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CAZyme Information: MGYG000000790_00067

You are here: Home > Sequence: MGYG000000790_00067

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 Fusobacterium nucleatum_E
Lineage Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium; Fusobacterium nucleatum_E
CAZyme ID MGYG000000790_00067
CAZy Family GH135
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
608 MGYG000000790_3|CGC1 69408.64 7.5457
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000790 2081813 MAG China Asia
Gene Location Start: 16689;  End: 18515  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000790_00067.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH135 114 294 1.1e-23 0.7721518987341772

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam12138 Spherulin4 4.05e-21 110 295 41 235
Spherulation-specific family 4. This protein is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 250 and 398 amino acids in length. There is a conserved NPG sequence motif and there are two completely conserved G residues that may be functionally important. Starvation will often induce spherulation - the production of spores - and this process may involve DNA-methylation. Changes in the methylation of spherulin4 are associated with the formation of spherules, but these changes are probably transient. Methylation of the gene accompanies its transcriptional activation, and spherulin4 mRNA is only detectable in late spherulating cultures and mature spherules. It is a spherulation-specific protein.
pfam03797 Autotransporter 3.59e-18 357 591 1 254
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 9.43e-16 359 598 1 267
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.
TIGR01414 autotrans_barl 2.04e-08 357 606 165 427
outer membrane autotransporter barrel domain. A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
pfam13505 OMP_b-brl 0.010 389 553 18 164
Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASQ47822.1 3.00e-241 34 608 142 707
QUB96211.1 1.34e-236 34 608 139 704
BBM45129.1 1.20e-157 56 603 219 760
BBM57219.1 3.77e-156 56 603 219 760
BBM53111.1 2.33e-67 1 431 1 451

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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.017057 0.965678 0.016271 0.000335 0.000310 0.000317

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000790_00067.