Chitin deacetylase precursor - Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

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P82476 (CDA_CRYNH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chitin deacetylase
EC=3.5.1.41

Gene names

ORF Names:

CNAG_01239

Organism

Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex ›

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
Catalytic activity	Chitin + H₂O = chitosan + acetate.
Sequence similarities	Belongs to the polysaccharide deacetylase family.
Caution	The protein characterized in Ref.2 is not a chitin deacetylase, the peptides sequenced being copurified contaminants of the protein under study.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Domain	Signal
Molecular function	Hydrolase
PTM	Cleavage on pair of basic residues Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	chitin deacetylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

18

Potential

Propeptide

21

PRO_0000024830

Chain

373

Chitin deacetylase

PRO_0000024831

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

4

PGPG → SSPP AA sequence Ref.2

Sequence conflict

1

P → R AA sequence Ref.2

Sequence conflict

1

G → K AA sequence Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P82476 [UniParc].

Last modified February 6, 2013. Version 3.
Checksum: C04C77223646E647
Show »

412

44,158

        10         20         30         40         50         60 
MYGHLSLSAL SLFAVVAAAP FRESWLQPRD SPVSQLFRRT APDPNSNDYM SYYPGPGSTP 

        70         80         90        100        110        120 
NVSTIPQAWL DKLATVNLPN VPVATPDGGR PTYPNNEDDG DSTICSFTDQ CRVEDDLYSP 

       130        140        150        160        170        180 
PGEKIWALSF DDGPTDVSPA LYDYLAQNNI SSSATHFMIG GNVITSPQSV LVAVKAGGHL 

       190        200        210        220        230        240 
AVHTWSHPYM TTLTNEQVVG ELGWTMQALS DLNGGRIPMY WRPPYGDVDN RVRAIAKEVF 

       250        260        270        280        290        300 
GLVTVLWDSD TNDWAITDEP GQYSVASVEA YFDTLVTGNR TQGLLLLEHE LDNNTVEVFE 

       310        320        330        340        350        360 
TEYPKAVGNG WTVKNVADAF NMEWYLNSGK GNNDVVTTMS VAGTLTTATP TNTSTYVASS 

       370        380        390        400        410 
TAASSASVTD SAGVSIASAA SSEASSSWAI ANRPSHFVIA IACGLALAAI MV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Cryptococcus neoformans grubii H99." The Broad Institute Genome Sequencing Platform Birren B., Cuomo C., Gargeya S., Jaffe D., Young S.K., Wortman J., Zeng Q., Alvarado L., Dietrich F., Allen A., Stajich J.E., Heitman J., Kronstad J. Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
[2]	"Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans." Chen S.C.A., Wright L.C., Golding J.C., Sorrell T.C. Biochem. J. 347:431-439(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-58; 73-91; 305-310 AND 315-330. Strain: BL-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003824 Genomic DNA. Translation: AFR94907.1.
3D structure databases
ProteinModelPortal	P82476.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.370. 1 hit.
InterPro	IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR002509. Polysac_deacetylase. [Graphical view]
Pfam	PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
SUPFAM	SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CDA_CRYNH

Accession

Primary (citable) accession number: P82476
Secondary accession number(s): J9VKC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 6, 2013
Last modified:	April 3, 2013
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents