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CAZyme Information: KLU88292.1

You are here: Home > Sequence: KLU88292.1

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 Magnaporthiopsis poae
Lineage Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
CAZyme ID KLU88292.1
CAZy Family GH31|GH31
CAZyme Description pectate lyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
325 GL876971|CGC3 33862.63 7.8699
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MpoaeATCC64411 12363 644358 200 12163
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.2:31

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 85 258 7.9e-85 0.9502762430939227

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 1.64e-66 85 262 9 190
Amb_all domain.
226384 PelB 7.45e-51 57 322 57 340
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 3.49e-41 86 258 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
2.98e-148 1 325 1 325
1.30e-146 1 325 1 323
1.99e-146 1 325 1 325
1.99e-146 1 325 1 325
2.82e-141 1 325 1 324

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.75e-36 40 260 6 248
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]
9.97e-32 34 266 4 284
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
9.15e-28 95 258 92 257
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]
2.42e-27 95 258 92 257
Chain A, Pectate lyase C [Dickeya chrysanthemi]
5.06e-26 47 244 20 222
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.43e-135 1 325 1 326
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
2.10e-129 9 325 8 325
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
3.09e-129 1 325 1 326
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
3.09e-129 1 325 1 326
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
1.33e-83 30 325 38 329
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
0.000330 0.999620 CS pos: 31-32. Pr: 0.2703

TMHMM  Annotations      help

There is no transmembrane helices in KLU88292.1.