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Database: UniProt
Entry: K1X987_MARBU
LinkDB: K1X987_MARBU
Original site: K1X987_MARBU 
ID   K1X987_MARBU            Unreviewed;       499 AA.
AC   K1X987;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=FAD dependent oxidoreductase family protein {ECO:0000313|EMBL:EKD17303.1};
GN   ORFNames=MBM_04880 {ECO:0000313|EMBL:EKD17303.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17303.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD17303.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17303.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
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DR   EMBL; JH921437; EKD17303.1; -; Genomic_DNA.
DR   RefSeq; XP_007292769.1; XM_007292707.1.
DR   AlphaFoldDB; K1X987; -.
DR   GeneID; 18760815; -.
DR   KEGG; mbe:MBM_04880; -.
DR   eggNOG; ENOG502R1TU; Eukaryota.
DR   HOGENOM; CLU_028280_0_0_1; -.
DR   InParanoid; K1X987; -.
DR   OMA; HAPFELH; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..499
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003852965"
SQ   SEQUENCE   499 AA;  52655 MW;  DD75DAF504C141F8 CRC64;
     MKFTQLVSPA LALWAYAATA QPVEDIGEAC ETDTGSTSTA APVEVDVDVA IIGGGSGGIH
     AAIQLQAAGA NVAVIEKENR IGGHCKTFYA PVDVPINTGV IIFENNTAVI SYFEQLNVNL
     TFTNPVTDVP ASTPAAQNFD FSLGIPIPAQ SANDAQAQQA AIAAAVQSYT TNILAVYPWI
     DNGYLVPDPV PADLLLPFGE LAKKFSFEPL LPIIAQFNWF IGDVATIPAL YGIKCFGPGL
     VQSFFAKFII PTSTDAEDLY RAAANMLGES IYYQSTIMEV KRTVEGASTN GTSVTVLINQ
     PGQPAKLIRA KKLVVAIPPT MSNIGTYDLT SEETDIFSKF AGMGHWAGVV QVPGLTNSVR
     NIGAMTPYNT PVIPGANGIE LSASPGYFST SVGFEDTNYT LADGENVVRS ALATLETVGG
     VPAGSSAAAT FPYSADHAPY NVRVSMDDIS QGFYKKLLAL QGQRNTYWTG AAFAAHNSGL
     IWKYNVETIV PGVIADLGL
//
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