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CAZyme Information: MGYG000000106_00316

You are here: Home > Sequence: MGYG000000106_00316

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 Enterococcus_D gallinarum
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_D; Enterococcus_D gallinarum
CAZyme ID MGYG000000106_00316
CAZy Family GH76
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
347 MGYG000000106_1|CGC8 40150.16 4.5317
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000106 3151412 Isolate Canada North America
Gene Location Start: 341216;  End: 342259  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000106_00316.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH76 20 321 9.3e-75 0.8463687150837989

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4833 COG4833 3.74e-92 6 345 5 350
Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism].
pfam03663 Glyco_hydro_76 8.81e-26 44 276 33 288
Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
COG1331 YyaL 0.006 30 180 399 565
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only].
cd04434 LanC_like 0.006 54 290 60 298
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCT90634.1 3.84e-258 1 347 1 347
QGR82046.1 5.45e-258 1 347 1 347
QOG28286.1 7.74e-258 1 347 1 347
EEV40360.1 2.53e-202 1 347 1 347
ASV95817.1 6.83e-177 1 345 1 339

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3K7X_A 6.99e-115 4 345 3 338
ChainA, Lin0763 protein [Listeria innocua]
6SHD_A 6.41e-50 35 347 78 389
Structureof the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_B Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_C Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6]
6Y8F_A 1.92e-48 35 347 79 390
ChainA, Alpha-1,6-endo-mannanase GH76A mutant [Salegentibacter sp. Hel_I_6]
6SHM_A 1.45e-47 35 347 79 390
Aninactive (D136A and D137A) variant of alpha-1,6-mannanase, GH76A of Salegentibacter sp. HEL1_6 in complex with alpha-1,6-mannotetrose [Salegentibacter sp. Hel_I_6]
4BOK_A 4.13e-28 35 287 28 283
ChainA, Alpha-1,6-mannanase [Niallia circulans]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000106_00316.