ID A0A1I4W8N8_9ACTN Unreviewed; 570 AA.
AC A0A1I4W8N8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=SAMN04487980_101169 {ECO:0000313|EMBL:SFN09777.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN09777.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFN09777.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFN09777.1,
RC ECO:0000313|Proteomes:UP000198530};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOUV01000011; SFN09777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4W8N8; -.
DR Proteomes; UP000198530; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR34876; -; 1.
DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS51318; TAT; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 25..570
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5011330665"
FT DOMAIN 30..139
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT ACT_SITE 509
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 507
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 570 AA; 59671 MW; 5F7B65CDF4451110 CRC64;
MSRTRTALLA AMALVAGAAG TAVAAVPDDA GVQAIPCTVD YKVQNQWSTG FTAAVTVTNN
SAAKSSWAVK WSYAGNQQVT SGWNSRITQS GSAVTAANET YNGTLATGGS VSFGFQASYS
GTNALPTTFT LDGVTCNVDD GGGGGTDPGP GTPGTKVDNP YSGAKVYVNP EWSAKAAAEP
GGSRISSQPT GVWLDRIAAI AGSGGKMGLR AHLDEALRQK GSGELAIQLV IYNLPGRDCA
ALASNGELGP TEIDKYKTQY IDPIKAILAD PKYAGLRIVT TVEIDSLPNL VTNTGSRPTA
TPQCDVMKAN GNYVKGVGYA LNKLGDVPNV YNYVDAGHHG WIGWDDNFGA SATVFKEAAT
AEGATVNDVH GFITNTANYS ALKENNFTIN SSVGGTSVRE SKWVDWNRYV DELSFAQAFR
NQLVSVGFNS NIGMLIDTSR NGWGGSARPS GPGATTNVDT FVNGGRYDRR IHIGNWCNQS
GAGLGERPKA APEAGIDAYV WMKPPGESDG SSSLIPNDEG KGFDRMCDPT YTGNPRNGNN
MSGALANAPI SGQWFSAQFQ QLMQNAYPAL
//