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Conserved domains on  [gi|37577089|ref|NP_932064|]
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dipeptidyl peptidase 8 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
 8-162 5.37e-112

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: 339.63  E-value: 5.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089     8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577089    88 RNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 162
Cdd:pfam19520  81 KNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 175-595 4.84e-92

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: 295.00  E-value: 4.84e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 37577089   570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
687-891 5.48e-70

Prolyl oligopeptidase family;


:

Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.58  E-value: 5.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 839
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 37577089   840 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 891
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
 
Name Accession Description Interval E-value
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
 8-162 5.37e-112

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: 339.63  E-value: 5.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089     8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577089    88 RNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 162
Cdd:pfam19520  81 KNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 175-595 4.84e-92

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: 295.00  E-value: 4.84e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 37577089   570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
687-891 5.48e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.58  E-value: 5.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 839
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 37577089   840 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 891
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
637-889 4.52e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 190.61  E-value: 4.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 637 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 716
Cdd:COG1506   1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 717 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 793
Cdd:COG1506  68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 794 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 873
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                       250
                ....*....|....*.
gi 37577089 874 EHYElHLLHYLQENLG 889
Cdd:COG1506 220 DYLE-RILDFLDRHLK 234
 
Name Accession Description Interval E-value
Dpp_8_9_N pfam19520
Dipeptidyl peptidase 8 and 9 N-terminal; Dipeptidyl peptidase (DPP) family members 8 and 9 are ...
 8-162 5.37e-112

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: 339.63  E-value: 5.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089     8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37577089    88 RNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 162
Cdd:pfam19520  81 KNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 175-595 4.84e-92

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: 295.00  E-value: 4.84e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 37577089   570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
687-891 5.48e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.58  E-value: 5.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 839
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 37577089   840 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 891
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
637-889 4.52e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 190.61  E-value: 4.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 637 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 716
Cdd:COG1506   1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 717 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 793
Cdd:COG1506  68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 794 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 873
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                       250
                ....*....|....*.
gi 37577089 874 EHYElHLLHYLQENLG 889
Cdd:COG1506 220 DYLE-RILDFLDRHLK 234
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
634-866 3.72e-13

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 69.61  E-value: 3.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 634 EIFSFESTTGFTLYGMLYKPHDlqpGKKYPTVLFI--YGGpqvqlVNNRFKGVkyfrLNTLASLGYVVVVID--NRGSch 709
Cdd:COG0412   4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDlyGRGG-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 710 RGLKFEGAFKYkMGQIEIDDQVE----GLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIfRVAIAgapvtlwi 785
Cdd:COG0412  70 PGDDPDEARAL-MGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AAAVS-------- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 786 FYdtgyterymGHPDQNEQGYYLGSVAMqaekfpsepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERH 865
Cdd:COG0412 139 FY---------GGLPADDLLDLAARIKA----------PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199


                .
gi 37577089 866 S 866
Cdd:COG0412 200 G 200
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 634-771 1.59e-12

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 68.40  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 634 EIFSFESTTGFTLYGMLYKPHDlqPGKKYPTVLFIYGgpqvqlvnnrFKGVKYFRL---NTLASLGYVVVVIDNRG---S 707
Cdd:COG1073  11 EDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFDYRGygeS 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37577089 708 chrglkfEGAFKYkMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDI 771
Cdd:COG1073  79 -------EGEPRE-EGSPERRDARAAVDYLRTL-PGVDPERIGLLGISLGGGYALNAAATDPRV 133
COG4099 COG4099
Predicted peptidase [General function prediction only];
650-867 5.11e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 54.59  E-value: 5.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 650 LYKPHDLQPGKKYPTVLFIYGG------PQVQLVNnrfKGVKYFRLNTLASLGYVVVVidnrGSCHRGlkfegafKYKMG 723
Cdd:COG4099  37 LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCPED-------DYWSD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 724 QIEIDDQVEGLQYLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFR--VAIAGAPvtlwifyDTGYTERYmghpdq 801
Cdd:COG4099 103 TKALDAVLALLDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG-------DPANAANL------ 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37577089 802 neqgyylgsvamqaEKFPsepnrLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSI 867
Cdd:COG4099 169 --------------KKVP-----VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 650-764 1.71e-06

