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Protein

Basic endochitinase C

Gene

rscc

Organism
Secale cereale (Rye)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.3 Publications

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.2 Publications

pH dependencei

Optimum pH is about 5.0. Stable between pH 4-8.1 Publication

Temperature dependencei

Enzyme activity is retained almost fully under 40 degrees Celsius and completely destroyed at 70 degrees Celsius. At 60 degrees Celsius the activity was 15-30% compared to the untreated enzyme.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei95 – 951May be involved in substrate-binding1 Publication
Sitei118 – 1181May be involved in substrate-binding1 Publication

GO - Molecular functioni

  • chitinase activity Source: UniProtKB
  • chitin binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Fungicide, Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Basic endochitinase C (EC:3.2.1.14)
Alternative name(s):
Rye seed chitinase-c
Short name:
RSC-c
Gene namesi
Name:rsccImported
OrganismiSecale cereale (Rye)
Taxonomic identifieri4550 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeSecale

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901E → Q: Abolishes chitinase activity. 1 Publication
Mutagenesisi95 – 951W → A: Chitinase activity is reduced to 51.2% of wild-type. Decreased anti-fungal activity. 1 Publication
Mutagenesisi112 – 1121E → Q: Chitinase activity is reduced to 0.33% of wild-type. Decreased anti-fungal activity. 1 Publication
Mutagenesisi118 – 1181D → A: Chitinase activity is reduced to 79% of wild-type. Decreased anti-fungal activity. 1 Publication
Mutagenesisi143 – 1431S → A: Chitinase activity is reduced to 1.2% of wild-type. Decreased anti-fungal activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23233 PublicationsAdd
BLAST
Chaini24 – 266243Basic endochitinase C1 PublicationPRO_0000042671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 1081 Publication
Disulfide bondi120 ↔ 1281 Publication
Disulfide bondi246 ↔ 2591 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Localized to the starchy endoderm of the seed May localize to other parts of the seed including the aleurone cells (at protein level).1 Publication

Developmental stagei

Levels increase from 23 to 40 days after flowering, and are maintained until maturation (at protein level).1 Publication

Interactioni

Protein-protein interaction databases

MINTiMINT-8388665.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 273Combined sources
Helixi31 – 377Combined sources
Turni38 – 425Combined sources
Turni47 – 515Combined sources
Helixi54 – 629Combined sources
Turni65 – 684Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 9018Combined sources
Helixi102 – 1043Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi123 – 1264Combined sources
Turni138 – 1414Combined sources
Helixi145 – 15511Combined sources
Turni159 – 1613Combined sources
Helixi165 – 1684Combined sources
Helixi170 – 18213Combined sources
Helixi191 – 1955Combined sources
Helixi203 – 2086Combined sources
Helixi214 – 22613Combined sources
Beta strandi227 – 2304Combined sources
Helixi233 – 24917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DWXX-ray1.80A/B24-266[»]
4DYGX-ray1.70A/B24-266[»]
4J0LX-ray1.90A24-266[»]
ProteinModelPortaliQ9FRV0.
SMRiQ9FRV0. Positions 24-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 19 family. Chitinase class II subfamily.Curated1 Publication

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FRV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLAVVVAV VATVAMAIGT AHGSVSSIIS HAQFDRMLLH RNDGACQAKG
60 70 80 90 100
FYTYDAFVAA ANAFPGFGAT GSTDARKRDV AAFLAQTSHE TTGGWATAPD
110 120 130 140 150
GAFAWGYCFK QERGAAADYC TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP
160 170 180 190 200
AGRAIGVDLL RNPDLVATDP TVSFKTALWF WMTAQAPKPS SHAVITGKWS
210 220 230 240 250
PSGADRAAGR APGFGVITNI INGGLECGHG QDSRVADRIG FYKRYCDILG
260
VGYGDNLDCY NQRPFA
Length:266
Mass (Da):28,302
Last modified:March 1, 2001 - v1
Checksum:iE5E22C5BE43DB589
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051579 mRNA. Translation: BAB18520.1.
PIRiJC7816.
JN0884.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051579 mRNA. Translation: BAB18520.1.
PIRiJC7816.
JN0884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DWXX-ray1.80A/B24-266[»]
4DYGX-ray1.70A/B24-266[»]
4J0LX-ray1.90A24-266[»]
ProteinModelPortaliQ9FRV0.
SMRiQ9FRV0. Positions 24-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8388665.

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, functional expression, and mutagenesis of cDNA encoding rye (Secale cereale) seed chitinase-c."
    Ohnuma T., Yagi M., Yamagami T., Taira T., Aso Y., Ishiguro M.
    Biosci. Biotechnol. Biochem. 66:277-284(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-28, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-90; TRP-95; GLU-112; ASP-118 AND SER-143.
    Tissue: Seed1 Publication.
  2. "The complete amino acid sequence of chitinase-c from the seeds of rye (Secale cereal)."
    Yamagami T., Funatsu G.
    Biosci. Biotechnol. Biochem. 57:1854-1861(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-266, DISULFIDE BONDS.
    Tissue: Seed1 Publication.
  3. "Purification and some properties of three chitinases from the seeds of rye (Secale cereale)."
    Yamagami T., Funatsu G.
    Biosci. Biotechnol. Biochem. 57:643-647(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-30, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  4. "Identification of the aspartic acid residue located at or near substrate-binding site of rye seed chitinase-c."
    Yamagami T., Funatsu G.
    Biosci. Biotechnol. Biochem. 62:383-385(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 114-133 AND 254-260, ROLE OF ASP-118 IN SUBSTRATE BINDING.
  5. "Identification of the tryptophan residue located at the substrate-binding site of rye seed chitinase-c."
    Yamagami T., Funatsu G.
    Biosci. Biotechnol. Biochem. 59:1076-1081(1995)
    Cited for: ROLE OF TRP-95 IN SUBSTRATE BINDING.
  6. "Localization, accumulation, and antifungal activity of chitinases in rye (Secale cereale) seed."
    Taira T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.
    Biosci. Biotechnol. Biochem. 65:2710-2718(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Antifungal activity of rye (Secale cereale) seed chitinases: the different binding manner of class I and class II chitinases to the fungal cell walls."
    Taira T., Ohnuma T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.
    Biosci. Biotechnol. Biochem. 66:970-977(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCHIC_SECCE
AccessioniPrimary (citable) accession number: Q9FRV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: February 17, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.