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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)DescriptionActionsGraphical viewLength
Sitei95May be involved in substrate-binding1 Publication1
Sitei118May be involved in substrate-binding1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi90E → Q: Abolishes chitinase activity. 1 Publication1
Mutagenesisi95W → A: Chitinase activity is reduced to 51.2% of wild-type. Decreased anti-fungal activity. 1 Publication1
Mutagenesisi112E → Q: Chitinase activity is reduced to 0.33% of wild-type. Decreased anti-fungal activity. 1 Publication1
Mutagenesisi118D → A: Chitinase activity is reduced to 79% of wild-type. Decreased anti-fungal activity. 1 Publication1
Mutagenesisi143S → A: Chitinase activity is reduced to 1.2% of wild-type. Decreased anti-fungal activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 233 PublicationsAdd BLAST23
ChainiPRO_000004267124 – 266Basic endochitinase C1 PublicationAdd BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 1081 Publication
Disulfide bondi120 ↔ 1281 Publication
Disulfide bondi246 ↔ 2591 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ9FRV0.

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

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 27Combined sources3
Helixi31 – 37Combined sources7
Turni38 – 42Combined sources5
Turni47 – 51Combined sources5
Helixi54 – 62Combined sources9
Turni65 – 68Combined sources4
Beta strandi69 – 72Combined sources4
Helixi73 – 90Combined sources18
Helixi102 – 104Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi123 – 126Combined sources4
Turni138 – 141Combined sources4
Helixi145 – 155Combined sources11
Turni159 – 161Combined sources3
Helixi165 – 168Combined sources4
Helixi170 – 182Combined sources13
Helixi191 – 195Combined sources5
Helixi203 – 208Combined sources6
Helixi214 – 226Combined sources13
Beta strandi227 – 230Combined sources4
Helixi233 – 249Combined sources17

3D structure databases

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

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DWXX-ray1.80A/B24-266[»]
4DYGX-ray1.70A/B24-266[»]
4J0LX-ray1.90A24-266[»]
ProteinModelPortaliQ9FRV0.
SMRiQ9FRV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8388665.

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Proteomic databases

PRIDEiQ9FRV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
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...

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: November 2, 2016
This is version 61 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.