|
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 ... |
145-569 |
6.36e-85 |
|
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: 275.35 E-value: 6.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 145 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 222
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 223 fcHQGSAGVldnpkSAGVATFVIQEE-FDRFTGCWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 299
Cdd:pfam00930 80 --SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 300 DSYRYPRTGSKNPKIALKLAELqtdHQGKIVSscekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQRLQLVL 379
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 380 LPPALFIPAVESEaqrqaaaravpknvqpfviyeEVTNVWINVHDIFHPFPQaegqQDFCFLRANEcKTGFCHLYRVtve 459
Cdd:pfam00930 213 CDAETGRTVVILE---------------------ETSDGWVELHQDPHFIKR----DGSGFLWISE-RDGYNHLYLY--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 460 lktkdydwteplsptEDEFKCPIkeevALTSGEWEVlsrhGSKIWVNEQTKLVYFQGTKDTPLEHHLYVVSYESAGEIVR 539
Cdd:pfam00930 264 ---------------DLDGKSPI----QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 255003757 540 LTTLGFSH--SCSMSQSFDMFVSHYSSVSTPP 569
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
661-862 |
4.20e-63 |
|
Prolyl oligopeptidase family;
:
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 211.32 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 661 LRLNTLASLGYAVVVIDGRGSCQRGLHFEGALKNQMGQVEIEDQVEGLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 740
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 741 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 814
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255003757 815 TNFLVSQLIRAGKPYQLQIYPNERHSIRCRESGEHYEVTLLHFLQEHL 862
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 ... |
23-134 |
3.63e-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: 165.13 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 23 FCVQKHSWDGLRSIIHGSRKSSGLIVSKAPHDFQFVQKPDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 102
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 255003757 103 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 134
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 ... |
145-569 |
6.36e-85 |
|
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: 275.35 E-value: 6.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 145 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 222
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 223 fcHQGSAGVldnpkSAGVATFVIQEE-FDRFTGCWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 299
Cdd:pfam00930 80 --SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 300 DSYRYPRTGSKNPKIALKLAELqtdHQGKIVSscekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQRLQLVL 379
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 380 LPPALFIPAVESEaqrqaaaravpknvqpfviyeEVTNVWINVHDIFHPFPQaegqQDFCFLRANEcKTGFCHLYRVtve 459
Cdd:pfam00930 213 CDAETGRTVVILE---------------------ETSDGWVELHQDPHFIKR----DGSGFLWISE-RDGYNHLYLY--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 460 lktkdydwteplsptEDEFKCPIkeevALTSGEWEVlsrhGSKIWVNEQTKLVYFQGTKDTPLEHHLYVVSYESAGEIVR 539
Cdd:pfam00930 264 ---------------DLDGKSPI----QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 255003757 540 LTTLGFSH--SCSMSQSFDMFVSHYSSVSTPP 569
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
661-862 |
4.20e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 211.32 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 661 LRLNTLASLGYAVVVIDGRGSCQRGLHFEGALKNQMGQVEIEDQVEGLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 740
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 741 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 814
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255003757 815 TNFLVSQLIRAGKPYQLQIYPNERHSIRCRESGEHYEVTLLHFLQEHL 862
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
611-862 |
1.30e-55 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 191.77 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 611 HFHTRADVQLYGMIYKPHtlqPGRKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglhfEG 690
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 691 ALKNQMGQVEIEDQVEGLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 767
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 768 RYMDVPENNQQGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcRESG 847
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 255003757 848 EHYEVTLLHFLQEHL 862
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 ... |
23-134 |
3.63e-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: 165.13 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 23 FCVQKHSWDGLRSIIHGSRKSSGLIVSKAPHDFQFVQKPDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 102
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 255003757 103 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 134
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 ... |
145-569 |
6.36e-85 |
|
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: 275.35 E-value: 6.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 145 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 222
Cdd:pfam00930 1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 223 fcHQGSAGVldnpkSAGVATFVIQEE-FDRFTGCWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 299
Cdd:pfam00930 80 --SDGSDGI-----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 300 DSYRYPRTGSKNPKIALKLAELqtdHQGKIVSscekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQRLQLVL 379
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 380 LPPALFIPAVESEaqrqaaaravpknvqpfviyeEVTNVWINVHDIFHPFPQaegqQDFCFLRANEcKTGFCHLYRVtve 459
Cdd:pfam00930 213 CDAETGRTVVILE---------------------ETSDGWVELHQDPHFIKR----DGSGFLWISE-RDGYNHLYLY--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 460 lktkdydwteplsptEDEFKCPIkeevALTSGEWEVlsrhGSKIWVNEQTKLVYFQGTKDTPLEHHLYVVSYESAGEIVR 539
Cdd:pfam00930 264 ---------------DLDGKSPI----QLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
|
410 420 430
....*....|....*....|....*....|..
