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CAZyme Information: MGYG000004044_01290

You are here: Home > Sequence: MGYG000004044_01290

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 UMGS1633 sp900553645
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1633; UMGS1633 sp900553645
CAZyme ID MGYG000004044_01290
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
355 MGYG000004044_60|CGC1 39915.1 5.2545
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004044 2665198 MAG United Kingdom Europe
Gene Location Start: 7305;  End: 8372  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004044_01290.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 28 334 2.6e-31 0.8654970760233918

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 2.82e-49 27 343 21 331
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 4.67e-29 42 329 8 277
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
QNM08403.1 7.17e-110 5 354 12 365
AOH43019.1 4.92e-88 19 355 21 358
AEL26177.1 6.36e-82 6 355 28 366
AKP51796.1 1.11e-78 6 355 35 373
QDU47982.1 4.27e-69 4 355 36 381

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4X6K_A 2.60e-08 133 334 271 455
Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]
4X47_A 2.61e-08 133 334 274 458
Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en [[Ruminococcus] gnavus ATCC 29149],4X49_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with oseltamivir carboxylate [[Ruminococcus] gnavus ATCC 29149],4X4A_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac [[Ruminococcus] gnavus ATCC 29149]
1SLI_A 6.92e-07 146 334 472 648
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]
7LBU_A 2.36e-06 6 303 74 384
ChainA, Exo-alpha-sialidase [Cutibacterium acnes],7LBV_A Chain A, Exo-alpha-sialidase [Cutibacterium acnes]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q27701 3.94e-06 146 334 552 728
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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004044_01290.