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Database: UniProt
Entry: A0A1I1R3D0_9ACTN
LinkDB: A0A1I1R3D0_9ACTN
Original site: A0A1I1R3D0_9ACTN 
ID   A0A1I1R3D0_9ACTN        Unreviewed;       638 AA.
AC   A0A1I1R3D0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN   ORFNames=SAMN05421773_112157 {ECO:0000313|EMBL:SFD28772.1};
OS   Streptomyces aidingensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=910347 {ECO:0000313|EMBL:SFD28772.1, ECO:0000313|Proteomes:UP000199207};
RN   [1] {ECO:0000313|EMBL:SFD28772.1, ECO:0000313|Proteomes:UP000199207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5739 {ECO:0000313|EMBL:SFD28772.1,
RC   ECO:0000313|Proteomes:UP000199207};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOLM01000012; SFD28772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1R3D0; -.
DR   STRING; 910347.SAMN05421773_112157; -.
DR   OrthoDB; 4902692at2; -.
DR   Proteomes; UP000199207; 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; 2.60.40.710; Endoglucanase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51172; CBM3; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199207};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..638
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011503941"
FT   DOMAIN          488..638
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..485
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   638 AA;  70074 MW;  5A752120B91A0133 CRC64;
     MSSFTRRRSK SRRPLAAAGL VLGALLAAGL PGLAGSAGAE PAPEESGPVQ TAGAAGTDWL
     TTDGNKITDQ AGNQVWLTGV NWFGFNTSER FFHGLWSANI EDVTRAVAER GFNIVRVPIS
     TQLLNEWKNG QAAVASGINT YVNPELEGRT TLGVFDYWLT LCEKYGLKVM LDVHSAEADN
     SGHVYPMWYK GEITSEIFYS TWEWVADRYK DNDTLVAFDI ENEPHGKANE TPRAKWDDST
     DEDNWKHACE TAGKRILAIN PNMLILCEGI EVYPREGVSW TSTTPTDYYG MWWGGNLRGV
     KDYPVDLGAG QDQLVYSPHD YGPSVWQQPW FEGDWNRTTL ERDVWDPNWL YIHKENTAPL
     LIGEWGGHLD GGDNEKWMTA LRDMMTDYGV HHTFWCLNPN SGDTGGLLGY DWASWDEEKY
     GFVEPALWSQ GGKFVGLDHE VKLGGSTSTT GISLNEYLGN PDPDPEPDPD PEPDPDPEPD
     PDPEPEPGDA ALAVEYKNND SSATDNAIRP SLRLRNTGDT PVDLSTVTLR YWFTRDGASS
     VSAWCDWAVV GCANLDLEVV HLPTAVNGAD SYLEVSFTSG SLAPGAGTGD LQLRMSKSDW
     SAFDETDDYS HGTGTAYAET ATVTAHVNGG LVWGTEPS
//
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