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CAZyme Information: MGYG000001374_00817

You are here: Home > Sequence: MGYG000001374_00817

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 Mediterraneibacter torques
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter torques
CAZyme ID MGYG000001374_00817
CAZy Family GH123
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1129 125489.72 4.4821
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001374 3092406 Isolate not provided not provided
Gene Location Start: 861594;  End: 864983  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.53 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH123 421 964 6e-149 0.9386617100371747

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13320 DUF4091 1.38e-17 861 932 1 65
Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important.
pfam07554 FIVAR 6.12e-07 1010 1071 1 69
FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
COG5492 YjdB 4.91e-06 316 401 177 261
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only].
pfam02368 Big_2 1.82e-05 321 385 1 66
Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.
smart00635 BID_2 0.004 319 385 1 71
Bacterial Ig-like domain 2.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUD71731.1 4.78e-225 36 1001 49 1001
AYE33261.1 9.76e-206 168 996 34 842
QAS61432.1 9.76e-206 168 996 34 842
QBJ76609.1 1.10e-192 407 992 6 577
ATD58699.1 1.10e-192 407 992 6 577

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FQE_A 4.40e-178 408 992 30 600
Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5FQG_A 6.80e-177 408 992 30 600
Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens]
5L7V_A 1.97e-74 436 932 53 516
ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]
5L7R_A 2.82e-74 436 932 68 531
ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0DTR5 1.01e-06 71 293 865 1061
A type blood alpha-D-galactosamine galactosaminidase OS=Flavonifractor plautii OX=292800 PE=1 SV=1

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
0.000278 0.999002 0.000182 0.000185 0.000161 0.000153

TMHMM  Annotations      download full data without filtering help

start end
7 29
1103 1122