ID A0A0D0Q546_KITGR Unreviewed; 451 AA.
AC A0A0D0Q546;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=TR51_18475 {ECO:0000313|EMBL:KIQ66128.1};
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ66128.1, ECO:0000313|Proteomes:UP000032066};
RN [1] {ECO:0000313|EMBL:KIQ66128.1, ECO:0000313|Proteomes:UP000032066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ66128.1,
RC ECO:0000313|Proteomes:UP000032066};
RA Arens J.C., Haltli B., Kerr R.G.;
RT "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT terpentecin and satosporin producer.";
RL Submitted (FEB-2015) 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:KIQ66128.1}.
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DR EMBL; JXZB01000002; KIQ66128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0Q546; -.
DR STRING; 2064.TR51_18475; -.
DR PATRIC; fig|2064.6.peg.3962; -.
DR Proteomes; UP000032066; 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 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 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; 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:UP000032066};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 24..451
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5005112292"
FT DOMAIN 342..451
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 317..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10057"
SQ SEQUENCE 451 AA; 45554 MW; 1AFE561E936A7DAB CRC64;
MLALAATATA LGLVAGVQGG ADAAVQGSLP AGTQFYRDPA SQVVKWVAAN PGDSRTPVIS
KRIASQPQAI WFSNYRPTTV TSDVRAVTAA AEQAGRTPVL VAYTVPNRDC GGASAGGAPD
LASYDAWVGK FAAGLGSSRS IVVLEPDSIA LTTCLNAQQQ SDRFASLARA VTTIHAASPA
TKVYLDGGHS TWNSASEQAN RLRSAGVLNA DGFFSNVSNF NTTAGETAFA HNVLSALGNP
GNLHAVIDTS RNGNGPAGST WCDPSGRAIG NYPTASTGDS AIDAFLWIKP PGEADGCAAA
AGTFVPDIAY QLAVNAADPT SAPSSQPPTS QPPSSQPPTS QPPSGGTSCS VAYRVNSWSA
GFTADITVKN TGNATIAGWK LGWTFPGDQK VTSAWNATVV QSGAAVTATD LGYNGTLAAG
ASTAFGLQAT YGSNNTAPSA FTLNGTACTL S
//
