ID A0A0V8T944_9CELL Unreviewed; 806 AA.
AC A0A0V8T944;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=ATM99_09905 {ECO:0000313|EMBL:KSW29083.1};
OS Cellulomonas sp. B6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29083.1, ECO:0000313|Proteomes:UP000054319};
RN [1] {ECO:0000313|EMBL:KSW29083.1, ECO:0000313|Proteomes:UP000054319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:KSW29083.1,
RC ECO:0000313|Proteomes:UP000054319};
RA Piccinni F.E., Campos E.;
RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT Isolated from Decaying Forest Soil.";
RL Submitted (NOV-2015) 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|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10059, ECO:0000256|RuleBase:RU361166}.
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:KSW29083.1}.
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DR EMBL; LNTD01000073; KSW29083.1; -; Genomic_DNA.
DR RefSeq; WP_062102133.1; NZ_LNTD01000073.1.
DR AlphaFoldDB; A0A0V8T944; -.
DR STRING; 1295626.ATM99_09905; -.
DR OrthoDB; 9758662at2; -.
DR Proteomes; UP000054319; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 40..806
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5006774140"
FT DOMAIN 499..650
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 698..806
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 647..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 455
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 806 AA; 86446 MW; AE18CC1E7E9EC330 CRC64;
MSRLSSPGPR PGRRRALWAG AAAAAVALGA LVPVQAAQAA PAYNYAEALQ KSMFFYQAQR
SGDLPDDFPV SWRGDSGLDD GKDVGKDLTG GWYDAGDHVK FGLPMAFTTT MLAWGAIESP
EGYAQAGQLD ELRDNLRWVN DYFVKAHTAP NELYVQVGKG DDDHKWWGPA EVMTMARPAY
KISATCPGSD AAGETAAALA SSSIVFRTTD PAYAATLLTH ATQLYSFADT YRGSYSDCVT
DAQSFYKSWS GYQDELVWGA YWLYKATGDA TYLAKAETEY DKLSNQNQTN LKSYKWTVAW
DDKSYAMYAL LAMETGKQRY VDDANRWLDY WTSGYNGERI TYSPGGMAVL DSWGALRYAA
NTSFVALVYS DWLTDPTRKA RYQAFGVRQI DYALGDNPRK SSYVVGFGAN PPQNPHHRTA
HGSWQDSSKV PVETRHVLYG ALVGGPGSAN DAYTDSRDDY VANEVATDYN AGFTSALAYL
AGRYGGTPLA GFPVAETPDQ DELFVEAKLN QPQSGAFTEV KAIIRNRSAF PARSLKDASI
RYWFTLDEGV PASSLSVSTN YSECGAQPAS VHQASGSLYY AEIACAGQDI HPGGQSQHRR
EIQFRVQGTL QWNALNDPSF AGLPATGDPV KTRAITLYDK GVLVWGTEPG GPTPTPTPTV
TATPTPTPTP TPTPTVSPTP TVTPTPTPSV TPTPTPTPTS GPATCAVTYT ASSWSTGFTA
SVRLKNTSAT PLTWSLTFDL ASGQQVTQGW SATWSQTGAR VTATGAAWNA TLAPGASVDL
GFNGSHTGQN PTPTAFAVNG TACVTG
//
