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CAZyme Information: EPrPAT00000014981-p1

You are here: Home > Sequence: EPrPAT00000014981-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 Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000014981-p1
CAZy Family AA17
CAZyme Description Di-N-acetylchitobiase.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
414 PaphDAOMBR444_SC0043|CGC1 46795.29 5.3207
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
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 86 393 2.9e-34 0.8445945945945946

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119354 GH18_chitobiase 6.55e-113 48 410 17 358
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 2.06e-29 128 393 88 333
Glyco_18 domain.
395573 Glyco_hydro_18 3.48e-22 106 392 58 305
Glycosyl hydrolases family 18.
119353 GH18_CFLE_spore_hydrolase 2.15e-20 107 389 54 300
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.
226376 YaaH 4.21e-18 126 389 186 405
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
1.75e-142 5 414 422 837
4.38e-129 42 414 27 385
9.38e-129 47 414 3 356
4.00e-111 36 397 10 365
5.67e-84 49 411 24 363

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.12e-09 129 390 117 404
Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution [Serratia marcescens],1GOI_B Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution [Serratia marcescens]
1.03e-08 128 393 98 349
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
1.28e-08 129 390 115 402
Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-s2 [Serratia marcescens],6JKF_B Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-s2 [Serratia marcescens]
1.28e-08 129 390 117 404
Chitinase B from Serratia Marcescens [Serratia marcescens],1E15_B Chitinase B from Serratia Marcescens [Serratia marcescens],1E6R_A Chitinase B from Serratia marcescens wildtype in complex with inhibitor allosamidin [Serratia marcescens],1E6R_B Chitinase B from Serratia marcescens wildtype in complex with inhibitor allosamidin [Serratia marcescens],1GPF_A CHITINASE B FROM SERRATIA MARCESCENS IN COMPLEX WITH INHIBITOR PSAMMAPLIN [Serratia marcescens],1GPF_B CHITINASE B FROM SERRATIA MARCESCENS IN COMPLEX WITH INHIBITOR PSAMMAPLIN [Serratia marcescens],1O6I_A Chitinase B from Serratia marcescens complexed with the catalytic intermediate mimic cyclic dipeptide CI4. [Serratia marcescens],1O6I_B Chitinase B from Serratia marcescens complexed with the catalytic intermediate mimic cyclic dipeptide CI4. [Serratia marcescens],1UR8_A Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone [Serratia marcescens],1UR8_B Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone [Serratia marcescens],1W1P_A Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(Gly-L-Pro) at 2.1 A resolution [Serratia marcescens],1W1P_B Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(Gly-L-Pro) at 2.1 A resolution [Serratia marcescens],1W1T_A Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(His-L-Pro) at 1.9 A resolution [Serratia marcescens],1W1T_B Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(His-L-Pro) at 1.9 A resolution [Serratia marcescens],1W1V_A Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Arg-L-Pro) at 1.85 A resolution [Serratia marcescens],1W1V_B Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Arg-L-Pro) at 1.85 A resolution [Serratia marcescens],1W1Y_A Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Tyr-L-Pro) at 1.85 A resolution [Serratia marcescens],1W1Y_B Crystal structure of S. marcescens chitinase B in complex with the cyclic dipeptide inhibitor cyclo-(L-Tyr-L-Pro) at 1.85 A resolution [Serratia marcescens]
1.28e-08 129 390 115 402
Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-14 [Serratia marcescens],6JK9_B Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-14 [Serratia marcescens],7C34_A Crystal structure of Serratia marcescens Chitinase B complexed with Berberine [Serratia marcescens],7C34_B Crystal structure of Serratia marcescens Chitinase B complexed with Berberine [Serratia marcescens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.01e-84 49 411 24 363
Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2
4.95e-81 49 411 40 379
Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1
1.15e-80 49 410 25 363
Di-N-acetylchitobiase OS=Rattus norvegicus OX=10116 GN=Ctbs PE=1 SV=1
1.70e-55 50 414 26 374
Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1
2.01e-53 48 414 21 370
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 SP

Other SP_Sec_SPI CS Position
0.000237 0.999742 CS pos: 26-27. Pr: 0.8741

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000014981-p1.