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CAZyme Information: OAG18124.1

You are here: Home > Sequence: OAG18124.1

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 Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG18124.1
CAZy Family GH109
CAZyme Description pectin lyase-like protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
334 KV441484|CGC3 36173.60 9.0628
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in OAG18124.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 79 252 2.7e-103 0.9886363636363636

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
226384 PelB 1.15e-63 25 334 33 344
Pectate lyase [Carbohydrate transport and metabolism].
214765 Amb_all 1.28e-57 83 251 14 186
Amb_all domain.
366158 Pec_lyase_C 6.83e-37 79 251 28 211
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
1.11e-192 1 334 1 335
4.37e-177 1 334 185 519
1.50e-167 1 334 1 336
1.92e-163 23 334 28 336
8.93e-159 23 334 28 333

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.95e-39 28 334 6 325
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]
1.30e-35 81 228 128 301
Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3.29e-35 27 334 7 331
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
6.21e-30 23 229 5 247
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
1.53e-27 71 228 111 295
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
1.74e-51 20 330 36 322
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
2.38e-51 13 277 27 294
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
2.38e-51 13 277 27 294
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
2.94e-51 55 330 61 316
Probable pectate lyase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyA PE=3 SV=1
2.94e-51 55 330 61 316
Probable pectate lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000232 0.999729 CS pos: 17-18. Pr: 0.9865

TMHMM  Annotations      help

There is no transmembrane helices in OAG18124.1.