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Database: UniProt
Entry: D8QLR8_SCHCM
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Original site: D8QLR8_SCHCM 
ID   D8QLR8_SCHCM            Unreviewed;       759 AA.
AC   D8QLR8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cellobiose dehydrogenase {ECO:0000313|EMBL:EFI91158.1};
DE            EC=1.1.99.18 {ECO:0000313|EMBL:EFI91158.1};
DE   Flags: Fragment;
GN   ORFNames=SCHCODRAFT_114791 {ECO:0000313|EMBL:EFI91158.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI91158.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; GL377319; EFI91158.1; -; Genomic_DNA.
DR   RefSeq; XP_003026061.1; XM_003026015.1.
DR   AlphaFoldDB; D8QLR8; -.
DR   SMR; D8QLR8; -.
DR   STRING; 578458.D8QLR8; -.
DR   GeneID; 9588658; -.
DR   KEGG; scm:SCHCO_02642438; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02642438; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   InParanoid; D8QLR8; -.
DR   OMA; IGYLQCA; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
DR   GO; GO:0047735; F:cellobiose dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 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.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000313|EMBL:EFI91158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..759
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003120955"
FT   DOMAIN          312..335
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          479..493
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          200..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         759
FT                   /evidence="ECO:0000313|EMBL:EFI91158.1"
SQ   SEQUENCE   759 AA;  80663 MW;  A36B6F8AF0214721 CRC64;
     MLWRAALSAL PLVGCALAQT GAQYTDPDNG ITFWGITDAS HSVTYGYVFP ETDTGEFIGE
     IVSPIEGAWV GVSPKGTMLN SLLLVAWANG GEVVHSARIA SGYVLPTPLE GPVITDLPST
     TVNATHWKWV YRCQNCTTWD GGSLDPTGSG APAWAYSTKA VDDPSDPDSD FAQHTDFGFY
     GLDFASAHAS QADYDNWAAG GTGGGGGSPP TTTTTTTTAP PTATATPDPV DYIVVGAGPA
     GIITADRLSE AGKSVLLLER GGPSTGETGG TYSAPWAEGS GLTKFDVPGL FETLFNDANS
     FWWCKDVNTF AGCLLGGGTT VNGALYWYPP DIDFSTDNGW PSEWTNHSPY TAKVKERLPS
     TDAPSTDGKR YLTQVHDVVA ELLKPLGFSS ITINDEPNRK DHVYGYSAYD FLDGKRAGPV
     ATYLQTAQKR ENFKLLMYTN ALNVVRNGTQ ILGVKTNDTS ILDGVYTLNP GGRVILSAGS
     LQTPRLLFQS GIGPKDMITL VQGNTDAAPN LPDEADWIDL PVGENVSDNP SVNLVFTHPD
     VDSYDNWAEV WDDPRPDDAD QYLKDQSGVL AAASPRLNFW RAYVGSDNVT RYMQGTARPG
     AASIDTDNDY NLANVFTITC YLSTGVTSRG RVGIDAALRA GPIVDPWLTD PVDKEVLLTG
     IQEIASAIGN VSDLVLITPD NTTTVAAYLD DYDLTAMNSN HWVGSASIGS VVDVNTKVKG
     TDNLFVVDAS IIPALPMGNP QGALMSAAEQ AVARILALN
//
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