ID A0A2A3I0W4_9ACTN Unreviewed; 746 AA.
AC A0A2A3I0W4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=BX265_1304 {ECO:0000313|EMBL:PBC76585.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC76585.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC76585.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC76585.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2017) 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:PBC76585.1}.
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DR EMBL; NSGV01000001; PBC76585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3I0W4; -.
DR Proteomes; UP000218662; 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 CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR013783; Ig-like_fold.
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 SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 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:UP000218662};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 36..746
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5011834015"
FT DOMAIN 462..547
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 557..642
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 641..746
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 450..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
SQ SEQUENCE 746 AA; 75588 MW; 4D8296623F7ADAAA CRC64;
MPSPIMRRLR TSAAAAALGV AAVLPLATAV QPASAAEAKL DNPYAGAKVY VNPDWSAKAA
AEPGGSAVAN QPTFVWMDRI AAITGSSAAK GLRAHLDAAL AQGANLVQIV IYDLPGRDCA
ALASNGELGA TEIGRYKTEY IDPIAAIMSD SKYAGLRIVN VIEPDSLPNL VTNAGGTAGS
TDACATMKAN GNYEAGVGYA LHTLAAIPNV YNYIDAAHHG WLGWDSNMGP AATEFKKAAT
TGGATVNDVA GFIVNTANYS ALVEPNFKVT DSVNGTTVRQ SKWVDWNYYV DELSFAQALR
TKLIGEGFNS TIGMLIDTSR NGWGGTARPA GPGPLTSVDD YVNGGRVDRR IHVGNWCNQS
GAGLGERPTT APATGIDAYV WAKPPGESDG ASQVIPNDEG KGFDRMCDPT YTGNGRNGNS
MSGALPNSPL AGAWFSAQFQ QLLANAYPPV GGSSTDTQAP TVPSGLTSPA KTSSSVSLSW
TASTDNVGVT GYDVYRGSAL VGSTATTSFT DTGLTASTAY SYTVKAKDAA GNVSAASAAL
SVTTSAGGTT DTQAPTVPSG LTSPAKTSSS VSLSWTASTD NVGVTGYDVY RGSALVGSTA
TTSFTDTGLT ASTAYSYTVK AKDAAGNVSA ASAALSVTTS GTGTGSGCTA TYKVSSDWGA
GFNADVTVTN TGTTAINGWK VTWTYGGQQK ISNLWNGSYT QTGQAVTVTN AAYNGAIGAG
GSAGFGFGAT NAGGSNAVPT LTCTAL
//
