ID A0A1C6RIR8_9ACTN Unreviewed; 535 AA.
AC A0A1C6RIR8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=GA0070616_1186 {ECO:0000313|EMBL:SCL17040.1};
OS Micromonospora nigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL17040.1, ECO:0000313|Proteomes:UP000199699};
RN [1] {ECO:0000313|EMBL:SCL17040.1, ECO:0000313|Proteomes:UP000199699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL17040.1,
RC ECO:0000313|Proteomes:UP000199699};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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DR EMBL; FMHT01000003; SCL17040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6RIR8; -.
DR STRING; 145857.GA0070616_1186; -.
DR OrthoDB; 9800955at2; -.
DR Proteomes; UP000199699; 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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF17; ENDOGLUCANASE; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 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.
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:UP000199699};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..535
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039539065"
FT DOMAIN 428..535
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 397..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57156 MW; 25FF04DA3D6D7909 CRC64;
MSSRVRKAGL ALLAATLTFA GTVYGVTRSA SADVVAQQNA SQLVADMGAG WNLGNTLEAN
NNGIPSETAW GNPVVTQALI DRVRASGFKT IRIPVSYLGH IGAGPNYTIN AAWLNRIQEV
VDYAHSRGLY VLINMHGDGY KTVTGSWLIC DAADQATIKD KYQKVWRQVA TRFQSYNDRL
IFESMNENFD GQYGNPTQPC YSNINAYNQI FVDTVRRTGG NNASRWLLVP GWNTNIDHTV
GSGFVLPTDH NRSSAIPANE QRIMISVHYY DPWDFAGQED GTITQWGAGT TNPAKRSVWG
QEDFLDGQMK KMYDTFVTRG YPVFVGEYGS IDKTTYDSAS NRYRADYARA VVATAKKYGA
ATAYWDNGWN GQHGFGLFNR NSATVTQQGI INAIMSAVGG SQPTTPPTTP PTTPPPTTTP
PTTPPPTSPG GTGACRVSSA VNAWNTGLTN SITITNTGTA AINGWALAFT LAAGQTIVSG
WSASYAPTSG TVTATNASYN GTLPPGGSAT IGYQASHNGN AAAPTAFRLN GTPCN
//
