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CAZyme Information: MGYG000003440_00590

You are here: Home > Sequence: MGYG000003440_00590

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 Anaerobiospirillum succiniciproducens
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; Anaerobiospirillum; Anaerobiospirillum succiniciproducens
CAZyme ID MGYG000003440_00590
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
628 69106.94 4.5845
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003440 3625053 MAG Fiji Oceania
Gene Location Start: 8404;  End: 10290  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003440_00590.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 4 283 5e-27 0.7309941520467836

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 8.11e-18 5 292 77 339
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.
pfam03797 Autotransporter 1.29e-10 360 553 13 224
Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.
smart00869 Autotransporter 4.64e-05 348 621 1 268
Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNM15078.1 3.91e-121 5 617 119 704
AMZ14174.1 1.14e-99 5 617 92 668
ASG76455.1 3.09e-99 5 617 38 614
AOV98594.1 6.31e-87 5 617 78 654
QPR26713.1 1.49e-86 5 617 116 692

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000065 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003440_00590.