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Database: UniProt
Entry: A0A495X157_9PSEU
LinkDB: A0A495X157_9PSEU
Original site: A0A495X157_9PSEU 
ID   A0A495X157_9PSEU        Unreviewed;       497 AA.
AC   A0A495X157;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN   ORFNames=DFJ66_0395 {ECO:0000313|EMBL:RKT67226.1};
OS   Saccharothrix variisporea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT67226.1, ECO:0000313|Proteomes:UP000272729};
RN   [1] {ECO:0000313|EMBL:RKT67226.1, ECO:0000313|Proteomes:UP000272729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT67226.1,
RC   ECO:0000313|Proteomes:UP000272729};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-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:RKT67226.1}.
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DR   EMBL; RBXR01000001; RKT67226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495X157; -.
DR   OrthoDB; 182870at2; -.
DR   Proteomes; UP000272729; 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; IPR018366; CBM2_CS.
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; PS00561; CBM2_A; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..497
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019722562"
FT   DOMAIN          27..137
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          132..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  53132 MW;  5851FF1F37585931 CRC64;
     MRHRQAVLAV GAAGALALAG IGMTALPASA ASGCSITYAV QSQWQGGFTA SVAITNLGDP
     VSSWTAAFDF PKTDQKVGQG WSATWTQSGT RVSAASLGWN GSLGTGASTT IGFVGSWRDA
     NPVPTSFSLN GTTCNGTVPT TTTTTTTTTT PPGDEPAPKL HVSGNKLVTA DGEPYRLLGV
     SRSSSEFACV QGKGMWDGGP VDQASVDAMK TWNIHAVRIP LNEECWLGVN GSPGGAAYQQ
     AVKDYVDLLV RNGISPILDL HWTWGAYTNS PDWHCKDEHA VCQKPMPDAK YAPQFWAGVA
     SVFKGNDAVV FDLFNEPYPE MAADWNKTLG WQCWRDGGTC TGLPYETAGM QDLVDAVRAT
     GATNVLLLGG LEWANDMREW LAYKPTDPRN NLAASWHAYS FNACATESCW DTQVAPLAQQ
     VPVVLGEFGQ DNCGFDYMGR LADWADAHHI SYLAWTWTPW GCTSGAVLIK DWAGTPEPGI
     GEGYKAHLLT QDPYATR
//
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