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Conserved domains on  [gi|767984563|ref|XP_011520032|]
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dipeptidyl peptidase 8 isoform X2 [Homo sapiens]

Protein Classification

S9 family peptidase( domain architecture ID 18341293)

S9 family peptidase catalyzes the cleavage of peptide bonds, such as human dipeptidyl peptidase 9 that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2

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 1.14e-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: 340.40  E-value: 1.14e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563    8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984563   88 RNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 162
Cdd:pfam19520  81 KNDPEGPHSDRVYYLAMSGENRENTLFYSEIPKTINKAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIG 155
DPPIV_N super family cl37636
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ...
 175-552 5.34e-74

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: 246.08  E-value: 5.34e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAE------------------------------------TSTAN 295
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGSrlaflrfdesevpiitlpyytdegpgpevreikypkAGAPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  296 PKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISPElfipvedd 375
Cdd:pfam00930 155 PTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDAE-------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  376 vmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkeskykrssGGL 455
Cdd:pfam00930 217 -------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD----------GKS 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  456 PapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSH--SCC 533
Cdd:pfam00930 270 P------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDDSGDHdySAS 333

                         410
                  ....*....|....*....
gi 767984563  534 ISQHCDFFISKYSNQKNPH 552
Cdd:pfam00930 334 FSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
644-848 5.75e-70

Prolyl oligopeptidase family;


:

Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 229.81  E-value: 5.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  644 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 723
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  724 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 796
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767984563  797 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 848
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 1.14e-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: 340.40  E-value: 1.14e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563    8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984563   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 ...
 175-552 5.34e-74

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: 246.08  E-value: 5.34e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAE------------------------------------TSTAN 295
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGSrlaflrfdesevpiitlpyytdegpgpevreikypkAGAPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  296 PKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISPElfipvedd 375
Cdd:pfam00930 155 PTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDAE-------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  376 vmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkeskykrssGGL 455
Cdd:pfam00930 217 -------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD----------GKS 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  456 PapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSH--SCC 533
Cdd:pfam00930 270 P------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDDSGDHdySAS 333

                         410
                  ....*....|....*....
gi 767984563  534 ISQHCDFFISKYSNQKNPH 552
Cdd:pfam00930 334 FSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
644-848 5.75e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 229.81  E-value: 5.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  644 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 723
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  724 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 796
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767984563  797 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 848
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
594-846 4.58e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 190.23  E-value: 4.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 594 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 673
Cdd:COG1506    1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 674 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 750
Cdd:COG1506   68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 751 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 830
Cdd:COG1506  143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                        250
                 ....*....|....*.
gi 767984563 831 EHYElHLLHYLQENLG 846
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 1.14e-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: 340.40  E-value: 1.14e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563    8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520   1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984563   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 ...
 175-552 5.34e-74

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: 246.08  E-value: 5.34e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930   3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAE------------------------------------TSTAN 295
Cdd:pfam00930  81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGSrlaflrfdesevpiitlpyytdegpgpevreikypkAGAPN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  296 PKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISPElfipvedd 375
Cdd:pfam00930 155 PTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDAE-------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  376 vmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkeskykrssGGL 455
Cdd:pfam00930 217 -------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD----------GKS 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  456 PapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSH--SCC 533
Cdd:pfam00930 270 P------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDDSGDHdySAS 333

                         410
                  ....*....|....*....
gi 767984563  534 ISQHCDFFISKYSNQKNPH 552
Cdd:pfam00930 334 FSPNGSYYVLTYSGPDTPP 352
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
644-848 5.75e-70

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 229.81  E-value: 5.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  644 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 723
Cdd:pfam00326   5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  724 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY-YLGSVAMQAEKFpsEPNRLLLLHGFLDENVHFA 796
Cdd:pfam00326  84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGYdYLSPYSPADNVK--VYPPLLLIHGLLDDRVPPW 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767984563  797 HTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSR 848
Cdd:pfam00326 162 QSLKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEYLGGT 213
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
594-846 4.58e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 190.23  E-value: 4.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 594 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKFEg 673
Cdd:COG1506    1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGESAG- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 674 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 750
Cdd:COG1506   68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 751 RYMGHPDQNEQGYYLGSVAMQAEKFPSepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESG 830
Cdd:COG1506  143 RLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219

                        250
                 ....*....|....*.
gi 767984563 831 EHYElHLLHYLQENLG 846
Cdd:COG1506  220 DYLE-RILDFLDRHLK 234
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
591-823 3.51e-13

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 69.61  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 591 EIFSFESTTGFTLYGMLYKPHDlqpGKKYPTVLFI--YGGpqvqlVNNRFKGVkyfrLNTLASLGYVVVVID--NRGSch 666
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDlyGRGG-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 667 RGLKFEGAFKYkMGQIEIDDQVE----GLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIfRVAIAgapvtlwi 742
Cdd:COG0412   70 PGDDPDEARAL-MGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AAAVS-------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 743 FYdtgyterymGHPDQNEQGYYLGSVAMqaekfpsepnRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERH 822
Cdd:COG0412  139 FY---------GGLPADDLLDLAARIKA----------PVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199


