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CAZyme Information: FFUJ_09899-t31_1-p1

You are here: Home > Sequence: FFUJ_09899-t31_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 Fusarium fujikuroi
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi
CAZyme ID FFUJ_09899-t31_1-p1
CAZy Family GH3
CAZyme Description probable pectate lyase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
328 HF679031|CGC1 35369.43 4.6199
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FfujikuroiIMI58289 15099 1279085 286 14813
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FFUJ_09899-t31_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 83 263 1e-105 0.989010989010989

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
226384 PelB 1.25e-64 51 327 48 345
Pectate lyase [Carbohydrate transport and metabolism].
214765 Amb_all 1.71e-62 89 264 12 190
Amb_all domain.
366158 Pec_lyase_C 1.20e-43 69 260 11 211
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
8.21e-242 1 328 1 328
8.21e-242 1 328 1 328
8.21e-242 1 328 1 328
8.21e-242 1 328 1 328
3.03e-228 1 327 1 327

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.06e-49 51 327 14 326
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]
1.04e-34 89 237 76 246
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
2.08e-32 91 238 130 302
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
8.13e-32 51 249 21 225
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
1.43e-31 48 324 42 341
Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.74e-62 15 286 17 286
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
4.76e-59 42 306 36 302
Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1
6.71e-59 42 306 36 302
Probable pectate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=plyA PE=3 SV=1
1.11e-57 45 283 37 280
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
1.14e-57 45 283 38 281
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000317 0.999666 CS pos: 23-24. Pr: 0.8254

TMHMM  Annotations      help

There is no transmembrane helices in FFUJ_09899-t31_1-p1.