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CAZyme Information: QRC97218.1

You are here: Home > Sequence: QRC97218.1

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 QRC97218.1
CAZy Family GH10
CAZyme Description Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2F403]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
315 CP069029|CGC5 32926.91 7.2106
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 QRC97218.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 71 250 3.2e-103 0.989010989010989

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 8.62e-61 66 250 1 189
Amb_all domain.
226384 PelB 6.16e-58 48 313 58 344
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 7.92e-40 81 247 34 211
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
1.50e-226 1 315 1 315
3.08e-176 1 315 1 317
3.32e-128 25 313 151 439
1.59e-123 26 315 117 407
3.73e-123 25 313 38 326

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.22e-40 80 313 78 325
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]
7.39e-36 77 248 76 277
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
9.69e-29 76 311 127 413
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
2.05e-28 76 311 122 396
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]
2.67e-28 76 311 143 417
Bacillus Subtilis 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
1.75e-65 37 309 45 319
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
8.00e-64 37 309 46 323
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
1.59e-63 37 309 46 323
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
1.59e-63 37 309 46 323
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
6.40e-61 21 309 35 326
Pectate lyase B OS=Colletotrichum gloeosporioides OX=474922 GN=PLB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000313 0.999658 CS pos: 24-25. Pr: 0.9614

TMHMM  Annotations      help

There is no transmembrane helices in QRC97218.1.