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CAZyme Information: MGYG000001004_00800

You are here: Home > Sequence: MGYG000001004_00800

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 CAG-56 sp900539525
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900539525
CAZyme ID MGYG000001004_00800
CAZy Family GH123
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1660 182025.57 5.366
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001004 2903340 MAG Austria Europe
Gene Location Start: 55613;  End: 60595  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001004_00800.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH123 257 825 5e-164 0.9869888475836431

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13320 DUF4091 5.56e-22 711 778 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.
sd00036 LRR_3 1.58e-17 1526 1639 14 116
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00036 LRR_3 8.78e-17 1545 1639 1 93
leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
pfam13306 LRR_5 1.83e-15 1524 1627 9 100
Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.
pfam13306 LRR_5 4.41e-15 1547 1624 1 74
Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFL05165.1 0.0 24 1446 41 1734
QRI58909.1 0.0 24 1446 20 1713
QTQ18982.1 0.0 24 1446 41 1734
BBA47625.1 0.0 24 1446 20 1713
ADP36622.1 0.0 24 1446 20 1713

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FQE_A 4.36e-100 258 790 30 554
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 5.23e-99 258 790 30 554
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 1.19e-83 287 781 54 519
ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482]
5L7R_A 1.76e-83 287 781 69 534
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      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
0.000256 0.999077 0.000194 0.000164 0.000150 0.000139

TMHMM  Annotations      download full data without filtering help

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