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CAZyme Information: MGYG000000493_01013

You are here: Home > Sequence: MGYG000000493_01013

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
Protein Length CGC Molecular Weight Isoelectric Point
666 MGYG000000493_6|CGC1 78275.95 7.5269
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000493 1815977 MAG Fiji Oceania
Gene Location Start: 74437;  End: 76437  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000493_01013.

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000493_01013.