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CAZyme Information: MGYG000002120_00035

You are here: Home > Sequence: MGYG000002120_00035

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 Porphyromonas pasteri
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas; Porphyromonas pasteri
CAZyme ID MGYG000002120_00035
CAZy Family GT101
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
398 MGYG000002120_3|CGC1 44958.86 6.2928
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002120 1877343 MAG Mongolia Asia
Gene Location Start: 6744;  End: 7940  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002120_00035.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT101 56 290 1.7e-70 0.9955357142857143

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR03728 glyco_access_1 1.15e-94 44 315 6 265
glycosyltransferase, SP_1767 family. Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion.
pfam08759 GT-D 5.18e-90 57 291 1 223
Glycosyltransferase GT-D fold. This domain is found at the C-terminus of proteins such as the probable glycosyltransferase Gly that also contain the glycosyl transferase domain at the N-terminus. It is also found N-terminal in numerous putative glycosyltransferases such as GalT1. GalT1 has been shown to catalyze the third step of Fap1 glycosylation. This domain is structurally distinct from all known GT folds of glycosyltransferases and contains a metal binding site. This new glycosyltransferase fold has been named GT-D.
COG2608 CopZ 2.46e-18 325 390 1 66
Copper chaperone CopZ [Inorganic ion transport and metabolism].
cd00371 HMA 1.42e-15 329 392 1 63
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.
pfam00403 HMA 3.06e-15 329 386 1 58
Heavy-metal-associated domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AJW64740.1 7.75e-95 8 295 3 287
QMW87124.1 8.41e-66 3 311 9 307
AAO75156.1 8.41e-66 3 311 9 307
AAO76286.1 3.06e-60 44 314 45 302
QMW88186.1 3.06e-60 44 314 45 302

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4PFX_A 7.11e-55 29 315 4 277
Thehighly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold [Streptococcus parasanguinis FW213]
4PHR_A 1.00e-54 44 315 19 277
Domainof unknown function 1792 (DUF1792) with manganese [Streptococcus parasanguinis FW213]
4PHS_A 5.99e-53 44 315 19 277
Selenomethioninesubstituted structure of domain of unknown function 1792 (DUF1792) [Streptococcus parasanguinis FW213]
5V4A_A 1.18e-51 44 316 13 273
ANew Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36],5V4A_B A New Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36]
2ROE_A 3.41e-08 332 393 6 64
ChainA, Heavy metal binding protein [Thermus thermophilus],2ROG_A Chain A, Heavy metal binding protein [Thermus thermophilus],5ZCZ_A Solution structure of the T. Thermophilus HB8 TTHA1718 protein in living eukaryotic cells by in-cell NMR spectroscopy [Thermus thermophilus HB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9AEU2 2.28e-47 44 316 422 681
Probable glycosyl transferase Gly OS=Streptococcus gordonii OX=1302 GN=gly PE=3 SV=2
A0A0H2URB1 3.31e-42 44 314 555 812
Glycosyltransferase GlyD OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyD PE=1 SV=1
Q5HCZ2 2.69e-07 329 389 5 65
Copper chaperone CopZ OS=Staphylococcus aureus (strain COL) OX=93062 GN=copZ PE=3 SV=1
Q6G6B6 2.69e-07 329 389 5 65
Copper chaperone CopZ OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=copZ PE=3 SV=1
Q6GDP0 2.69e-07 329 389 5 65
Copper chaperone CopZ OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=copZ PE=3 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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002120_00035.