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CAZyme Information: ASPACDRAFT_35786-t33_1-p1

You are here: Home > Sequence: ASPACDRAFT_35786-t33_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 aculeatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus aculeatus
CAZyme ID ASPACDRAFT_35786-t33_1-p1
CAZy Family GH28
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
373 KV878988|CGC4 38931.40 3.9444
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AaculeatusATCC16872 11165 690307 322 10843
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.10:25

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 113 297 1.7e-90 0.9893048128342246

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 1.21e-57 111 299 2 190
Amb_all domain.
226384 PelB 1.53e-16 123 297 97 275
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 7.42e-15 123 295 30 211
Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.77e-234 1 373 1 373
6.77e-234 1 373 1 373
3.41e-227 1 373 1 373
3.41e-227 1 373 1 373
2.34e-211 1 373 1 373

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.08e-174 20 373 1 359
Pectin Lyase A [Aspergillus niger]
1.25e-173 20 373 1 359
Pectin Lyase A [Aspergillus niger],1IDJ_B Pectin Lyase A [Aspergillus niger]
4.08e-153 21 354 2 338
Pectin Lyase B [Aspergillus niger]
3.41e-11 128 298 80 249
Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
4.96e-09 123 302 128 340
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.47e-235 1 373 1 373
Probable pectin lyase D OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pelD PE=3 SV=1
1.20e-234 1 373 1 373
Pectin lyase D OS=Aspergillus niger OX=5061 GN=pelD PE=1 SV=1
2.88e-201 1 373 1 375
Pectin lyase 2 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=pel2 PE=1 SV=1
2.88e-201 1 373 1 375
Probable pectin lyase D OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=pelD PE=3 SV=1
4.30e-196 1 373 1 375
Probable pectin lyase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=pelB PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000287 0.999705 CS pos: 19-20. Pr: 0.8933

TMHMM  Annotations      help

There is no transmembrane helices in ASPACDRAFT_35786-t33_1-p1.