logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001292_00665

You are here: Home > Sequence: MGYG000001292_00665

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 Bifidobacterium infantis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium infantis
CAZyme ID MGYG000001292_00665
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
760 MGYG000001292_1|CGC15 82562.07 5.3616
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001292 2832748 Isolate not provided not provided
Gene Location Start: 742898;  End: 745180  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 323 742 2.6e-89 0.9473684210526315

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 6.45e-85 325 750 1 339
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 4.97e-19 464 735 27 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4409 NanH 3.41e-14 323 738 260 700
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
smart00282 LamG 0.002 186 262 2 79
Laminin G domain.
cd00110 LamG 0.005 178 317 18 149
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEG40809.1 0.0 1 760 1 760
BAJ68244.1 0.0 1 760 3 762
ACJ51753.1 0.0 1 760 1 760
QUF87127.1 0.0 1 760 1 760
QKY12994.1 0.0 1 760 1 760

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 1.76e-71 327 738 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 1.80e-70 327 738 12 429
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 1.95e-70 327 738 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]
3H72_A 1.11e-58 316 754 1 468
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]
7A54_A 1.79e-58 314 754 22 491
ChainA, Sialidase A [Streptococcus pneumoniae],7A54_B Chain B, Sialidase A [Streptococcus pneumoniae],7A5X_A Chain A, Sialidase A [Streptococcus pneumoniae],7A5X_B Chain B, Sialidase A [Streptococcus pneumoniae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P29767 6.17e-67 172 756 212 828
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62576 8.74e-59 175 754 145 784
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P62575 8.74e-59 175 754 145 784
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
Q02834 1.37e-28 320 755 49 402
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
Q27701 3.48e-27 273 739 223 730
Anhydrosialidase OS=Macrobdella decora OX=6405 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
1.000045 0.000006 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001292_00665.