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Protein

Endochitinase

Gene

CTS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chitinase is required for cell separation during growth of Saccharomyces cerevisiae.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei157Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

  • chitin binding Source: UniProtKB-KW
  • endochitinase activity Source: SGD

GO - Biological processi

  • cell separation after cytokinesis Source: SGD
  • cell wall organization Source: UniProtKB-KW
  • chitin catabolic process Source: SGD
  • polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Chitin degradation, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

BioCyciYEAST:YLR286C-MONOMER.
BRENDAi3.2.1.14. 984.

Protein family/group databases

CAZyiCBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase (EC:3.2.1.14)
Alternative name(s):
Soluble cell wall protein 2
Gene namesi
Name:CTS1
Synonyms:SCW2
Ordered Locus Names:YLR286C
ORF Names:L8003.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR286C.
SGDiS000004276. CTS1.

Subcellular locationi

  • Secreted 1 Publication
  • Secretedcell wall 1 Publication

  • Note: Most of the enzyme is secreted, but a significant amount of chitinase is also found associated with the cell wall through binding of C-terminal domain to chitin.

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • extracellular region Source: SGD
  • fungal-type cell wall Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1293195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
ChainiPRO_000001193621 – 562EndochitinaseAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi553N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Extensively glycosylated with a series of short O-linked mannose oligosaccharides ranging in size from Man2 to Man5.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP29029.
PRIDEiP29029.

Interactioni

Protein-protein interaction databases

BioGridi31551. 17 interactors.
MINTiMINT-4495746.

Chemistry databases

BindingDBiP29029.

Structurei

Secondary structure

1562
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 35Combined sources8
Helixi44 – 48Combined sources5
Beta strandi50 – 52Combined sources3
Beta strandi54 – 64Combined sources11
Turni65 – 67Combined sources3
Helixi72 – 74Combined sources3
Helixi87 – 98Combined sources12
Beta strandi102 – 108Combined sources7
Beta strandi110 – 114Combined sources5
Helixi119 – 133Combined sources15
Turni143 – 146Combined sources4
Beta strandi150 – 155Combined sources6
Helixi164 – 175Combined sources12
Beta strandi178 – 180Combined sources3
Beta strandi183 – 186Combined sources4
Beta strandi189 – 193Combined sources5
Turni195 – 197Combined sources3
Helixi198 – 203Combined sources6
Beta strandi207 – 212Combined sources6
Beta strandi214 – 216Combined sources3
Beta strandi219 – 223Combined sources5
Helixi226 – 235Combined sources10
Beta strandi243 – 251Combined sources9
Beta strandi254 – 257Combined sources4
Helixi263 – 273Combined sources11
Beta strandi279 – 285Combined sources7
Helixi287 – 292Combined sources6
Beta strandi294 – 299Combined sources6
Helixi300 – 311Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]
ProteinModelPortaliP29029.
SMRiP29029.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29029.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 327CatalyticAdd BLAST307
Regioni481 – 562Chitin-binding, high affinityAdd BLAST82

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi328 – 480Ser/Thr-richAdd BLAST153

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000160027.
InParanoidiP29029.
KOiK01183.
OMAiFNWDTWL.
OrthoDBiEOG092C49QH.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005089. CBM_fam19.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03427. CBM_19. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 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.

