Endochitinase 1 precursor - Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus)

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P0CB51 (CHI1_COCPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 9. History...

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

Documents (3) |

Third-party data

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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:
Endochitinase 1
EC=3.2.1.14

Alternative name(s):
CiX1
Complement-fixation antigen
Short name=CF-AG
Short name=CF-antigen

Gene names

Name:	CTS1
ORF Names:	CPSG_08657

Organism

Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus) [Complete proteome]

Taxonomic identifier

443226 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides

Protein attributes

Sequence length	427 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)

Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0. Active from pH 4 to 8. Ref.9
Sequence caution	The sequence BAE20289.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20290.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20291.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20292.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20293.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20294.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20295.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20298.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20301.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20302.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20304.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20305.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20306.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20307.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase 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

1 – 17

Ref.5

Chain

18 – 427

410

Endochitinase 1

PRO_0000011927

Sites

Active site

171

Proton donor

Site

169

Transition state stabilizer

Amino acid modifications

Glycosylation

387

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

T → I in strain: IFM 50993.

Natural variant

Y → S in strain: IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1 and RMSCC 2128 / TX1. Ref.6

Natural variant

103

N → K in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.

Natural variant

109

I → T in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.

Experimental info

Mutagenesis

169

D → N: Loss of function.

Mutagenesis

171

E → Q: Loss of function. Ref.10

Sequence conflict

S → P AA sequence Ref.5

Sequence conflict

E → G AA sequence Ref.5

Sequence conflict

S → A AA sequence Ref.8

Sequence conflict

W → R AA sequence Ref.8

Sequence conflict

199

K → N in AAA96515. Ref.1

Sequence conflict

199

K → N in AAB06687. Ref.1

Secondary structure

427

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0CB51 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 911CE4777F35D2D9
Show »

FASTA

427

47,474

        10         20         30         40         50         60 
MRFLIGALLT LQTLVQASSM SSMPNYYPVP EAPAEGGFRS VVYFVNWAIY GRGHNPQDLK 

        70         80         90        100        110        120 
ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE PGNNVYGCIK QMYLLKKNNR 

       130        140        150        160        170        180 
NLKTLLSIGG WTYSPNFKTP ASTEEGRKKF ADTSLKLMKD LGFDGIDIDW EYPEDEKQAN 

       190        200        210        220        230        240 
DFVLLLKACR EALDAYSAKH PNGKKFLLTI ASPAGPQNYN KLKLAEMDKY LDFWNLMAYD 

       250        260        270        280        290        300 
FSGSWDKVSG HMSNVFPSTT KPESTPFSSD KAVKDYIKAG VPANKIVLGM PLYGRAFAST 

       310        320        330        340        350        360 
DGIGTSFNGV GGGSWENGVW DYKDMPQQGA QVTELEDIAA SYSYDKNKRY LISYDTVKIA 

       370        380        390        400        410        420 
GKKAEYITKN GMGGGMWWES SSDKTGNESL VGTVVNGLGG TGKLEQRENE LSYPESVYDN 


LKNGMPS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the Coccidioides immitis complement fixation/chitinase antigen." Yang C., Zhu Y., Magee D.M., Cox R.A. Infect. Immun. 64:1992-1997(1996) [PubMed: 8675298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: RMSCC 757 / Silveira.
[2]	"Cloning and expression of the complement fixation antigen-chitinase of Coccidioides immitis." Zimmermann C.R., Johnson S.M., Martens G.W., White A.G., Pappagianis D. Infect. Immun. 64:4967-4975(1996) [PubMed: 8945534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: RMSCC 757 / Silveira.
[3]	"The genome sequence of Coccidioides posadasii strain Silveira." The Broad Institute Genome Sequencing Center for Infectious Disease Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J., Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E. Birren B. Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RMSCC 757 / Silveira.
[4]	"Reexamination of Coccidioides spp. reserved in the Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, based on a multiple gene analysis." Sano A., Miyaji M., Kamei K., Mikami Y., Nishimura K. Nippon Ishinkin Gakkai Zasshi 47:113-117(2006) [PubMed: 16699492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-151. Strain: IFM 45809 / Silveira, IFM 45810 / Silveira, IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195 and IFM 54196.
[5]	"Amino-terminal sequence analysis of the Coccidioides immitis chitinase/immunodiffusion-complement fixation protein." Johnson S.M., Zimmermann C.R., Pappagianis D. Infect. Immun. 61:3090-3092(1993) [PubMed: 8514419] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-38. Strain: RMSCC 757 / Silveira.
[6]	"Concordance of gene genealogies reveals reproductive isolation in the pathogenic fungus Coccidioides immitis." Koufopanou V., Burt A., Taylor J.W. Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997) [PubMed: 9144263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-145, VARIANT SER-26. Strain: RMSCC 1036 / AZ1, RMSCC 2128 / TX1 and RMSCC 757 / Silveira.
[7]	Erratum Koufopanou V., Burt A., Taylor J.W. Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998)
[8]	"Purification and amino-terminal sequence analysis of the complement-fixing and precipitin antigens from Coccidioides immitis." Resnick S., Zimmer B., Pappagianis D., Eakin A., McKerrow J. J. Clin. Microbiol. 28:385-388(1990) [PubMed: 2312685] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-52. Strain: RMSCC 757 / Silveira.
[9]	"Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis." Fukamizo T., Sasaki C., Schelp E., Bortone K., Robertus J.D. Biochemistry 40:2448-2454(2001) [PubMed: 11327866] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES. Strain: RMSCC 757 / Silveira.
[10]	"The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis." Hollis T., Monzingo A.F., Bortone K., Ernst S., Cox R.A., Robertus J.D. Protein Sci. 9:544-551(2000) [PubMed: 10752616] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 36-427, PROTEIN SEQUENCE OF 27-41, MUTAGENESIS OF GLU-171. Strain: RMSCC 757 / Silveira.
[11]	"The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism." Bortone K., Monzingo A.F., Ernst S., Robertus J.D. J. Mol. Biol. 320:293-302(2002) [PubMed: 12079386] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 36-427 OF WILD-TYPE IN COMPLEX WITH INHIBITOR AND OF MUTANTS ASN-169 AND GLN-171. Strain: RMSCC 757 / Silveira.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U51271 Genomic DNA. Translation: AAA96515.1.
U33265 mRNA. Translation: AAB06687.1.
U60806 Genomic DNA. Translation: AAB48566.1.
U60807 mRNA. Translation: AAB48567.1.
GL636504 Genomic DNA. Translation: EFW14650.1.
AB232745 Genomic DNA. Translation: BAE20289.1. Sequence problems.
AB232746 Genomic DNA. Translation: BAE20290.1. Sequence problems.
AB232747 Genomic DNA. Translation: BAE20291.1. Sequence problems.
AB232748 Genomic DNA. Translation: BAE20292.1. Sequence problems.
AB232749 Genomic DNA. Translation: BAE20293.1. Sequence problems.
AB232750 Genomic DNA. Translation: BAE20294.1. Sequence problems.
AB232751 Genomic DNA. Translation: BAE20295.1. Sequence problems.
AB232754 Genomic DNA. Translation: BAE20298.1. Sequence problems.
AB232757 Genomic DNA. Translation: BAE20301.1. Sequence problems.
AB232758 Genomic DNA. Translation: BAE20302.1. Sequence problems.
AB232760 Genomic DNA. Translation: BAE20304.1. Sequence problems.
AB232761 Genomic DNA. Translation: BAE20305.1. Sequence problems.
AB232762 Genomic DNA. Translation: BAE20306.1. Sequence problems.
AB232763 Genomic DNA. Translation: BAE20307.1. Sequence problems.
AJ408862 Genomic DNA. Translation: CAC29128.1.
AJ408863 Genomic DNA. Translation: CAC29129.1.
AJ408864 Genomic DNA. Translation: CAC29130.1.

PIR

JC4565.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2K	X-ray	2.20	A	36-427	[»]
1LL4	X-ray	2.80	A/B/C/D	36-427	[»]
1LL6	X-ray	2.80	A/B/C/D	36-427	[»]
1LL7	X-ray	2.00	A/B	36-427	[»]

ProteinModelPortal

P0CB51.

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHI1_COCPS

Accession

Primary (citable) accession number: P0CB51
Secondary accession number(s): E9DFQ8

Q9C2W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	May 31, 2011
This is version 9 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents