ID   F8MEW1_NEUT8            Unreviewed;      1401 AA.
AC   F8MEW1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NEUTE1DRAFT_76458 {ECO:0000313|EMBL:EGO60885.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60885.1};
RN   [1] {ECO:0000313|EMBL:EGO60885.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60885.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; GL891302; EGO60885.1; -; Genomic_DNA.
DR   RefSeq; XP_009848067.1; XM_009849765.1.
DR   GeneID; 20829893; -.
DR   KEGG; nte:NEUTE1DRAFT76458; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_76458; -.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   OrthoDB; 1945480at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          222..474
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          651..719
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1401 AA;  155275 MW;  0E64DDF8472CCBBC CRC64;
     MSAEPGNRFC LSPHESNRSS PGTDTDRRSA QPSSSLAYTS RTHQSNGAPS PPPTPACSGH
     QLGVKTDTAG LFLGSTHTNG DSDASFTESP ASDFPPTPRR SPKQQPQDYS RSKQESHQIP
     TEGIHDHQPG GPRARANTKV RSYVADQDRQ AFPRISKPVE LIQVAYDVVV IGSGYGGGVA
     ASRMARTGSS VCVLERGREK WPGEYPTGAA DAFKELHTSG TFAPGSLDGI PVETGDPTGM
     YHLIFGKGQN AVVANGLGGT SLMNANVFME ADKGTLAMKA WPPEIRNKVD SLDKYYEKVE
     KVLEPAEYPD DWPELPKAKL LKKQAQYMGY GDKWRKVKQT TRFQNGPNSC GVEMSASALT
     GQDATGVNDG SKTTTLVTYL ADAWNWGAEL FCECEVRYVE KAKDENGNDD GYLVYFAWHG
     RNRGHFKANL HGDLMWVRAR KAVFLGAGAL ATPEILLRSK AMGLEMSNLV GQNMSGNGDI
     LAFGYNTDET VNGIGRAYPS PYNPIGPCIT SVIDCRHNLE NPLDGFVIEE GSVPHALAHF
     LQAMLDLMPG SEEPKNLTVL DKAHSALARY GSRFLGPYFK KGAIERTQVY LIMSHDSNQA
     MLTLQDDKPV LEFLGVGRSD HVKKLNNLLA QATQAVGGTY VKSPFDAMMG NQQITVHPIG
     GACMARDNTG RTGVTNHVGE VFTGLGSETH DGLIVTDAAV IPTALGTNPF ATIAALAERS
     VEAYCQRQGL HISEEENGIL DLFGEPQHKP KQHLPVRTVS KIEAMEEGHS LGYATRAIQM
     AKELCSSGMG FTEVMSGFIH HDPTMKTDER STYELAYRTA KSRCESARFF LSVQAFDTFR
     TLSHAQHRAM LTGTFVCPAI PGSPFMVRRG EFNLFIIDDK APGTRNLTYD FDMTGVDGRR
     LHFHGYKVVD SSVALDPLQF WRSTSTLYVT VSEHVDGMCS NLDDENAWRR GKVLAKGIMN
     IQPKHFLSEI MTMTPTGSNL LKKVASAASF LTFFTRKSLS LFMAPLTPLE YPSMMPTGYV
     NNTAPTKSFA IYADDGVCTR LHMWEPTHYP DNDKKNIKNL FMVPGAAVDH HIFALPTIRY
     NAVNYFRRAG YRVFITVHRI GQLMVAEHNW TTYDARLDIK ACMQYIREHY GKEKIYTIAH
     CMGSVALSTG MLDGTIPTDW FLGVSCSQVF MNPIWQTMNL IKATTGPYDK IYKALAGNWF
     SCSTSRNDSY VQQALNQLLR LYPQPRKEIC NNAACHRTSL VFGRCWNHSN LNEATHRQID
     RFFGGVNMKL LHLLMKQGAE GHVMANEPLC QRLDTPENIQ RLKGIPFLLF VGRDQAVLSP
     ESTERTYEIL CDTFGMDDTS YKRRVVPGYG HLDVWMGRNA WKDVYPFVRE EVDRVCRGET
     YKFVEPQDEF KAMVDSGELL H
//