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Protein

Basic 30 kDa endochitinase

Gene

CHI9

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
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:
Basic 30 kDa endochitinase (EC:3.2.1.14)
Gene namesi
Name:CHI9
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
Proteomesi
  • UP000004994 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell wall, Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000000530123 – 315Basic 30 kDa endochitinaseAdd BLAST293
PropeptideiPRO_0000005302316 – 322Removed in mature form7

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 40PROSITE-ProRule annotation
Disulfide bondi34 ↔ 46PROSITE-ProRule annotation
Disulfide bondi39 ↔ 53PROSITE-ProRule annotation
Disulfide bondi58 ↔ 62PROSITE-ProRule annotation
Modified residuei664-hydroxyprolineBy similarity1
Modified residuei684-hydroxyprolineBy similarity1
Disulfide bondi93 ↔ 156PROSITE-ProRule annotation
Disulfide bondi168 ↔ 176PROSITE-ProRule annotation
Disulfide bondi275 ↔ 307PROSITE-ProRule annotation

Post-translational modificationi

The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.By similarity

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiQ05538.
PRIDEiQ05538.

Expressioni

Inductioni

By fungal infection.

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc10g055810.1.1.

Structurei

3D structure databases

ProteinModelPortaliQ05538.
SMRiQ05538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 64Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST42

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.
InParanoidiQ05538.
KOiK20547.
OMAiRNDANCP.
OrthoDBiEOG09360IMR.

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.

Q05538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSEFTTLF LLFSVLLLSA SAEQCGSQAG GALCASGLCC SKFGWCGNTN
60 70 80 90 100
EYCGPGNCQS QCPGGPGPSG DLGGVISNSM FDQMLNHRND NACQGKNNFY
110 120 130 140 150
SYNAFVTAAG SFPGFGTTGD ITARKREIAA FLAQTSHETT GGWPTAPDGP
160 170 180 190 200
YAWGYCFLRE QGSPGDYCTP SSQWPCAPGR KYFGRGPIQI SHNYNYGPCG
210 220 230 240 250
RAIGVDLLNN PDLVATDPVI SFKSAIWFWM TPQSPKPSCH DVITGRWQPS
260 270 280 290 300
GADQAANRVP GFGVITNIIN GGLECGHGSD SRVQDRIGFY RRYCGILGVS
310 320
PGENLDCGNQ RSFGNGLLVD IM
Length:322
Mass (Da):34,345
Last modified:June 1, 1994 - v1
Checksum:iD13A9191AEE8FC5A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34C → R AA sequence (PubMed:9188482).Curated1
Sequence conflicti36Missing AA sequence (PubMed:9188482).Curated1
Sequence conflicti106V → I AA sequence (Ref. 3) Curated1
Sequence conflicti107T → N AA sequence (Ref. 3) Curated1
Sequence conflicti107T → S AA sequence (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15140 mRNA. Translation: CAA78845.1.
PIRiS37344.
RefSeqiNP_001234403.1. NM_001247474.2.
UniGeneiLes.3406.

Genome annotation databases

EnsemblPlantsiSolyc10g055810.1.1; Solyc10g055810.1.1; Solyc10g055810.1.
GeneIDi544148.
GrameneiSolyc10g055810.1.1; Solyc10g055810.1.1; Solyc10g055810.1.
KEGGisly:544148.

Similar proteinsi

Entry informationi

Entry nameiCHIC_SOLLC
AccessioniPrimary (citable) accession number: Q05538
Secondary accession number(s): P80800
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 7, 2017
This is version 122 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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