ID A0A3N4R9W7_9ACTN Unreviewed; 618 AA.
AC A0A3N4R9W7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=EDD38_6621 {ECO:0000313|EMBL:RPE29466.1};
OS Kitasatospora cineracea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE29466.1, ECO:0000313|Proteomes:UP000266906};
RN [1] {ECO:0000313|EMBL:RPE29466.1, ECO:0000313|Proteomes:UP000266906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44781 {ECO:0000313|EMBL:RPE29466.1,
RC ECO:0000313|Proteomes:UP000266906};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
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:RPE29466.1}.
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DR EMBL; RKQG01000002; RPE29466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4R9W7; -.
DR Proteomes; UP000266906; 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 CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..618
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018244671"
FT DOMAIN 426..511
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 512..617
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 618 AA; 64090 MW; 086DFC5DC9CE9416 CRC64;
MRLQLRRRLS RRLAGCAAAL AAALVTTLAA PAAPAAQAAT TTAGSAGTAA ASTAGAGYWH
TSGRQILDEA GNPVRIAGIN WFGFETSNYV PHGLWSRDYK SMIDQMKSLG YNTIRMPYSD
DIFKGTTPSS INTSGGMNAD LVGLNSLGVM DKLVNYAGSI GMKVILDRHR PDSAGQSALW
YTASVPETTW LANLKSIAAR YANNPAVIGI DLHNEPHDPA CWGCGDQATD WRLAAQRGGE
AVLSANPKLL IFVEGVQSFN GSSYWWGGNL QGAGQYPVQL SVPNRVVYSA HDYATSVAQQ
TWFSDPSFPS NMPGVWDKNW GYLFNQNIAP VWVGEFGTTL QSTVDQAWLK ALVQYLRPTA
TSGADSFQWT FWSWNPNSGD TGGILNDDWT TVNTVKDGYL ASVKAPGFGS STGGNPGGGD
VQAPSVPGGL AVGATTASSV SLSWTASTDD TAVTGYDVYR NGTKVGSSTG TSYTDSGLSA
ATAYSYTVRA KDAAGNVSAA SAAVTATTAT AGGGTNAGCS AAVSLNDWGS GLTATVTVTN
TGTTAAKGWQ VSWTWPTSLQ ISSSWSANVT RSGQTVTATN LPYNGALAPA ASTSFGVQAT
RTDASAAATA TAVCTATS
//
