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CAZyme Information: QRD02177.1

You are here: Home > Sequence: QRD02177.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRD02177.1
CAZy Family GH31
CAZyme Description Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2FBD5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
335 36403.76 8.0972
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in QRD02177.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 79 252 9.8e-98 0.9829545454545454

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
226384 PelB 1.50e-55 26 335 34 344
Pectate lyase [Carbohydrate transport and metabolism].
214765 Amb_all 1.56e-53 83 253 14 187
Amb_all domain.
366158 Pec_lyase_C 4.18e-33 83 252 32 211
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
9.69e-249 1 335 1 335
5.41e-161 22 335 27 336
7.28e-159 22 335 27 336
2.52e-156 22 335 27 333
2.52e-156 22 335 27 333

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.30e-36 62 335 43 325
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]
2.44e-32 83 230 130 302
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1.74e-27 45 335 26 331
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
2.12e-26 36 253 16 277
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
4.83e-25 83 230 125 296
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.88e-49 51 331 63 322
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
9.97e-49 57 331 63 316
Probable pectate lyase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyA PE=3 SV=1
9.97e-49 57 331 63 316
Probable pectate lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyA PE=3 SV=1
3.89e-48 57 331 63 316
Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1
6.22e-47 51 331 59 318
Pectate lyase A OS=Aspergillus niger OX=5061 GN=plyA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000264 0.999703 CS pos: 22-23. Pr: 0.6735

TMHMM  Annotations      help

There is no transmembrane helices in QRD02177.1.