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Reviewed, UniProtKB/Swiss-Prot P29026 (CHI1_RHIOL)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1
    EC=3.2.1.14
Gene names
Name: CHI1
OrganismRhizopus oligosporus
Taxonomic identifier4847 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesMucoraceaeRhizopus

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probably involved in the apical growth and branching of fungal hyphae.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Secreted Probable.

Post-translational modification

O-glycosylated.

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
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide 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 – 2222 Ref.1
Chain23 – 417395Chitinase 1
PRO_0000011930
Propeptide418 – 540123 Potential
PRO_0000011931

Regions

Region23 – 312290Catalytic
Region353 – 40452Chitin-binding, high affinity
Compositional bias313 – 35240Ser/Thr-rich

Sites

Active site1661Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P29026-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: C7A8590D03881F1B

FASTA54056,227
        10         20         30         40         50         60 
MLARTFLGMA ISAFLASTGV QAAWSSNGPN VMYYWGQNSA GGSNTQASLG TYCESGQVDA 

        70         80         90        100        110        120 
VLLSFLHVFN VGGTPEINLS SACAGTYFPN TQLLSCPAVG ADIKKCQDKG VKVILSLGGA 

       130        140        150        160        170        180 
AGVYGFTSDA QGQQFAQTIW NLFGGGSSDT RPFGDAVIDG VDLDIEGGAS TGYAAFVNAL 

       190        200        210        220        230        240 
RQKFSSNFLI GAAPQCPFPD AILGSVLNSA SFDYVNVQFY NNYCSATGSS FNFDTWDNWA 

       250        260        270        280        290        300 
KTTSPNKNVK IMFTIPGSPT AAGSGYVPMS TLQTIVPSLA SEYSSYGGVS VWDASQAWNN 

       310        320        330        340        350        360 
GDFSSQLYSL VHSGGSTPPP SSSTIKTTTK ATTTSTKTTT TAAPTATSAP GSCPVANQSC 

       370        380        390        400        410        420 
STQNQYACTA DGKYAVCDHG KWVVSSCPSG TVCIPTTDGT SIYCGYATGS GSTCPSASAL 

       430        440        450        460        470        480 
EIAAASFGSK NGPVPRPYKA SKVAAQLAVT STDKNSFEAV INARRTTLTP FEKSVTIEFT 

       490        500        510        520        530        540 
TPSNIKFTES DMGPVRQVGN KVRIQAKNDY NESMTLVVKV KGSINSGVFV APSTSAWKFK 

« Hide

References

[1]"Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes."
Yanai K., Takaya N., Kojima N., Horiuchi H., Ohta A., Takagi M.
J. Bacteriol. 174:7398-7406(1992) [PubMed: 1429462] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-52.
Strain: ATCC 22959 / AS 3.4818 / CBS 338.62 / IFO 8631 / NRRL 2710.

Cross-references

Sequence databases

D10157 Genomic DNA. Translation: BAA01021.1.
PIRA47022.

3D structure databases

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

Protein family/group databases

CAZyCBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA3.2.1.14. 81726.

Family and domain databases

InterProIPR001223. Glyco_hydro18cat.
IPR005089. Glyco_hydro_18_carb-bd.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF03427. CBM_19. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI1_RHIOL
AccessionPrimary (citable) accession number: P29026
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

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