|
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 ... |
229-653 |
2.03e-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: 267.26 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 229 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 306
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 307 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 383
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 384 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 463
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 464 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 543
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 544 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 623
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 768004617 624 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 653
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
745-946 |
1.02e-63 |
|
Prolyl oligopeptidase family; :
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 214.02 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 745 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 824
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 825 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 898
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768004617 899 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 946
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 ... |
107-218 |
1.22e-47 |
|
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: 166.67 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 107 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 186
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 768004617 187 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 218
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 ... |
229-653 |
2.03e-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: 267.26 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 229 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 306
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 307 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 383
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 384 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 463
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 464 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 543
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 544 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 623
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 768004617 624 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 653
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
745-946 |
1.02e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 214.02 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 745 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 824
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 825 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 898
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768004617 899 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 946
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
695-946 |
8.55e-55 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 189.84 E-value: 8.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 695 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 774
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 775 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 851
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 852 RYMDVPENNQHGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcPESG 931
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 768004617 932 EHYEVTLLHFLQEYL 946
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 ... |
107-218 |
1.22e-47 |
|
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: 166.67 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 107 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 186
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 768004617 187 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 218
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 ... |
229-653 |
2.03e-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: 267.26 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 229 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 306
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 307 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 383
Cdd:pfam00930 80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 384 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 463
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 464 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 543
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 544 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 623
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 768004617 624 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 653
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
745-946 |
1.02e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 214.02 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 745 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 824
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 825 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 898
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768004617 899 TNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL 946
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
695-946 |
8.55e-55 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 189.84 E-value: 8.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 695 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 774
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 775 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 851
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 852 RYMDVPENNQHGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcPESG 931
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 768004617 932 EHYEVTLLHFLQEYL 946
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 ... |
107-218 |
1.22e-47 |
|
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: 166.67 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 107 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 186
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 768004617 187 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 218
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
692-933 |
8.89e-10 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 59.98 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 692 EIFHFHTRSDVRLYGMIYKPHAlqpGKKHPTVLFV--YGGpqvqlVNNSFKGIkylrLNTLASLGYAVVVIDGRGScQRG 769
Cdd:COG0412 4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDLYGR-GGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 770 LRFEGALKNQMGQVEIEDQVE----GLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVfK--VAIAGAPVTvwm 843
Cdd:COG0412 71 GDDPDEARALMGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 844 aydtgyterymdvpennqhgyeagsvALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERH 923
Cdd:COG0412 146 --------------------------DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199
|
250
....*....|
gi 768004617 924 SIRCPESGEH 933
Cdd:COG0412 200 GFTNPGRPRY 209
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
694-925 |
1.87e-08 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 56.13 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 694 FHFHTRSDVRLYGmIYKPHALQPGKKHPTVLFVYGG------PQVQLVNnsfKGIKYLRLNTLASLGYAVVVidgrGSCQ 767
Cdd:COG4099 24 FTDPSDGDTLPYR-LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 768 RGLRFEGAlknqmgqvEIEDQVEGL-QFVAEKYGfIDLSRVAIHGWSYGGFLSLMGLIHKPQVFK--VAIAGAPvtvwma 844
Cdd:COG4099 96 EDDYWSDT--------KALDAVLALlDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 845 yDTGYTERYMDVPennqhgyeagsvalhveklpnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHS 924
Cdd:COG4099 161 -DPANAANLKKVP-------------------------VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHN 214
|
.
gi 768004617 925 I 925
Cdd:COG4099 215 S 215
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
685-816 |
1.71e-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: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 685 PPDYVPPEIFHFHTRSDVRLYGMIYKPHAlqPGKKHPTVLFVYGgpqvqlvnnsFKGIKYLRL---NTLASLGYAVVVID 761
Cdd:COG1073 4 PSDKVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFD 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004617 762 GRG---ScqrglrfEGALKnQMGQVEIEDQVEGLQFVaEKYGFIDLSRVAIHGWSYGG 816
Cdd:COG1073 72 YRGygeS-------EGEPR-EEGSPERRDARAAVDYL-RTLPGVDPERIGLLGISLGG 120
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
690-944 |
1.82e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 50.00 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 690 PPEIFHFHTRSDVRLYGMIYKPhalqPGKKHPTVLFVYGGpqvqlvnNSFKGiKYLRL-NTLASLGYAVVVIDGRG---S 765
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGL-------GEHSG-RYAELaEALAAAGYAVLAFDLRGhgrS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 766 CQRGLRFEGAlknqmgQVEIEDQVEGLQFVAEKYGfidlSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPvtvwmay 845
Cdd:COG2267 70 DGPRGHVDSF------DDYVDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 846 dtgyteRYMDVPEN--NQHGYEAGSVALHVEKL--PnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGkpyQLQIYPNE 921
Cdd:COG2267 133 ------AYRADPLLgpSARWLRALRLAEALARIdvP-----VLVLHGGADRVVPPEAARRLAARLSPDV---ELVLLPGA 198
|
250 260
....*....|....*....|....
