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Database: UniProt
Entry: A0A094FIY2_9PEZI
LinkDB: A0A094FIY2_9PEZI
Original site: A0A094FIY2_9PEZI 
ID   A0A094FIY2_9PEZI        Unreviewed;       611 AA.
AC   A0A094FIY2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=V498_06689 {ECO:0000313|EMBL:KFY88693.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY88693.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY88693.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFY88693.1}.
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DR   EMBL; JPKA01001734; KFY88693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094FIY2; -.
DR   HOGENOM; CLU_001570_17_5_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          196..488
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  67803 MW;  555C1D17A5206791 CRC64;
     MAIRTKTTSH CIPEEPPVDN ISPRSAVPSL TSNSSADEEE IPKEPRRRRA STVLISQNAD
     DARRIIGESG TRLIETCCGG GCCMLAPKAD SQSFEYVPLP DNDAFRGLGL NLGQLPKKLT
     AIHELPPRTV SLSPVRDTKA PAIVGADPDE RPFNPAVDQS IDFTPHTAEI DEKLQHARTP
     TSSEHPPKFV KPHPPYEVFS AKIFNTRELT RAGAQKRTFH FDLDVSDYPA ETGVDFKVGG
     AIGVQAPNEE EMVEEIMDLL SIPRVARDRK VLVTTTSGRW PTIWGEDKPR SLVSTRRDLL
     TWCADIQSYP PTKALLRVLA EHTTDPNERK ILTYLCSAEG QGKFCDLRTG PHLTLAQLLH
     AFPSAKPPLD HLLAVLKQLM PRFYSLSNDP HENCVPVKGC SRLIEIAVTV HETESWRGDR
     TGLSSGFFER QARKFIAAEK RGEKPDLRIP MFKGLMSNPL AREFISDGPM LLIGAGVGVA
     PFRGFVQRRL KSANCANKVW VLQGVRDSLL DELYSGEWGV HEDEVKKVVQ SRTGVGRYVQ
     EEVVAQKDLC WFVINALDGR IFVCGSSKGM GEGVESSLVQ VGMEMGNMSR AESEEFWRLK
     KEAGQYIAET W
//
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