NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-38.
STRAIN=ATCC 22959 / AS 3.4818 / CBS 338.62 / IFO 8631 / NRRL 2710;
PubMed=1429462 [NCBI, ExPASy, EBI, Israel, Japan]
Yanai K., Takaya N., Kojima N., Horiuchi H., Ohta A., Takagi M.;
"Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes.";
J. Bacteriol. 174:7398-7406(1992).

Comments

FUNCTION: Probably involved in the apical growth and branching of fungal hyphae.
CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted (Probable).
PTM: O-glycosylated.
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

D10158; BAA01022.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B47022; B47022.

3D structure databases

HSSP

P23472; 2HVM. [HSSP ENTRY / PDB]

ModBase

P29027.

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:0008061;	Molecular function: chitin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004568;	Molecular function: chitinase activity (inferred from electronic annotation from EC).
GO:0006032;	Biological process: chitin catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001223; Glyco_hydro18cat.
IPR005089; Glyco_hydro_18_carb-bd.
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

PF03427; CBM_19; 1.
PF00704; Glyco_hydro_18; 1.
Pfam 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; Chitin-binding; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 446`	`424`	`Chitinase 2.`	`PRO_0000011932`
`PROPEP`	`447 542`	`96`	`Potential.`	`PRO_0000011933`
`REGION`	`23 312`	`290`	`Catalytic.`
`REGION`	`355 406`	`52`	`Chitin-binding, high affinity.`
`COMPBIAS`	`313 354`	`42`	`Ser/Thr-rich.`
`ACT_SITE`	`166 166`		`Proton donor (By similarity).`

Sequence information

Length: 542 AA [This is the length of the unprocessed precursor]

Molecular weight: 56528 Da [This is the MW of the unprocessed precursor]

CRC64: 3E8F17DA551FD0A7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTRTFLGMA ISAFLASTGV QAAWSSHGPN VMYYWGQNSA GGSNTQASLG TYCESGQVDA 

        70         80         90        100        110        120 
VLLSFLHVFN VGGIPEINLS SACAGTYFPN TQLLSCPAVG ADIKKCQDKG VKVILSLGGA 

       130        140        150        160        170        180 
AGVYGFTSDA QGQQFAQTIW NLFGGGNSDT RPFGDAVIDG VDLDIEGGSS TGYVAFVNAL 

       190        200        210        220        230        240 
RQKFSSNFLI GAAPQCPFPD AILGSVLNSA SFDYVNVQFY NNYCSATGSS FNFDTWDNWA 

       250        260        270        280        290        300 
KTTSPNKNVK IMFTVPGSST AAGSGYVPMS TLQTIVPSLA SKYSSYGGVS VWDASQAWNN 

       310        320        330        340        350        360 
GGFNSQLYSL VHSGGSTPPP PSSSSATKTT TKTTATSTKT TTTTAPTATS TPGSCPVANQ 

       370        380        390        400        410        420 
PCSTQNQYAC TADGKYAVCD HGKWVASSCP SNTVCIPTTD GASIYCGYAT GSGSTCPSVS 

       430        440        450        460        470        480 
ALEITAASLG SKNGPVPRPY KASKVAAQLA VTSTDKNSFE AVINARRTTL TPFEKSVTIE 

       490        500        510        520        530        540 
FTTPSNIKFT ESDMGPVRQV GNKVRIQAKN DYNESMTLVV KVKGSINSGV FVAPSTSAWN 


FK

P29027 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