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CAZyme Information: MGYG000003145_00820

You are here: Home > Sequence: MGYG000003145_00820

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 UMGS822 sp900545825
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; UMGS822; UMGS822 sp900545825
CAZyme ID MGYG000003145_00820
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
746 MGYG000003145_6|CGC1 79704.23 4.6797
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003145 2320952 MAG United States North America
Gene Location Start: 9513;  End: 11753  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003145_00820.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 313 725 1.4e-84 0.9298245614035088

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 3.41e-83 312 730 2 330
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 2.99e-20 492 720 79 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4409 NanH 6.97e-17 324 673 275 645
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd00110 LamG 4.26e-05 13 99 20 107
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.
smart00282 LamG 3.25e-04 16 100 1 87
Laminin G domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ65718.1 4.67e-224 14 740 11 772
ACR18588.1 2.60e-223 14 740 11 782
QRP10095.1 2.60e-223 14 740 11 782
QRP14191.1 4.18e-222 14 740 11 782
BDA65121.1 6.76e-209 6 741 11 752

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 2.60e-62 306 724 6 431
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 1.37e-61 306 724 5 430
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 1.48e-61 306 724 5 430
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 3.86e-48 319 728 21 453
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 4.35e-48 319 728 25 457
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 2.54e-59 306 725 377 811
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62575 3.80e-45 319 728 341 773
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
P62576 3.80e-45 319 728 341 773
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
Q27701 1.69e-31 252 724 216 730
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
Q02834 5.41e-28 317 723 60 386
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
1.000035 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003145_00820.