GenomeNet

Database: UniProt
Entry: A0A101N5U3_9ACTN
LinkDB: A0A101N5U3_9ACTN
Original site: A0A101N5U3_9ACTN 
ID   A0A101N5U3_9ACTN        Unreviewed;       549 AA.
AC   A0A101N5U3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN   ORFNames=AQI94_17465 {ECO:0000313|EMBL:KUM87144.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM87144.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM87144.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM87144.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
RL   Submitted (OCT-2015) 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:KUM87144.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMWM01000018; KUM87144.1; -; Genomic_DNA.
DR   RefSeq; WP_031044610.1; NZ_KQ948147.1.
DR   AlphaFoldDB; A0A101N5U3; -.
DR   OrthoDB; 9801198at2; -.
DR   Proteomes; UP000053039; 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; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42754:SF1; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42754; ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00041; fn3; 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; 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|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..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..549
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007101157"
FT   DOMAIN          352..441
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          439..549
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   549 AA;  56848 MW;  B4BCE5E0E459FF63 CRC64;
     MSRTRKSPLR TFLARLAALV GLVVLGALCP GTAQAAQQPA AQAAGLHISN GRLVESNGND
     FVMRGVNHAH TWYPNELGSL ADIKAQGANT VRVVLADGHR WTANTAADVT NVVAQCKANR
     LICVLEVHDT TGYGEDSAAG TLDQAADYWI GLKDVLAGQE NYIIINIGNE PWGNTDPAGW
     TAPTIAAIKK LRNAGFEHTI MVDAPNWGQD WQQVMRTNAQ SVYAADTTGN LVFSIHMYSV
     FDTAAEITDY LNAFVSAKLP LVIGEFGGPA DQWGDPDEDT MMAAAEQLHI GYLAWSWSGN
     TDPILDLVLD FDPARMTSWG QRIFNGANGI AQTAKEATVF GGGSSDTQAP TAPGTPTASA
     VTATSARLTW TASTDNVGVA GYDVVRVSGG TETKVAAATT NSVTVTGLTA GTAYSFAVYA
     RDAAGNRSAR SATVGVTTAN TPAGSCSVGY RVVGDWQGGF QGEIVIRNTG TAAVTGWKLG
     FTFADGQSVT NMWGGTAAQS AGAVTVTPAS YTNTIAAGGS VTLGFIGSKG STNTAPAAFT
     LNGAACVNG
//
DBGET integrated database retrieval system