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CAZyme Information: MGYG000002471_01918

You are here: Home > Sequence: MGYG000002471_01918

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 Yersinia mollaretii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia mollaretii
CAZyme ID MGYG000002471_01918
CAZy Family GH19
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
772 MGYG000002471_3|CGC2 88623.07 6.7697
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002471 4663229 Isolate Finland Europe
Gene Location Start: 229316;  End: 231634  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002471_01918.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam11860 Muraidase 1.03e-55 603 768 1 170
N-acetylmuramidase. Endolysins are bacteriophage encoded proteins synthesized at the end of the lytic infection cycle. They degrade the peptidoglycan (PG) of the host bacterium to allow viral progeny release. This domain family is found in bacteria and viruses. It is also found associated with pfam01471. One of the family members is the modular Gp110 endolysin found in the Salmonella phage. This domain represents the catalytic region found in the C-terminal of Gp110. It has been demonstrated to have N-acetylmuramidase (lysozyme) activity cleaving the beta-(1,4) glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues in the sugar backbone of the PG. Furthermore, sequence alignments containing this domain show that the Gp110 E101 residue is conserved (suggesting that is is the catalytic residue), and followed by serine (a common feature in lysozymes). The structure of endolysins varies depending on their origin. In general, most of the endolysins from phages infecting Gram-positive bacteria have a modular structure consisting of one or two N-terminal enzymatic active domains (EADs) and a C-terminal cell wall binding domain (CBD) separated by a short linker. In silico analysis indicate that this endolysin has a modular structure harboring this EAD family at the C-terminus and a PG_binding_1 CBD at the N-terminus.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHE70536.1 3.03e-259 1 662 1 671
AWF50744.1 3.90e-258 1 563 2 564
ANA25340.1 6.98e-256 1 563 1 563
ANA29683.1 6.98e-256 1 563 1 563
ANA21118.1 6.98e-256 1 563 1 563

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7Q4S_AAA 1.53e-34 588 770 23 204
ChainAAA, Endolysin [Pseudomonas phage JG004],7Q4S_BBB Chain BBB, Endolysin [Pseudomonas phage JG004],7Q4T_AAA Chain AAA, Endolysin [Pseudomonas phage JG004]
5NM7_A 7.21e-26 588 769 75 259
Crystalstructure of Burkholderia AP3 phage endolysin [Burkholderia],5NM7_G Crystal structure of Burkholderia AP3 phage endolysin [Burkholderia]
7RUM_A 4.12e-24 586 770 94 283
ChainA, Endolysin [Salmonella phage GEC_vB_GOT],7RUM_B Chain B, Endolysin [Salmonella phage GEC_vB_GOT]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002471_01918.