Species | Paenibacillus amylolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus | |||||||||||
CAZyme ID | MGYG000003072_01935 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 200674; End: 201948 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 189 | 375 | 1.2e-23 | 0.5033783783783784 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07833 | Cu_amine_oxidN1 | 5.31e-30 | 55 | 149 | 3 | 93 | Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other. |
cd02874 | GH18_CFLE_spore_hydrolase | 3.78e-28 | 160 | 405 | 6 | 304 | Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis. |
smart00636 | Glyco_18 | 1.73e-16 | 238 | 375 | 83 | 235 | Glyco_18 domain. |
pfam00704 | Glyco_hydro_18 | 6.53e-16 | 232 | 388 | 74 | 235 | Glycosyl hydrolases family 18. |
COG3858 | YaaH | 3.08e-15 | 232 | 405 | 176 | 409 | Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QZN74124.1 | 1.10e-280 | 1 | 424 | 1 | 424 |
QOS78913.1 | 1.23e-254 | 1 | 424 | 1 | 424 |
AVV58010.1 | 5.00e-254 | 1 | 424 | 1 | 424 |
ANA82903.1 | 5.00e-254 | 1 | 424 | 1 | 424 |
AWP27170.1 | 5.83e-253 | 1 | 424 | 1 | 424 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4S3J_A | 3.49e-08 | 209 | 375 | 153 | 324 | Crystalstructure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876],4S3J_B Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876],4S3J_C Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL [Bacillus cereus ATCC 10876] |
1HKK_A | 4.87e-06 | 233 | 388 | 81 | 261 | Highresoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens] |
1HKI_A | 4.88e-06 | 233 | 388 | 81 | 261 | Crystalstructure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens] |
1LG1_A | 4.88e-06 | 233 | 388 | 81 | 261 | CrystalStructure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens] |
4WJX_A | 5.03e-06 | 233 | 388 | 81 | 261 | Crystalstructure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0DPJ9 | 5.89e-07 | 209 | 375 | 152 | 323 | Cortical fragment-lytic enzyme OS=Bacillus anthracis OX=1392 GN=sleL PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.006061 | 0.749356 | 0.243128 | 0.000933 | 0.000269 | 0.000239 |
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