ID Q0CI33_ASPTN Unreviewed; 994 AA.
AC Q0CI33;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 03-MAY-2023, entry version 79.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=ATEG_06651 {ECO:0000313|EMBL:EAU33195.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU33195.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CH476602; EAU33195.1; -; Genomic_DNA.
DR RefSeq; XP_001215829.1; XM_001215829.1.
DR AlphaFoldDB; Q0CI33; -.
DR STRING; 341663.Q0CI33; -.
DR EnsemblFungi; EAU33195; EAU33195; ATEG_06651.
DR GeneID; 4322183; -.
DR VEuPathDB; FungiDB:ATEG_06651; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_1_0_1; -.
DR OMA; MIVAVNW; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:EnsemblFungi.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:EnsemblFungi.
DR GO; GO:0000103; P:sulfate assimilation; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 653..883
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 994 AA; 109089 MW; 63DE9B7B42977B3F CRC64;
MASLSALSGP TYVTAQTLIQ QVAYALSDKI FSYSPESFDL DAALREWAAR KETNANGESP
AVKAMETRQG AGNIALGYLF SQDFDLKKRH VPQGIVASSA TLPYMRSALE QLSLLYSVAS
PVAAHVAAVD YAEEGLVSDY ASALSLAEEL GLGLVSSASV HEAQHMALLT TLLASVLPSV
HIYDGVRVGR DHTRVIDVLD QAGLSRTYES VRKTLEDTRS RHLDNQGKLL ELLQALNGEL
GTDYGLFEYH GHAEPVSVLV AFGTVEASLT AQVARSLAKD GIPVGVINVR VYRPFVEEEF
LRVLPQSVKT VGVLGQVADE QAVQEQGIRS ALYEDVLAAL TFATGREHAP TCVDIKYPRS
QRWDLINTAA AFQLVFEKPI VPADGQSAPL QLLDPASVQE YSFWDVDSSV CDAAAIELSQ
ALAADSASNV TTSKVHDNLI QGGAVRVDIR KSSKIVDAPY AVTAADTTYV GDIKLLSEID
ILASVKENGK LIVNAPAVKD DELEKKLPAA FKQAVSQRGV SLYVVDPSVA EDSTLSSVVL
QTAFLRVALP SLESVGVKKL GSINGKTEAL QKVSDDLNKM LRQIEIPEAW KTPEEGAEAP
QLPKDISLNS FVSFDKDVAE PAPLLKDWQA AAKGLVFKEA YGTKTALRPD TAAKTFTVHV
SENRRLTPVT YDRNIFHIEF DLGDSGLKYD IGEALGVHAE NDPQDVAEFI KFYGLNPDDI
VEVPSREDPA VLENRTVHQA LVQNIDIFGR PPKRFYEALA EFATDEKEKK LLLTLGSADG
AVEFKRRSEV DTINFADLLL EFPSARPDFH DLIRIVGPLK RREYSIASCQ KVTPNSVALM
IVAVNWTDPK GRERYGLATR YLSRLQPGTP VTVSVKSSVM KLPPKREEYC YGEEWEAYQE
AGVITVLGRA FSRDQPEKIY IQDRMRQTLP EIIQAYIREE GAFYLCGPTW PVPDVTAVLE
EAIATEAKNN GKKVETRKEI EKLKDEERYV LEVY
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