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CAZyme Information: MGYG000000959_00494

You are here: Home > Sequence: MGYG000000959_00494

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 sp900752785
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900752785
CAZyme ID MGYG000000959_00494
CAZy Family CE1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
456 49793.8 4.3524
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000959 2365658 MAG Denmark Europe
Gene Location Start: 315;  End: 1685  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000959_00494.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE1 220 452 3.1e-31 0.9647577092511013

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG2382 Fes 3.49e-28 212 456 70 298
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism].
COG2819 YbbA 1.35e-13 231 364 29 171
Predicted hydrolase of the alpha/beta superfamily [General function prediction only].
cd14256 Dockerin_I 8.38e-13 94 149 1 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam00756 Esterase 5.55e-11 218 446 1 239
Putative esterase. This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
cd14254 Dockerin_II 3.97e-10 95 149 1 54
Type II dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAB93667.1 2.79e-103 3 455 324 792
AAR39816.1 1.74e-94 1 424 331 780
CAA90271.1 1.74e-94 1 424 331 780
CBL17231.1 5.95e-92 8 456 642 1074
CBL17903.1 6.01e-88 9 455 522 954

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5CXU_A 1.46e-66 212 456 27 272
Structureof the CE1 ferulic acid esterase AmCE1/Fae1A, from the anaerobic fungi Anaeromyces mucronatus in the absence of substrate [Anaeromyces mucronatus],5CXX_A Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_B Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus],5CXX_C Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid [Anaeromyces mucronatus]
1JJF_A 3.31e-40 214 456 35 260
ChainA, Endo-1,4-beta-xylanase Z [Acetivibrio thermocellus]
1JT2_A 8.97e-40 214 456 35 260
ChainA, PROTEIN (ENDO-1,4-BETA-XYLANASE Z) [Acetivibrio thermocellus]
7B5V_A 1.20e-11 213 455 141 386
ChainA, Carbohydrate Esterase family 1 protein with an N-terminal carbohydrate binding module family 48 [Dysgonomonas mossii DSM 22836],7B5V_B Chain B, Carbohydrate Esterase family 1 protein with an N-terminal carbohydrate binding module family 48 [Dysgonomonas mossii DSM 22836],7B6B_A Chain A, Carbohydrate Esterase family 1 protein with an N-terminal carbohydrate binding module family 48 [Dysgonomonas mossii DSM 22836],7B6B_B Chain B, Carbohydrate Esterase family 1 protein with an N-terminal carbohydrate binding module family 48 [Dysgonomonas mossii DSM 22836]
6RZN_A 6.69e-11 213 362 134 296
Crystalstructure of the N-terminal carbohydrate binding module family 48 and ferulic acid esterase from the multi-enzyme CE1-GH62-GH10 [uncultured bacterium],6RZN_B Crystal structure of the N-terminal carbohydrate binding module family 48 and ferulic acid esterase from the multi-enzyme CE1-GH62-GH10 [uncultured bacterium]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10478 1.76e-36 214 456 54 279
Endo-1,4-beta-xylanase Z OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xynZ PE=1 SV=3
P51584 2.57e-22 8 357 642 973
Endo-1,4-beta-xylanase Y OS=Acetivibrio thermocellus OX=1515 GN=xynY PE=1 SV=1
Q53317 2.71e-14 3 117 327 461
Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2
D5EXZ4 3.54e-10 214 364 434 589
Carbohydrate acetyl esterase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe1-6A PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000029 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000959_00494.