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Database: UniProt
Entry: A1DIY3_NEOFI
LinkDB: A1DIY3_NEOFI
Original site: A1DIY3_NEOFI 
ID   A1DIY3_NEOFI            Unreviewed;       791 AA.
AC   A1DIY3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Cellobiose dehydrogenase {ECO:0000313|EMBL:EAW19340.1};
GN   ORFNames=NFIA_093020 {ECO:0000313|EMBL:EAW19340.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19340.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; DS027696; EAW19340.1; -; Genomic_DNA.
DR   RefSeq; XP_001261237.1; XM_001261236.1.
DR   AlphaFoldDB; A1DIY3; -.
DR   STRING; 331117.A1DIY3; -.
DR   EnsemblFungi; EAW19340; EAW19340; NFIA_093020.
DR   GeneID; 4587795; -.
DR   KEGG; nfi:NFIA_093020; -.
DR   VEuPathDB; FungiDB:NFIA_093020; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   OMA; IGYLQCA; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000006702; 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   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..791
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002634541"
FT   DOMAIN          31..220
FT                   /note="Cellobiose dehydrogenase cytochrome"
FT                   /evidence="ECO:0000259|Pfam:PF16010"
FT   DOMAIN          254..555
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          648..782
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   791 AA;  84426 MW;  C5ABA45E60D3BB52 CRC64;
     MKLLNRLSAA FFAASIVLEP CWAQSSTPVV YTDPATGITF DTWTVPTSQT AGGLTFGVAL
     PSTALTTDAT EFIGYLQCAS TDATKTGWCG ISLKGSMTSN LLLMAWPYKD EILTSFRFSS
     GYTMPDVYAG NATLTQISSS VNATHYTLLF RCQGCLAWNH NGVTGSAPTS AKQLVLGWAQ
     AVAAPGSPSC PAQITLQQHD AQGIWVAKLD ASAASASYEQ WAALANKTVP GDCSGGGGGT
     DPVGVPVPPG TTFDYVVVGG GAGGIVVADR LSEAGHSVLL IEKGPPSSGR WGGTMKPDWL
     VGTNLTRFDV PGLCNQIWHD SAGIACDDID QMAGCVLGGG TAVNAALWWK PYPLDWTYNF
     PAGWQAEDMV SPTNRVFNRI PWTVHPSADG KIYMQQGYNV IAGGLQAAGW KELTLNDNPS
     WKNHTYGHTP YMFSHGERGG PMATYLVSAS KRNNFKLWMN TTVKRVVRTA DGHVTGVEVE
     PFLDGGYEGV VNVTAKTGRV VLSAGTFGSA RILMRSGIGP SDQLDIVKSS SDGPTMIDKS
     AWINLPVGMN LVDHVNTDTV ATHPDIVFYD FYAAYDDPIK SDASSYLNNR IGILTQSAPN
     IGPIFFDEIR GADGITRQIQ WTARMEGGHD TPDDHAVVMS QYLGRGSTSR GRMTITANLD
     TVVSTLPYLR DQHDVDAVIQ GLVNMQNALK GVGLNWTYPA PNITAEEFVN TMEITASTRR
     ANHWLGTCKM GTDDGRKGGT AVVDTNTKVY GTDNLFVVDG SIFPGMVTSN PSAYIVIAAE
     RAADRILALA T
//
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