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 49.87  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   650 LYKPhdLQPGKKYPTVLFIYGGPQvqlvnnrFKGVKY----FRLNTLASL---GYVVVVIDNRGSCHRglKFEGAfkykm 722
Cdd:pfam20434   3 IYLP--KNAKGPYPVVIWIHGGGW-------NSGDKEadmgFMTNTVKALlkaGYAVASINYRLSTDA--KFPAQ----- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 37577089   723 gqieIDDQVEGLQYL---ASRYDfIDLDRVGIHGWSYGGYLSLMA 764
Cdd:pfam20434  67 ----IQDVKAAIRFLranAAKYG-IDTNKIALMGFSAGGHLALLA 106
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
632-867 6.13e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 48.07  E-value: 6.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 632 PPEIFSFESTTGFTLYGMLYKPHDlQPGkkyPTVLFIYGGpqvqlvnnRFKGVKYFRL-NTLASLGYVVVVIDNRG---S 707
Cdd:COG2267   2 TRRLVTLPTRDGLRLRGRRWRPAG-SPR---GTVVLVHGL--------GEHSGRYAELaEALAAAGYAVLAFDLRGhgrS 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 708 CHRGLKFEGAFKYkmgqieIDDQVEGLQYLASRYDfidlDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvtlwify 787
Cdd:COG2267  70 DGPRGHVDSFDDY------VDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 788 dtgyteRYMGHPDQNEQGYYLGSVAMQAE----KFPsepnrLLLLHGFLDENVHFAHTsilLSFLVRAGKPYDLQIYPQE 863
Cdd:COG2267 133 ------AYRADPLLGPSARWLRALRLAEAlariDVP-----VLVLHGGADRVVPPEAA---RRLAARLSPDVELVLLPGA 198


                ....
gi 37577089 864 RHSI 867
Cdd:COG2267 199 RHEL 202
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
692-775 1.66e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.79  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 692 LASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEI------D-----DQVEGLQYLASRY-DFIDLDRVGIHGWSYGGY 759
Cdd:COG4188  85 LASHGYVVAAPDHPGSNAADLSAALDGLADALDPEElwerplDlsfvlDQLLALNKSDPPLaGRLDLDRIGVIGHSLGGY 164

                        90
                ....*....|....*.
gi 37577089 760 LSLMALMQRSDIFRVA 775
Cdd:COG4188 165 TALALAGARLDFAALR 180
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
650-790 4.56e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 46.18  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   650 LYKPhdLQPGKKYPTVLFI--YGGPqvqlvNNRFKGVKYFRLN-TLASLGYVVVVIDNRGSchRGLkfEGAFKYKMGQiE 726
Cdd:pfam02129   9 IYRP--TKTGGPVPALLTRspYGAR-----RDGASDLALAHPEwEFAARGYAVVYQDVRGT--GGS--EGVFTVGGPQ-E 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37577089   727 IDDQVEGLQYLASRYDFIDldRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLW--IFYDTG 790
Cdd:pfam02129  77 AADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLydYYREGG 140
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
650-889 6.84e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 44.86  E-value: 6.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 650 LYKPHDlqPGKKYPTVLFIYGGpqvqlvnnrfkgvkYFRLNTL-----------ASLGYVVVVIDNRgschrgL----KF 714
Cdd:COG0657   3 VYRPAG--AKGPLPVVVYFHGG--------------GWVSGSKdthdplarrlaARAGAAVVSVDYR------LapehPF 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 715 EGAfkykmgqieIDDQVEGLQYLASRYDF--IDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGA----PVtlwifYD 788
Cdd:COG0657  61 PAA---------LEDAYAALRWLRANAAElgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQvliyPV-----LD 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 789 TGYTerymghPdqneqgyylgsVAMQAEKFPsepnRLLLLHG----FLDENVHFAHTsillsfLVRAGKPYDLQIYPQER 864
Cdd:COG0657 127 LTAS------P-----------LRADLAGLP----PTLIVTGeadpLVDESEALAAA------LRAAGVPVELHVYPGGG 179

