Species | Haemophilus_D parainfluenzae_M | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_D; Haemophilus_D parainfluenzae_M | |||||||||||
CAZyme ID | MGYG000003189_01140 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22570; End: 24570 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR03755 | conj_TIGR03755 | 0.0 | 43 | 457 | 1 | 418 | integrating conjugative element protein, PFL_4711 family. Members of this protein family are found in genomic regions associated with conjugative transfer and integrated TOL-like plasmids. The specific function is unknown. [Mobile and extrachromosomal element functions, Plasmid functions] |
cd00737 | lyz_endolysin_autolysin | 3.23e-12 | 524 | 616 | 4 | 86 | endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan. |
COG3772 | RrrD | 3.92e-07 | 516 | 615 | 6 | 96 | Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]. |
cd16900 | endolysin_R21-like | 6.38e-07 | 515 | 615 | 2 | 91 | endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan. |
cd00735 | T4-like_lys | 2.28e-04 | 524 | 615 | 5 | 93 | bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASE07600.1 | 8.58e-223 | 3 | 529 | 1 | 540 |
AAP95805.1 | 8.58e-223 | 3 | 529 | 1 | 540 |
ANF70987.1 | 1.37e-221 | 31 | 529 | 2 | 509 |
ANF74266.1 | 1.37e-221 | 31 | 529 | 2 | 509 |
ANF74701.1 | 1.37e-221 | 31 | 529 | 2 | 509 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000351 | 0.998812 | 0.000292 | 0.000191 | 0.000189 | 0.000160 |
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