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Protein

Basic endochitinase A

Gene

rsca

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, lateral walls and septa of fungi and degrades mature chitin.4 Publications

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.3 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 over 80% compared to the untreated enzyme.1 Publication

GO - Molecular functioni

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

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

Enzyme and pathway databases

BRENDAi3.2.1.14. 5654.

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Basic endochitinase A (EC:3.2.1.14)
Alternative name(s):
Rye seed chitinase-a
Short name:
RSC-a
Gene namesi
Name:rscaImported
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
Mutagenesisi42W → A: Reduces chitinase activity towards soluble chitin to 65.5% and towards insoluble chitin. Reduces chitin-binding activity and anti-fungal activity. 1 Publication1
Mutagenesisi145E → Q: Abolishes chitinase activity towards insoluble and soluble chitin. Abolishes chitin-binding activity and anti-fungal activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 193 PublicationsAdd BLAST19
ChainiPRO_000004267020 – 321Basic endochitinase A1 PublicationAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi22 ↔ 37PROSITE-ProRule annotation1 Publication
Disulfide bondi31 ↔ 43PROSITE-ProRule annotation1 Publication
Disulfide bondi34 ↔ 61PROSITE-ProRule annotation1 Publication
Disulfide bondi36 ↔ 50PROSITE-ProRule annotation1 Publication
Disulfide bondi54 ↔ 58PROSITE-ProRule annotation1 Publication
Disulfide bondi101 ↔ 163PROSITE-ProRule annotation1 Publication
Disulfide bondi175 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi301 ↔ 314PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ9FRV1.

Expressioni

Tissue specificityi

Localized in the aleurone cells of the seed endosperm (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

Structurei

3D structure databases

ProteinModelPortaliQ9FRV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 60Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 79Hinge region (Gly/Pro/Thr-rich)Sequence analysisAdd BLAST18
Regioni80 – 321CatalyticSequence analysisAdd BLAST242

Sequence similaritiesi

Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.1 Publication
Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. 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]

Sequencei

Sequence statusi: Complete.

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

Q9FRV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAFALFAVL AMAVTMAVAE QCGSQAGGAT CPNCLCCSRF GWCGSTSDYC
60 70 80 90 100
GDGCQSQCAG CGGGGTPVTP TPTPSGGGGV SSIVSRALFD RMLLHRNDGA
110 120 130 140 150
CQAKGFYTYD AFVAAAGAFP GFGTTGSTDT RKREVAAFLA QTSHETTGGW
160 170 180 190 200
ATAPDGAFAW GYCFKQERGA TSNYCTPSAQ WPCAPGKSYY GRGPIQLSHN
210 220 230 240 250
YNYGPAGRAI GVDLLRNPDL VATDPTVSFK TAMWFWMTAQ APKPSSHAVI
260 270 280 290 300
TGQWSPSGTD RAAGRVPGFG VITNIVNGGI ECGHGQDSRV ADRIGFYKRY
310 320
CDILRVGYGN NLDCYNQRPF A
Length:321
Mass (Da):33,642
Last modified:March 1, 2001 - v1
Checksum:i76E5902BBC337C8E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti305R → G AA sequence (PubMed:7764543).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051578 mRNA. Translation: BAB18519.1.
PIRiJC2071.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051578 mRNA. Translation: BAB18519.1.
PIRiJC2071.

3D structure databases

ProteinModelPortaliQ9FRV1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

PRIDEiQ9FRV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.14. 5654.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCHIA_SECCE
AccessioniPrimary (citable) accession number: Q9FRV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: October 5, 2016
This is version 71 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

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.