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CAZyme Information: EJT69795.1

You are here: Home > Sequence: EJT69795.1

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 Gaeumannomyces tritici
Lineage Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
CAZyme ID EJT69795.1
CAZy Family AA4
CAZyme Description Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:J3PGP9]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
339 GL385403|CGC3 36496.83 6.5513
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1 14749 644352 291 14458
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EJT69795.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 84 257 7.9e-102 0.9943181818181818

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 1.03e-58 74 256 1 186
Amb_all domain.
226384 PelB 1.52e-58 35 339 35 344
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 6.49e-36 85 256 28 211
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
6.05e-180 31 339 27 335
2.02e-179 3 339 8 350
7.88e-178 8 339 3 335
2.15e-177 31 339 12 323
2.23e-175 1 339 1 336

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.70e-32 92 339 80 325
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]
5.62e-24 89 234 130 302
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3.81e-22 91 234 127 296
Structural insights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
4.56e-22 91 234 148 317
Bacillus Subtilis Pectate Lyase [Bacillus subtilis]
1.15e-21 91 234 148 317
Chain A, PROTEIN (PECTATE LYASE) [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.99e-50 36 282 39 294
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
2.99e-50 36 282 39 294
Probable pectate lyase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyB PE=3 SV=1
6.25e-49 36 282 38 293
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
6.60e-47 57 335 57 316
Probable pectate lyase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyA PE=3 SV=1
6.60e-47 57 335 57 316
Probable pectate lyase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000188 0.999826 CS pos: 21-22. Pr: 0.9696

TMHMM  Annotations      help

There is no transmembrane helices in EJT69795.1.