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CAZyme Information: MGYG000003587_00493

You are here: Home > Sequence: MGYG000003587_00493

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 Ruminococcus_D sp900770285
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp900770285
CAZyme ID MGYG000003587_00493
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
496 MGYG000003587_10|CGC1 55317.31 4.368
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003587 1561142 MAG Fiji Oceania
Gene Location Start: 75268;  End: 76758  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 58 418 1.2e-116 0.9967741935483871

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 1.36e-47 57 413 1 272
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 1.66e-34 51 420 32 370
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
ADU21575.1 1.09e-261 38 492 36 485
CBL16847.1 1.03e-216 1 478 1 475
AEV70372.1 1.31e-207 16 478 7 468
CAA49187.1 2.29e-206 35 478 31 472
ABN54070.1 2.29e-206 35 478 31 472

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ECE_A 6.90e-59 48 419 5 331
AcidothermusCellulolyticus 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]
1VRX_A 2.01e-57 48 419 5 331
ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
2ZUM_A 5.01e-48 64 453 61 415
FunctionalAnalysis 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]
3AXX_A 5.01e-48 64 453 61 415
Functionalanalysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_B Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_C Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3VVG_A 1.22e-47 64 447 28 376
TheCrystal 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q05332 4.58e-207 35 478 31 472
Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1
P10474 1.31e-142 38 479 619 1028
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
P04956 6.86e-121 45 479 38 474
Endoglucanase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celB PE=3 SV=1
P50400 1.46e-115 19 476 16 443
Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P23548 1.23e-70 48 419 38 362
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000267 0.999057 0.000180 0.000181 0.000159 0.000141

TMHMM  Annotations      download full data without filtering help

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