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CAZyme Information: MGYG000002403_05073

You are here: Home > Sequence: MGYG000002403_05073

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 Robinsoniella peoriensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
CAZyme ID MGYG000002403_05073
CAZy Family GH136
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1512 MGYG000002403_132|CGC6 164964.91 4.3875
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002403 7202103 Isolate not provided not provided
Gene Location Start: 251779;  End: 256317  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002403_05073.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH136 65 639 8.8e-153 0.9959266802443992
CBM32 1084 1198 9.5e-24 0.9274193548387096
CBM57 924 1065 9.5e-19 0.9863945578231292

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00754 F5_F8_type_C 1.98e-17 1083 1195 1 123
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam11721 Malectin 1.19e-14 922 1054 1 142
Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan.
cd00057 FA58C 1.90e-11 1076 1202 6 143
Substituted updates: Jan 31, 2002
pfam11721 Malectin 1.14e-09 776 900 4 146
Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan.
PLN03150 PLN03150 6.39e-05 837 1067 92 359
hypothetical protein; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIY85170.1 0.0 1 1512 1 1469
AQM59543.1 0.0 1 1512 1 1469
ASU31098.1 0.0 5 1512 5 1517
ANU78288.1 0.0 5 1512 5 1517
QQQ91631.1 0.0 5 1512 5 1517

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7V6M_A 1.18e-56 63 641 6 578
ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
7V6I_A 2.82e-43 65 641 13 610
ChainA, Lacto-N-biosidase [Bifidobacterium saguini DSM 23967]
5GQC_A 1.81e-42 65 641 17 598
Crystalstructure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_C Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_D Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_E Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_F Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_G Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_H Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQF_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQF_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum]
6KQT_A 3.74e-33 65 483 244 638
CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]
6KQS_A 1.55e-32 65 483 244 638
CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - selenomethionine derivative [Eubacterium ramulus ATCC 29099]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000401 0.998674 0.000230 0.000270 0.000207 0.000180

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002403_05073.