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Database: UniProt
Entry: A0A2T2ZWH2_9PEZI
LinkDB: A0A2T2ZWH2_9PEZI
Original site: A0A2T2ZWH2_9PEZI 
ID   A0A2T2ZWH2_9PEZI        Unreviewed;       539 AA.
AC   A0A2T2ZWH2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:PSR78430.1};
GN   ORFNames=BD289DRAFT_443940 {ECO:0000313|EMBL:PSR78430.1};
OS   Coniella lustricola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX   NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR78430.1, ECO:0000313|Proteomes:UP000241462};
RN   [1] {ECO:0000313|EMBL:PSR78430.1, ECO:0000313|Proteomes:UP000241462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR78430.1,
RC   ECO:0000313|Proteomes:UP000241462};
RA   Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA   Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT   "Coniella lustricola, a new species from submerged detritus.";
RL   Mycol. Prog. 17:191-203(2018).
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DR   EMBL; KZ678607; PSR78430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2ZWH2; -.
DR   STRING; 2025994.A0A2T2ZWH2; -.
DR   InParanoid; A0A2T2ZWH2; -.
DR   Proteomes; UP000241462; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847:SF150; OXIDOREDUCTASE TDA3-RELATED; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000241462}.
FT   DOMAIN          9..114
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          240..518
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          114..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  57127 MW;  E8ED46E9B374AF47 CRC64;
     MANPQEKKKI VIVGGGIIGA TTAYYLTRHP KFDPALHTVI LLEAAAIAAG ASGKAGGLLA
     LWAYPECLVP LSYRLHKELA DEHDGVQKWG YRRVNCGTIG AVVKPADLER AVQQTQMEAV
     EDAKAEAESK ASAKAPAAQP GMSALQASST STSAPQAEIG GTSLAVLEGN KPSETGTAAS
     EAPEARPATA NSGEKSNGSI SNGTAETHPV KEEKDWEKLP KQDSAAVSLL ETSTLPSDLD
     WIDSKLVQSY EQMGRRGFTE TSQVHPFHFT AAIAELARSA GVDIRLGAKV TDIRSSPGDG
     GSSSSSSSSS SATDPGPPSL RIVEYQDRND GDAVKTIENV TDVIITAGPW TGKLLPRSKI
     EGLRAHSIVY EAEVTPYAVF TDIQLPTDYV PEHRAKAGQK RRHKGNVDPE VYARPFGEVY
     ACGEPDKTVP LPETADQVQA DTAQCDDLAA YLATVSPTLA AAPIRARQAC YLPQHVRFGT
     ERGPLIGPTA APRIWIASGH TCWGIQNGPA TGYLMAQWLL DGEPTAADID VLHPAKFKV
//
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