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Protein
Submitted name:

Acid chitinase

Gene
N/A
Organism
Nepenthes rafflesiana
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16643.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Submitted name:
Acid chitinaseImported
Submitted name:
Acidic endochitinaseImported
OrganismiNepenthes rafflesianaImported
Taxonomic identifieri150990 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesNepenthaceaeNepenthes

Structurei

3D structure databases

ProteinModelPortaliQ06SN0.
SMRiQ06SN0. Positions 28-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06SN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTHYSSAIL PILTLFVFLS INPSHGSGIA VYWGQNGNEG TLSDTCATGN
60 70 80 90 100
YNYVLVSFLT TFGNGQTPVL NLAGHCDPSS NGCTGLSTDI TSCQNQGIKV
110 120 130 140 150
LLSLGGASGS YSLVSTDDAD QVAAYLWNNY LGGQSDSRPL GSAVLDGIDF
160 170 180 190 200
DIESGSDNYW GDLATALKNY SQSVLVSAAP QCPYPDAHLD LAIATGIFDY
210 220 230 240 250
VWVQFYNNEQ CEYVTDDTNL LSAWNQWTSS QANVVFLGLP ASTDAASSGY
260 270 280 290
ISPDVLISQV LPSIKASSKY GGVMLWSKYY DNGYSSAIKD SV
Length:292
Mass (Da):31,107
Last modified:October 31, 2006 - v1
Checksum:iF2B9B0B2A545C1D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ530442 mRNA. Translation: ABF74624.1.
GQ338257 Genomic DNA. Translation: ACU31854.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ530442 mRNA. Translation: ABF74624.1.
GQ338257 Genomic DNA. Translation: ACU31854.1.

3D structure databases

ProteinModelPortaliQ06SN0.
SMRiQ06SN0. Positions 28-292.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16643.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of a Chitinase from Nepenthes rafflesiana."
    Stieber R., Mithofer A.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes."
    Rottloff S., Stieber R., Maischak H., Turini F.G., Heubl G., Mithofer A.
    J. Exp. Bot. 62:4639-4647(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ06SN0_9CARY
AccessioniPrimary (citable) accession number: Q06SN0
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 2006
Last sequence update: October 31, 2006
Last modified: October 1, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.