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CAZyme Information: MGYG000000493_01013
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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 | UBA2883 sp002103075 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; UBA2883; UBA2883 sp002103075 | |||||||||||
| CAZyme ID | MGYG000000493_01013 | |||||||||||
| CAZy Family | GT101 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 74437; End: 76437 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT101 | 97 | 318 | 2.1e-87 | 0.9910714285714286 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR03728 | glyco_access_1 | 7.09e-111 | 79 | 337 | 1 | 260 | 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 | 1.24e-104 | 97 | 319 | 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. |
| pfam04991 | LicD | 4.03e-36 | 435 | 630 | 1 | 224 | LicD family. The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily. |
| COG3475 | LicD | 4.71e-26 | 416 | 638 | 6 | 255 | Phosphorylcholine metabolism protein LicD [Lipid transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QWH18731.1 | 4.77e-80 | 77 | 337 | 34 | 294 |
| QWI12255.1 | 6.69e-80 | 77 | 337 | 34 | 294 |
| QWH29821.1 | 2.60e-79 | 77 | 337 | 34 | 294 |
| ABY44566.1 | 3.65e-79 | 77 | 337 | 34 | 294 |
| QWG83469.1 | 3.65e-79 | 77 | 337 | 34 | 294 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5V4A_A | 2.35e-69 | 79 | 344 | 8 | 274 | ANew Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36],5V4A_B A New Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36] |
| 4PFX_A | 2.64e-59 | 71 | 337 | 9 | 272 | Thehighly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold [Streptococcus parasanguinis FW213] |
| 4PHR_A | 2.64e-59 | 71 | 337 | 9 | 272 | Domainof unknown function 1792 (DUF1792) with manganese [Streptococcus parasanguinis FW213] |
| 4PHS_A | 9.97e-59 | 71 | 337 | 9 | 272 | Selenomethioninesubstituted structure of domain of unknown function 1792 (DUF1792) [Streptococcus parasanguinis FW213] |
| 6KAJ_A | 1.74e-11 | 434 | 539 | 292 | 397 | Crystalstructure of FKRP in complex with Ba ion [Homo sapiens],6KAJ_B Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAJ_C Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAJ_D Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAK_A Crystal structure of FKRP in complex with Mg ion [Homo sapiens],6KAK_B Crystal structure of FKRP in complex with Mg ion [Homo sapiens],6KAK_C Crystal structure of FKRP in complex with Mg ion [Homo sapiens],6KAK_D Crystal structure of FKRP in complex with Mg ion [Homo sapiens],6KAL_A Crystal structure of FKRP in complex with Mg ion and CMP [Homo sapiens],6KAL_B Crystal structure of FKRP in complex with Mg ion and CMP [Homo sapiens],6KAL_C Crystal structure of FKRP in complex with Mg ion and CMP [Homo sapiens],6KAL_D Crystal structure of FKRP in complex with Mg ion and CMP [Homo sapiens],6KAM_A Crystal structure of FKRP in complex with Ba ion, CDP-ribtol, and sugar acceptor [Homo sapiens],6KAM_B Crystal structure of FKRP in complex with Ba ion, CDP-ribtol, and sugar acceptor [Homo sapiens],6KAM_C Crystal structure of FKRP in complex with Ba ion, CDP-ribtol, and sugar acceptor [Homo sapiens],6KAM_D Crystal structure of FKRP in complex with Ba ion, CDP-ribtol, and sugar acceptor [Homo sapiens],6KAN_A Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAN_B Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAN_C Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6KAN_D Crystal structure of FKRP in complex with Ba ion [Homo sapiens],6L7S_A Crystal structure of FKRP in complex with Mg ion, Zinc peak data [Homo sapiens],6L7S_B Crystal structure of FKRP in complex with Mg ion, Zinc peak data [Homo sapiens],6L7S_C Crystal structure of FKRP in complex with Mg ion, Zinc peak data [Homo sapiens],6L7S_D Crystal structure of FKRP in complex with Mg ion, Zinc peak data [Homo sapiens],6L7T_A Crystal structure of FKRP in complex with Mg ion, Zinc low remote data [Homo sapiens],6L7T_B Crystal structure of FKRP in complex with Mg ion, Zinc low remote data [Homo sapiens],6L7T_C Crystal structure of FKRP in complex with Mg ion, Zinc low remote data [Homo sapiens],6L7T_D Crystal structure of FKRP in complex with Mg ion, Zinc low remote data [Homo sapiens],6L7U_A Crystal structure of FKRP in complex with Ba ion, Ba-SAD data [Homo sapiens],6L7U_B Crystal structure of FKRP in complex with Ba ion, Ba-SAD data [Homo sapiens],6L7U_C Crystal structure of FKRP in complex with Ba ion, Ba-SAD data [Homo sapiens],6L7U_D Crystal structure of FKRP in complex with Ba ion, Ba-SAD data [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9AEU2 | 7.23e-63 | 84 | 344 | 422 | 682 | Probable glycosyl transferase Gly OS=Streptococcus gordonii OX=1302 GN=gly PE=3 SV=2 |
| A0A0H2URB1 | 1.45e-56 | 79 | 337 | 550 | 808 | Glycosyltransferase GlyD OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyD PE=1 SV=1 |
| P14184 | 5.63e-18 | 417 | 636 | 6 | 249 | Lipopolysaccharide cholinephosphotransferase LicD OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=licD PE=3 SV=2 |
| Q68W49 | 1.69e-11 | 427 | 532 | 110 | 220 | Uncharacterized protein RT0683 OS=Rickettsia typhi (strain ATCC VR-144 / Wilmington) OX=257363 GN=RT0683 PE=3 SV=1 |
| Q9H9S5 | 1.06e-10 | 434 | 539 | 332 | 437 | Ribitol 5-phosphate transferase FKRP OS=Homo sapiens OX=9606 GN=FKRP 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 |
|---|---|---|---|---|---|
| 1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |