|
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 ... |
175-599 |
2.79e-81 |
|
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: 266.11 E-value: 2.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 1860299491 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
691-892 |
2.08e-63 |
|
Prolyl oligopeptidase family;
:
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 212.47 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 844
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860299491 845 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 892
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 ... |
53-164 |
8.36e-48 |
|
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: 167.06 E-value: 8.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 1860299491 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 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 ... |
175-599 |
2.79e-81 |
|
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: 266.11 E-value: 2.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 1860299491 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
691-892 |
2.08e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 212.47 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 844
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860299491 845 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 892
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
641-892 |
1.02e-54 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 189.46 E-value: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 641 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 720
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 721 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 797
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 798 RYMDVPENNQHGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcPESG 877
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 1860299491 878 EHYEVTLLHFLQEYL 892
Cdd:COG1506 219 PDYLERILDFLDRHL 233
|
|
| Dpp_8_9_N |
pfam19520 |
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ... |
53-164 |
8.36e-48 |
|
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: 167.06 E-value: 8.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 1860299491 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 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 ... |
175-599 |
2.79e-81 |
|
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: 266.11 E-value: 2.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 1860299491 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
691-892 |
2.08e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 212.47 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 844
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860299491 845 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 892
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
641-892 |
1.02e-54 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 189.46 E-value: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 641 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 720
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 721 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 797
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 798 RYMDVPENNQHGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcPESG 877
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 1860299491 878 EHYEVTLLHFLQEYL 892
Cdd:COG1506 219 PDYLERILDFLDRHL 233
|
|
| Dpp_8_9_N |
pfam19520 |
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ... |
53-164 |
8.36e-48 |
|
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: 167.06 E-value: 8.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 1860299491 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
638-879 |
8.30e-10 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 59.98 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 638 EIFHFHTRSDVRLYGMIYKPHAlqpGKKHPTVLFV--YGGpqvqlVNNSFKGIkylrLNTLASLGYAVVVIDGRGScQRG 715
Cdd:COG0412 4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDLYGR-GGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 716 LRFEGALKNQMGQVEIEDQVE----GLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVfK--VAIAGAPVTvwm 789
Cdd:COG0412 71 GDDPDEARALMGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 790 aydtgyterymdvpennqhgyeagsvALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERH 869
Cdd:COG0412 146 --------------------------DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199
|
250
....*....|
gi 1860299491 870 SIRCPESGEH 879
Cdd:COG0412 200 GFTNPGRPRY 209
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
640-871 |
1.83e-08 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 56.13 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 640 FHFHTRSDVRLYGmIYKPHALQPGKKHPTVLFVYGG------PQVQLVNnsfKGIKYLRLNTLASLGYAVVVidgrGSCQ 713
Cdd:COG4099 24 FTDPSDGDTLPYR-LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 714 RGLRFEGAlknqmgqvEIEDQVEGL-QFVAEKYGfIDLSRVAIHGWSYGGFLSLMGLIHKPQVFK--VAIAGAPvtvwma 790
Cdd:COG4099 96 EDDYWSDT--------KALDAVLALlDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 791 yDTGYTERYMDVPennqhgyeagsvalhveklpnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHS 870
Cdd:COG4099 161 -DPANAANLKKVP-------------------------VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHN 214
|
.
gi 1860299491 871 I 871
Cdd:COG4099 215 S 215
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
631-762 |
1.86e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 53.38 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 631 PPDYVPPEIFHFHTRSDVRLYGMIYKPHAlqPGKKHPTVLFVYGgpqvqlvnnsFKGIKYLRL---NTLASLGYAVVVID 707
Cdd:COG1073 4 PSDKVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFD 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860299491 708 GRG---ScqrglrfEGALKnQMGQVEIEDQVEGLQFVaEKYGFIDLSRVAIHGWSYGG 762
Cdd:COG1073 72 YRGygeS-------EGEPR-EEGSPERRDARAAVDYL-RTLPGVDPERIGLLGISLGG 120
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
636-890 |
1.68e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 50.00 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 636 PPEIFHFHTRSDVRLYGMIYKPhalqPGKKHPTVLFVYGGpqvqlvnNSFKGiKYLRL-NTLASLGYAVVVIDGRG---S 711
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGL-------GEHSG-RYAELaEALAAAGYAVLAFDLRGhgrS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 712 CQRGLRFEGAlknqmgQVEIEDQVEGLQFVAEKYGfidlSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPvtvwmay 791
Cdd:COG2267 70 DGPRGHVDSF------DDYVDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 792 dtgyteRYMDVPEN--NQHGYEAGSVALHVEKL--PnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGkpyQLQIYPNE 867
Cdd:COG2267 133 ------AYRADPLLgpSARWLRALRLAEALARIdvP-----VLVLHGGADRVVPPEAARRLAARLSPDV---ELVLLPGA 198
|
250 260
....*....|....*....|....
