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P29027 (CHI2_RHIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitinase 2

EC=3.2.1.14
Gene names
Name:CHI2
OrganismRhizopus oligosporus
Taxonomic identifier4847 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesMucoraceaeRhizopus

Protein attributes

Sequence length542 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

   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 – 446424Chitinase 2
PRO_0000011932
Propeptide447 – 54296 Potential
PRO_0000011933

Regions

Region23 – 312290Catalytic
Region355 – 40652Chitin-binding, high affinity
Compositional bias313 – 35442Ser/Thr-rich

Sites

Active site1661Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P29027 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 3E8F17DA551FD0A7

FASTA54256,528
        10         20         30         40         50         60 
MLTRTFLGMA ISAFLASTGV QAAWSSHGPN VMYYWGQNSA GGSNTQASLG TYCESGQVDA 

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

       130        140        150        160        170        180 
AGVYGFTSDA QGQQFAQTIW NLFGGGNSDT RPFGDAVIDG VDLDIEGGSS TGYVAFVNAL 

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

       250        260        270        280        290        300 
KTTSPNKNVK IMFTVPGSST AAGSGYVPMS TLQTIVPSLA SKYSSYGGVS VWDASQAWNN 

       310        320        330        340        350        360 
GGFNSQLYSL VHSGGSTPPP PSSSSATKTT TKTTATSTKT TTTTAPTATS TPGSCPVANQ 

       370        380        390        400        410        420 
PCSTQNQYAC TADGKYAVCD HGKWVASSCP SNTVCIPTTD GASIYCGYAT GSGSTCPSVS 

       430        440        450        460        470        480 
ALEITAASLG SKNGPVPRPY KASKVAAQLA VTSTDKNSFE AVINARRTTL TPFEKSVTIE 

       490        500        510        520        530        540 
FTTPSNIKFT ESDMGPVRQV GNKVRIQAKN DYNESMTLVV KVKGSINSGV FVAPSTSAWN 


FK 

« 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 23-38.
Strain: ATCC 22959 / CBS 338.62 / NBRC 8631 / NRRL 2710 / AS 3.4818.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10158 Genomic DNA. Translation: BAA01022.1.
PIRB47022.

3D structure databases

ProteinModelPortalP29027.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005089. CBM_fam19.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[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]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI2_RHIOL
AccessionPrimary (citable) accession number: P29027
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 21, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families