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CAZyme Information: MGYG000001100_00439

You are here: Home > Sequence: MGYG000001100_00439

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 Weissella viridescens
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Weissella; Weissella viridescens
CAZyme ID MGYG000001100_00439
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
217 MGYG000001100_74|CGC1 21549.85 4.6966
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001100 1591687 MAG China Asia
Gene Location Start: 382;  End: 1035  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001100_00439.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3942 COG3942 6.26e-25 55 217 13 168
Surface antigen [Cell wall/membrane/envelope biogenesis].
PRK08581 PRK08581 1.03e-23 110 216 502 616
amidase domain-containing protein.
pfam05257 CHAP 9.10e-22 114 197 3 83
CHAP domain. This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Escherichia coli gss, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.
cd00118 LysM 1.61e-14 30 73 2 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257 LysM 5.55e-13 32 71 3 42
Lysin motif.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOD86307.1 3.89e-123 1 217 1 220
AWF96365.1 1.39e-54 1 217 1 294
ALI32729.1 1.57e-53 1 217 1 294
QMU89117.1 4.55e-53 1 217 1 295
QDG80722.1 4.55e-53 1 217 1 295

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4CGK_A 4.56e-23 113 200 284 365
Crystalstructure of the essential protein PcsB from Streptococcus pneumoniae [Streptococcus pneumoniae D39],4CGK_B Crystal structure of the essential protein PcsB from Streptococcus pneumoniae [Streptococcus pneumoniae D39]
2LRJ_A 1.23e-20 109 211 4 103
ChainA, Staphyloxanthin biosynthesis protein, putative [Staphylococcus aureus subsp. aureus COL]
2K3A_A 1.49e-18 94 210 30 143
ChainA, CHAP domain protein [Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292]
5T1Q_A 3.11e-14 113 214 245 351
ChainA, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_B Chain B, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_C Chain C, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_D Chain D, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325]
2MKX_A 7.00e-06 32 77 8 52
Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8DVU8 6.89e-25 26 198 27 181
Putative hydrolase SMU_367 OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=SMU_367 PE=3 SV=1
Q2G0D4 8.85e-22 27 211 87 256
Probable autolysin SsaALP OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=SAOUHSC_00671 PE=1 SV=1
Q49UX4 7.89e-19 32 199 153 304
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q7A1T4 3.73e-16 32 199 161 311
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sle1 PE=3 SV=1
Q6GC24 3.73e-16 32 199 161 311
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 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
0.000256 0.998987 0.000173 0.000207 0.000179 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001100_00439.