[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Seedling; DOI=10.1007/BF00023999; PubMed=1893114 [NCBI, ExPASy, EBI, Israel, Japan] Huang J.K., Wen L., Swegle M., Tran H.C., Thin T.H., Naylor H.M., Muthukrishnan S., Reeck G.R.; "Nucleotide sequence of a rice genomic clone that encodes a class I endochitinase."; Plant Mol. Biol. 16:479-480(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00280194; PubMed=7901749 [NCBI, ExPASy, EBI, Israel, Japan] Nishizawa Y., Kishimoto N., Saito A., Hibi T.; "Sequence variation, differential expression and chromosomal location of rice chitinase genes."; Mol. Gen. Genet. 241:1-10(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; The international rice genome sequencing project (IRGSP) consortium; "Oryza sativa nipponbare chromosome 6 genomic DNA sequence."; Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Nipponbare; DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan] The rice full-length cDNA consortium; "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."; Science 301:376-379(2003).

Comments

FUNCTION: Defense against chitin containing fungal pathogens.
CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily [view classification].
SIMILARITY: Contains 1 chitin-binding type-1 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54367; CAA38249.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16223; BAA03751.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003685; BAD61708.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP004685; BAD61800.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK061280; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

S14948; S14948.

NP_001058626.1; -.

3D structure databases

HSSP

P02877; 1HEV. [HSSP ENTRY / PDB]

SMR

P24626; 19-317.

ModBase

P24626.

Organism-specific databases

Gramene

P24626; -.

Ontologies

GO:0008061;	Molecular function: chitin binding (inferred from electronic annotation from InterPro).
GO:0004568;	Molecular function: chitinase activity (inferred from electronic annotation from InterPro).
GO:0016998;	Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0006032;	Biological process: chitin catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001002; Chitin_bd_1.
IPR016283; Glyco_hydro_19.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.60.10; Chitin_bd_1; 1.

PANTHER

PTHR22595; Glyco_hydro_19_cat; 1.

Pfam

PF00187; Chitin_bind_1; 1.
PF00182; Glyco_hydro_19; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001060; Endochitinase; 1.

PRINTS

PR00451; CHITINBINDNG.

ProDom

PD000609; Chitin_binding_1; 1.
PD354900; Glyco_hydro_19; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00270; ChtBD1; 1.
SMART graphical view of domain structure.

PROSITE

PS00026; CHIT_BIND_I_1; 1.
PS50941; CHIT_BIND_I_2; 1.
PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

4342114; -.

KEGG

osa:4342114; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`CHAIN`	`19 320`	`302`	`Basic endochitinase 1.`	`PRO_0000005305`
`DOMAIN`	`19 59`	`41`	`Chitin-binding type-1.`
`DISULFID`	`21 36`		`By similarity.`
`DISULFID`	`30 42`		`By similarity.`
`DISULFID`	`35 49`		`By similarity.`
`DISULFID`	`53 57`		`By similarity.`
`DISULFID`	`97 159`		`By similarity.`
`DISULFID`	`172 180`		`By similarity.`
`DISULFID`	`279 311`		`By similarity.`
`CONFLICT`	`98 98`		`A -> R (in Ref. 1; CAA38249).`
`CONFLICT`	`122 122`		`G -> R (in Ref. 1; CAA38249).`
`CONFLICT`	`183 183`		`G -> A (in Ref. 1; CAA38249).`
`CONFLICT`	`202 206`		`PAGQA -> RGAG (in Ref. 1; CAA38249).`
`CONFLICT`	`223 223`		`Missing (in Ref. 1; CAA38249).`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 33681 Da [This is the MW of the unprocessed precursor]

CRC64: D7331BF4A6B592E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRALALAVVA MAVVAVRGEQ CGSQAGGALC PNCLCCSQYG WCGSTSDYCG AGCQSQCSGG 

        70         80         90        100        110        120 
CGGGPTPPSS GGGSGVASII SPSLFDQMLL HRNDQACAAK GFYTYDAFVA AANAYPDFAT 

       130        140        150        160        170        180 
TGDADTCKRE VAAFLAQTSH ETTGGWPTAP DGPYSWGYCF KEENNGNAPT YCEPKPEWPC 

       190        200        210        220        230        240 
AAGKKYYGRG PIQITYNYNY GPAGQAIGSD LLNNPDLVAS DATVSFKTAF WFWMTPQSPK 

       250        260        270        280        290        300 
PSCHAVITGQ WTPSADDQAA GRVPGYGEIT NIINGGVECG HGADDKVADR IGFYKRYCDM 

       310        320 
LGVSYGDNLD CYNQRPYPPS

P24626 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools