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Reviewed, UniProtKB/Swiss-Prot Q1E3R8 (CHI1_COCIM)

Last modified January 19, 2010. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Endochitinase 1
    EC=3.2.1.14
Alternative name(s):
    Complement-fixation antigen
      Short name=CF-antigen
      Short name=CF-AG
Gene names
Name: CTS1
ORF Names: CIMG_02795
OrganismCoccidioides immitis (Valley fever fungus) [Complete proteome]
Taxonomic identifier5501 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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.

Sequence caution

The sequence BAE20296.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAE20297.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAE20299.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAE20300.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAE20303.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   DomainSignal
   LigandChitin-binding
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 427410Endochitinase 1
PRO_0000252286

Amino acid modifications

Glycosylation3871N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q1E3R8-1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: F55F6DF8D0FCB15D

FASTA42747,398
        10         20         30         40         50         60 
MRFLIGALLT LQTLVQASSM SSMPNSYPVP 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' references
[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RS.
[2]"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 45815, IFM 45816, IFM 46868, IFM 50992 and IFM 50995.
[3]"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.
Strain: RMSCC 1694 / CA2, RMSCC 2019 / CA4 and RMSCC 2267 / CA1.
[4]Erratum
Koufopanou V., Burt A., Taylor J.W.
Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476726 Genomic DNA. Translation: EAS37441.1.
AB232752 Genomic DNA. Translation: BAE20296.1. Sequence problems.
AB232753 Genomic DNA. Translation: BAE20297.1. Sequence problems.
AB232755 Genomic DNA. Translation: BAE20299.1. Sequence problems.
AB232756 Genomic DNA. Translation: BAE20300.1. Sequence problems.
AB232759 Genomic DNA. Translation: BAE20303.1. Sequence problems.
AJ408865 Genomic DNA. Translation: CAC29131.1.
AJ408866 Genomic DNA. Translation: CAC29132.1.
AJ408867 Genomic DNA. Translation: CAC29133.1.
RefSeqXP_001249024.1.

3D structure databases

SMRQ1E3R8. Positions 36-427.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Genome annotation databases

GeneID4566471.

Phylogenomic databases

OrthoDBEOG97PZP0.
PhylomeDBQ1E3R8.

Enzyme and pathway databases

BRENDA3.2.1.14. 97654.

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI1_COCIM
AccessionPrimary (citable) accession number: Q1E3R8
Secondary accession number(s): Q400W2, Q9C0M7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 11, 2006
Last modified: January 19, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents