ID A0A1I0B9L1_9FIRM Unreviewed; 1102 AA.
AC A0A1I0B9L1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=SAMN04487772_10719 {ECO:0000313|EMBL:SET03226.1};
OS [Clostridium] polysaccharolyticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=29364 {ECO:0000313|EMBL:SET03226.1, ECO:0000313|Proteomes:UP000199800};
RN [1] {ECO:0000313|EMBL:SET03226.1, ECO:0000313|Proteomes:UP000199800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1801 {ECO:0000313|EMBL:SET03226.1,
RC ECO:0000313|Proteomes:UP000199800};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966};
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DR EMBL; FOHN01000007; SET03226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0B9L1; -.
DR STRING; 29364.SAMN04487772_10719; -.
DR OrthoDB; 9800955at2; -.
DR Proteomes; UP000199800; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR040946; CBM46.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF18448; CBM46; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000199800};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1102
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011594402"
FT DOMAIN 219..505
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT DOMAIN 631..729
FT /note="Endoglucanase B carbohydrate binding"
FT /evidence="ECO:0000259|Pfam:PF18448"
FT DOMAIN 983..1044
FT /note="CBM3"
FT /evidence="ECO:0000259|Pfam:PF00942"
FT REGION 905..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 122158 MW; E61C1A800B051537 CRC64;
MKKMKKGLSV LLSFVMIITS LCFTTVKAAE TNSSLTEISL LSQSVTASDE EARGTGDGYD
GLITTVRDVD VDYLKIAYTI DNPSRLQSWT WLFNFMPFTS SWAGWECNAV TLSDSALENG
EYIAYIPMKA IKDSCAEGDV AGVNLNYCEV EGVKLQLTGF WACTGKLATE PEATGKKDIA
SGQETVQKDI PDTASNQFML AFNNGWNLGN TFDSFDTNLN VEDLKENTWG NPNVTKELLH
AIRQEGFDSI RIPMTTYRRA SKVNGRYVID ESWLARYKEV VDWAVEEGFY VMINMHHDSS
WLRSWNGNKS AEEFIRFTQS WEQIADYFKE EPAQVCFETI NEPQFDYPTA HNTIYDMLDA
VNLASYNIIR KSGGKNATRM IVLPTYNTNQ NPESLDDLYN LIKGLQDENV IATIHYYSEW
CFSGNLGTTG FDDPVNGGET TSRDAIYSTF KTVYDKFIAN GIGIIVGEYG LLGTNEVGEY
VKYLECVNAV GHTYGMSMVF WDAGNYINRR DKNYAWNEPR LGEMVDASMT GRSSTAACLD
ELYFQGELSE DVTIPLIING PEFKGIKGLT EGSDYTYNKE KAVITVKASY VNRKLKAFGS
NEFGTFDELL IQFTSGAVWH EYLCKNAEAS AGKATGNTNG VTIPFTYNGA KVRRISAYQR
NGCVGPTHSW CKYLTFNGDF TPDYAGNKLV LSSSFLKDSS VLDGPILVNV EMWNGQTVKV
WMNKKGTSIE VDSQYAENTS AEIKKPEKMV VYVGEKQIPS QYLGLPEGGS IYGTWITDSS
VIKMDGWPAA MTFSSTPTDF TAGGILVYFY DIQEYVNGMF AVKAMPKVEG VTLKAGEKKA
VTVKDVAKDA VITYAVEDPF VATVENGVIK AKNAGKTSVI VTVSQYGRTD DFTASVHVED
SLIPSAEPAE SEAPASSMEP AESEAPTSSV EPVVSEVPVS STEPAVSETP VSSAEPVVSE
TPFPSQVPVA KEKPDVIVQT EISSQVRQNY TISSGTIKEF DLSKLVLRYY FIKDSQKEQN
IWIDNAAVSC NCSPYYIGYT SNVKCNVTEE YVEFAFTKAQ LLYGGTFNIQ TRMNYSDWSP
YINFQSAGLE VYYDGTLVEQ KN
//
