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Protein

Basic endochitinase A

Gene

rsca

Organism
Secale cereale (Rye)
Status
Reviewed-Annotation score: -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 endo-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

Keywordsi

Molecular functionAntimicrobial, Fungicide, Glycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation
LigandChitin-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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
SMRiQ9FRV1
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

Keywords - Domaini

Signal

Family and domain databases

CDDicd00325 chitinase_glyco_hydro_19, 1 hit
Gene3Di3.30.60.10, 1 hit
InterProiView protein in InterPro
IPR001002 Chitin-bd_1
IPR018371 Chitin-binding_1_CS
IPR036861 Endochitinase-like_sf
IPR016283 Glyco_hydro_19
IPR000726 Glyco_hydro_19_cat
IPR023346 Lysozyme-like_dom_sf
PfamiView protein in Pfam
PF00187 Chitin_bind_1, 1 hit
PF00182 Glyco_hydro_19, 1 hit
PIRSFiPIRSF001060 Endochitinase, 1 hit
PRINTSiPR00451 CHITINBINDNG
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609 Chitin_bd_1, 1 hit
SMARTiView protein in SMART
SM00270 ChtBD1, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
SSF57016 SSF57016, 1 hit
PROSITEiView protein in PROSITE
PS00026 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

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

Similar proteinsi

Entry informationi

Entry nameiCHIA_SECCE
AccessioniPrimary (citable) accession number: Q9FRV1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2001
Last modified: November 22, 2017
This is version 75 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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