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Database: UniProt
Entry: L8X939_THACA
LinkDB: L8X939_THACA
Original site: L8X939_THACA 
ID   L8X939_THACA            Unreviewed;      1020 AA.
AC   L8X939;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cellobiose dehydrogenase {ECO:0000313|EMBL:ELU45612.1};
GN   ORFNames=AG1IA_00372 {ECO:0000313|EMBL:ELU45612.1};
OS   Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS   (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU45612.1, ECO:0000313|Proteomes:UP000011668};
RN   [1] {ECO:0000313|EMBL:ELU45612.1, ECO:0000313|Proteomes:UP000011668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX   PubMed=23361014; DOI=10.1038/ncomms2427;
RA   Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA   Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA   Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA   Wang L., Liu H., Li P.;
RT   "The evolution and pathogenic mechanisms of the rice sheath blight
RT   pathogen.";
RL   Nat. Commun. 4:1424-1424(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELU45612.1}.
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DR   EMBL; AFRT01000060; ELU45612.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8X939; -.
DR   STRING; 983506.L8X939; -.
DR   HOGENOM; CLU_296152_0_0_1; -.
DR   Proteomes; UP000011668; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        121..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          497..785
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          883..1009
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   1020 AA;  112167 MW;  E6466846AA127A22 CRC64;
     MLRPDRALPR LDYDVQQVAL VPSAGSDIYQ ASTRGYAHTM KATRRVLVTN RFVELRLNNM
     FVVSVALTNV RTIAQRLSSA KYELDGIITR WIGARLDWSH QNKYHGGNPL WNWMFSFWER
     VYPVAICFIM AAFNASSTAF VLFDWVDKKY GIVFFTPVAI LLTGNFHQKW KYVYSSMVLV
     LRPHSCTSLT GPPNAYQKQM VSQENQLSDN PASAVTYGTI STGEPSSEQP RHPDPKDTFV
     GIMSGRPFIR TTLDASVAIL IIGVSYGGLG MTSLVATQII LLDYFEAIGV IDLSFIVGDY
     CGKIGDYSRW VIQFDTRPNR QFGQESTAWK LQPNQQRMVD FRDRKVTVLG IQVSFDIAPK
     TGCLLQSSSH DLAHHAVSLG RRYYTHHRII LPTTKALNWR LASRDSLPAF TLIFSLLKEV
     TCFIADIFLV PNWARKLHLL LIISRKGWAE LVVYKPPCRD GSSTTSAAML CLFLFSVFAG
     ATLAQGSVNN STATTRYDYI VVGAGASGII VADRLSEAGK DVLLIERGGP STLATGGTEV
     PPWPSKTNLF ISILTWANLD IQAGAACLIG GGTAVNGLLY WYPTDAEWDT SNGWPKGWQQ
     PNAALNKVKA RLPSTDIPST DGKRYLTQVY DVVKSILKTQ NYSAITINED RNSKNRIYGH
     PNYYIQDGKR TGPMDTYLKT ARARSNFKLI TNTKVLSVIR NGAQITGVQT NDNSLNGNVI
     IQLTSKGRVI LSAGAFGTAK ILFGSGIGPS DQIALIAGNS ALSKHLPPSS QYINLPVGMN
     VKDKPGVNLI FTHPSVDWYD NFAPIWSNPR VSDANQYVRD RSGVFAGSSP RINFWRQYNG
     SDGKTRYVQG TSRPGAWGVS TIYPYNITAQ FVITLYLATG LTSTGRIGMK DTSLAMSAIV
     KPWFTDPVDK EVMINAMNDI LSTYKQVPDL VLVAPDNVTS IDRHIAQVLH TPNHWTGSTR
     IGTSSSDSVV DTTTKVWGTD NLFVVDSGIM PGMTAGNPQG AIFVMAENAV AKIIALAGGP
//
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