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Conserved domains on  [gi|1860299423|ref|NP_001371557|]
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dipeptidyl peptidase 9 isoform 8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

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 2.34e-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: 265.72  E-value: 2.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930   1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930  80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1860299423 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
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 4.27e-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: 167.83  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423  53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520  44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1860299423 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
Peptidase_S9 super family cl47529
Prolyl oligopeptidase family;
691-826 5.96e-41

Prolyl oligopeptidase family;


The actual alignment was detected with superfamily member pfam00326:

Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 149.69  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299423 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEP 826
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP 145
 
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 2.34e-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: 265.72  E-value: 2.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930   1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930  80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1860299423 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
53-164 4.27e-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: 167.83  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423  53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520  44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1860299423 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
691-826 5.96e-41

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 149.69  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299423 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEP 826
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP 145
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
641-823 3.81e-40

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 147.86  E-value: 3.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 641 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 720
Cdd:COG1506     1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 721 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 797
Cdd:COG1506    64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
                         170       180
                  ....*....|....*....|....*.
gi 1860299423 798 RYMDVPENNQHGYEAGSVALHVEKLP 823
Cdd:COG1506   143 RLMGGPWEDPEAYAARSPLAYADKLK 168
 
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 2.34e-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: 265.72  E-value: 2.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 175 SESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCS--GPRMDPKICPaDPAFFSFINNSDLWVANIETGEERRLT 252
Cdd:pfam00930   1 SPDGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPgeGKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 253 fcHQGlSNVLddpkSAGVATFVIQEE-FDRFTGYWWCPTASwegseglktlRILYEEVDESEVEVIHVPSPALEER--KT 329
Cdd:pfam00930  80 --SDG-SDGI----FNGVADWVYEEEvLGSNSAVWWSPDGS----------RLAFLRFDESEVPIITLPYYTDEGPgpEV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 330 DSYRYPRTGSKNPKIALKLAEFqtdSQGKIVStqekelVQPFSSLFPKVEYIARAGWTRDGKyAWAMFLDRPQQWLQLVL 409
Cdd:pfam00930 143 REIKYPKAGAPNPTVELFVYDL---ASGKTVE------VVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 410 LPPAlfipsteneeqrlaSARAVPRNvqpyvvyEEVTNVWINVHDIFYPFPQSEGEdelcFLRANEcKTGFCHLYKVTAV 489
Cdd:pfam00930 213 CDAE--------------TGRTVVIL-------EETSDGWVELHQDPHFIKRDGSG----FLWISE-RDGYNHLYLYDLD 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 490 LKSQgydwsepfspgedefkcpikeeIALTSGEWEVlarhGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVR 569
Cdd:pfam00930 267 GKSP----------------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTC 320
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1860299423 570 LTTPGFSH--SCSMSQNFDMFVSHYSSVSTPP 599
Cdd:pfam00930 321 LTDDSGDHdySASFSPNGSYYVLTYSGPDTPP 352
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
53-164 4.27e-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: 167.83  E-value: 4.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423  53 FQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLL 132
Cdd:pfam19520  44 FYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLML 123
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1860299423 133 SWKQMLDHFQATPHHGVYSREEELLRERKRLG 164
Cdd:pfam19520 124 SWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
691-826 5.96e-41

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 149.69  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 691 LRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLI 770
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQ-GYTDPDRLAIWGGSYGGYLTGAALN 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299423 771 HKPQVFKVAIAGAPVTVWMAYDTG----YTERYMD--VPENNQHGYEAGSVALHVEKLPNEP 826
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEwgNPWDNEEGYDYLSPYSPADNVKVYP 145
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
641-823 3.81e-40

