ID A0A423WN32_9PEZI Unreviewed; 844 AA.
AC A0A423WN32;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=VPNG_07433 {ECO:0000313|EMBL:ROW04606.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Cytosporaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW04606.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW04606.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW04606.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:ROW04606.1}.
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DR EMBL; LKEB01000047; ROW04606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WN32; -.
DR STRING; 1230097.A0A423WN32; -.
DR InParanoid; A0A423WN32; -.
DR OrthoDB; 413885at2759; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09630; CDH_like_cytochrome; 1.
DR FunFam; 2.60.40.1210:FF:000004; Cellobiose dehydrogenase; 1.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 3.30.410.10; Cholesterol Oxidase, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR015920; Cellobiose_DH-like_cyt.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR053208; GMC_Oxidoreductase_CD.
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; PF00734; CBM_1; 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 SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 790..826
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 844 AA; 88964 MW; 0E6CAD7F8A61A660 CRC64;
MPYLRPISAQ SSTAVVYTDP DTGIVFDTWT VPQSSTNGTW TFGTALPSDA LTTDATEFIG
YLQCASPDPT VQGWCGISFG GAMTNSLLLA IWPNDGEILT SFRYATGYVM PDVYTGNATL
TQISSTINTT HYTLIFRCQG CLSWDQDGAT GSVSTSSKFW LIGWAQANPS PGNPDCPDDI
TLVQHDNGQS LFPATLDESA ANASYASWAA LATKTVTGSC TTASSTTTAT ATATASSATG
VPVPTATYDY IVVGAGAGGI PIADKLSESG KSVLLIEKGP PSSGRWGGTM KPDWLVGTNL
TRFDVPGLCN EIWVDSAGIA CSDTDQMAGC VLGGGTAVNA GLWWKPNTVD WDYNFPAGWQ
STDMAAATSR VFSRIPGTDH PSLDGQLYLQ QGFDVITSGL GAAGWESVTA NDVPDQKNHT
YAHTEYMYSN GERGGPMATY LVTASARSNF ELWTGTSVRR VVRQGGHVTG VEVEPYLSGG
YAGVVNLTSV TGRVVLSAGT FGTAKLLMRS GIGPADQLSV VAGSAEDGPT MVGNQSWIPL
PVGYNLDDHV NTDTVVQHPN VTFYDFYAAY DSPNTTDADD YLDKRVGILT QAAPNIGPVF
WDEIAGADGV TRQLQWTARV EGSDGTADGK AMTMSQYLGR GATSRGRTTI TSGLDMVVST
LPYLRDAEDV AAVVQGIKNL QASLASVEGL VWTYPGANTS AEDFVSGMVV SYTNRRANHW
IGTAKIGTDD GRVDGGSAVV DLDARVYGTD NLFVADASIF PGHVTANPSS YVVAVAERAS
ERILALAANA ARAQYAQCGG LTWDGGFTCA APYTCTYQNV FYWQELTLVG SPNVNPDLDN
GDVT
//
