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CAZyme Information: EEU42650.1

You are here: Home > Sequence: EEU42650.1

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 Fusarium vanettenii
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
CAZyme ID EEU42650.1
CAZy Family GH47
CAZyme Description Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7YZQ8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
404 GG698904|CGC4 41897.31 4.4805
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Fvanettenii77134 15708 660122 0 15708
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EEU42650.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 160 340 7.8e-98 0.989010989010989

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 5.41e-58 160 340 6 189
Amb_all domain.
226384 PelB 1.94e-57 144 403 69 344
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 7.48e-42 191 337 57 211
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
1.71e-249 1 404 1 440
2.02e-188 1 403 1 403
3.84e-186 1 403 1 403
3.84e-186 1 403 1 403
3.84e-186 1 403 1 403

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.68e-47 173 403 82 325
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]
1.35e-32 126 314 17 246
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
1.41e-32 125 326 19 225
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
1.35e-31 165 401 127 413
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
2.21e-28 165 320 122 301
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.96e-63 126 356 46 277
Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1
4.45e-62 126 356 45 276
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
3.56e-61 126 356 46 277
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
3.56e-61 126 356 46 277
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
6.17e-59 118 399 40 322
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001882 0.998112 CS pos: 15-16. Pr: 0.9527

TMHMM  Annotations      help

There is no transmembrane helices in EEU42650.1.