ID A0A1H6SNC8_9ACTN Unreviewed; 464 AA.
AC A0A1H6SNC8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=SAMN05443287_101722 {ECO:0000313|EMBL:SEI67414.1};
OS Micromonospora phaseoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEI67414.1, ECO:0000313|Proteomes:UP000198707};
RN [1] {ECO:0000313|Proteomes:UP000198707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA Varghese N., Submissions S.;
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; FNYV01000001; SEI67414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6SNC8; -.
DR STRING; 1144548.SAMN05443287_101722; -.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000198707; 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..35
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 36..464
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5011332840"
FT DOMAIN 357..464
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
SQ SEQUENCE 464 AA; 47312 MW; 2BCEE27EA0ADA111 CRC64;
MRTRSTFALV GAVATALTVA ATVGVGALRP SPAAAADSAF YVDPQTSAAR WVAANPNDSK
TAVIRDRIAS VPQARWFTTT NTSSVRAEVN SFVGAAAAAG KIPILVVYNI PNRDCSNHSG
GGAPDHATYR QWVDQVAAGL GGRPATIILE PDVLPIMTSC MNASVQAEVR ASMAYAGKAL
KAGSSAAKVY FDIGHGGWLA PGEAAARLTA SDIANSADGI SVNVSNYRRT ADEVSYAKSI
IAATGISRLK AVVDTSRNGN GPAGSEWCDP PGRAIGTPST TATGDAAIDA FLWVKLPGEA
DGCIAAAGQF VPQRAYDLAV AAGPVPTTAP PTTTPPTTTP PTTTPPTTTP PTTTPPTTPP
SGGCTVTYTP NAWTGGFTAE IRATNRGAAL TSWTLAFTAG SGVRLTNGWN GEWSQSGDRI
QVRNVAWNGN LPANGTLSVG FQGTFTGSSL PPFGGFTLNG TTCA
//
