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CAZyme Information: MGYG000001448_00451

You are here: Home > Sequence: MGYG000001448_00451

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 Dermabacter hominis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Dermabacteraceae; Dermabacter; Dermabacter hominis
CAZyme ID MGYG000001448_00451
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
745 MGYG000001448_1|CGC6 81427.98 4.9305
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001448 2361290 Isolate not provided not provided
Gene Location Start: 464143;  End: 466380  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001448_00451.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 315 721 5.7e-92 0.9327485380116959

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 3.89e-95 316 731 3 339
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.
pfam13088 BNR_2 1.56e-20 496 716 79 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4409 NanH 1.04e-17 291 719 240 700
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd00110 LamG 8.11e-04 168 275 18 124
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
pfam02210 Laminin_G_2 0.001 29 98 7 76
Laminin G domain. This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATH95834.1 0.0 1 745 1 745
ANP28539.1 0.0 1 745 1 745
QAU52491.1 1.74e-245 19 741 33 764
AZA13443.1 1.31e-244 19 741 31 762
AZA09383.1 3.21e-243 5 741 6 764

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 4.82e-74 316 719 13 430
Crystalstructure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124],5TSP_B Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124]
2BF6_A 2.56e-73 316 719 12 429
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 2.78e-73 316 719 12 429
TheStructure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK6_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_B The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens]
2W20_A 2.44e-64 322 719 21 448
Structureof the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6],2W20_B Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6]
3H72_A 2.82e-64 322 719 25 452
Crystalstructure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H72_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H73_A Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6],3H73_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P29767 6.94e-73 246 745 295 836
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62576 4.56e-60 322 719 341 768
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P62575 4.56e-60 322 719 341 768
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
Q27701 7.35e-39 166 720 137 730
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
Q02834 9.98e-31 307 737 46 403
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1

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
1.000059 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001448_00451.