                       250       260
                ....*....|....*....|....*....
gi 37577089 865 HS----IRVPESGEHYElHLLHYLQENLG 889
Cdd:COG0657 180 HGfgllAGLPEARAALA-EIAAFLRRALA 207
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
645-768 3.17e-04

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 44.53  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 645 TLYGMLYKPHDLQpgKKYPTVLFI--YGgpqvqlVNNRFKGVKYFRLNTLASLGYVVVVIDNRG---SchrglkfEGAFk 719
Cdd:COG2936  24 RLAADIYRPKDAE--GPVPVILERtpYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGtggS-------EGEF- 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 37577089 720 YKMGQIEIDDQVEGLQYLAsrydfiDLD----RVGIHGWSYGGYLSLMALMQR 768
Cdd:COG2936  88 DPYRVDEQTDGYDTIDWLA------KQPwsngKVGMIGISYGGFTQLAAAADR 134
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
736-866 1.03e-03

Predicted hydrolase of the alpha/beta superfamily [General function prediction only];


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 41.89  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 736 YLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvTLWIfydtgyterymghpdqnEQGYYLGSVAmQA 815
Cdd:COG2819 120 YIDKRYR-TDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP-SLWW-----------------DDGALLDEAE-AL 179

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 37577089 816 EKFPSEPNRLLLLHGFLDE---NVHFAHTSILLSFLVRAGKP---YDLQIYPQERHS 866
Cdd:COG2819 180 LKRSPLPKRLYLSVGTLEGdsmDGMVDDARRLAEALKAKGYPglnVKFEVFPGETHG 236
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 663-835 1.58e-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: 41.34  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   663 PTVLFIYGGPQVqlvnnrfkGVKYFRL-NTLASLGYVVVVIDNRGSCH-RGLKFEGAFkykmgqiEIDDQVEGLQYLASR 740
Cdd:pfam00561   1 PPVLLLHGLPGS--------SDLWRKLaPALARDGFRVIALDLRGFGKsSRPKAQDDY-------RTDDLAEDLEYILEA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089   741 YDfidLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPS 820
Cdd:pfam00561  66 LG---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAK 142

                         170
                  ....*....|....*
gi 37577089   821 EPNRLLLLHGFLDEN 835
Cdd:pfam00561 143 LLALLLLRLRLLKAL 157
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
650-777 2.27e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 40.99  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 650 LYKPHD-LQPGKKYPTVLFIYGGPQVQlvnNRFkgVKYFRLNT-LASL-------GYVVVVIDNRGSCHRGLKFEGAFKY 720
Cdd:COG2382  99 VYLPPGyDNPGKKYPVLYLLDGGGGDE---QDW--FDQGRLPTiLDNLiaagkipPMIVVMPDGGDGGDRGTEGPGNDAF 173

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37577089 721 kmgQIEIDDQVegLQYLASRYDFI-DLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIA 777
Cdd:COG2382 174 ---ERFLAEEL--IPFVEKNYRVSaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
691-786 2.70e-03

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 40.15  E-value: 2.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37577089 691 TLASLGYVVVVIDNRG---SchrglkfEGAFKYkmGQIEIDDQVEGLQYLASRYdfidLDRVGIHGWSYGGYLSLMALMQ 767
Cdd:COG2945  50 ALVAAGFAVLRFNFRGvgrS-------EGEFDE--GRGELDDAAAALDWLRAQN----PLPLWLAGFSFGAYVALQLAMR 116

                        90
                ....*....|....*....
gi 37577089 768 RSDIFRVAIAGAPVTLWIF 786
Cdd:COG2945 117 LPEVEGLILVAPPVNRYDF 135
 
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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