|
Name |
Accession |
Description |
Interval |
E-value |
| DPPIV_N super family |
cl37636 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
171-592 |
1.74e-82 |
|
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.
The actual alignment was detected with superfamily member pfam00930:
Pssm-ID: 395744 [Multi-domain] Cd Length: 352 Bit Score: 269.19 E-value: 1.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 171 SGLFLFQASNSLFYCRDGGHNGFIQAaPMKPMEIKTQCS--GIRMDPKISPgDPSFIAFINNNDLWVTNIETAEERRLTf 248
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIY-DLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 249 cHKGLNNVkedpkSAGVATFVIQEE-FDRFTGYWWSPaatedaDGGKtlqLLYEEVDESEVEIIHVPSPALEER--KADV 325
Cdd:pfam00930 80 -SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSP------DGSR---LAFLRFDESEVPIITLPYYTDEGPgpEVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 326 YRYPRTGSKNPQISLKLAEIRTdqqGKMISaqnkelVLPFTTLFPGVEYIARAGWTKDGKFaWAVLLDRSQQKLQLVLLp 405
Cdd:pfam00930 145 IKYPKAGAPNPTVELFVYDLAS---GKTVE------VVPPDDLSDADYYITRVKWVPDGKL-LVQWLNRDQNRLKVVLC- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 406 palfipvsvdDPQWEEHVeampegvqpfIIYEEITDIWINVHDIFYPFIQTSNdkiSFLWVNESQtGFCHLYRITSLLKp 485
Cdd:pfam00930 214 ----------DAETGRTV----------VILEETSDGWVELHQDPHFIKRDGS---GFLWISERD-GYNHLYLYDLDGK- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 486 gchqwsreySPSeddfkcsteeevALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYESPGEIVRLTK 565
Cdd:pfam00930 269 ---------SPI------------QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTD 323
|
410 420
....*....|....*....|....*....
gi 221219063 566 PGFSH--SCSVSQNFDMFISHYSNVSTPP 592
Cdd:pfam00930 324 DSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
684-885 |
8.83e-64 |
|
Prolyl oligopeptidase family;
:
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 213.63 E-value: 8.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 684 LRLNTLASLGYAVVVIDGRGSCQRGLKFEGALKNKMGQVEIEDQVEGLQFVAEKYkFIDLSRVAIHGWSYGGFLSLMGLI 763
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 764 HRPNIFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVDKLPNEPnRLLILHGFLDENVHFFH 837
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221219063 838 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEIMLLYFLQQHL 885
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| Dpp_8_9_N super family |
cl44934 |
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ... |
30-158 |
3.01e-50 |
|
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are similar to DPP4, consisting of one N-terminal beta-propeller and a C-terminal alpha/beta hydrolase domain, which form a functional homodimer. This entry represents the N-terminal beta-propeller of DPP8 and 9 which consists of eight blades and enlaces a central round pore. It provides the key arginine residue fundamental for substrate fixation which is located in the R-segment, at the interconnecting loop between blades 1 and 2. Ligand binding to DPP8/9 induces a rearrangement at the active site through a disorder-order transition in a loop segment which includes the key arginine residue and partially folds in an alpha-helix (R-helix). DPP8 and DPP9 play a role in the immune system and in preadipocyte differentiation. DPP9 is also essential for neonatal survival and plays a role in antigen maturation, cell migration, and cell adhesion.
The actual alignment was detected with superfamily member pfam19520:
Pssm-ID: 466112 Cd Length: 155 Bit Score: 173.99 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 30 DISDSTEVVEMEDVP--SQFFVEKHSWDGLRDIIHNSRMYSGMVINKAPHDFQFVQKHDESGPHSHRLYYLGMPYGSREN 107
Cdd:pfam19520 25 ETAECEENVESEDSPklEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENREN 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221219063 108 SLLYSEIPKKIRKEALLVLSWKQMLDHFQATPHHGVYSREEELLRERKRLG 158
Cdd:pfam19520 105 TLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DPPIV_N |
pfam00930 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
171-592 |
1.74e-82 |
|
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.
