ID   A0A1M7MUA0_9ACTN        Unreviewed;       448 AA.
AC   A0A1M7MUA0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   ORFNames=SAMN05443668_102252 {ECO:0000313|EMBL:SHM94145.1};
OS   Cryptosporangium aurantiacum.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=134849 {ECO:0000313|EMBL:SHM94145.1, ECO:0000313|Proteomes:UP000184440};
RN   [1] {ECO:0000313|EMBL:SHM94145.1, ECO:0000313|Proteomes:UP000184440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46144 {ECO:0000313|EMBL:SHM94145.1,
RC   ECO:0000313|Proteomes:UP000184440};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRCS01000002; SHM94145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7MUA0; -.
DR   STRING; 134849.SAMN05443668_102252; -.
DR   Proteomes; UP000184440; 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   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; 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:UP000184440};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          15..126
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          124..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..160
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        282
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        429
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ   SEQUENCE   448 AA;  46554 MW;  5F3220CB96E237D1 CRC64;
     MVVIGGTSLV AANATSEPDH SCAAAYTVRH TWSTGFSAEV AVTNTGEDPV KNWNVNWSFD
     GGKAVVKGWE GEWQQDDGLV TVRAGEDSVR LEPGKTLTLR FTGWHPQGKA PDAAQFALNG
     VSCQVGGDKE ETPESASPTP SSIALPPGLP ASPAPTGKPT KPAAGPLGSL FVDPSGQAVE
     WVEANSGDPR AAVIRERIAE QPQAHWLAAN NPGEVESDVR GYTSRAHSRG KVPVLVAYNM
     TNRDCGGASA GGADSADGYR TWINNFADGL GSGTSIVILE PDALGHLTTC LSADQQQERL
     DLLEYAGKTI KQASPKARVF YDVGHSAWID AGEAASRAKQ AGAGQYGDGI ALNTSNYNTS
     SSEVSYGKRV LASLGSGQMV VDTSRNGAGP AGGEWCDPAG RKLGKYPTTA TGDPKVAAYL
     WVKRPGESDG CSGSAGSFIP ETAYDLSS
//