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CAZyme Information: MGYG000003396_02967

You are here: Home > Sequence: MGYG000003396_02967

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 Clostridium sp900766315
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900766315
CAZyme ID MGYG000003396_02967
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1665 MGYG000003396_152|CGC1 180384.74 4.3319
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003396 3926186 MAG United States North America
Gene Location Start: 7447;  End: 12444  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 377 809 2e-98 0.9678362573099415
CBM40 191 358 8.4e-41 0.9720670391061452
CBM40 964 1131 1.2e-38 0.9497206703910615
CBM32 54 176 7.9e-19 0.9193548387096774

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 2.36e-85 380 811 2 339
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.
COG4409 NanH 4.71e-30 290 801 187 703
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam02973 Sialidase 5.56e-26 184 361 1 188
Sialidase, N-terminal domain.
pfam02973 Sialidase 1.86e-21 954 1132 1 188
Sialidase, N-terminal domain.
pfam13088 BNR_2 1.69e-15 556 795 79 280
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
ATD57534.1 0.0 1 1665 1 1299
QBJ75069.1 0.0 1 1665 1 1299
ATD54786.1 0.0 1 1665 1 1299
SLK16343.1 0.0 1 1665 1 1299
AYE33273.1 3.38e-312 1 1525 1 1222

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 1.29e-191 374 816 6 448
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 1.74e-190 374 816 5 447
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 1.94e-190 374 816 5 447
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]
1SLI_A 1.25e-86 180 818 1 668
LeechIntramolecular Trans-Sialidase Complexed With Dana [Macrobdella decora],1SLL_A Sialidase L From Leech Macrobdella Decora [Macrobdella decora],2SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac, The Reaction Product [Macrobdella decora],3SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac Prepared By Soaking With 3'-Sialyllactose [Macrobdella decora],4SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2- Propenyl-Neu5ac, An Inactive Substrate Analogue [Macrobdella decora]
2VVZ_A 2.06e-81 376 831 6 480
Structureof the catalytic domain of Streptococcus pneumoniae sialidase NanA [Streptococcus pneumoniae],2VVZ_B Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA [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 4.36e-298 1 930 1 937
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62576 1.51e-85 182 892 116 849
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P62575 1.51e-85 182 892 116 849
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
Q27701 1.79e-85 173 818 74 748
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
Q54727 8.08e-38 197 811 51 682
Sialidase B OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=nanB PE=1 SV=2

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
0.002124 0.997004 0.000233 0.000240 0.000182 0.000168

TMHMM  Annotations      download full data without filtering help

start end
7 29
1639 1661