Pssm-ID: 395744 [Multi-domain] Cd Length: 352 Bit Score: 269.19 E-value: 1.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 171 SGLFLFQASNSLFYCRDGGHNGFIQAaPMKPMEIKTQCS--GIRMDPKISPgDPSFIAFINNNDLWVTNIETAEERRLTf 248
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIY-DLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 249 cHKGLNNVkedpkSAGVATFVIQEE-FDRFTGYWWSPaatedaDGGKtlqLLYEEVDESEVEIIHVPSPALEER--KADV 325
Cdd:pfam00930 80 -SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSP------DGSR---LAFLRFDESEVPIITLPYYTDEGPgpEVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 326 YRYPRTGSKNPQISLKLAEIRTdqqGKMISaqnkelVLPFTTLFPGVEYIARAGWTKDGKFaWAVLLDRSQQKLQLVLLp 405
Cdd:pfam00930 145 IKYPKAGAPNPTVELFVYDLAS---GKTVE------VVPPDDLSDADYYITRVKWVPDGKL-LVQWLNRDQNRLKVVLC- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 406 palfipvsvdDPQWEEHVeampegvqpfIIYEEITDIWINVHDIFYPFIQTSNdkiSFLWVNESQtGFCHLYRITSLLKp 485
Cdd:pfam00930 214 ----------DAETGRTV----------VILEETSDGWVELHQDPHFIKRDGS---GFLWISERD-GYNHLYLYDLDGK- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 486 gchqwsreySPSeddfkcsteeevALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYESPGEIVRLTK 565
Cdd:pfam00930 269 ---------SPI------------QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTD 323
|
410 420
....*....|....*....|....*....
gi 221219063 566 PGFSH--SCSVSQNFDMFISHYSNVSTPP 592
Cdd:pfam00930 324 DSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
684-885 |
8.83e-64 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 213.63 E-value: 8.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 684 LRLNTLASLGYAVVVIDGRGSCQRGLKFEGALKNKMGQVEIEDQVEGLQFVAEKYkFIDLSRVAIHGWSYGGFLSLMGLI 763
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 764 HRPNIFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVDKLPNEPnRLLILHGFLDENVHFFH 837
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221219063 838 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEIMLLYFLQQHL 885
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
634-885 |
6.58e-57 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 195.62 E-value: 6.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 634 SFPASSGFRLYGMLYKPhnlKPGKKHPTILFVYGGPQVQlvNNSYkgvkYLRLNTLASLGYAVVVIDGRGscqrglkfEG 713
Cdd:COG1506 1 TFKSADGTTLPGWLYLP---ADGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 714 ALKNKMGQVEIEDQVEGLQFVAEKyKFIDLSRVAIHGWSYGGFLSLMGLIHRPNIFKVAIAGAPVTVWMAYDTG---YTE 790
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 791 RYMDVPENNQQGYEAGSVALHVDKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESG 870
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219
|
250
....*....|....*
gi 221219063 871 EHYEIMlLYFLQQHL 885
Cdd:COG1506 220 DYLERI-LDFLDRHL 233
|
|
| Dpp_8_9_N |
pfam19520 |
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ... |
30-158 |
3.01e-50 |
|
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are similar to DPP4, consisting of one N-terminal beta-propeller and a C-terminal alpha/beta hydrolase domain, which form a functional homodimer. This entry represents the N-terminal beta-propeller of DPP8 and 9 which consists of eight blades and enlaces a central round pore. It provides the key arginine residue fundamental for substrate fixation which is located in the R-segment, at the interconnecting loop between blades 1 and 2. Ligand binding to DPP8/9 induces a rearrangement at the active site through a disorder-order transition in a loop segment which includes the key arginine residue and partially folds in an alpha-helix (R-helix). DPP8 and DPP9 play a role in the immune system and in preadipocyte differentiation. DPP9 is also essential for neonatal survival and plays a role in antigen maturation, cell migration, and cell adhesion.
