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CAZyme Information: MGYG000000605_01695

You are here: Home > Sequence: MGYG000000605_01695

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C;
CAZyme ID MGYG000000605_01695
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
773 85620.15 3.995
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000605 2224694 MAG Madagascar Africa
Gene Location Start: 130;  End: 2451  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000605_01695.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 91 373 2.3e-80 0.9930795847750865
CBM23 503 666 3.3e-47 0.9938271604938271

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3934 COG3934 1.54e-21 89 388 24 289
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism].
pfam03425 CBM_11 8.09e-16 504 666 7 173
Carbohydrate binding domain (family 11).
cd14256 Dockerin_I 2.76e-12 707 763 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.
pfam00150 Cellulase 9.33e-10 87 375 23 270
Cellulase (glycosyl hydrolase family 5).
pfam03442 CBM_X2 2.42e-07 404 489 2 83
Carbohydrate binding domain X2. This domain binds to cellulose and to bacterial cell walls. It is found in glycosyl hydrolases and in scaffolding proteins of cellulosomes (multiprotein glycosyl hydrolase complexes). In the cellulosome it may aid cellulose degradation by anchoring the cellulosome to the bacterial cell wall and by binding it to its substrate. This domain has an Ig-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL52789.1 5.30e-201 27 727 604 1361
BAV13033.1 5.30e-201 27 727 604 1361
ADZ85047.1 3.21e-185 41 495 636 1097
QEH70547.1 1.01e-182 41 495 636 1097
AEY66038.1 6.87e-144 37 406 30 395

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1RH9_A 6.46e-51 43 381 6 344
ChainA, endo-beta-mannanase [Solanum lycopersicum]
4QP0_A 1.06e-42 43 372 4 325
CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
3PZ9_A 4.81e-40 48 371 18 340
Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
6TN6_A 4.17e-38 48 371 1 326
X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
3WH9_A 3.81e-32 43 389 2 324
Theligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger],3WH9_B The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9FZ29 3.23e-54 39 377 25 367
Mannan endo-1,4-beta-mannosidase 1 OS=Arabidopsis thaliana OX=3702 GN=MAN1 PE=2 SV=1
Q6Z310 4.03e-54 25 372 20 367
Putative mannan endo-1,4-beta-mannosidase 9 OS=Oryza sativa subsp. japonica OX=39947 GN=MAN9 PE=2 SV=2
Q9SG94 9.09e-54 23 381 11 375
Mannan endo-1,4-beta-mannosidase 3 OS=Arabidopsis thaliana OX=3702 GN=MAN3 PE=2 SV=1
Q7Y223 9.74e-53 43 373 42 379
Mannan endo-1,4-beta-mannosidase 2 OS=Arabidopsis thaliana OX=3702 GN=MAN2 PE=2 SV=1
Q9M0H6 1.76e-52 42 372 40 377
Mannan endo-1,4-beta-mannosidase 5 OS=Arabidopsis thaliana OX=3702 GN=MAN5 PE=2 SV=1

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
0.000351 0.996725 0.002304 0.000220 0.000201 0.000164

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000605_01695.