logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001024_01265

You are here: Home > Sequence: MGYG000001024_01265

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 HGM11521 sp900751885
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11521; HGM11521 sp900751885
CAZyme ID MGYG000001024_01265
CAZy Family CE6
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1071 MGYG000001024_49|CGC1 114537.77 4.3535
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001024 2614111 MAG Sweden Europe
Gene Location Start: 43436;  End: 46651  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001024_01265.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE6 107 205 1.1e-23 0.98989898989899

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03629 SASA 1.80e-59 33 281 2 226
Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.
pfam12733 Cadherin-like 1.51e-06 793 867 9 86
Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT42077.1 4.29e-48 34 285 32 267
BCA48725.1 1.08e-47 34 285 32 267
QMW86523.1 1.48e-47 34 285 32 267
QUT69878.1 1.48e-47 34 285 32 267
AAO79285.1 1.48e-47 34 285 32 267

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2APJ_A 1.45e-14 105 272 91 248
X-RayStructure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_B X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_C X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_D X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L9J9 1.77e-14 35 272 24 248
Probable carbohydrate esterase At4g34215 OS=Arabidopsis thaliana OX=3702 GN=At4g34215 PE=1 SV=2
D5EXZ4 3.73e-10 30 294 41 306
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000437 0.998774 0.000274 0.000171 0.000156 0.000154

TMHMM  Annotations      download full data without filtering help

start end
7 29