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Protein

Endochitinase

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation
LigandChitin-binding

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase (EC:3.2.1.14)
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Subcellular locationi

  • Vacuole By similarity

  • Note: Vacuolar and protoplast.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000000531128 – 317EndochitinaseAdd BLAST290
PropeptideiPRO_0000005312318 – 328Removed in mature formCuratedAdd BLAST11

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 45PROSITE-ProRule annotation
Disulfide bondi39 ↔ 51PROSITE-ProRule annotation
Disulfide bondi44 ↔ 58PROSITE-ProRule annotation
Disulfide bondi62 ↔ 66PROSITE-ProRule annotation
Disulfide bondi97 ↔ 159PROSITE-ProRule annotation
Disulfide bondi170 ↔ 178PROSITE-ProRule annotation
Disulfide bondi277 ↔ 309PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP06215.
ProMEXiP06215.

Expressioni

Inductioni

By ethylene.

Structurei

3D structure databases

ProteinModelPortaliP06215.
SMRiP06215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 68Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST41

Sequence similaritiesi

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.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
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.

P06215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNRMMMMI WSVGVVWMLL LVGGSYGEQC GRQAGGALCP GGNCCSQFGW
60 70 80 90 100
CGSTTDYCGP GCQSQCGGPS PAPTDLSALI SRSTFDQMLK HRNDGACPAK
110 120 130 140 150
GFYTYDAFIA AAKAYPSFGN TGDTATRKRE IAAFLGQTSH ETTGGWATAP
160 170 180 190 200
DGPYAWGYCF VRERNPSTYC SATPQFPCAP GQQYYGRGPI QISWNYNYGQ
210 220 230 240 250
CGRAIGVDLL NKPDLVATDS VISFKSALWF WMTAQSPKPS SHDVITSRWT
260 270 280 290 300
PSSADVAARR LPGYGTVTNI INGGLECGRG QDSRVQDRIG FFKRYCDLLG
310 320
VGYGNNLDCY SQTPFGNSLL LSDLVTSQ
Length:328
Mass (Da):35,444
Last modified:January 1, 1988 - v1
Checksum:i0B5A73626C776C8A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40P → L in AAA33757 (PubMed:16665863).Curated1
Sequence conflicti54T → S AA sequence (Ref. 2) Curated1
Sequence conflicti56D → E AA sequence (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti88M → V. 1
Natural varianti168T → A. 1
Natural varianti210L → F. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13968 mRNA. Translation: AAA33756.1.
M19052 mRNA. Translation: AAA33757.1.

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.

Entry informationi

Entry nameiCHIT_PHAVU
AccessioniPrimary (citable) accession number: P06215
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 10, 2017
This is version 117 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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families