gi 768004617 922 RHSI-RCPESGEHYEvTLLHFLQE 944
Cdd:COG2267 199 RHELlNEPAREEVLA-AILAWLER 221
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
698-846 |
1.23e-05 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 49.15 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 698 TRSDVRLYGMIYKPHALQpgKKHPTVLF--VYGgpqvqlVNNSFKGIKYLRLNTLASLGYAVVVIDGRGscqrglRF--E 773
Cdd:COG2936 19 MRDGVRLAADIYRPKDAE--GPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRG------TGgsE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768004617 774 GALKNqMGQVEIEDQVEGLQFVAEkygfIDLS--RVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYD 846
Cdd:COG2936 85 GEFDP-YRVDEQTDGYDTIDWLAK----QPWSngKVGMIGISYGGFTQLAAAADRPPALKAIVPQAPTSDRYDDD 154
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
750-946 |
2.63e-05 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 46.05 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 750 LASLGYAVVVIDGRGSCQRG------LRFEGALKNQMGQVEIEDQVEglQFVAE---KYGfIDLSRVAIHGWSYGGFLSL 820
Cdd:COG0400 28 LALPGAAVLAPRAPVPEGPGgrawfdLSFLEGREDEEGLAAAAEALA--AFIDEleaRYG-IDPERIVLAGFSQGAAMAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 821 MGLIHKPQVFKVAIAgapvtvwmaydtgyteryMdvpennqHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTN 900
Cdd:COG0400 105 SLALRRPELLAGVVA------------------L-------SGYLPGEEALPAPEAALAGTPVFLAHGTQDPVIPVERAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768004617 901 FLVSQLIRAGKPYQLQIYPNErHSIrCPEsgehyEVT-LLHFLQEYL 946
Cdd:COG0400 160 EAAEALEAAGADVTYREYPGG-HEI-SPE-----ELAdARAWLAERL 199
|
|
| Peptidase_S15 |
pfam02129 |
X-Pro dipeptidyl-peptidase (S15 family); |
702-845 |
2.33e-04 |
|
X-Pro dipeptidyl-peptidase (S15 family);
Pssm-ID: 396621 [Multi-domain] Cd Length: 264 Bit Score: 43.87 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 702 VRLYGMIYKPhaLQPGKKHPTVLF--VYGGPqvqlvnNSFKGIKYLRLN--TLASLGYAVVVIDGRGscQRGLrfEGALK 777
Cdd:pfam02129 3 VRLAADIYRP--TKTGGPVPALLTrsPYGAR------RDGASDLALAHPewEFAARGYAVVYQDVRG--TGGS--EGVFT 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004617 778 NQMGQvEIEDQVEGLQFVAEKYGFIDlsRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAY 845
Cdd:pfam02129 71 VGGPQ-EAADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDY 135
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
750-822 |
3.20e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 43.94 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 750 LASLGYAVVVIDGRGSCQRGL-RFEGALKNQMGQVEIEDQVEGLQFV-----------AEKYGFIDLSRVAIHGWSYGGF 817
Cdd:COG4188 85 LASHGYVVAAPDHPGSNAADLsAALDGLADALDPEELWERPLDLSFVldqllalnksdPPLAGRLDLDRIGVIGHSLGGY 164
|
....*..
gi 768004617 818 --LSLMG 822
Cdd:COG4188 165 taLALAG 171
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
708-842 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004617 708 IYKPHALQPGKKHPTVLFVYGGPQ--VQLVNNSfkgikylRLNTLA-SLGYAVVVIDG-RGSCQRGLRFEGALKNQMGQV 783
Cdd:COG3509 41 LYVPAGYDGGAPLPLVVALHGCGGsaADFAAGT-------GLNALAdREGFIVVYPEGtGRAPGRCWNWFDGRDQRRGRD 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004617 784 EIE--DQVegLQFVAEKYGfIDLSRVAIHGWSYGGFLSL-MGLIHkPQVFK--VAIAGAPVTVW 842
Cdd:COG3509 114 DVAfiAAL--VDDLAARYG-IDPKRVYVTGLSAGGAMAYrLACEY-PDVFAavAPVAGLPYGAA 173
|
|
|