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Protein

Basic 30 kDa endochitinase

Gene

CHI9

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: -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

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

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

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
OMAiAPGRKYY
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
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.

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: May 23, 2018
This is version 126 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

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