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Protein

Endochitinase 1

Gene

CTS1

Organism
Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 6.0. Active from pH 4 to 8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1691Transition state stabilizer
Active sitei171 – 1711Proton donor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.
mycoCLAPiCHI18A_COCIM.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CTS1
ORF Names:CPSG_08657
OrganismiCoccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus)
Taxonomic identifieri443226 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisCoccidioides
Proteomesi
  • UP000002497 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1691D → N: Loss of function.
Mutagenesisi171 – 1711E → Q: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 427410Endochitinase 1PRO_0000011927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 458Combined sources
Helixi46 – 494Combined sources
Turni50 – 523Combined sources
Helixi56 – 583Combined sources
Helixi61 – 633Combined sources
Beta strandi65 – 7410Combined sources
Beta strandi80 – 834Combined sources
Helixi85 – 884Combined sources
Beta strandi101 – 1033Combined sources
Helixi107 – 11812Combined sources
Beta strandi123 – 1297Combined sources
Helixi130 – 1334Combined sources
Helixi134 – 1363Combined sources
Helixi138 – 1414Combined sources
Helixi144 – 16118Combined sources
Beta strandi164 – 1696Combined sources
Helixi176 – 19823Combined sources
Beta strandi207 – 2137Combined sources
Helixi216 – 2194Combined sources
Helixi224 – 2285Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi246 – 2483Combined sources
Helixi262 – 2643Combined sources
Helixi269 – 27810Combined sources
Helixi283 – 2853Combined sources
Beta strandi286 – 29712Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi319 – 3213Combined sources
Helixi322 – 3243Combined sources
Beta strandi331 – 3355Combined sources
Turni336 – 3394Combined sources
Beta strandi340 – 3456Combined sources
Turni346 – 3494Combined sources
Beta strandi350 – 3534Combined sources
Helixi357 – 36913Combined sources
Beta strandi374 – 3785Combined sources
Helixi386 – 3883Combined sources
Helixi390 – 3978Combined sources
Helixi401 – 4033Combined sources
Helixi419 – 4224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2KX-ray2.20A36-427[»]
1LL4X-ray2.80A/B/C/D36-427[»]
1LL6X-ray2.80A/B/C/D36-427[»]
1LL7X-ray2.00A/B36-427[»]
ProteinModelPortaliP0CB51.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CB51.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OrthoDBiEOG7WQ826.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CB51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFLIGALLT LQTLVQASSM SSMPNYYPVP EAPAEGGFRS VVYFVNWAIY
60 70 80 90 100
GRGHNPQDLK ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE
110 120 130 140 150
PGNNVYGCIK QMYLLKKNNR NLKTLLSIGG WTYSPNFKTP ASTEEGRKKF
160 170 180 190 200
ADTSLKLMKD LGFDGIDIDW EYPEDEKQAN DFVLLLKACR EALDAYSAKH
210 220 230 240 250
PNGKKFLLTI ASPAGPQNYN KLKLAEMDKY LDFWNLMAYD FSGSWDKVSG
260 270 280 290 300
HMSNVFPSTT KPESTPFSSD KAVKDYIKAG VPANKIVLGM PLYGRAFAST
310 320 330 340 350
DGIGTSFNGV GGGSWENGVW DYKDMPQQGA QVTELEDIAA SYSYDKNKRY
360 370 380 390 400
LISYDTVKIA GKKAEYITKN GMGGGMWWES SSDKTGNESL VGTVVNGLGG
410 420
TGKLEQRENE LSYPESVYDN LKNGMPS
Length:427
Mass (Da):47,474
Last modified:November 3, 2009 - v1
Checksum:i911CE4777F35D2D9
GO

Sequence cautioni

The sequence BAE20289.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20290.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20291.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20292.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20293.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20294.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20295.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20298.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20301.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20302.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20304.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20305.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20306.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAE20307.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191S → P AA sequence (PubMed:8514419).Curated
Sequence conflicti31 – 311E → G AA sequence (PubMed:8514419).Curated
Sequence conflicti40 – 401S → A AA sequence (PubMed:2312685).Curated
Sequence conflicti47 – 471W → R AA sequence (PubMed:2312685).Curated
Sequence conflicti199 – 1991K → N in AAA96515 (PubMed:8675298).Curated
Sequence conflicti199 – 1991K → N in AAB06687 (PubMed:8675298).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131T → I in strain: IFM 50993.
Natural varianti26 – 261Y → 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. 1 Publication
Natural varianti103 – 1031N → K in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.
Natural varianti109 – 1091I → T in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC4565.

Genome annotation databases

EnsemblFungiiEFW14650; EFW14650; CPSG_08657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC4565.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2KX-ray2.20A36-427[»]
1LL4X-ray2.80A/B/C/D36-427[»]
1LL6X-ray2.80A/B/C/D36-427[»]
1LL7X-ray2.00A/B36-427[»]
ProteinModelPortaliP0CB51.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.
mycoCLAPiCHI18A_COCIM.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFW14650; EFW14650; CPSG_08657.

Phylogenomic databases

OrthoDBiEOG7WQ826.

Miscellaneous databases

EvolutionaryTraceiP0CB51.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: RMSCC 757 / Silveira.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiCHI1_COCPS
AccessioniPrimary (citable) accession number: P0CB51
Secondary accession number(s): E9DFQ8
, P54196, Q00432, Q00435, Q400W4, Q400W5, Q400W6, Q9C0M7, Q9C2W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: May 11, 2016
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.