ID A0A3N1AR97_9ACTN Unreviewed; 454 AA.
AC A0A3N1AR97;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=EDC02_0946 {ECO:0000313|EMBL:ROO59158.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO59158.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO59158.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO59158.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-2018) 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,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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:ROO59158.1}.
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DR EMBL; RJJY01000001; ROO59158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1AR97; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000275308; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000275308};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..454
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017980544"
FT DOMAIN 351..454
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 327..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 47955 MW; EE70E9AEF05AF1C2 CRC64;
MKTRLSVAAA ALLALVTSVV VLVQPAHAAV GLHVSDGRLV EANGTPFVLR GVNHAHTWYP
SQTSSFANIK SLGANAVRVV LSNGHRWTRN DASDVANVIS LCKANRLICV LEVHDTTGYG
EEGAAATLSS AAGYWISLAS VLRGQENYVI INIGNEPFGN SGYQNWASHT TSAVQRLRDA
GFEHAIMVDA PNWGQDWTFT MRDNAQSVWT ADPARNLIFS IHMYGVFDTA AEISDYLGRF
RSAGLPIVVG EFGHNHSDGD PDEDSILSYT SQHGIGWLGW SWSGNSGGVE YLDMVNNFDV
NSLTTWGQRL FNGSNGIRET AREATVYSGA TPPPTTAPPT TAPPTTAPPT TPPPAGACTA
TYLVVGQWQG GFQGEVRVTA GGSALSGWRV SWTFASGQSV NQAWNATVTG NGASVSATNV
SYNGNLGAGQ STTFGFIGSW SGSNPVPTLS CAAR
//
