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Reviewed, UniProtKB/Swiss-Prot P40953 (CHI2_CANAL)

Last modified November 3, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 · Relevant documents

Names and origin

Protein namesRecommended name:
    Chitinase 2
    EC=3.2.1.14
Gene names
Name: CHT2
ORF Names: CaO19.3895
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   LigandChitin-binding
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

chitinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 583564Chitinase 2
PRO_0000011925

Sites

Active site1531Proton donor By similarity

Amino acid modifications

Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P40953-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 113F26576340BEB5

FASTA58360,851
        10         20         30         40         50         60 
MLSFKSLLAA AVVASSALAS ASNQVALYWG QNGAGGQERL AQYCQETDVD IVLLSFLNLF 

        70         80         90        100        110        120 
PDPLNVNFAN QCGNTFESGL LHCSQIGADI KTCQSLGKTV LLSLGGGVGD YGFSDVASAT 

       130        140        150        160        170        180 
KFADTLWNKF GAGEDPERPF DDAVVDGFDF DIEHGGATGY PELATALRGK FAKDTSKNYF 

       190        200        210        220        230        240 
LSAAPQCPYP DASLGDLLSK VPLDFAFIQF YNNYCSINGQ FNYDTWSKFA DSAPNKNIKL 

       250        260        270        280        290        300 
FVGVPATSNI AGYVDTSKLS SAIEEIKCDS HFAGVSLWDA SGAWLNTDEK GENFVVQVKN 

       310        320        330        340        350        360 
VLNQNACVAP SSSATTQSTT TTSSAVTQST TTTSAAITQS ATTTSAAVTT KSNQIVTSSS 

       370        380        390        400        410        420 
SSSSSIFYGN STTESSTGIA TGTVLPTGSN ENAATTGSGS NTKLAISTVT DVQKTVITIT 

       430        440        450        460        470        480 
SCSEHKCVAT PVTTGVVVVT DIDTVYTTYC PLTNSQVYVP VQTVVCTEET CVPSPTSTAQ 

       490        500        510        520        530        540 
KPKASTTIKG VEKGQTTSYP VVGTTEGVKK IVTTSAQTVG SSTKYVTIEL TSTITPVTYP 

       550        560        570        580 
TSVASNGTNT TVPVFTFEGG AAVANSLNSV WFPVPFLLAA FAF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of chitinase genes from Candida albicans."
McCreath K.J., Specht C.A., Robbins P.W.
Proc. Natl. Acad. Sci. U.S.A. 92:2544-2548(1995) [PubMed: 7708682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10261 / CBS 2718 / IFO 1061.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.

Cross-references

Sequence databases

U15800 Genomic DNA. Translation: AAA68015.1.
AACQ01000012 Genomic DNA. Translation: EAL03025.1.
RefSeqXP_721807.1.

3D structure databases

HSSPHSSP built from PDB template 2HVM based on UniProtKB P23472.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Genome annotation databases

GeneID3636523.
KEGGcal:CaO19.3895.

Organism-specific databases

CGDCAL0002204. CHT2.

Phylogenomic databases

OMAPTKGAES.

Enzyme and pathway databases

BRENDA3.2.1.14. 1124.

Family and domain databases

InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI2_CANAL
AccessionPrimary (citable) accession number: P40953
Secondary accession number(s): Q5AKC5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Candida albicans

Candida albicans: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents