ID A0A1G4BQX2_9PEZI Unreviewed; 477 AA.
AC A0A1G4BQX2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=CORC01_00694 {ECO:0000313|EMBL:OHF03832.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF03832.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF03832.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF03832.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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:OHF03832.1}.
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DR EMBL; MJBS01000004; OHF03832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BQX2; -.
DR STRING; 1209926.A0A1G4BQX2; -.
DR OrthoDB; 275141at2759; -.
DR Proteomes; UP000176998; 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:UP000176998};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 19..477
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5009364086"
FT DOMAIN 26..62
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT ACT_SITE 207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1,
FT ECO:0000256|PROSITE-ProRule:PRU10057"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 477 AA; 49544 MW; 14BAAF17688EEEDB CRC64;
MAARALFTVA LLGTAALAVP IEERQSCGAV WAQCGGQGFT GPTCCASGST CVVNNAYYSQ
CLPGSASSSS SAAASSTIRS SSSAVVSPSR TSTTAGAGTT TTLVGTATTS APVVTGGATY
TGNPFAGVNL WANSYYASEI TTLAIPSLSP ALATAAAAVA KVPTFMWMDT RAKIPLVDST
LADIRKANAA GGNYAGQFVV YDLPDRDCAA AASNGEYSIA DGGVAKYKEY IDAIRTMVLK
YSDIRILLVI EPDSLANLVT NLNVAKCSGA QAAYLECTNY AVTQLNLPNV AMYLDGGHAG
WLGWTANLGP AANMYAKVYK DAGSPKALRG IVTNVANYNA WSVSSPPSYT SGNSNYDEKH
YIEALQPLLA AQGWNAQFIV DQGRSGKQPT GQQAWGDWCN AIGTGFGLRP SSNTGSPLVD
AFVWVKPGGE SDGTSDTTAT RYDYNCGKSD ALKPAPEAGT WFQAYFEQLL VNANPAF
//