gi 1860299491 868 RHSI-RCPESGEHYEvTLLHFLQE 890
Cdd:COG2267 199 RHELlNEPAREEVLA-AILAWLER 221
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
644-792 |
1.05e-05 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 49.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 644 TRSDVRLYGMIYKPHALQpgKKHPTVLF--VYGgpqvqlVNNSFKGIKYLRLNTLASLGYAVVVIDGRGscqrglRF--E 719
Cdd:COG2936 19 MRDGVRLAADIYRPKDAE--GPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRG------TGgsE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299491 720 GALKNqMGQVEIEDQVEGLQFVAEkygfIDLS--RVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYD 792
Cdd:COG2936 85 GEFDP-YRVDEQTDGYDTIDWLAK----QPWSngKVGMIGISYGGFTQLAAAADRPPALKAIVPQAPTSDRYDDD 154
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
696-892 |
2.10e-05 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 46.44 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 696 LASLGYAVVVIDGRGSCQRG------LRFEGALKNQMGQVEIEDQVEglQFVAE---KYGfIDLSRVAIHGWSYGGFLSL 766
Cdd:COG0400 28 LALPGAAVLAPRAPVPEGPGgrawfdLSFLEGREDEEGLAAAAEALA--AFIDEleaRYG-IDPERIVLAGFSQGAAMAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 767 MGLIHKPQVFKVAIAgapvtvwmaydtgyteryMdvpennqHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTN 846
Cdd:COG0400 105 SLALRRPELLAGVVA------------------L-------SGYLPGEEALPAPEAALAGTPVFLAHGTQDPVIPVERAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1860299491 847 FLVSQLIRAGKPYQLQIYPNErHSIrCPEsgehyEVT-LLHFLQEYL 892
Cdd:COG0400 160 EAAEALEAAGADVTYREYPGG-HEI-SPE-----ELAdARAWLAERL 199
|
|
| Peptidase_S15 |
pfam02129 |
X-Pro dipeptidyl-peptidase (S15 family); |
648-791 |
2.10e-04 |
|
X-Pro dipeptidyl-peptidase (S15 family);
Pssm-ID: 396621 [Multi-domain] Cd Length: 264 Bit Score: 43.87 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 648 VRLYGMIYKPhaLQPGKKHPTVLF--VYGGPqvqlvnNSFKGIKYLRLN--TLASLGYAVVVIDGRGscQRGLrfEGALK 723
Cdd:pfam02129 3 VRLAADIYRP--TKTGGPVPALLTrsPYGAR------RDGASDLALAHPewEFAARGYAVVYQDVRG--TGGS--EGVFT 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860299491 724 NQMGQvEIEDQVEGLQFVAEKYGFIDlsRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAY 791
Cdd:pfam02129 71 VGGPQ-EAADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDY 135
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
696-768 |
2.98e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 43.94 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 696 LASLGYAVVVIDGRGSCQRGL-RFEGALKNQMGQVEIEDQVEGLQFV-----------AEKYGFIDLSRVAIHGWSYGGF 763
Cdd:COG4188 85 LASHGYVVAAPDHPGSNAADLsAALDGLADALDPEELWERPLDLSFVldqllalnksdPPLAGRLDLDRIGVIGHSLGGY 164
|
....*..
gi 1860299491 764 --LSLMG 768
Cdd:COG4188 165 taLALAG 171
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
654-788 |
2.93e-03 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 40.76 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 654 IYKPHALQPGKKHPTVLFVYGGPQ--VQLVNNSfkgikylRLNTLA-SLGYAVVVIDG-RGSCQRGLRFEGALKNQMGQV 729
Cdd:COG3509 41 LYVPAGYDGGAPLPLVVALHGCGGsaADFAAGT-------GLNALAdREGFIVVYPEGtGRAPGRCWNWFDGRDQRRGRD 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860299491 730 EIE--DQVegLQFVAEKYGfIDLSRVAIHGWSYGGFLSL-MGLIHkPQVFK--VAIAGAPVTVW 788
Cdd:COG3509 114 DVAfiAAL--VDDLAARYG-IDPKRVYVTGLSAGGAMAYrLACEY-PDVFAavAPVAGLPYGAA 173
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
667-793 |
9.92e-03 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 38.64 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299491 667 PTVLFVYGGPQVqlVNNSFKGIKYLrlntlASLGYAVVVIDGRGSCQrglrfEGALKNQmGQVEIEDQVEGLQFVAEKYG 746
Cdd:pfam00561 1 PPVLLLHGLPGS--SDLWRKLAPAL-----ARDGFRVIALDLRGFGK-----SSRPKAQ-DDYRTDDLAEDLEYILEALG 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1860299491 747 fidLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDT 793
Cdd:pfam00561 68 ---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDE 111
|
|
| |
