ID A0A194VGW3_9PEZI Unreviewed; 489 AA.
AC A0A194VGW3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=VP1G_10400 {ECO:0000313|EMBL:KUI63255.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI63255.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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DR EMBL; KN714881; KUI63255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VGW3; -.
DR STRING; 694573.A0A194VGW3; -.
DR OrthoDB; 275141at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; -; 1.
DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361186};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361186};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 19..489
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5008443802"
FT DOMAIN 27..63
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 90..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 265
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1,
FT ECO:0000256|PROSITE-ProRule:PRU10057"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 489 AA; 51157 MW; 78B408247C0EA5B1 CRC64;
MASRRLILAA VLSVTALAAP LVEERQSCAS LYGQCGGTSW TGATCCVSGS VCTYGNDYYS
QCLPGTASSS STITTSSKAT SSVATSTTSK ASSSSATTTT SASTSKASTT TSVKTSTTVT
GGASTTTSYT GNPFSGIQQW ANSYYASEIS AYAIPTLSAA QASQAAEVAE VPTFQWLDTA
AKVSTLMAET LADIRSANAA GASPPYSAQL VVYDLPDRDC AAAASNGEYS IADDGLTHYK
AYVDAIRQQL ISYSDIRTIL IIEPDSLANM VTNLNVAKCA NAQSTYYTGV NYAITQLNLP
NVAMYLDAGH AGWLGWSANL QPAATLFAQV YNNASQPASV RGLATNVANY NAWNISSAPS
YTSGDSNYDE NLYVQALAPL LSSAGFDAHF ITDQGRSGKQ PTGQTAWGDW CNAIGTGFGT
RPTTDTGLDL EDAFVWVKPG GESDGTSNTT STRYDYHCGY SDALQPAPEA GTWFEAYFEQ
LLTNADPAF
//
