logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: PHYCI_231974T0-p1

You are here: Home > Sequence: PHYCI_231974T0-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phytophthora cinnamomi
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
CAZyme ID PHYCI_231974T0-p1
CAZy Family GH16
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
221 24970.19 4.3953
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22 26201 1048749 70 26131
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-:18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 2 198 3.9e-29 0.5202702702702703

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119354 GH18_chitobiase 2.05e-79 2 215 153 358
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.
214753 Glyco_18 3.38e-28 1 198 149 333
Glyco_18 domain.
119353 GH18_CFLE_spore_hydrolase 3.82e-23 10 194 145 300
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
395573 Glyco_hydro_18 1.53e-19 1 197 141 305
Glycosyl hydrolases family 18.
226376 YaaH 4.62e-16 17 194 262 405
Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.10e-114 2 219 629 837
1.08e-75 2 214 148 351
2.49e-75 2 214 177 380
4.49e-60 2 215 160 363
4.49e-60 2 215 160 363

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.67e-11 6 194 159 306
Chain A, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168],3CZ8_B Chain B, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168]
2.63e-08 2 194 246 410
Chain A, Spore germination protein YaaH [Priestia megaterium QM B1551]
4.79e-07 3 205 161 352
The crystal structures of YKL-39 in the absence of chitooligosaccharides was solved to resolutions of 2.4 angstrom [Homo sapiens],4P8V_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc2) were solved to resolutions of 1.5 angstrom [Homo sapiens],4P8W_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc4) were solved to resolutions of 1.9 angstrom [Homo sapiens],4P8X_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc6) were solved to resolutions of 2.48 angstrom [Homo sapiens]
8.36e-07 19 197 175 331
Crystal structure of a plant class V chitinase mutant from Cycas revoluta in complex with (GlcNAc)3 [Cycas revoluta]
8.36e-07 19 197 175 331
Crystal Structure of GH18 Chitinase from Cycad, Cycas revoluta [Cycas revoluta],4MNK_A Crystal Structure of GH18 Chitinase from Cycas revoluta in complex with (GlcNAc)3 [Cycas revoluta],4R5E_A Chain A, Chitinase A [Cycas revoluta]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.97e-61 2 215 160 363
Di-N-acetylchitobiase OS=Rattus norvegicus OX=10116 GN=Ctbs PE=1 SV=1
1.37e-58 2 215 159 362
Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2
6.22e-58 2 215 175 378
Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1
2.44e-46 2 219 160 374
Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1
2.68e-36 2 219 158 370
Probable di-N-acetylchitobiase 1 OS=Dictyostelium discoideum OX=44689 GN=ctbs1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000003

TMHMM  Annotations      help

There is no transmembrane helices in PHYCI_231974T0-p1.