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Conserved domains on  [gi|1003701564|ref|NP_001307805|]
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dipeptidyl peptidase 8 isoform 1 [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 ...
 1-146 3.70e-107

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: 326.91  E-value: 3.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564   1 MAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHS 80
Cdd:pfam19520  10 MAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHS 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003701564  81 DRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 146
Cdd:pfam19520  90 DRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 159-579 7.52e-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: 294.23  E-value: 7.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 159 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 236
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 237 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 313
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 314 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 393
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 394 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 473
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 474 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 553
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 1003701564 554 GYSH--SCCISQHCDFFISKYSNQKNPH 579
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
671-875 7.37e-70

Prolyl oligopeptidase family;


:

Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.19  E-value: 7.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 671 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 750
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 751 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 823
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003701564 824 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 875
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 ...
 1-146 3.70e-107

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: 326.91  E-value: 3.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564   1 MAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHS 80
Cdd:pfam19520  10 MAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHS 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003701564  81 DRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 146
Cdd:pfam19520  90 DRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 159-579 7.52e-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: 294.23  E-value: 7.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 159 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 236
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 237 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 313
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 314 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 393
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 394 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 473
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 474 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 553
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 1003701564 554 GYSH--SCCISQHCDFFISKYSNQKNPH 579
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
671-875 7.37e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.19  E-value: 7.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 671 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 750
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 751 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 823
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003701564 824 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 875
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
621-873 8.54e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 189.46  E-value: 8.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 621 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 700
Cdd:COG1506     1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 701 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 777
Cdd:COG1506    68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 778 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 857
Cdd:COG1506   143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                         250
                  ....*....|....*.
gi 1003701564 858 EHYElHLLHYLQENLG 873
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 ...
 1-146 3.70e-107

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: 326.91  E-value: 3.70e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564   1 MAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHS 80
Cdd:pfam19520  10 MAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVKKNDPEGPHS 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003701564  81 DRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 146
Cdd:pfam19520  90 DRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N pfam00930
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 159-579 7.52e-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: 294.23  E-value: 7.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 159 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 236
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 237 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 313
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 314 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 393
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 394 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 473
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 474 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 553
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324

                         410       420
                  ....*....|....*....|....*...
gi 1003701564 554 GYSH--SCCISQHCDFFISKYSNQKNPH 579
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
671-875 7.37e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 230.19  E-value: 7.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 671 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 750
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 751 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 823
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1003701564 824 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 875
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
621-873 8.54e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 189.46  E-value: 8.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 621 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 700
Cdd:COG1506     1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 701 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 777
Cdd:COG1506    68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 778 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 857
Cdd:COG1506   143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                         250
                  ....*....|....*.
gi 1003701564 858 EHYElHLLHYLQENLG 873
Cdd:COG1506   220 DYLE-RILDFLDRHLK 234
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
618-850 3.64e-13

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 69.61  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 618 EIFSFESTTGFTLYGMLYKPHDlqpGKKYPTVLFI--YGGpqvqlVNNRFKGVkyfrLNTLASLGYVVVVID--NRGSch 693
Cdd:COG0412     4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDlyGRGG-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 694 RGLKFEGAFKYkMGQIEIDDQVE----GLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIfRVAIAgapvtlwi 769
Cdd:COG0412    70 PGDDPDEARAL-MGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AAAVS-------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 770 FYdtgyterymGHPDQNEQGYYLGSVAMqaekfpsepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERH 849
Cdd:COG0412   139 FY---------GGLPADDLLDLAARIKA----------PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199


