NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00037049; PubMed=1912489 [NCBI, ExPASy, EBI, Israel, Japan]
Davis J.M., Clarke H.R.G., Bradshaw H.D. Jr., Gordon M.P.;
"Populus chitinase genes: structure, organization, and similarity of translated sequences to herbaceous plant chitinases.";
Plant Mol. Biol. 17:631-639(1991).

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.
INDUCTION: By wounding.
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

X59995; CAA42614.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P02877; 1HEV. [HSSP ENTRY / PDB]

ModBase

P29032.

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.
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.

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; PARTIAL.
PS00774; CHITINASE_19_2; PARTIAL.
PROSITE graphical view of domain structure (profiles).

Other

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 22`	`22`	`By similarity.`
`CHAIN`	`23 >121`	`>99`	`Acidic endochitinase WIN6.2C.`	`PRO_0000005318`
`DOMAIN`	`23 63`	`41`	`Chitin-binding type-1.`
`REGION`	`78 121`	`44`	`Catalytic.`
`COMPBIAS`	`64 77`	`14`	`Gly-rich.`
`DISULFID`	`25 40`		`By similarity.`
`DISULFID`	`34 46`		`By similarity.`
`DISULFID`	`39 53`		`By similarity.`
`DISULFID`	`57 61`		`By similarity.`
`NON_TER`	`121 121`

Sequence information

Length: 121 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 12689 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: A89DFC96795FE87F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVWAFFAFF SLFLSLSVRG SAEQCGRQAG DALCPGGLCC SFYGWCGTTV DYCGDGCQSQ 

        70         80         90        100        110        120 
CDGGDGCDGG GGGGGDGDDG YLSDIIPKST FDALLKFRND PRCHAVGFYT YDAFISAAKE 


F

P29032 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