gi 255003757 540 LTTLGFSH--SCSMSQSFDMFVSHYSSVSTPP 569
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
661-862 |
4.20e-63 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 211.32 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 661 LRLNTLASLGYAVVVIDGRGSCQRGLHFEGALKNQMGQVEIEDQVEGLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 740
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 741 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQQGYEAGSVALHVEKLPNEPnRLLILHGFLDENVHFFH 814
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP-PLLLIHGLLDDRVPPWQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255003757 815 TNFLVSQLIRAGKPYQLQIYPNERHSIRCRESGEHYEVTLLHFLQEHL 862
Cdd:pfam00326 163 SLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYL 210
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
611-862 |
1.30e-55 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 191.77 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 611 HFHTRADVQLYGMIYKPHtlqPGRKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglhfEG 690
Cdd:COG1506 1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 691 ALKNQMGQVEIEDQVEGLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 767
Cdd:COG1506 64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 768 RYMDVPENNQQGYEAGSVALHVEKLpnePNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRcRESG 847
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKL---KTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS-GAGA 218
|
250
....*....|....*
gi 255003757 848 EHYEVTLLHFLQEHL 862
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 ... |
23-134 |
3.63e-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: 165.13 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 23 FCVQKHSWDGLRSIIHGSRKSSGLIVSKAPHDFQFVQKPDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 102
Cdd:pfam19520 44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
|
90 100 110
....*....|....*....|....*....|..
gi 255003757 103 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 134
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
608-840 |
1.67e-09 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 58.82 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 608 EIFHFHTRADVQLYGMIYKPHTlqpGRKHPTVLFV--YGGpqvqlVNNSFKGIkylrLNTLASLGYAVVVIDGRGScQRG 685
Cdd:COG0412 4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDLYGR-GGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 686 LHFEGALKNQMGQVEIEDQVE----GLQYVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVfK--VAIAGAPVTvwm 759
Cdd:COG0412 71 GDDPDEARALMGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 760 aydtgyterymdvpennqqgyeagsvALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERH 839
Cdd:COG0412 146 --------------------------DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199
|
.
gi 255003757 840 S 840
Cdd:COG0412 200 G 200
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
610-841 |
9.97e-09 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 56.90 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 610 FHFHTRADVQLYGmIYKPHTLQPGRKHPTVLFVYGG------PQVQLVNnsfKGIKYLRLNTLASLGYAVVVidgrGSCQ 683
Cdd:COG4099 24 FTDPSDGDTLPYR-LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 684 RGLHFEGAlknqmgqvEIEDQVEGL-QYVAEKYGfIDLSRVAIHGWSYGGFLSLMGLIHKPQVFK--VAIAGAPvtvwma 760
Cdd:COG4099 96 EDDYWSDT--------KALDAVLALlDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 761 yDTGYTERYMDVPennqqgyeagsvalhveklpnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHS 840
Cdd:COG4099 161 -DPANAANLKKVP-------------------------VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHN 214
|
.
gi 255003757 841 I 841
Cdd:COG4099 215 S 215
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
601-732 |
7.11e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 51.45 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 601 PPDYVPPEIFHFHTRADVQLYGMIYKPHTLQPgrKHPTVLFVYGgpqvqlvnnsFKGIKYLRL---NTLASLGYAVVVID 677
Cdd:COG1073 4 PSDKVNKEDVTFKSRDGIKLAGDLYLPAGASK--KYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFD 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 255003757 678 GRG---ScqrglhfEGALKnQMGQVEIEDQVEGLQYVaEKYGFIDLSRVAIHGWSYGG 732
Cdd:COG1073 72 YRGygeS-------EGEPR-EEGSPERRDARAAVDYL-RTLPGVDPERIGLLGISLGG 120
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
606-860 |
2.82e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 49.23 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 606 PPEIFHFHTRADVQLYGMIYKPhtlqPGRKHPTVLFVYGGpqvqlvnNSFKGiKYLRL-NTLASLGYAVVVIDGRG---S 681
