[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ETHM 483; DOI=10.1016/0378-1119(92)90099-B; PubMed=1398137 [NCBI, ExPASy, EBI, Israel, Japan] Blaiseau P.-L., Lafay J.-F.; "Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: similarity to bacterial chitinases."; Gene 120:243-248(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-67, AND PROTEIN SEQUENCE OF 35-67. DOI=10.1007/BF00318656; PubMed=1735126 [NCBI, ExPASy, EBI, Israel, Japan] Blaiseau P.-L., Kunz C., Grison R., Bertheau Y., Brygoo Y.; "Cloning and expression of a chitinase gene from the hyperparasitic fungus Aphanocladium album."; Curr. Genet. 21:61-66(1992).

Comments

CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily [view classification].

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

X64104; CAA45468.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S81303; AAB21333.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ1975; JQ1975.
S26859; S26859.

3D structure databases

HSSP

P54196; 1D2K. [HSSP ENTRY / PDB]

ModBase

P32470.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0004568;	Molecular function: chitinase activity (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

IPR011583; Chitinase_II.
IPR001223; Glyco_hydro18cat.
IPR001579; Glyco_hydro_18_chit_AS.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

Pfam

PF00704; Glyco_hydro_18; 1.
Pfam graphical view of domain structure.

ProDom

PD000471; Chitinase_II; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00636; Glyco_18; 1.
SMART graphical view of domain structure.

PROSITE

PS01095; CHITINASE_18; 1.

Other

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

Keywords

Carbohydrate metabolism; Chitin degradation; Cleavage on pair of basic residues; Direct protein sequencing; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 34`	`12`	`Potential.`	`PRO_0000011922`
`CHAIN`	`35 423`	`389`	`Chitinase 1.`	`PRO_0000011923`
`ACT_SITE`	`171 171`		`Proton donor (By similarity).`

Sequence information

Length: 423 AA [This is the length of the unprocessed precursor]

Molecular weight: 46059 Da [This is the MW of the unprocessed precursor]

CRC64: 55DFB25B73443F31 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSFVKKSIA LVAALQAVTA LATPISSEAG VEKRGSGFAN AVYFTNWGIY GRNFQPADLP 

        70         80         90        100        110        120 
ASEITHVLYS FMNVRADGTI FSGDTYADYE KHYAGDSWND VGTNAYGCVK QLYLLKKQNR 

       130        140        150        160        170        180 
NMKVMLSIGG WTWSTNFPAA ASSAATRKTF AQSAVGFMKD WGFDGIDIDW EYPADATQAQ 

       190        200        210        220        230        240 
NMVLLLQAVR SELDSYAAQY AKGHHFLLSI AAPAGPDNYN KLKFAELGKV LDYINLMAYD 

       250        260        270        280        290        300 
YAGSWSNYTG HDANIYANPQ NPNATPYNTD DAVQAYINGG VPANKIVLGM PIYGRSFQQT 

       310        320        330        340        350        360 
EGIGKPYNGI GSGSWENGIW DYKALPKAGA TVKCDDTAKG CYSYDPSTKE LISFDTPAMI 

       370        380        390        400        410        420 
STKVSWLKGK GLGGTMFWEA SASKKGSDSL ISTSHQGLGS QDSTQNYLDY PNSKYDNIKK 


GMN

P32470 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