                  .
gi 1003701564 850 S 850
Cdd:COG0412   200 G 200
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 618-755 1.82e-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: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 618 EIFSFESTTGFTLYGMLYKPHDlqPGKKYPTVLFIYGgpqvqlvnnrFKGVKYFRL---NTLASLGYVVVVIDNRG---S 691
Cdd:COG1073    11 EDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFDYRGygeS 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003701564 692 chrglkfEGAFKYkMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDI 755
Cdd:COG1073    79 -------EGEPRE-EGSPERRDARAAVDYLRTL-PGVDPERIGLLGISLGGGYALNAAATDPRV 133
COG4099 COG4099
Predicted peptidase [General function prediction only];
634-851 5.43e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 54.59  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 634 LYKPHDLQPGKKYPTVLFIYGG------PQVQLVNnrfKGVKYFRLNTLASLGYVVVVidnrGSCHRGlkfegafKYKMG 707
Cdd:COG4099    37 LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCPED-------DYWSD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 708 QIEIDDQVEGLQYLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFR--VAIAGAPvtlwifyDTGYTERYmghpdq 785
Cdd:COG4099   103 TKALDAVLALLDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG-------DPANAANL------ 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003701564 786 neqgyylgsvamqaEKFPsepnrLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSI 851
Cdd:COG4099   169 --------------KKVP-----VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 634-748 1.68e-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: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 634 LYKPhdLQPGKKYPTVLFIYGGPQvqlvnnrFKGVKY----FRLNTLASL---GYVVVVIDNRGSCHRglKFEGAfkykm 706
Cdd:pfam20434   3 IYLP--KNAKGPYPVVIWIHGGGW-------NSGDKEadmgFMTNTVKALlkaGYAVASINYRLSTDA--KFPAQ----- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1003701564 707 gqieIDDQVEGLQYL---ASRYDfIDLDRVGIHGWSYGGYLSLMA 748
Cdd:pfam20434  67 ----IQDVKAAIRFLranAAKYG-IDTNKIALMGFSAGGHLALLA 106
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
616-851 8.14e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 47.69  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 616 PPEIFSFESTTGFTLYGMLYKPHDlQPGkkyPTVLFIYGGpqvqlvnnRFKGVKYFRL-NTLASLGYVVVVIDNRG---S 691
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPAG-SPR---GTVVLVHGL--------GEHSGRYAELaEALAAAGYAVLAFDLRGhgrS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 692 CHRGLKFEGAFKYkmgqieIDDQVEGLQYLASRYDfidlDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvtlwify 771
Cdd:COG2267    70 DGPRGHVDSFDDY------VDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 772 dtgyteRYMGHPDQNEQGYYLGSVAMQAE----KFPsepnrLLLLHGFLDENVHFAHTsilLSFLVRAGKPYDLQIYPQE 847
Cdd:COG2267   133 ------AYRADPLLGPSARWLRALRLAEAlariDVP-----VLVLHGGADRVVPPEAA---RRLAARLSPDVELVLLPGA 198


                  ....
gi 1003701564 848 RHSI 851
Cdd:COG2267   199 RHEL 202
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
676-759 1.62e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.79  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 676 LASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEI------D-----DQVEGLQYLASRY-DFIDLDRVGIHGWSYGGY 743
Cdd:COG4188    85 LASHGYVVAAPDHPGSNAADLSAALDGLADALDPEElwerplDlsfvlDQLLALNKSDPPLaGRLDLDRIGVIGHSLGGY 164

                          90
                  ....*....|....*.
gi 1003701564 744 LSLMALMQRSDIFRVA 759
Cdd:COG4188   165 TALALAGARLDFAALR 180
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
634-774 4.42e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 46.18  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 634 LYKPhdLQPGKKYPTVLFI--YGGPqvqlvNNRFKGVKYFRLN-TLASLGYVVVVIDNRGSchRGLkfEGAFKYKMGQiE 710
Cdd:pfam02129   9 IYRP--TKTGGPVPALLTRspYGAR-----RDGASDLALAHPEwEFAARGYAVVYQDVRGT--GGS--EGVFTVGGPQ-E 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1003701564 711 IDDQVEGLQYLASRYDFIDldRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLW--IFYDTG 774
Cdd:pfam02129  77 AADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLydYYREGG 140
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
634-873 6.70e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 44.86  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 634 LYKPHDlqPGKKYPTVLFIYGGpqvqlvnnrfkgvkYFRLNTL-----------ASLGYVVVVIDNRgschrgL----KF 698
Cdd:COG0657     3 VYRPAG--AKGPLPVVVYFHGG--------------GWVSGSKdthdplarrlaARAGAAVVSVDYR------LapehPF 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 699 EGAfkykmgqieIDDQVEGLQYLASRYDF--IDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGA----PVtlwifYD 772
Cdd:COG0657    61 PAA---------LEDAYAALRWLRANAAElgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQvliyPV-----LD 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 773 TGYTerymghPdqneqgyylgsVAMQAEKFPsepnRLLLLHG----FLDENVHFAHTsillsfLVRAGKPYDLQIYPQER 848
Cdd:COG0657   127 LTAS------P-----------LRADLAGLP----PTLIVTGeadpLVDESEALAAA------LRAAGVPVELHVYPGGG 179

