ID A0A0D2A1L7_9EURO Unreviewed; 602 AA.
AC A0A0D2A1L7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_01061 {ECO:0000313|EMBL:KIW34271.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW34271.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW34271.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW34271.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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; KN847040; KIW34271.1; -; Genomic_DNA.
DR RefSeq; XP_016254487.1; XM_016387559.1.
DR AlphaFoldDB; A0A0D2A1L7; -.
DR GeneID; 27340255; -.
DR VEuPathDB; FungiDB:PV07_01061; -.
DR HOGENOM; CLU_453400_0_0_1; -.
DR OrthoDB; 445965at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 602 AA; 67421 MW; A1C6B518186D2712 CRC64;
MKRVVIVGAG PCGLAALKEM VESGHETILF ERSGQLGGVF ASATAYPNLH LTISNWAMAF
SDFPDPTRLH YSTAQEYLHY LHEYARHFHL ERRIRYHTEV RSASLRDDGL WSLEIQTLMG
SEQSIFHLQA DALIVATGSN GLPNAPPAGL SEFDGRVIHS SQYDEAFKQE VAEKKLKVLV
VGGGESGADI SAELGDLSPN VTVWLRRPIC VGPRYLNKKD EMEQVEANMA VDFPANGFLE
AATTNRMSAA QNVYAYGFFR RLLWCTPVLN GTLSRMSLAS TASAFLRNDQ ATYVTKNQRM
CEALHDGKIE VVVAPSMSAR GRSCEFQLAD GTTQRRDFDA VVLCTGFRVE FPWIRLPGKL
TLSSTPRSWY LHCFPEGLGH CLFFVGYARP HQGGVPVMAE MLSRYIALLL RGERELPPDY
SAQAKRDAAA SREYYNLSPN LHTLVDYNAF LESAARRIGC EPRLPLLCIL LFNFHMLTVL
LLALQLCHPT LLWWGIRSTL LMWAVSMAGF FVLYDGLLIK WWFYPHWAVW YRQRGPNADP
ALLDGVLNRV NLWKSTAITS GYSPPYIAGC PAPAKALCIA RLPMAAVRSL HAMRSLGWYR
CR
//
