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CAZyme Information: MGYG000001304_00963

You are here: Home > Sequence: MGYG000001304_00963

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 Erysipelatoclostridium spiroforme
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme
CAZyme ID MGYG000001304_00963
CAZy Family GH123
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1963 220688.9 4.4815
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001304 2507485 Isolate not provided North America
Gene Location Start: 56237;  End: 62128  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001304_00963.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH123 405 970 4e-165 0.9907063197026023
GH33 1375 1608 2.9e-16 0.6695906432748538

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13320 DUF4091 2.11e-20 854 918 2 63
Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important.
cd15482 Sialidase_non-viral 3.85e-15 1381 1688 17 332
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam02368 Big_2 8.51e-13 989 1067 2 77
Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.
pfam13385 Laminin_G_3 2.54e-12 1133 1260 17 150
Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
pfam13088 BNR_2 1.08e-10 1360 1615 35 264
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBA55846.1 0.0 171 1864 17 1714
QTQ18982.1 0.0 171 1864 38 1735
VEG17315.1 0.0 171 1863 38 1734
BAQ98792.1 0.0 171 1863 17 1713
ALE12069.1 0.0 171 1863 10 1706

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FQE_A 1.68e-96 405 973 29 606
Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5FQG_A 1.94e-95 405 973 29 606
Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5L7V_A 2.02e-74 414 923 34 519
ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]
5L7R_A 2.91e-74 414 923 49 534
ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]

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
0.000540 0.998684 0.000222 0.000190 0.000165 0.000156

TMHMM  Annotations      download full data without filtering help

start end
1934 1953