Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ; | |||||||||||
CAZyme ID | MGYG000000346_00688 | |||||||||||
CAZy Family | GH0 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 826; End: 2088 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01471 | PG_binding_1 | 6.36e-14 | 345 | 406 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
COG3409 | PGRP | 3.65e-08 | 336 | 408 | 117 | 185 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
COG3409 | PGRP | 5.43e-08 | 339 | 406 | 38 | 102 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
pfam13620 | CarboxypepD_reg | 4.94e-06 | 22 | 115 | 5 | 81 | Carboxypeptidase regulatory-like domain. |
TIGR02669 | SpoIID_LytB | 0.002 | 293 | 316 | 237 | 260 | SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QRV22093.1 | 1.54e-217 | 9 | 420 | 4 | 416 |
ASN94441.1 | 2.19e-217 | 9 | 419 | 7 | 415 |
QRP40879.1 | 2.19e-217 | 9 | 419 | 7 | 415 |
QJU21247.1 | 6.26e-217 | 9 | 419 | 7 | 415 |
QJU14725.1 | 1.51e-216 | 4 | 419 | 5 | 420 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1LBU_A | 1.70e-08 | 334 | 409 | 5 | 76 | HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P00733 | 1.47e-07 | 334 | 409 | 47 | 118 | Zinc D-Ala-D-Ala carboxypeptidase OS=Streptomyces albus G OX=1962 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000044 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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