Pssm-ID: 466112 Cd Length: 155 Bit Score: 173.99 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 30 DISDSTEVVEMEDVP--SQFFVEKHSWDGLRDIIHNSRMYSGMVINKAPHDFQFVQKHDESGPHSHRLYYLGMPYGSREN 107
Cdd:pfam19520 25 ETAECEENVESEDSPklEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENREN 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221219063 108 SLLYSEIPKKIRKEALLVLSWKQMLDHFQATPHHGVYSREEELLRERKRLG 158
Cdd:pfam19520 105 TLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DPPIV_N |
pfam00930 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
171-592 |
1.74e-82 |
|
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.
Pssm-ID: 395744 [Multi-domain] Cd Length: 352 Bit Score: 269.19 E-value: 1.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 171 SGLFLFQASNSLFYCRDGGHNGFIQAaPMKPMEIKTQCS--GIRMDPKISPgDPSFIAFINNNDLWVTNIETAEERRLTf 248
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIY-DLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 249 cHKGLNNVkedpkSAGVATFVIQEE-FDRFTGYWWSPaatedaDGGKtlqLLYEEVDESEVEIIHVPSPALEER--KADV 325
Cdd:pfam00930 80 -SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSP------DGSR---LAFLRFDESEVPIITLPYYTDEGPgpEVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 326 YRYPRTGSKNPQISLKLAEIRTdqqGKMISaqnkelVLPFTTLFPGVEYIARAGWTKDGKFaWAVLLDRSQQKLQLVLLp 405
Cdd:pfam00930 145 IKYPKAGAPNPTVELFVYDLAS---GKTVE------VVPPDDLSDADYYITRVKWVPDGKL-LVQWLNRDQNRLKVVLC- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 406 palfipvsvdDPQWEEHVeampegvqpfIIYEEITDIWINVHDIFYPFIQTSNdkiSFLWVNESQtGFCHLYRITSLLKp 485
Cdd:pfam00930 214 ----------DAETGRTV----------VILEETSDGWVELHQDPHFIKRDGS---GFLWISERD-GYNHLYLYDLDGK- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 486 gchqwsreySPSeddfkcsteeevALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYESPGEIVRLTK 565
Cdd:pfam00930 269 ---------SPI------------QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTD 323
|
410 420
....*....|....*....|....*....
gi 221219063 566 PGFSH--SCSVSQNFDMFISHYSNVSTPP 592
Cdd:pfam00930 324 DSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
684-885 |
8.83e-64 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 213.63 E-value: 8.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 684 LRLNTLASLGYAVVVIDGRGSCQRGLKFEGALKNKMGQVEIEDQVEGLQFVAEKYkFIDLSRVAIHGWSYGGFLSLMGLI 763
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 764 HRPNIFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVDKLPNEPnRLLILHGFLDENVHFFH 837
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221219063 838 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEIMLLYFLQQHL 885
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
634-885 |
6.58e-57 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 195.62 E-value: 6.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 634 SFPASSGFRLYGMLYKPhnlKPGKKHPTILFVYGGPQVQlvNNSYkgvkYLRLNTLASLGYAVVVIDGRGscqrglkfEG 713
Cdd:COG1506 1 TFKSADGTTLPGWLYLP---ADGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 714 ALKNKMGQVEIEDQVEGLQFVAEKyKFIDLSRVAIHGWSYGGFLSLMGLIHRPNIFKVAIAGAPVTVWMAYDTG---YTE 790
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 791 RYMDVPENNQQGYEAGSVALHVDKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESG 870
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219
|
250
....*....|....*
gi 221219063 871 EHYEIMlLYFLQQHL 885
Cdd:COG1506 220 DYLERI-LDFLDRHL 233
|
|
| Dpp_8_9_N |
pfam19520 |
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ... |
30-158 |
3.01e-50 |
|
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are similar to DPP4, consisting of one N-terminal beta-propeller and a C-terminal alpha/beta hydrolase domain, which form a functional homodimer. This entry represents the N-terminal beta-propeller of DPP8 and 9 which consists of eight blades and enlaces a central round pore. It provides the key arginine residue fundamental for substrate fixation which is located in the R-segment, at the interconnecting loop between blades 1 and 2. Ligand binding to DPP8/9 induces a rearrangement at the active site through a disorder-order transition in a loop segment which includes the key arginine residue and partially folds in an alpha-helix (R-helix). DPP8 and DPP9 play a role in the immune system and in preadipocyte differentiation. DPP9 is also essential for neonatal survival and plays a role in antigen maturation, cell migration, and cell adhesion.