P29029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLYIILLF TQFLLLPTDA FDRSANTNIA VYWGQNSAGT QESLATYCES
60 70 80 90 100
SDADIFLLSF LNQFPTLGLN FANACSDTFS DGLLHCTQIA EDIETCQSLG
110 120 130 140 150
KKVLLSLGGA SGSYLFSDDS QAETFAQTLW DTFGEGTGAS ERPFDSAVVD
160 170 180 190 200
GFDFDIENNN EVGYSALATK LRTLFAEGTK QYYLSAAPQC PYPDASVGDL
210 220 230 240 250
LENADIDFAF IQFYNNYCSV SGQFNWDTWL TYAQTVSPNK NIKLFLGLPG
260 270 280 290 300
SASAAGSGYI SDTSLLESTI ADIASSSSFG GIALWDASQA FSNELNGEPY
310 320 330 340 350
VEILKNLLTS ASQTATTTVA TSKTSAASTS SASTSSASTS QKKTTQSTTS
360 370 380 390 400
TQSKSKVTLS PTASSAIKTS ITQTTKTLTS STKTKSSLGT TTTESTLNSV
410 420 430 440 450
AITSMKTTLS SQITSAALVT PQTTTTSIVS SAPIQTAITS TLSPATKSSS
460 470 480 490 500
VVSLQTATTS TLSPTTTSTS SGSTSSGSTS SDSTARTLAK ELNAQYAAGK
510 520 530 540 550
LNGKSTCTEG EIACSADGKF AVCDHSAWVY MECASGTTCY AYDSGDSVYT
560
QCNFSYLESN YF
Length:562
Mass (Da):59,015
Last modified:October 1, 1996 - v2
Checksum:i0ABCEFBF448E1E19
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti168A → R in AAA34539 (PubMed:1918080).Curated1
Sequence conflicti168A → R in AAA34538 (PubMed:1918080).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti16L → P in strain: DBY939. 1
Natural varianti23R → S in strain: DBY939 and SEY6210. 1
Natural varianti321T → S in strain: DBY939. 1
Natural varianti336 – 340Missing in strain: DBY939. 5
Natural varianti399S → A in strain: DBY939. 1
Natural varianti433 – 434PI → SL in strain: DBY939. 2
Natural varianti461T → K in strain: DBY939. 1
Natural varianti477 – 481Missing in strain: DBY939. 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74070 Genomic DNA. Translation: AAA34539.1.
M74069 Genomic DNA. Translation: AAA34538.1.
U17243 Genomic DNA. Translation: AAB67331.1.
AY693040 Genomic DNA. Translation: AAT93059.1.
BK006945 Genomic DNA. Translation: DAA09597.1.
PIRiA41035.
B41035.
S50371.
RefSeqiNP_013388.1. NM_001182173.1.

Genome annotation databases

EnsemblFungiiYLR286C; YLR286C; YLR286C.
GeneIDi850992.
KEGGisce:YLR286C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74070 Genomic DNA. Translation: AAA34539.1.
M74069 Genomic DNA. Translation: AAA34538.1.
U17243 Genomic DNA. Translation: AAB67331.1.
AY693040 Genomic DNA. Translation: AAT93059.1.
BK006945 Genomic DNA. Translation: DAA09597.1.
PIRiA41035.
B41035.
S50371.
RefSeqiNP_013388.1. NM_001182173.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]
ProteinModelPortaliP29029.
SMRiP29029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31551. 17 interactors.
MINTiMINT-4495746.

Chemistry databases

BindingDBiP29029.
ChEMBLiCHEMBL1293195.

Protein family/group databases

CAZyiCBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Proteomic databases

MaxQBiP29029.
PRIDEiP29029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR286C; YLR286C; YLR286C.
GeneIDi850992.
KEGGisce:YLR286C.

Organism-specific databases

EuPathDBiFungiDB:YLR286C.
SGDiS000004276. CTS1.

Phylogenomic databases

HOGENOMiHOG000160027.
InParanoidiP29029.
KOiK01183.
OMAiFNWDTWL.
OrthoDBiEOG092C49QH.

Enzyme and pathway databases

BioCyciYEAST:YLR286C-MONOMER.
BRENDAi3.2.1.14. 984.

Miscellaneous databases

EvolutionaryTraceiP29029.
PROiP29029.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005089. CBM_fam19.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03427. CBM_19. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHIT_YEAST
AccessioniPrimary (citable) accession number: P29029
Secondary accession number(s): D6VYT1, P29028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6350 molecules/cell in log phase SD medium.1 Publication

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
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.