ID A0A072PHP5_9EURO Unreviewed; 479 AA.
AC A0A072PHP5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=A1O9_04230 {ECO:0000313|EMBL:KEF59386.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59386.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF59386.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59386.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF59386.1}.
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DR EMBL; AMGV01000003; KEF59386.1; -; Genomic_DNA.
DR RefSeq; XP_013261976.1; XM_013406522.1.
DR AlphaFoldDB; A0A072PHP5; -.
DR STRING; 1182545.A0A072PHP5; -.
DR GeneID; 25279163; -.
DR VEuPathDB; FungiDB:A1O9_04230; -.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OrthoDB; 981595at2759; -.
DR Proteomes; UP000027920; 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; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-RELATED; 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:UP000027920}.
FT DOMAIN 8..361
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 479 AA; 53011 MW; F1608EB80EFC0390 CRC64;
MSRQRRNVHV GLCGGGLGGL MAAIALARGG AQVTVLEAAA ELGEIGAGIQ MTPNVARFLQ
RWGISDIIGA NLVQCERINI RAADGSLIAF SDFKRILRDY GFPWWVVNRY HLLAGLAESC
KRHGVEIVLD ARVDEIVFSD DVDSKVSVVT EKGARHAFDL LVGSDGVKSV VRKKLFPDVK
PTALTMNAAY RAVIPYEEVF AKIPEAKSVL GNNIDVWTAP GSYFISYPMT AGTDFNAVLS
HHTRDNHIVE DVEEADMVEL RESFEHYDPI VQKIIHLIPE SKRWPLLMTG PLESWSNKVK
NVVLMGDAAH SMVNHLAQGA ATSMEDGVFL GRVISDVVRG ILSLPEAVEI YEKTRMPRAW
TKQQVSFTSG QATFAAEPEL SRRNLASRIE THGYFKNPVD PAHPPPAYRS WNLWGYPDSV
PGVYAYDAES DADNAVCEFL GKQGPVDPTT RVSQRLREKW WSWSVVEAED AQRGEKSKL
//
