Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endochitinase

Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan.1 Publication

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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. 1191.

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase (EC:3.2.1.14)
OrganismiCarica papaya (Papaya)
Taxonomic identifieri3649 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

Subcellular locationi

  • Vacuole By similarity

  • Note: Vacuolar and protoplast.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243EndochitinasePRO_0000285971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 85By similarity
Disulfide bondi97 ↔ 105By similarity
Disulfide bondi223 ↔ 236By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi8 – 147Combined sources
Turni15 – 195Combined sources
Turni24 – 285Combined sources
Helixi31 – 399Combined sources
Turni42 – 454Combined sources
Helixi50 – 6718Combined sources
Helixi79 – 813Combined sources
Beta strandi101 – 1033Combined sources
Turni115 – 1184Combined sources
Helixi122 – 13211Combined sources
Turni136 – 1383Combined sources
Helixi140 – 1445Combined sources
Helixi147 – 15913Combined sources
Helixi168 – 1725Combined sources
Helixi180 – 1856Combined sources
Helixi191 – 20313Combined sources
Beta strandi204 – 2074Combined sources
Helixi210 – 22617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQLX-ray1.50A/B1-243[»]
ProteinModelPortaliP85084.
SMRiP85084. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP85084.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P85084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GIEKIISRSM FDQMLKHRNN PACPAKGFYT YDAFLAAAKS FPSFGTTGST
60 70 80 90 100
DVRKRELAAF LGQTSHETTG GWPSAPDGPY AWGYCFLKER NPSSNYCAPS
110 120 130 140 150
PRYPCAPGKS YYGRGPLQLS WNYNYGPCGE ALRVNLLGNP DLVATDRVLS
160 170 180 190 200
FKTALWFWMT PQAPKPSCHD VLTGRWQPSA ADTAAGRLPG YGVLTNLLNG
210 220 230 240
GLECGKGPNP QVADRLGFFR RYCGLLGVGT GNNLDCYNQR PFG
Length:243
Mass (Da):26,541
Last modified:May 1, 2007 - v1
Checksum:i51F48F5F9A722703
GO

Mass spectrometryi

Molecular mass is 26534 Da from positions 1 - 243. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQLX-ray1.50A/B1-243[»]
ProteinModelPortaliP85084.
SMRiP85084. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.14. 1191.

Miscellaneous databases

EvolutionaryTraceiP85084.

Family and domain databases

InterProiIPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases."
    Huet J., Wyckmans J., Wintjens R., Boussard P., Raussens V., Vandenbussche G., Ruysschaert J.M., Azarkan M., Looze Y.
    Cell. Mol. Life Sci. 63:3042-3054(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY.
    Tissue: Latex1 Publication.

Entry informationi

Entry nameiCHIT_CARPA
AccessioniPrimary (citable) accession number: P85084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: December 9, 2015
This is version 39 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.