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 147.86  E-value: 3.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 641 HFHTRSDVRLYGMIYKPHalqPGKKHPTVLFVYGGPQVQlvNNSFkgikYLRLNTLASLGYAVVVIDGRGscqrglrfEG 720
Cdd:COG1506     1 TFKSADGTTLPGWLYLPA---DGKKYPVVVYVHGGPGSR--DDSF----LPLAQALASRGYAVLAPDYRG--------YG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 721 ALKNQMGQVEIEDQVEGLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTG---YTE 797
Cdd:COG1506    64 ESAGDWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
                         170       180
                  ....*....|....*....|....*.
gi 1860299423 798 RYMDVPENNQHGYEAGSVALHVEKLP 823
Cdd:COG1506   143 RLMGGPWEDPEAYAARSPLAYADKLK 168
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
631-762 1.52e-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: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 631 PPDYVPPEIFHFHTRSDVRLYGMIYKPHAlqPGKKHPTVLFVYGgpqvqlvnnsFKGIKYLRL---NTLASLGYAVVVID 707
Cdd:COG1073     4 PSDKVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFD 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1860299423 708 GRG---ScqrglrfEGALKnQMGQVEIEDQVEGLQFVaEKYGFIDLSRVAIHGWSYGG 762
Cdd:COG1073    72 YRGygeS-------EGEPR-EEGSPERRDARAAVDYL-RTLPGVDPERIGLLGISLGG 120
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
638-786 2.35e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.58  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 638 EIFHFHTRSDVRLYGMIYKPHAlqpGKKHPTVLFV--YGGpqvqlVNNSFKGIkylrLNTLASLGYAVVVIDGRGScQRG 715
Cdd:COG0412     4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDLYGR-GGP 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299423 716 LRFEGALKNQMGQVEIEDQVE----GLQFVAEKyGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVfK--VAIAGAPVT 786
Cdd:COG0412    71 GDDPDEARALMGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA 145
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
644-792 1.10e-05

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 49.15  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 644 TRSDVRLYGMIYKPHALQpgKKHPTVLF--VYGgpqvqlVNNSFKGIKYLRLNTLASLGYAVVVIDGRGscqrglRF--E 719
Cdd:COG2936    19 MRDGVRLAADIYRPKDAE--GPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRG------TGgsE 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299423 720 GALKNqMGQVEIEDQVEGLQFVAEkygfIDLS--RVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYD 792
Cdd:COG2936    85 GEFDP-YRVDEQTDGYDTIDWLAK----QPWSngKVGMIGISYGGFTQLAAAADRPPALKAIVPQAPTSDRYDDD 154
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
636-784 7.73e-05

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.99  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 636 PPEIFHFHTRSDVRLYGMIYKPhalqPGKKHPTVLFVYGGpqvqlvnNSFKGiKYLRL-NTLASLGYAVVVIDGRG---S 711
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGL-------GEHSG-RYAELaEALAAAGYAVLAFDLRGhgrS 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860299423 712 CQRGLRFEGAlknqmgQVEIEDQVEGLQFVAEKYGfidlSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAP 784
Cdd:COG2267    70 DGPRGHVDSF------DDYVDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
648-791 2.20e-04

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 43.87  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 648 VRLYGMIYKPhaLQPGKKHPTVLF--VYGGPqvqlvnNSFKGIKYLRLN--TLASLGYAVVVIDGRGscQRGLrfEGALK 723
Cdd:pfam02129   3 VRLAADIYRP--TKTGGPVPALLTrsPYGAR------RDGASDLALAHPewEFAARGYAVVYQDVRG--TGGS--EGVFT 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860299423 724 NQMGQvEIEDQVEGLQFVAEKYGFIDlsRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAY 791
Cdd:pfam02129  71 VGGPQ-EAADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDY 135
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
696-768 2.85e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 43.94  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 696 LASLGYAVVVIDGRGSCQRGL-RFEGALKNQMGQVEIEDQVEGLQFV-----------AEKYGFIDLSRVAIHGWSYGGF 763
Cdd:COG4188    85 LASHGYVVAAPDHPGSNAADLsAALDGLADALDPEELWERPLDLSFVldqllalnksdPPLAGRLDLDRIGVIGHSLGGY 164

                  ....*..
gi 1860299423 764 --LSLMG 768
Cdd:COG4188   165 taLALAG 171
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
654-788 2.80e-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: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 654 IYKPHALQPGKKHPTVLFVYGGPQ--VQLVNNSfkgikylRLNTLA-SLGYAVVVIDG-RGSCQRGLRFEGALKNQMGQV 729
Cdd:COG3509    41 LYVPAGYDGGAPLPLVVALHGCGGsaADFAAGT-------GLNALAdREGFIVVYPEGtGRAPGRCWNWFDGRDQRRGRD 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860299423 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 6.02e-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: 39.41  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299423 667 PTVLFVYGGPQVqlVNNSFKGIKYLrlntlASLGYAVVVIDGRGSCQrglrfEGALKNQmGQVEIEDQVEGLQFVAEKYG 746
Cdd:pfam00561   1 PPVLLLHGLPGS--SDLWRKLAPAL-----ARDGFRVIALDLRGFGK-----SSRPKAQ-DDYRTDDLAEDLEYILEALG 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1860299423 747 fidLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDT 793
Cdd:pfam00561  68 ---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDE 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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