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

26 kDa endochitinase 2

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens.

Catalytic activityi

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

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

Enzyme and pathway databases

BRENDAi3.2.1.14. 2687.

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
26 kDa endochitinase 2 (EC:3.2.1.14)
Alternative name(s):
CHI-26
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000000529724 – 26626 kDa endochitinase 2Add BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 108
Disulfide bondi120 ↔ 128
Disulfide bondi227 ↔ 259

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP23951.

Interactioni

Protein-protein interaction databases

STRINGi4513.MLOC_6801.1.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 27Combined sources3
Helixi31 – 37Combined sources7
Turni38 – 42Combined sources5
Turni47 – 51Combined sources5
Helixi54 – 61Combined sources8
Turni65 – 68Combined sources4
Beta strandi70 – 72Combined sources3
Helixi73 – 90Combined sources18
Helixi102 – 104Combined sources3
Beta strandi124 – 126Combined sources3
Turni138 – 141Combined sources4
Helixi145 – 155Combined sources11
Turni159 – 161Combined sources3
Helixi165 – 168Combined sources4
Helixi170 – 182Combined sources13
Helixi191 – 195Combined sources5
Helixi203 – 207Combined sources5
Helixi214 – 226Combined sources13
Beta strandi227 – 230Combined sources4
Helixi233 – 249Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CNSX-ray1.91A/B24-266[»]
2BAAX-ray1.80A24-266[»]
ProteinModelPortaliP23951.
SMRiP23951.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23951.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLAVVVAV VATVAMAIGT ARGSVSSIVS RAQFDRMLLH RNDGACQAKG
60 70 80 90 100
FYTYDAFVAA AAAFPGFGTT GSADAQKREV AAFLAQTSHE TTGGWATAPD
110 120 130 140 150
GAFAWGYCFK QERGASSDYC TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP
160 170 180 190 200
AGRAIGVDLL ANPDLVATDA TVGFKTAIWF WMTAQPPKPS SHAVIAGQWS
210 220 230 240 250
PSGADRAAGR VPGFGVITNI INGGIECGHG QDSRVADRIG FYKRYCDILG
260
VGYGNNLDCY SQRPFA
Length:266
Mass (Da):28,156
Last modified:March 1, 1992 - v1
Checksum:i0949BE88CC20B664
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173G → A AA sequence (PubMed:1899089).Curated1
Sequence conflicti205D → S AA sequence (PubMed:1899089).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti205D → S.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34210 Genomic DNA. Translation: AAA56786.1.
M62904 mRNA. Translation: AAA32941.1.
PIRiA29104.
A38664.
UniGeneiHv.23168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34210 Genomic DNA. Translation: AAA56786.1.
M62904 mRNA. Translation: AAA32941.1.
PIRiA29104.
A38664.
UniGeneiHv.23168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CNSX-ray1.91A/B24-266[»]
2BAAX-ray1.80A24-266[»]
ProteinModelPortaliP23951.
SMRiP23951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4513.MLOC_6801.1.

Protein family/group databases

CAZyiGH19. Glycoside Hydrolase Family 19.

Proteomic databases

PRIDEiP23951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG4742. Eukaryota.
COG3979. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.14. 2687.

Miscellaneous databases

EvolutionaryTraceiP23951.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
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...

Entry informationi

Entry nameiCHI2_HORVU
AccessioniPrimary (citable) accession number: P23951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 103 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.