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CAZyme Information: ASPNIDRAFT2_1149968-t41_1-p1

You are here: Home > Sequence: ASPNIDRAFT2_1149968-t41_1-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 Aspergillus niger
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
CAZyme ID ASPNIDRAFT2_1149968-t41_1-p1
CAZy Family GH27
CAZyme Description Glycoside Hydrolase Family 28 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
368 ACJE01000004.1|CGC14 38108.49 4.0429
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnigerATCC1015 11910 380704 6 11904
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.15:80

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH28 48 367 3.1e-75 0.9538461538461539

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395231 Glyco_hydro_28 4.93e-150 52 368 3 321
Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes are important in cell wall metabolism.
215540 PLN03010 6.43e-27 88 367 122 394
polygalacturonase
177865 PLN02218 1.73e-26 87 362 143 420
polygalacturonase ADPG
215426 PLN02793 8.40e-24 104 359 145 406
Probable polygalacturonase
215120 PLN02188 1.83e-23 76 362 97 390
polygalacturonase/glycoside hydrolase family protein

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.54e-263 1 368 1 368
2.54e-263 1 368 1 368
5.48e-258 1 368 1 368
5.48e-258 1 368 1 368
1.00e-246 1 367 1 367

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.32e-243 33 368 1 336
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_B Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_C Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_D Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_E Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger],1NHC_F Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger [Aspergillus niger]
3.07e-162 30 368 6 344
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.77e-161 30 368 6 344
Chain A, endo-polygalacturonase [Evansstolkia leycettana]
3.10e-160 35 368 3 336
Chain A, Endo-polygalacturonase [Evansstolkia leycettana]
1.73e-148 35 366 3 335
Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_B Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_C Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_D Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_E Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_F Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini],2IQ7_G Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins [Colletotrichum lupini]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.51e-264 1 368 1 368
Endopolygalacturonase I OS=Aspergillus niger OX=5061 GN=pgaI PE=1 SV=1
4.51e-264 1 368 1 368
Probable endopolygalacturonase I OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pgaI PE=3 SV=1
4.00e-219 1 368 1 368
Probable endopolygalacturonase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=pgaA PE=3 SV=1
1.09e-216 1 368 1 368
Probable endopolygalacturonase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pgaA PE=3 SV=1
1.09e-216 1 368 1 368
Probable endopolygalacturonase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=pgaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000264 0.999698 CS pos: 18-19. Pr: 0.9802

TMHMM  Annotations      help

There is no transmembrane helices in ASPNIDRAFT2_1149968-t41_1-p1.