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Reviewed, UniProtKB/Swiss-Prot P48827 (CHI4_TRIHA)

Last modified September 22, 2009. Version 64. 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:
    42 kDa endochitinase
    EC=3.2.1.14
Gene names
Name: chit42
OrganismTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifier5544 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeHypocrea

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Morphogenetic role during apical growth, cell division and differentiation (cell wall morphogenesis). Antifungal agent.

Catalytic activity

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

Subcellular location

Secreted.

Induction

Specifically induced by chitin and is catabolite repressed.

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
   PTMCleavage on pair of basic residues
Glycoprotein
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 Potential
Propeptide23 – 3412
PRO_0000011934
Chain35 – 42338942 kDa endochitinase
PRO_0000011935

Sites

Active site1711Proton donor By similarity

Amino acid modifications

Glycosylation2181N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P48827-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: DF90378EED1C30BE

FASTA42346,057
        10         20         30         40         50         60 
MLSFLGKSVA LLAALQATLS SPKPGHRRAS VEKRANGYAN SVYFTNWGIY DRNFQPADLV 

        70         80         90        100        110        120 
ASDVTHVIYS FMNLQADGTV ISGDTYADYE KHYADDSWND VGTNAYGCVK QLFKVKKANR 

       130        140        150        160        170        180 
GLKVLLSIGG WTWSTNFPSA ASTDANRKNF AKTAITFMKD WGFDGIDIDW EYPADATQAS 

       190        200        210        220        230        240 
NMILLLKEVR SQRDAYAAQY APGYHFLLTI AAPAGKDNYS KLRLADLGQV LDYINLMAYD 

       250        260        270        280        290        300 
YAGSFSPLTG HDANLFNNPS NPNATPFNTD SAVKDYINGG VPANKIVLGM PIYGRSFQNT 

       310        320        330        340        350        360 
AGIGQTYNGV GSGSWEAGIW DYKALPKAGA TVQYDSVAKG YYSYNSATKE LISFDTPDMI 

       370        380        390        400        410        420 
NTKVAYLKSL GLGGSMFWEA SADKKGADSV IGTSHRALGG LDTTQNLLSY PNSKYDNIKN 


GLN 

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References

[1]"Cloning and characterization of a chitinase (chit42) cDNA from the mycoparasitic fungus Trichoderma harzianum."
Garcia I., Lora J.M., de la Cruz J., Benitez T., Llobell A., Pintor-Toro J.A.
Curr. Genet. 27:83-89(1994) [PubMed: 7750151] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-52; 93-107; 371-385 AND 397-414.

Cross-references

Sequence databases

S78423 mRNA. Translation: AAB34355.1.
PIRS51369.

3D structure databases

HSSPHSSP built from PDB template 1LL7 based on UniProtKB P54196.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA3.2.1.14. 3745.

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR001223. 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]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI4_TRIHA
AccessionPrimary (citable) accession number: P48827
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 22, 2009
This is version 64 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