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Reviewed, UniProtKB/Swiss-Prot Q1EAR5 (CHI2_COCIM)

Last modified November 3, 2009. Version 26. 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 2
    EC=3.2.1.14
Gene names
Name: CTS2
ORF Names: CIMG_00348
OrganismCoccidioides immitis (Valley fever fungus) [Complete proteome]
Taxonomic identifier5501 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

May be associated with endosporulation.

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Sequence caution

The sequence EAS34994.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentCell membrane
Membrane
   DomainSignal
   LigandChitin-binding
   Molecular functionGlycosidase
Hydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

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 – 2222 Potential
Chain23 – 866844Endochitinase 2
PRO_0000252287
Propeptide867 – 89529Removed in mature form Potential
PRO_0000252288

Regions

Compositional bias346 – 840495Ser/Thr-rich

Amino acid modifications

Lipidation8661GPI-anchor amidated glycine Potential
Glycosylation901N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q1EAR5-1 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: C34ECF3D2609C3CF

FASTA89594,380
        10         20         30         40         50         60 
MGLTNILAAF IAVSSLFIQS LALNPYAKSN LAVYWGQGAG QNRLSYFCEK TSFDIIVVGF 

        70         80         90        100        110        120 
INVFPDQGPA GWPGSNFGNQ CADSYYYTKN GTKTKLLDGC YQIKEDLPKC KALGKTILLS 

       130        140        150        160        170        180 
LGGGAVHDFY EVKSEESALN FADFLWGAFG PLTPDWTGPR PFGEASVDGF DFDIEKGSNF 

       190        200        210        220        230        240 
GYSIMVRRLR ELFLQDPLNR YYISAAPQCI MPDKYLSHAI SNSAFDFIFI QFYNNPSCSA 

       250        260        270        280        290        300 
KRWVTNPKSV TYTVDDWVKY IRKSGNPLAK LFIGLPASKS AAAKEDYLTP GEATKIVSTY 

       310        320        330        340        350        360 
MAKYPSTFGG MMVWEATASE NNKLGGLPYA DIMKEVLLRC DPDPPTSTVT STISASTSTQ 

       370        380        390        400        410        420 
TSSQSTTMET KTLSASTTPS SPSTVSPSST MQTTSTGSTS TGTGTTSSQV TSSTTISTRS 

       430        440        450        460        470        480 
ASTETVTTRS QEPPSTTIST RPASTETVTT RSQEPPSSTI STRSASTETV TTRSQEPPSS 

       490        500        510        520        530        540 
TISTRSASTE TSTSSQDSPS TTISTKSAPT GTVTTRSQDL PSTTISTRSP ETETETVTTK 

       550        560        570        580        590        600 
SQDSPSITLS TRSSSAETVS TRSQHSSSTT ISTKSAPTET GTTSEHSTSM PVSTRSASTE 

       610        620        630        640        650        660 
TVITRSQNSD SQSMTVSTRS PSTESITTRS QGSPSETFST KSVPVDTIST ELPSQTHSTT 

       670        680        690        700        710        720 
DSTPVSSSPT IPSGSTTIIP GTASDPVSAP TTTVPPNPTL TLAPSSSTTE DRTTITTIIT 

       730        740        750        760        770        780 
TSYVTVCPTG FTTVTITYTT TYCPETASLT PTQAPIPGAP APPPDGWTTI VTVCPQCAPT 

       790        800        810        820        830        840 
PTTVTLTVPT RSAFLPAPTE TRPVVTVVPV PENPIKNVKP SESGDFVTVT TVAPATVTKT 

       850        860        870        880        890 
LEYNNPVDSD VNVQPTGGSS PVEFEGGAMT VRSMDVVAKA LITAGAAVLG LFLGL 

« Hide

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.

Cross-references

Sequence databases

CH476726 Genomic DNA. Translation: EAS34994.1. Sequence problems.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.14. 97654.

Family and domain databases

InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
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]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHI2_COCIM
AccessionPrimary (citable) accession number: Q1EAR5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: November 3, 2009
This is version 26 of the entry and version 2 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