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Conserved domains on  [gi|255003757|ref|NP_766212|]
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dipeptidyl peptidase 9 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

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 6.10e-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: 6.10e-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 6.36e-63

Prolyl oligopeptidase family;


:

Pssm-ID: 425609 [Multi-domain]  Cd Length: 213  Bit Score: 210.93  E-value: 6.36e-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 3.95e-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: 437352  Cd Length: 155  Bit Score: 165.09  E-value: 3.95e-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 6.10e-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: 6.10e-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 6.36e-63

Prolyl oligopeptidase family;


Pssm-ID: 425609 [Multi-domain]  Cd Length: 213  Bit Score: 210.93  E-value: 6.36e-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];
525-862 2.06e-58

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 224423 [Multi-domain]  Cd Length: 620  Bit Score: 210.85  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 525 HLYVVSYESAGEIVRLTTLGFSHSCSMSQSFDMFVSHYSSVSTPPcvHVYKLSGPDDDPLHKQPRFWASmmeaancPPDY 604
Cdd:COG1506  292 SSPLFRVDDLGGGVEGLSGDDGGVPGFDVDGRKLALAYSSPTEPP--EIYLYDRGEEAKLTSSNNSGLK-------KVKL 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 605 VPPEIFHFHTRADVQLYGMIYKPHTLQPGRKHPTVLFVYGGPQVQlVNNSFkgikYLRLNTLASLGYAVVVIDGRGSCQR 684
Cdd:COG1506  363 AEPEPVTYKSNDGETIHGWLYKPPGFDPRKKYPLIVYIHGGPSAQ-VGYSF----NPEIQVLASAGYAVLAPNYRGSTGY 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 685 GLHFEGALKNQMGQVEIEDQVEGLQYVaEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPqVFKVAIAGAPVTVWMAYDTG 764
Cdd:COG1506  438 GREFADAIRGDWGGVDLEDLIAAVDAL-VKLPLVDPERIGITGGSYGGYMTLLAATKTP-RFKAAVAVAGGVDWLLYFGE 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 765 YTERYMDVPENNQQG-------YEAGSVALHVEKLPNepnRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNE 837
Cdd:COG1506  516 STEGLRFDPEENGGGppedrekYEDRSPIFYADNIKT---PLLLIHGEEDDRVPIEQAEQLVDALKRKGKPVELVVFPDE 592
                        330       340
                 ....*....|....*....|....*
gi 255003757 838 RHSIRCRESGEHYEVTLLHFLQEHL 862
Cdd:COG1506  593 GHGFSRPENRVKVLKEILDWFKRHL 617
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
23-134 3.95e-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: 437352  Cd Length: 155  Bit Score: 165.09  E-value: 3.95e-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 6.10e-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: 6.10e-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 6.36e-63

Prolyl oligopeptidase family;


Pssm-ID: 425609 [Multi-domain]  Cd Length: 213  Bit Score: 210.93  E-value: 6.36e-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];
525-862 2.06e-58

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 224423 [Multi-domain]  Cd Length: 620  Bit Score: 210.85  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 525 HLYVVSYESAGEIVRLTTLGFSHSCSMSQSFDMFVSHYSSVSTPPcvHVYKLSGPDDDPLHKQPRFWASmmeaancPPDY 604
Cdd:COG1506  292 SSPLFRVDDLGGGVEGLSGDDGGVPGFDVDGRKLALAYSSPTEPP--EIYLYDRGEEAKLTSSNNSGLK-------KVKL 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 605 VPPEIFHFHTRADVQLYGMIYKPHTLQPGRKHPTVLFVYGGPQVQlVNNSFkgikYLRLNTLASLGYAVVVIDGRGSCQR 684
Cdd:COG1506  363 AEPEPVTYKSNDGETIHGWLYKPPGFDPRKKYPLIVYIHGGPSAQ-VGYSF----NPEIQVLASAGYAVLAPNYRGSTGY 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 685 GLHFEGALKNQMGQVEIEDQVEGLQYVaEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPqVFKVAIAGAPVTVWMAYDTG 764
Cdd:COG1506  438 GREFADAIRGDWGGVDLEDLIAAVDAL-VKLPLVDPERIGITGGSYGGYMTLLAATKTP-RFKAAVAVAGGVDWLLYFGE 515
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 765 YTERYMDVPENNQQG-------YEAGSVALHVEKLPNepnRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNE 837
Cdd:COG1506  516 STEGLRFDPEENGGGppedrekYEDRSPIFYADNIKT---PLLLIHGEEDDRVPIEQAEQLVDALKRKGKPVELVVFPDE 592
                        330       340
                 ....*....|....*....|....*
gi 255003757 838 RHSIRCRESGEHYEVTLLHFLQEHL 862
Cdd:COG1506  593 GHGFSRPENRVKVLKEILDWFKRHL 617
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
23-134 3.95e-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: 437352  Cd Length: 155  Bit Score: 165.09  E-value: 3.95e-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
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
618-761 9.26e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 45.02  E-value: 9.26e-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
FrsA COG1073
Fermentation-respiration switch protein FrsA, has esterase activity, DUF1100 family [Signal ...
612-862 1.57e-03

