTHSPKA GQGMNTAFLD AQNLAWKIHH VESGFADRGI
     LETYESERKL VAENLLNFDA KYAALFSQRP PAAHDVKAAS EGATSNAGEE NIFIKTFKES
     CEFTSGYGVA YMPNPLNWSP DHPAKSPLIH PDGTTLRTGR ILINANVTRV VDANVVHLEQ
     EIPTNGSYRI YVFAGEQAVT RNALFDFSTN LDKKGSFYSS YRRADKTSIS YHERHNPESL
     FYTLCTIFAS KRADIEVSQD VPATLARYRD HIYADDIWDQ RVPNATAAAH AKMGLDQKKG
     GVVVVRPDGY VGIVVSLVEG SGTVDALNEY FAAFCTKKLG ELRGQL
//
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