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CAZyme Information: RL4_JR_05682-RA-p1

You are here: Home > Sequence: RL4_JR_05682-RA-p1

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 Raffaelea lauricola
Lineage Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
CAZyme ID RL4_JR_05682-RA-p1
CAZy Family GH3
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
558 61522.33 6.5623
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_RlauricolaRL4 10461 N/A 146 10315
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in RL4_JR_05682-RA-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 211 524 1.6e-153 0.9904761904761905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395098 Cellulase 1.58e-26 247 520 29 270
Cellulase (glycosyl hydrolase family 5).
225344 BglC 6.29e-16 224 527 50 368
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.45e-222 121 555 29 477
7.75e-221 125 555 83 512
5.21e-220 157 555 13 410
1.46e-218 148 555 3 412
7.90e-217 163 555 21 415

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.42e-44 206 540 8 338
Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
6.56e-44 206 540 8 338
Chain A, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
6.38e-26 221 554 30 376
The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
1.58e-25 221 554 30 376
Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
1.68e-25 221 554 63 409
Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.92e-49 206 540 41 369
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
7.42e-42 206 540 49 379
Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
1.83e-34 200 552 27 396
Glycosyl hydrolase 5 family protein OS=Chamaecyparis obtusa OX=13415 PE=1 SV=1
9.41e-23 204 540 46 400
Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
1.21e-22 209 538 32 354
Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000063 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
145 164