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CAZyme Information: FFUJ_00071-t31_1-p1

You are here: Home > Sequence: FFUJ_00071-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_00071-t31_1-p1
CAZy Family AA1
CAZyme Description probable pectin lyase precursor
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
377 39921.27 9.5841
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

EC 4.2.2.10:25

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 111 296 2.7e-88 0.9946524064171123

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 4.71e-57 109 298 1 190
Amb_all domain.
226384 PelB 2.05e-18 66 301 28 280
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 5.60e-18 115 294 23 211
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
5.90e-278 1 377 1 377
5.90e-278 1 377 1 377
5.90e-278 1 377 1 377
5.90e-278 1 377 1 377
5.43e-274 1 377 1 377

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.59e-141 25 359 7 341
Pectin Lyase B [Aspergillus niger]
1.08e-139 24 359 6 340
Pectin Lyase A [Aspergillus niger]
8.76e-139 24 359 6 340
Pectin Lyase A [Aspergillus niger],1IDJ_B Pectin Lyase A [Aspergillus niger]
7.02e-14 26 297 5 249
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]
2.89e-11 26 294 12 330
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
2.97e-146 1 370 1 372
Probable pectin lyase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pelA PE=3 SV=1
3.31e-145 16 359 17 360
Pectin lyase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=pelB PE=2 SV=1
5.23e-144 25 359 25 359
Probable pectin lyase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=pelB PE=3 SV=1
5.23e-144 25 359 25 359
Probable pectin lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=pelA PE=3 SV=1
1.72e-142 25 359 26 359
Probable pectin lyase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pelA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000221 0.999742 CS pos: 19-20. Pr: 0.9762

TMHMM  Annotations      help

There is no transmembrane helices in FFUJ_00071-t31_1-p1.