Pssm-ID: 466112 Cd Length: 155 Bit Score: 173.99 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 30 DISDSTEVVEMEDVP--SQFFVEKHSWDGLRDIIHNSRMYSGMVINKAPHDFQFVQKHDESGPHSHRLYYLGMPYGSREN 107
Cdd:pfam19520 25 ETAECEENVESEDSPklEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENREN 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221219063 108 SLLYSEIPKKIRKEALLVLSWKQMLDHFQATPHHGVYSREEELLRERKRLG 158
Cdd:pfam19520 105 TLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
628-872 |
7.97e-12 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 65.76 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 628 IPPEIFSFPASSGFRLYGMLYKPhnlKPGKKHPTILFV--YGGpqvqlVNNSYKGVkylrLNTLASLGYAVVVIDGRGSc 705
Cdd:COG0412 1 MTTETVTIPTPDGVTLPGYLARP---AGGGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDLYGR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 706 QRGLKFEGALKNKMGQVEIEDQVE----GLQFVAEKyKFIDLSRVAIHGWSYGGFLSLMGLIHRPNIfK--VAIAGAPVT 779
Cdd:COG0412 68 GGPGDDPDEARALMGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 780 vwmaydtgyterymdvpennqqgyeagsvALHVDKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPN 859
Cdd:COG0412 146 -----------------------------DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPG 196
|
250
....*....|...
gi 221219063 860 ERHSIRCPESGEH 872
Cdd:COG0412 197 AGHGFTNPGRPRY 209
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
647-864 |
2.65e-09 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 58.44 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 647 LYKPHNLKPGKKHPTILFVYGG------PQVQLVNnsyKGVKYLRLNTLASLGYAVVVidgrGSCQRGLKFEGAlknkmg 720
Cdd:COG4099 37 LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCPEDDYWSDT------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 721 qvEIEDQVEGL-QFVAEKYKfIDLSRVAIHGWSYGGFLSLMGLIHRPNIFK--VAIAGAPvtvwmayDTGYTERYMDVPe 797
Cdd:COG4099 104 --KALDAVLALlDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG-------DPANAANLKKVP- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221219063 798 nnqqgyeagsvalhvdklpnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSI 864
Cdd:COG4099 173 ------------------------VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
631-779 |
8.34e-09 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 57.23 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 631 EIFSFPASSGFRLYGMLYKPHNlkPGKKHPTILFVYGgpqvqlvnnsYKGVKYLRL---NTLASLGYAVVVIDGRG---S 704
Cdd:COG1073 11 EDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFDYRGygeS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221219063 705 cqrglkfEGALKNkMGQVEIEDQVEGLQFVaEKYKFIDLSRVAIHGWSYGGFLSLMGLIHRPNIfKVAIAGAPVT 779
Cdd:COG1073 79 -------EGEPRE-EGSPERRDARAAVDYL-RTLPGVDPERIGLLGISLGGGYALNAAATDPRV-KAVILDSPFT 143
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
629-864 |
2.21e-07 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 52.70 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 629 PPEIFSFPASSGFRLYGMLYKPhnlkPGKKHPTILFVYGGpqvqlvnnSYKGVKYLRL-NTLASLGYAVVVIDGRGScqr 707
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGL--------GEHSGRYAELaEALAAAGYAVLAFDLRGH--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 708 glkfeGALKNKMGQVE-----IEDQVEGLQFVAEKYKfidlSRVAIHGWSYGGFLSLMGLIHRPNIFKVAIAGAPVTVWM 782
Cdd:COG2267 67 -----GRSDGPRGHVDsfddyVDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 783 AYdTGYTERYMdvpennqQGYEAGSVALHVDkLPnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGkpyQLQIYPNERH 862
Cdd:COG2267 138 PL-LGPSARWL-------RALRLAEALARID-VP-----VLVLHGGADRVVPPEAARRLAARLSPDV---ELVLLPGARH 200
|
..