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGL-------GEHSG-RYAELaEALAAAGYAVLAFDLRGhgrS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 682 CQRGLHFEGAlknqmgQVEIEDQVEGLQYVAEKYGfidlSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAY 761
Cdd:COG2267 70 DGPRGHVDSF------DDYVDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 762 dTGYTERYMdvpennqQGYEAGSVALHVeKLPnepnrLLILHGFLDENVHFFHTNFLVSQLIRAGkpyQLQIYPNERHSI 841
Cdd:COG2267 140 -LGPSARWL-------RALRLAEALARI-DVP-----VLVLHGGADRVVPPEAARRLAARLSPDV---ELVLLPGARHEL 202
|
250 260
....*....|....*....|
gi 255003757 842 -RCRESGEHYEvTLLHFLQE 860
Cdd:COG2267 203 lNEPAREEVLA-AILAWLER 221
|
|
| Peptidase_S15 |
pfam02129 |
X-Pro dipeptidyl-peptidase (S15 family); |
618-761 |
9.66e-05 |
|
X-Pro dipeptidyl-peptidase (S15 family);
Pssm-ID: 396621 [Multi-domain] Cd Length: 264 Bit Score: 45.02 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 618 VQLYGMIYKPhtLQPGRKHPTVLF--VYGGPqvqlvnNSFKGIKYLRLN--TLASLGYAVVVIDGRGSCQRGLHFEGalk 693
Cdd:pfam02129 3 VRLAADIYRP--TKTGGPVPALLTrsPYGAR------RDGASDLALAHPewEFAARGYAVVYQDVRGTGGSEGVFTV--- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255003757 694 nqMGQVEIEDQVEGLQYVAEKYGFIDlsRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAY 761
Cdd:pfam02129 72 --GGPQEAADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDY 135
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
624-758 |
2.73e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 43.84 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 624 IYKPHTLQPGRKHPTVLFVYGGPQ--VQLVNNSfkgikylRLNTLA-SLGYAVVVIDG-RGSCQRGLHFEGALKNQMGQV 699
Cdd:COG3509 41 LYVPAGYDGGAPLPLVVALHGCGGsaADFAAGT-------GLNALAdREGFIVVYPEGtGRAPGRCWNWFDGRDQRRGRD 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255003757 700 EIE--DQVegLQYVAEKYGfIDLSRVAIHGWSYGGFLSL-MGLIHkPQVFK--VAIAGAPVTVW 758
Cdd:COG3509 114 DVAfiAAL--VDDLAARYG-IDPKRVYVTGLSAGGAMAYrLACEY-PDVFAavAPVAGLPYGAA 173
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
618-762 |
5.22e-04 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 43.76 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 618 VQLYGMIYKPHTLQpgRKHPTVLF--VYGgpqvqlVNNSFKGIKYLRLNTLASLGYAVVVIDGRG---ScqrglhfEGAL 692
Cdd:COG2936 23 VRLAADIYRPKDAE--GPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGtggS-------EGEF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255003757 693 KNqMGQVEIEDQVEGLQYVAEkygfIDLS--RVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYD 762
Cdd:COG2936 88 DP-YRVDEQTDGYDTIDWLAK----QPWSngKVGMIGISYGGFTQLAAAADRPPALKAIVPQAPTSDRYDDD 154
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
624-738 |
1.17e-03 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 42.02 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 624 IYKPHTLQP----GRKHPTVLFV--YGGpqvqlvnnSFKGIKYLRlNTLASLGYAVVVIDGRGSCQRGLhfEGALKNQMG 697
Cdd:COG4188 46 VWYPATAPAdapaGGPFPLVVLShgLGG--------SREGYAYLA-EHLASHGYVVAAPDHPGSNAADL--SAALDGLAD 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 255003757 698 QVEIE-------------DQVEGL-QYVAEKYGFIDLSRVAIHGWSYGGF--LSLMG 738
Cdd:COG4188 115 ALDPEelwerpldlsfvlDQLLALnKSDPPLAGRLDLDRIGVIGHSLGGYtaLALAG 171
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
637-763 |
7.16e-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: 39.02 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 637 PTVLFVYGGPQVqlVNNSFKGIKYLrlntlASLGYAVVVIDGRGSCQrglhfEGALKNQmGQVEIEDQVEGLQYVAEKYG 716
Cdd:pfam00561 1 PPVLLLHGLPGS--SDLWRKLAPAL-----ARDGFRVIALDLRGFGK-----SSRPKAQ-DDYRTDDLAEDLEYILEALG 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 255003757 717 fidLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDT 763
Cdd:pfam00561 68 ---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDE 111
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
628-861 |
9.73e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 38.44 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 628 HTLQPGRKHPTVLFVYGGPQVQlvnNSFKGIkylrLNTLASlGYAVVVIDGRGSCQRGLHFEGalknqmgqVEIEDQVEG 707
Cdd:COG0596 15 HYREAGPDGPPVVLLHGLPGSS---YEWRPL----IPALAA-GYRVIAPDLRGHGRSDKPAGG--------YTLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 708 LQYVAEKYGfidLSRVAIHGWSYGGFLSL-MGLIHKPQVFKVAIAGAPVTVWMaydtgyteRYMDVPENNQQGYEAGSVA 786
Cdd:COG0596 79 LAALLDALG---LERVVLVGHSMGGMVALeLAARHPERVAGLVLVDEVLAALA--------EPLRRPGLAPEALAALLRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255003757 787 LHVEKLPNEPNRL----LILHGFLDENVHFFHTNFLVSQLIRAgkpyQLQIYPNERHSIrCRESGEHYEVTLLHFLQEH 861
Cdd:COG0596 148 LARTDLRERLARItvptLVIWGEKDPIVPPALARRLAELLPNA----ELVVLPGAGHFP-PLEQPEAFAAALRDFLARL 221
|
|
| |
