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CAZyme Information: EFQ25829.1

You are here: Home > Sequence: EFQ25829.1

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 Colletotrichum graminicola
Lineage Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola
CAZyme ID EFQ25829.1
CAZy Family AA3
CAZyme Description Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:E3Q562]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
325 33722.83 9.2428
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CgraminicolaM1-001 12400 645133 380 12020
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 77 258 4.5e-87 0.994475138121547

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214765 Amb_all 2.72e-70 77 261 1 189
Amb_all domain.
226384 PelB 1.46e-59 54 322 55 340
Pectate lyase [Carbohydrate transport and metabolism].
366158 Pec_lyase_C 1.08e-41 73 258 1 211
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
9.40e-210 1 325 1 325
9.40e-210 1 325 1 325
1.85e-200 1 325 1 325
7.21e-170 1 325 1 324
9.26e-166 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
4.60e-39 39 260 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]
6.94e-35 35 318 6 330
Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
1.47e-31 46 247 20 225
Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
1.22e-26 95 322 92 339
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]
3.23e-26 95 322 92 339
Chain A, Pectate lyase C [Dickeya chrysanthemi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.16e-160 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
9.79e-159 1 325 1 325
Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
2.37e-157 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
2.37e-157 1 325 1 326
Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
1.89e-104 35 325 44 329
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
0.000359 0.999602 CS pos: 23-24. Pr: 0.9600

TMHMM  Annotations      help

There is no transmembrane helices in EFQ25829.1.