Fermentation-respiration switch protein FrsA, has esterase activity, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 223999 [Multi-domain]  Cd Length: 299  Bit Score: 41.62  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 612 FHTRADVQLYGMIYKPHTLQPGRKHPTVLFVYG-GPQVQLVNNSFKgikylrlnTLASLGYAVVVIDGRGSCQRGLHFEG 690
Cdd:COG1073   25 LANRTGIALAAVLHLPPSGNEEKKLPAVVFLHGfGSSKEQSLGYAV--------LLAEKGYRVLAGDASLFGESGGDPRG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 691 ALKNqMGQVE-------IEDQVEGLQYVAEKYGFiDLSRVAIHGWSYGGFLSLMGLIHKP--------QVFKVAIAGAPV 755
Cdd:COG1073   97 LADS-EGYAEdfsaavlLLLSEGVLDKDYRLLGA-SLGPRILAGLSLGGPSAGALLAWGPtrldasriVVWGESLGGALA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 756 ------------TVWMAYDT--GYTERYMDVPENNQQGYEAGSVALH-----VEKLPNEPnrLLILHGFLDENVHFFHTN 816
Cdd:COG1073  175 llllganpelarELIDYLITpgGFAPLPAPEAPLDTLPLRAVLLLLLdpfddAEKISPRP--VLLVHGERDEVVPLRDAE 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 255003757 817 FLVSQLirAGKPYQLQIYPNERHSIRC--RESGEHYEVTLLHFLQEHL 862
Cdd:COG1073  253 DLYEAA--RERPKKLLFVPGGGHIDLYdnPPAVEQALDKLAEFLERHL 298
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
579-839 2.11e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 223730 [Multi-domain]  Cd Length: 312  Bit Score: 41.07  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 579 PDDDPLHKQPRFWASMMEAANCPPDYV-PPEIFHFHTRADVQLYGMIYKPhTLQPGRKHPTVLFVYGGPQVQLVNNSFkg 657
Cdd:COG0657   22 PAGLGIAARRRLYAALAAPLVAPLPPAtSPEDVALAGPSGDGVPVRVYRP-DRKAAATAPVVLYLHGGGWVLGSLRTH-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 658 iKYLRLNTLASLGYAVVVIDGRGSCQRGLhfegalknqmgQVEIEDQVEGLQYV---AEKYGfIDLSRVAIHGWSYGGFL 734
Cdd:COG0657   99 -DALVARLAAAAGAVVVSVDYRLAPEHPF-----------PAALEDAYAAYRWLranAAELG-IDPSRIAVAGDSAGGHL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 735 SLMGLIHKPQVFKVAIAGA----PVT----VWMAYDTGYTERYMDVPENNQ----QGYEAGSVALHVEKLPNEPNRL--- 799
Cdd:COG0657  166 ALALALAARDRGLPLPAAQvlisPLLdltsSAASLPGYGEADLLDAAAILAwfadLYLGAAPDREDPEASPLASDDLsgl 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 255003757 800 ---LILHG----FLDENVHFFHtnflvsQLIRAGKPYQLQIYPNERH 839
Cdd:COG0657  246 pptLIQTAefdpLRDEGEAYAE------RLRAAGVPVELRVYPGMIH 286
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
617-745 3.22e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223489 [Multi-domain]  Cd Length: 236  Bit Score: 40.06  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003757 617 DVQLYGMIYKPhtlQPGRKHPTVLFV---YG-GPQVQLVNNSfkgikylrlntLASLGYAVVVID-------GRGSCQRG 685
Cdd:COG0412   11 DGELPAYLARP---AGAGGFPGVIVLheiFGlNPHIRDVARR-----------LAKAGYVVLAPDlygrqgdPTDIEDEP 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255003757 686 LHFEGALKNQMGQVE-IEDQVEGLQYVAeKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQV 745
Cdd:COG0412   77 AELETGLVERVDPAEvLADIDAALDYLA-RQPQVDPKRIGVVGFCMGGGLALLAATRAPEV 136
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
637-763 6.87e-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: 6.87e-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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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