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Database: UniProt
Entry: A0A2T3Z6A3_9HYPO
LinkDB: A0A2T3Z6A3_9HYPO
Original site: A0A2T3Z6A3_9HYPO 
ID   A0A2T3Z6A3_9HYPO        Unreviewed;       413 AA.
AC   A0A2T3Z6A3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=M441DRAFT_170546 {ECO:0000313|EMBL:PTB40325.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB40325.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB40325.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB40325.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KZ679263; PTB40325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3Z6A3; -.
DR   STRING; 1042311.A0A2T3Z6A3; -.
DR   OrthoDB; 2158278at2759; -.
DR   Proteomes; UP000240493; 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; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR   PANTHER; PTHR47356:SF3; FAD-DEPENDENT MONOOXYGENASE SRDH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
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:UP000240493}.
FT   DOMAIN          4..330
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   413 AA;  45415 MW;  A13D2E78B398E38F CRC64;
     MAFKVIIIGG GPVGLFLANG LQASGIDYVL FEKRSTIPPS TAFGIFLWPQ VTRMMHQLGL
     LDSLRKVSHP MTGMIHSMPT GELLSSDTNF SKSYKTHGYP VVVTDRGSLA QVLLSGIDKP
     EERIHTGKQL TNVITRPDRV TVEFADGTSF EGSIVIGADG IWSTVRNQIS QYAPDGLFLD
     NPYQASYQGV FGRAPLLEGI TSGQGIEVHG DGWLIQAFPS QKETHLFIYK SIKTTNERVP
     FSPNVPEELI AEFANVRLTD NVTFKDLWNQ RFAQGTANFE EGVVEMWHWD RIALIGDAVL
     KISPKQGVAA NVGMESAACL TNKLAALLQN NPKPTTQEVS KVFSAYQCEL EGKVSTWQRL
     SRFNLDSAVS KNGPRLEAMG AVAARVPAIV SRSFKFERVP FADQNAADMP WVH
//
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