                         250       260
                  ....*....|....*....|....*....
gi 1003701564 849 HS----IRVPESGEHYElHLLHYLQENLG 873
Cdd:COG0657   180 HGfgllAGLPEARAALA-EIAAFLRRALA 207
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
629-752 3.74e-04

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 44.15  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 629 TLYGMLYKPHDLQpgKKYPTVLFI--YGgpqvqlVNNRFKGVKYFRLNTLASLGYVVVVIDNRG---SchrglkfEGAFk 703
Cdd:COG2936    24 RLAADIYRPKDAE--GPVPVILERtpYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGtggS-------EGEF- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1003701564 704 YKMGQIEIDDQVEGLQYLAsrydfiDLD----RVGIHGWSYGGYLSLMALMQR 752
Cdd:COG2936    88 DPYRVDEQTDGYDTIDWLA------KQPwsngKVGMIGISYGGFTQLAAAADR 134
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
720-850 1.15e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 41.51  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 720 YLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvTLWIfydtgyterymghpdqnEQGYYLGSVAmQA 799
Cdd:COG2819   120 YIDKRYR-TDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP-SLWW-----------------DDGALLDEAE-AL 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1003701564 800 EKFPSEPNRLLLLHGFLDE---NVHFAHTSILLSFLVRAGKP---YDLQIYPQERHS 850
Cdd:COG2819   180 LKRSPLPKRLYLSVGTLEGdsmDGMVDDARRLAEALKAKGYPglnVKFEVFPGETHG 236
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 647-819 1.78e-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: 40.95  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 647 PTVLFIYGGPQVqlvnnrfkGVKYFRL-NTLASLGYVVVVIDNRGSCH-RGLKFEGAFkykmgqiEIDDQVEGLQYLASR 724
Cdd:pfam00561   1 PPVLLLHGLPGS--------SDLWRKLaPALARDGFRVIALDLRGFGKsSRPKAQDDY-------RTDDLAEDLEYILEA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 725 YDfidLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPS 804
Cdd:pfam00561  66 LG---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAK 142

                         170
                  ....*....|....*
gi 1003701564 805 EPNRLLLLHGFLDEN 819
Cdd:pfam00561 143 LLALLLLRLRLLKAL 157
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
634-761 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 634 LYKPHD-LQPGKKYPTVLFIYGGPQVQlvnNRFkgVKYFRLNT-LASL-------GYVVVVIDNRGSCHRGLKFEGAFKY 704
Cdd:COG2382    99 VYLPPGyDNPGKKYPVLYLLDGGGGDE---QDW--FDQGRLPTiLDNLiaagkipPMIVVMPDGGDGGDRGTEGPGNDAF 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003701564 705 kmgQIEIDDQVegLQYLASRYDFI-DLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIA 761
Cdd:COG2382   174 ---ERFLAEEL--IPFVEKNYRVSaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
675-770 2.64e-03

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 40.15  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003701564 675 TLASLGYVVVVIDNRG---SchrglkfEGAFKYkmGQIEIDDQVEGLQYLASRYdfidLDRVGIHGWSYGGYLSLMALMQ 751
Cdd:COG2945    50 ALVAAGFAVLRFNFRGvgrS-------EGEFDE--GRGELDDAAAALDWLRAQN----PLPLWLAGFSFGAYVALQLAMR 116

                          90
                  ....*....|....*....
gi 1003701564 752 RSDIFRVAIAGAPVTLWIF 770
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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