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Unreviewed, UniProtKB/TrEMBL Q93X60 (Q93X60_CICIN)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Fructan 1-exohydrolase IIa EMBL CAC37922.1
    EC=3.2.1.80
Gene names
Name: 1-feh IIa EMBL CAC37922.1
OrganismCichorium intybus (Chicory) EMBL CAC37922.1
Taxonomic identifier13427 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsAsteralesAsteraceaeCichorioideaeCichorieaeCichorium

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 32 family. RuleBase RU000449V1

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase RuleBase RU000449V1
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionfructan beta-fructosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential EMBL CAC37922.1
Chain39 – 581543fructan 1-exohydrolase IIa EMBL CAC37922.1
PRO_5000066514

Sequences

Sequence LengthMass (Da)Tools
Q93X60-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8E5233D54C3B98BB

FASTA58165,279
        10         20         30         40         50         60 
MKKSLSSFIV LCFLVIILET GRVKATSRNL NDVIMLANQQ IEQPYRTGYH FQPPSNWMND 

        70         80         90        100        110        120 
PNGPMLYQGV YHFFYQYNPY AATFGDVIIW GHAVSYDLVN WIHLDPAIYP TQEADSKSCW 

       130        140        150        160        170        180 
SGSATILPGN IPAMLYTGSD SKSRQVQDLA WPKNLSDPFL REWVKHPKNP LITPPEGVKD 

       190        200        210        220        230        240 
DCFRDPSTAW LGPDGVWRIV VGGDRDNNGM AFLYQSTDFV NWKRYDQPLS SADATGTWEC 

       250        260        270        280        290        300 
PDFYPVPLNS TNGLDTSVYG GSVRHVMKAG FEGHDWYTIG TYSPDRENFL PQNGLSLTGS 

       310        320        330        340        350        360 
TLDLRYDYGQ FYASKSFFDD AKNRRVLWAW VPETDSQADD IEKGWAGLQS FPRALWIDRN 

       370        380        390        400        410        420 
GKQLIQWPVE EIEELRQNQV NLQNKNLKPG SVLEIHGIAA SQADVTISFK LEGLKEAEVL 

       430        440        450        460        470        480 
DTTLVDPQAL CNERGASSRG ALGPFGLLAM ASKDLKEQSA IFFRVFQNQL GRYSVLMCSD 

       490        500        510        520        530        540 
LSRSTVRSNI DTTSYGAFVD IDPRSEEISL RNLIDHSIIE SFGAGGKTCI TSRIYPKFVN 

       550        560        570        580 
NEEAHLFVFN NGTQNVKISE MSAWSMKNAK FVVDQSVKSA A 

« Hide

References

[1]"Defoliation induces fructan 1-exohydrolase II in Witloof chicory roots. Cloning and purification of two isoforms, fructan 1-exohydrolase IIa and fructan 1-exohydrolase IIb. Mass fingerprint of the fructan 1-exohydrolase II enzymes."
Van den Ende W., Michiels A., Van Wonterghem D., Clerens S.P., De Roover J., Van Laere A.J.
Plant Physiol. 126:1186-1195(2001) [PubMed: 11457968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Root EMBL CAC37922.1.
[2]"Expression analysis of a chicory fructan 1-exohydrolase gene reveals complex regulation by cold."
Michiels A., Van Laere A., Van den Ende W., Tucker M.
J. Exp. Bot. 55:1325-1333(2004) [PubMed: 15133058] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY323935 Genomic DNA. Translation: AAP85536.1.
AJ295033 mRNA. Translation: CAC37922.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ST8X-ray2.35A39-581[»]
2ADDX-ray2.50A39-581[»]
2ADEX-ray2.65A39-581[»]
2AEYX-ray3.27A39-581[»]
2AEZX-ray3.05A39-581[»]
ModBaseSearch...

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Family and domain databases

InterProIPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
[Graphical view]
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ93X60_CICIN
AccessionPrimary (citable) accession number: Q93X60
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information