ID V5FZA2_BYSSN Unreviewed; 562 AA.
AC V5FZA2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PVAR5_2572 {ECO:0000313|EMBL:GAD93952.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93952.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:GAD93952.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAUL01000072; GAD93952.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FZA2; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_024886_0_0_1; -.
DR InParanoid; V5FZA2; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00469; PNDRDTASEII.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT REGION 487..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 63320 MW; AAA99815605B6CF1 CRC64;
MGLFNYIVSW IYQVIQFFIS KLFSPTPPPP QRRISNPRRI AVIGAGITGV SSAAHCVGHG
FEVTIFEAND RDHLGGIWSR VNPTSSLQIH SLMYRFHPSV RFKHEYPHRD AIIREVTDLW
KKYRLDERTE FEVPVHSIWK DEKTGKWFVE DPSYGGFDGV IAAVGTCGDP KMPHMPGQEK
FAGQIYHSSD LAGKDVRDKN VIVIGGGASA VEAVEFAVQG GAAQTTILAR SDKWIIPRNA
VVDALLSFNI FGEETEFSWV PELLLKLFFY RDLEDLAPTR RGLYTDTPMV NDDILQQVRK
GRVKWLRGDI KEFAEPGIIF NHRAKGVPKG GPGKETTIKG DICVMATGYH RPSLSFLPDD
VFGEPYKPPN WFLQTFPIGH TDICANNCTY VHGIGTVGNV HIGLYTRLLL MFLADPRTRP
STAWMRIWVD WTRMCKRAAP AGALEFFTYS ELVWWIVFNI FSSPWRWKWI FFVLWGWGSI
PANRAGNENP IANGSARPQA DTKGSESRGP RNERLGPNSK PTYSAALASN MQKGQPRETN
LKEEPPFADA HGQQAKEEKK KA
//
