Species | Bacteroides oleiciplenus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus | |||||||||||
CAZyme ID | MGYG000001422_01811 | |||||||||||
CAZy Family | CE1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 118858; End: 119781 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE1 | 65 | 275 | 1.1e-16 | 0.8634361233480177 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00326 | Peptidase_S9 | 7.80e-49 | 99 | 293 | 3 | 210 | Prolyl oligopeptidase family. |
COG1506 | DAP2 | 2.36e-39 | 1 | 274 | 322 | 594 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
COG0412 | DLH | 4.56e-10 | 106 | 287 | 50 | 215 | Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]. |
COG1073 | FrsA | 1.19e-05 | 68 | 294 | 40 | 299 | Fermentation-respiration switch protein FrsA, has esterase activity, DUF1100 family [Signal transduction mechanisms]. |
pfam00561 | Abhydrolase_1 | 3.48e-05 | 78 | 213 | 1 | 121 | alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AJY87077.1 | 3.31e-104 | 2 | 302 | 652 | 950 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EOP_A | 1.99e-29 | 47 | 297 | 633 | 887 | DPP8- SLRFLYEG, space group 20 [Homo sapiens],6EOP_B DPP8 - SLRFLYEG, space group 20 [Homo sapiens],6EOP_C DPP8 - SLRFLYEG, space group 20 [Homo sapiens] |
6EOO_A | 1.99e-29 | 47 | 297 | 633 | 887 | DPP8- Apo, space group 20 [Homo sapiens],6EOO_B DPP8 - Apo, space group 20 [Homo sapiens],6EOO_C DPP8 - Apo, space group 20 [Homo sapiens],6EOS_A DPP8 - Apo, space group 19 [Homo sapiens],6EOS_B DPP8 - Apo, space group 19 [Homo sapiens],6EOS_C DPP8 - Apo, space group 19 [Homo sapiens],6EOS_D DPP8 - Apo, space group 19 [Homo sapiens],6EOS_E DPP8 - Apo, space group 19 [Homo sapiens],6EOS_F DPP8 - Apo, space group 19 [Homo sapiens],6EOT_A DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6EOT_B DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6EOT_D DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6EOT_G DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6EOT_I DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6EOT_K DPP8 - SLRFLYEG, space group 19 [Homo sapiens],6HP8_A Crystal structure of DPP8 in complex with Val-BoroPro [Homo sapiens],6HP8_B Crystal structure of DPP8 in complex with Val-BoroPro [Homo sapiens],6HP8_C Crystal structure of DPP8 in complex with Val-BoroPro [Homo sapiens],6QZW_A DPP8 bound to a dipeptide (MP) from the N-terminus of BRCA2 [Homo sapiens],6QZW_B DPP8 bound to a dipeptide (MP) from the N-terminus of BRCA2 [Homo sapiens],6QZW_C DPP8 bound to a dipeptide (MP) from the N-terminus of BRCA2 [Homo sapiens],7A3G_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7A3G_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7A3I_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7A3I_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7A3I_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens],7A3J_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7A3J_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7A3J_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens],7A3K_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7A3K_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7A3K_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens],7A3L_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7A3L_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7A3L_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens],7AYQ_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7AYQ_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7AYR_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7AYR_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7OR4_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7OR4_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],7OZ7_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],7OZ7_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens] |
6TRW_A | 2.00e-29 | 47 | 297 | 638 | 892 | ChainA, Dipeptidyl peptidase 8 [Homo sapiens],6TRW_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],6TRW_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens],6TRX_A Chain A, Dipeptidyl peptidase 8 [Homo sapiens],6TRX_B Chain B, Dipeptidyl peptidase 8 [Homo sapiens],6TRX_C Chain C, Dipeptidyl peptidase 8 [Homo sapiens] |
4Q1V_A | 1.41e-26 | 2 | 279 | 415 | 694 | Crystalstructure of a putative dipeptidyl aminopeptidase IV (BACOVA_01349) from Bacteroides ovatus ATCC 8483 at 2.48 A resolution [Bacteroides ovatus ATCC 8483],4Q1V_B Crystal structure of a putative dipeptidyl aminopeptidase IV (BACOVA_01349) from Bacteroides ovatus ATCC 8483 at 2.48 A resolution [Bacteroides ovatus ATCC 8483] |
7CRW_C | 2.08e-26 | 47 | 294 | 607 | 858 | ChainC, Dipeptidyl peptidase 9 [Rattus norvegicus],7CRW_D Chain D, Dipeptidyl peptidase 9 [Rattus norvegicus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q6V1X1 | 1.09e-28 | 47 | 297 | 633 | 887 | Dipeptidyl peptidase 8 OS=Homo sapiens OX=9606 GN=DPP8 PE=1 SV=1 |
Q80YA7 | 1.47e-28 | 47 | 297 | 627 | 881 | Dipeptidyl peptidase 8 OS=Mus musculus OX=10090 GN=Dpp8 PE=1 SV=1 |
Q8BVG4 | 1.14e-25 | 47 | 294 | 607 | 858 | Dipeptidyl peptidase 9 OS=Mus musculus OX=10090 GN=Dpp9 PE=1 SV=2 |
Q86TI2 | 2.09e-25 | 47 | 294 | 608 | 859 | Dipeptidyl peptidase 9 OS=Homo sapiens OX=9606 GN=DPP9 PE=1 SV=3 |
B2RJX3 | 7.32e-24 | 43 | 279 | 475 | 716 | Prolyl tripeptidyl peptidase OS=Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) OX=431947 GN=ptpA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000041 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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