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P05315 (CHIT_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Defense against chitin containing fungal pathogens.

Catalytic activity

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

Subcellular location

Vacuole By similarity. Note: Vacuolar and protoplast By similarity.

Induction

By ethylene.

Sequence similarities

Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.

Contains 1 chitin-binding type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 321295Endochitinase
PRO_0000005327
Propeptide322 – 3287Removed in mature form Probable
PRO_0000005328

Regions

Domain27 – 6842Chitin-binding type-1

Amino acid modifications

Disulfide bond29 ↔ 44 By similarity
Disulfide bond38 ↔ 50 By similarity
Disulfide bond43 ↔ 57 By similarity
Disulfide bond62 ↔ 66 By similarity
Disulfide bond100 ↔ 162 By similarity
Disulfide bond174 ↔ 182 By similarity
Disulfide bond281 ↔ 313 By similarity

Secondary structure

..................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05315 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 669B82159BC176EF

FASTA32835,407
        10         20         30         40         50         60 
MRRHKEVNFV AYLLFSLLVL VSAALAQNCG SQGGGKACAS GQCCSKFGWC GNTNDYCGSG 

        70         80         90        100        110        120 
NCQSQCPGGG PGPGPGGDLG SAISNSMFDQ MLKHRNENSC QGKNFYSYNA FINAARSFPG 

       130        140        150        160        170        180 
FGTSGDINAR KREIAAFFAQ TSHETTGGWA SAPDGPYAWG YCFLRERGNP GDYCPPSSQW 

       190        200        210        220        230        240 
PCAPGRKYFG RGPIQISHNY NYGPCGRAIG VDLLNNPDLV ATDPVISFKT ALWFWMTPQS 

       250        260        270        280        290        300 
PKPSCHDVII GRWNPSSADR AANRLPGFGV ITNIINGGLE CGRGTDNRVQ DRIGFYRRYC 

       310        320 
SILGVTPGDN LDCVNQRWFG NALLVDTL 

« Hide

References

[1]"Primary structure of an endochitinase mRNA from Solanum tuberosum."
Gaynor J.J.
Nucleic Acids Res. 16:5210-5210(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Russet Burbank-0.
Tissue: Leaf.
[2]"Sequence analysis of a genomic clone encoding an endochitinase from Solanum tuberosum."
Gaynor J.J., Unkenholz K.M.
Nucleic Acids Res. 17:5855-5855(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Russet Burbank-0.
[3]"Endochitinase [precursor] function as a defense against chitin containing fungal pathogens."
Rao G.S.
Submitted (MAY-2003) to the PDB data bank
Cited for: 3D-STRUCTURE MODELING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07130 mRNA. Translation: CAA30142.1.
X15494 Genomic DNA. Translation: CAA33517.1.
PIRS05426.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P3Zmodel-A1-328[»]
ProteinModelPortalP05315.
SMRP05315. Positions 27-320.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.60.10. 1 hit.
InterProIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFPIRSF001060. Endochitinase. 1 hit.
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHIT_SOLTU
AccessionPrimary (citable) accession number: P05315
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: February 19, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries