ID A0A0N0TRZ8_9PSEU Unreviewed; 454 AA.
AC A0A0N0TRZ8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=ADK67_20025 {ECO:0000313|EMBL:KOX23716.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX23716.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX23716.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX23716.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-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:KOX23716.1}.
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DR EMBL; LGED01000197; KOX23716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0TRZ8; -.
DR STRING; 1415542.ADK67_20025; -.
DR PATRIC; fig|1415542.3.peg.4325; -.
DR Proteomes; UP000037722; 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.
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..29
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 30..454
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5005732785"
FT DOMAIN 348..454
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 319..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
SQ SEQUENCE 454 AA; 46229 MW; D52B8F986C0CE752 CRC64;
MAAAGALSSA LVASAVALVL GGGATTAQAA DSAFYVDPNT SAARWVAQNP NDSRAAVIRD
RIVNTPQARW FTTTNTSEVR GQVDAFVGAA AAAGKIPILV VYNVPNRDCG GASGGGAPSH
SAYRAWVDQV AAGIAGRPAS IVLEPDVLPI MTNCQSSSQQ AETMASMAYA GKKLKSGSAQ
TKVYFDIGHS AWLTPAEAGQ RLRGADIANS ADGISTNVSN YRHTRDEVAF AKAVLNNLGD
SRFKAVIDTS RNGNGPLGDE WCDPAGRAIG TASTTNTGDS QIDAFLWIKL PGEADGCIAG
AGQFVPQRAY DMAIAAGPTS TTSLSTSTST TTSTTTTTST TTSTTTTTPP PGDGCRVTHR
VVSQWSGGYT GEIVIENRGA ALNGWTLTFS APGVTVSQGW NGTWTDGGDI VRVGNAAWNG
GLATGGTATI GYNASFSGGT PPFTSPTLNG VACG
//
