UniProt: A0A166CDF9

Database: UniProt
Entry: A0A166CDF9_DAUCS

LinkDB:  A0A166CDF9_DAUCS 
Original site:  A0A166CDF9_DAUCS

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   A0A166CDF9_DAUCS        Unreviewed;       504 AA.
AC   A0A166CDF9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DCAR_012377 {ECO:0000313|EMBL:KZN03621.1};
OS   Daucus carota subsp. sativus (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN03621.1};
RN   [1] {ECO:0000313|EMBL:KZN03621.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZN03621.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA   Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
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   -!- 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:KZN03621.1}.
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DR   EMBL; LNRQ01000003; KZN03621.1; -; Genomic_DNA.
DR   RefSeq; XP_017242265.1; XM_017386776.1.
DR   AlphaFoldDB; A0A166CDF9; -.
DR   STRING; 79200.A0A166CDF9; -.
DR   EnsemblPlants; KZN03621; KZN03621; DCAR_012377.
DR   GeneID; 108214651; -.
DR   Gramene; KZN03621; KZN03621; DCAR_012377.
DR   KEGG; dcr:108214651; -.
DR   OMA; NWDSKTP; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000077755; Chromosome 3.
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; 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:SF55; ENDOGLUCANASE 17; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 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   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:UP000077755};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           21..504
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5007748725"
FT   DOMAIN          46..493
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        472
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        481
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   504 AA;  56407 MW;  D0A577FF00F742B7 CRC64;
     MTFSVFSTLF LLALFHFTLS SFLDNATVSA AQFHRQPHRR YASHNYKDAL TKSILYFEGQ
     RSGKLPPNQR VTWRKDSGLS DGSAMNVDLV GGYYDAGDNV KFGFPMAFTT TMLSWSVIEF
     GGLMKSELLN AKEAIRWATD YLLKATVHPD TIYVQVGDAN KDHACWERPE DMDTLRTVVK
     IDKYNPGTEV AAETAAALAA ASLVFRRTDR TYSKLLAARA ISVFAFANKY RGVYSSTLRK
     WVCPFYCDFS GYEDELLWGA AWLHKATRNP MYLRYIQVNG QTLGANEGDN TFGWDNKHVG
     ARILLSKAFL VQKVQSLQDY KGHADNFICS LIPQSQYTPG GLLFKMADTN MQYVTSTSFL
     LVTYAKYLTN AKKVVTCGGS IVTPKKLRTL AKQQVDYLLG DNPMKMSYMV GYGPRYPQRI
     HHRGSSLPSI ASHPFKIQCT AGFSVMKSQS PNPNILIGAV VGGPDRRDRF LDQRSDYFQS
     EPATYINAPL VGSLAYLAHS FGQL
//

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