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Database: UniProt
Entry: A0A397H2W5_9EURO
LinkDB: A0A397H2W5_9EURO
Original site: A0A397H2W5_9EURO 
ID   A0A397H2W5_9EURO        Unreviewed;       362 AA.
AC   A0A397H2W5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=CDV55_103652 {ECO:0000313|EMBL:RHZ57059.1}, CFD26_105532
GN   {ECO:0000313|EMBL:RLL96218.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ57059.1, ECO:0000313|Proteomes:UP000215394};
RN   [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL96218.1}, and HMR AF 23
RC   {ECO:0000313|EMBL:RHZ57059.1};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:RHZ57059.1}.
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DR   EMBL; NKHV02000139; RHZ57059.1; -; Genomic_DNA.
DR   EMBL; NIDN02000119; RLL96218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397H2W5; -.
DR   STRING; 1245748.A0A397H2W5; -.
DR   OrthoDB; 981595at2759; -.
DR   Proteomes; UP000215289; Unassembled WGS sequence.
DR   Proteomes; UP000215394; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR13789:SF311; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10180)-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000215289}.
FT   DOMAIN          1..298
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   362 AA;  40347 MW;  1A531FE9EB1F50F1 CRC64;
     MRELGLLPQI EEKGMKLESM DLRRYKDGRI ITSMPCGETI VQDVIHRADY HQILLDKATS
     LGVEIRLGAL VEKVLVDETA VIVGDETITG DVIIGADGLW SKVRKVVVDE PHPPEETGDL
     AYRATFSRAQ LLALNDPAVK ALCEKQGVTA WLGPKKHAVF YPVRGGQEYN LVLLQPDDLP
     PGVRTTQGDV DEMRYGYREW DPTLGKMLSC IPTVLKWKLC HLPELPRWTK GSVTLLGDAC
     HPTLPYQAQG AAMAVEDGAV LGMLLHHVAS SQDYISKIPQ ALKLYEDIRK SRTAQNVQGA
     IRNRGGFHLS DGILQRLRDL VLRWSGLTRE TDWLGLMSSR QRAVLGFDVL QEVEQRMPEL
     SA
//
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