UniProt: S8CW33

Database: UniProt
Entry: S8CW33_9LAMI

LinkDB:  S8CW33_9LAMI 
Original site:  S8CW33_9LAMI

All links

Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (18)   

Download RDF

ID   S8CW33_9LAMI            Unreviewed;       626 AA.
AC   S8CW33;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=M569_03731 {ECO:0000313|EMBL:EPS71030.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS71030.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS71030.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:RU361166};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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:EPS71030.1}.
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; AUSU01001437; EPS71030.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8CW33; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR019028; CBM_49.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF19; ENDOGLUCANASE 19-RELATED; 1.
DR   Pfam; PF09478; CBM49; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01063; CBM49; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           23..626
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005146678"
FT   DOMAIN          529..614
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        468
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        477
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   626 AA;  68764 MW;  A2102EB0024103D9 CRC64;
     MGRATAASLI LLIGALLTPA FAGHDYAQAL SKSILFFEAQ RSGYLPGNQR VQWRGNSGLG
     DGKLNGVDLV GGYYDAGDNV KFGLPMAFTV TMMSWSIIEY GKQIAGAGEL GHALEAVKWG
     TDYLIKAHPE PYVLYGEVGD GNTDHYCWQR PEDMTTSRAA YKIDPEHPGS DLAGETAAAM
     AAASIVFRRY DPAYSKELLN HAYQKLLSQL FDFADKYRGK YDGSITIAQK YYRSVSGYAD
     ELLWAAAWLH KATNNRYYLN YLGNNGDSLG GTGWGMTEFG WDVKYAGVQT LVSKLLMAGR
     GREHSPVFER YQEKAEYFMC SCVGKGTQNA QKTPGGLIFR QRWNNMQFVT SAAFLMTVYS
     DYLSSAGKYL RCSSGNVSPA ELLAVAKSQV DYILGDNPRA TSYMVGYGNN YPRQVHHRGS
     SIVSYKVDPS FVSCRGGYAT WFSRRANDPN VLTGAIVGGP DAYDNFADER DNYEQTEPAT
     YNNAPLVGIL ARFHGGYNQH HLLSLELELP PPLDHHHRAG SGVSVDDPIE ITQRETGSWV
     YNGKTFHRYS ATITNKSSNK LQDLKLEISG LYGPLRGLAK LNNDSASSFS LPSWVNNSLA
     PGKSVGFVYI QPASPAEVSV SSFNLA
//

DBGET integrated database retrieval system