gi 221219063 863 SI 864
Cdd:COG2267 201 EL 202
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
618-785 |
1.21e-04 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 45.69 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 618 MEATGCRPDYIPPEIFsFPASSGFRLYGMLYKPHNlkPGKKHPTILF--VYGgpqvqlVNNSYKGVKYLRLNTLASLGYA 695
Cdd:COG2936 1 MKRAAPADVYVKEDVW-IPMRDGVRLAADIYRPKD--AEGPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 696 VVVIDGRG---ScqrglkfEGALKNkMGQVEIEDQVEGLQFVAEkykfIDLS--RVAIHGWSYGGFLSLMGLIHRPNIFK 770
Cdd:COG2936 72 VVVQDVRGtggS-------EGEFDP-YRVDEQTDGYDTIDWLAK----QPWSngKVGMIGISYGGFTQLAAAADRPPALK 139
|
170
....*....|....*
gi 221219063 771 VAIAGAPVTVWMAYD 785
Cdd:COG2936 140 AIVPQAPTSDRYDDD 154
|
|
| Peptidase_S15 |
pfam02129 |
X-Pro dipeptidyl-peptidase (S15 family); |
640-784 |
2.38e-04 |
|
X-Pro dipeptidyl-peptidase (S15 family);
Pssm-ID: 396621 [Multi-domain] Cd Length: 264 Bit Score: 43.87 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 640 GFRLYGMLYKPhnLKPGKKHPTILF--VYGGP--QVQLVNNSYKGVKYLRLntlaslGYAVVVIDGRGSCQRGLKFEGal 715
Cdd:pfam02129 2 GVRLAADIYRP--TKTGGPVPALLTrsPYGARrdGASDLALAHPEWEFAAR------GYAVVYQDVRGTGGSEGVFTV-- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219063 716 knkMGQVEIEDQVEGLQFVAEKYKFIDlsRVAIHGWSYGGFLSLMGLIHRPNIFKVAIAGAPVTVWMAY 784
Cdd:pfam02129 72 ---GGPQEAADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDY 135
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
631-781 |
4.67e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 43.07 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 631 EIFSFPASSGFRLYgMLYKPHNLKPGKKHPTILFVYGGPQ--VQLVNNSykgvkylRLNTLA-SLGYAVVVIDG-RGSCQ 706
Cdd:COG3509 26 FERTFTVGGGTRTY-RLYVPAGYDGGAPLPLVVALHGCGGsaADFAAGT-------GLNALAdREGFIVVYPEGtGRAPG 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219063 707 RGLKFEGALKNKMGQVEIE--DQVegLQFVAEKYKfIDLSRVAIHGWSYGGFLSLMGLIHRPNIFK--VAIAGAPVTVW 781
Cdd:COG3509 98 RCWNWFDGRDQRRGRDDVAfiAAL--VDDLAARYG-IDPKRVYVTGLSAGGAMAYRLACEYPDVFAavAPVAGLPYGAA 173
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
696-782 |
4.09e-03 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 40.22 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 696 VVVIDGRGSCQRGlkFEGALKNKMGQVEIEDqVegLQFVAEKYKFI-DLSRVAIHGWSYGGFLSLMGLIHRPNIFKVAIA 774
Cdd:COG2382 152 VVMPDGGDGGDRG--TEGPGNDAFERFLAEE-L--IPFVEKNYRVSaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226
|
....*...
gi 221219063 775 GAPVTVWM 782
Cdd:COG2382 227 FSGSFWWP 234
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
689-761 |
6.17e-03 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 39.71 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219063 689 LASLGYAVVVIDGRGSCQRGLK-FEGALKNKMGQVEIEDQVEGLQFV-----------AEKYKFIDLSRVAIHGWSYGGF 756
Cdd:COG4188 85 LASHGYVVAAPDHPGSNAADLSaALDGLADALDPEELWERPLDLSFVldqllalnksdPPLAGRLDLDRIGVIGHSLGGY 164
|
....*..
gi 221219063 757 --LSLMG 761
Cdd:COG4188 165 taLALAG 171
|
|
| |
