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CAZyme Information: MGYG000002531_02116

You are here: Home > Sequence: MGYG000002531_02116

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 Pseudobutyrivibrio fibrisolvens_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Pseudobutyrivibrio; Pseudobutyrivibrio fibrisolvens_A
CAZyme ID MGYG000002531_02116
CAZy Family CBM2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
587 MGYG000002531_1|CGC22 65636.9 4.6283
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002531 3116879 Isolate not provided not provided
Gene Location Start: 2003210;  End: 2004973  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4 3.2.1.91 3.2.1.73

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 184 536 2.9e-119 0.9967741935483871
CBM2 43 121 1.2e-19 0.7821782178217822

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00150 Cellulase 1.07e-38 183 531 1 272
Cellulase (glycosyl hydrolase family 5).
COG2730 BglC 9.44e-37 177 568 32 402
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
smart00637 CBD_II 2.67e-17 46 120 2 77
CBD_II domain.
pfam00553 CBM_2 2.15e-13 43 119 5 83
Cellulose binding domain. Two tryptophan residues are involved in cellulose binding. Cellulose binding domain found in bacteria.
COG5297 CelA1 7.60e-07 34 115 459 539
Cellulase/cellobiase CelA1 [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK74877.1 0.0 1 587 1 587
QFJ53706.1 0.0 30 587 6 587
ADL34236.1 0.0 3 587 4 616
AEV70372.1 2.43e-181 172 587 37 469
CBL16847.1 6.90e-181 172 586 44 475

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ECE_A 2.43e-66 170 549 1 343
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 1.37e-64 170 549 1 343
ChainA, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]
3VVG_A 2.73e-60 181 557 19 376
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]
3W6M_A 2.73e-60 181 557 19 376
Contributionof 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]
3AXX_A 2.84e-60 181 563 52 415
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q05332 1.86e-174 172 586 42 472
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 1.83e-155 172 587 627 1028
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
P50400 3.08e-154 166 584 37 439
Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1
P04956 7.46e-128 172 583 39 468
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
P23548 5.96e-75 166 553 30 378
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
0.000290 0.999027 0.000175 0.000187 0.000155 0.000141

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002531_02116.