                 .
gi 767984563 823 S 823
Cdd:COG0412  200 G 200
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 591-728 1.58e-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: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 591 EIFSFESTTGFTLYGMLYKPHDlqPGKKYPTVLFIYGgpqvqlvnnrFKGVKYFRL---NTLASLGYVVVVIDNRG---S 664
Cdd:COG1073   11 EDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFDYRGygeS 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984563 665 chrglkfEGAFKYkMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDI 728
Cdd:COG1073   79 -------EGEPRE-EGSPERRDARAAVDYLRTL-PGVDPERIGLLGISLGGGYALNAAATDPRV 133
COG4099 COG4099
Predicted peptidase [General function prediction only];
607-824 5.33e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 54.59  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 607 LYKPHDLQPGKKYPTVLFIYGG------PQVQLVNnrfKGVKYFRLNTLASLGYVVVVidnrGSCHRGlkfegafKYKMG 680
Cdd:COG4099   37 LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCPED-------DYWSD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 681 QIEIDDQVEGLQYLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFR--VAIAGAPvtlwifyDTGYTERYmghpdq 758
Cdd:COG4099  103 TKALDAVLALLDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGG-------DPANAANL------ 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984563 759 neqgyylgsvamqaEKFPsepnrLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSI 824
Cdd:COG4099  169 --------------KKVP-----VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 607-721 1.62e-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: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  607 LYKPhdLQPGKKYPTVLFIYGGPQvqlvnnrFKGVKY----FRLNTLASL---GYVVVVIDNRGSCHRglKFEGAfkykm 679
Cdd:pfam20434   3 IYLP--KNAKGPYPVVIWIHGGGW-------NSGDKEadmgFMTNTVKALlkaGYAVASINYRLSTDA--KFPAQ----- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767984563  680 gqieIDDQVEGLQYL---ASRYDfIDLDRVGIHGWSYGGYLSLMA 721
Cdd:pfam20434  67 ----IQDVKAAIRFLranAAKYG-IDTNKIALMGFSAGGHLALLA 106
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
589-824 5.95e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 48.07  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 589 PPEIFSFESTTGFTLYGMLYKPHDlQPGkkyPTVLFIYGGpqvqlvnnRFKGVKYFRL-NTLASLGYVVVVIDNRG---S 664
Cdd:COG2267    2 TRRLVTLPTRDGLRLRGRRWRPAG-SPR---GTVVLVHGL--------GEHSGRYAELaEALAAAGYAVLAFDLRGhgrS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 665 CHRGLKFEGAFKYkmgqieIDDQVEGLQYLASRYDfidlDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvtlwify 744
Cdd:COG2267   70 DGPRGHVDSFDDY------VDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 745 dtgyteRYMGHPDQNEQGYYLGSVAMQAE----KFPsepnrLLLLHGFLDENVHFAHTsilLSFLVRAGKPYDLQIYPQE 820
Cdd:COG2267  133 ------AYRADPLLGPSARWLRALRLAEAlariDVP-----VLVLHGGADRVVPPEAA---RRLAARLSPDVELVLLPGA 198


                 ....
gi 767984563 821 RHSI 824
Cdd:COG2267  199 RHEL 202
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
649-732 1.56e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.79  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 649 LASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEI------D-----DQVEGLQYLASRY-DFIDLDRVGIHGWSYGGY 716
Cdd:COG4188   85 LASHGYVVAAPDHPGSNAADLSAALDGLADALDPEElwerplDlsfvlDQLLALNKSDPPLaGRLDLDRIGVIGHSLGGY 164

                         90
                 ....*....|....*.
gi 767984563 717 LSLMALMQRSDIFRVA 732
Cdd:COG4188  165 TALALAGARLDFAALR 180
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
607-747 4.34e-05

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 46.18  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  607 LYKPhdLQPGKKYPTVLFI--YGGPqvqlvNNRFKGVKYFRLN-TLASLGYVVVVIDNRGSchRGLkfEGAFKYKMGQiE 683
Cdd:pfam02129   9 IYRP--TKTGGPVPALLTRspYGAR-----RDGASDLALAHPEwEFAARGYAVVYQDVRGT--GGS--EGVFTVGGPQ-E 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984563  684 IDDQVEGLQYLASRYDFIDldRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLW--IFYDTG 747
Cdd:pfam02129  77 AADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLydYYREGG 140
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
607-846 6.46e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 44.86  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 607 LYKPHDlqPGKKYPTVLFIYGGpqvqlvnnrfkgvkYFRLNTL-----------ASLGYVVVVIDNRgschrgL----KF 671
Cdd:COG0657    3 VYRPAG--AKGPLPVVVYFHGG--------------GWVSGSKdthdplarrlaARAGAAVVSVDYR------LapehPF 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 672 EGAfkykmgqieIDDQVEGLQYLASRYDF--IDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGA----PVtlwifYD 745
Cdd:COG0657   61 PAA---------LEDAYAALRWLRANAAElgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQvliyPV-----LD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 746 TGYTerymghPdqneqgyylgsVAMQAEKFPsepnRLLLLHG----FLDENVHFAHTsillsfLVRAGKPYDLQIYPQER 821
Cdd:COG0657  127 LTAS------P-----------LRADLAGLP----PTLIVTGeadpLVDESEALAAA------LRAAGVPVELHVYPGGG 179

                        250       260
                 ....*....|....*....|....*....
gi 767984563 822 HS----IRVPESGEHYElHLLHYLQENLG 846
Cdd:COG0657  180 HGfgllAGLPEARAALA-EIAAFLRRALA 207
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
602-725 2.98e-04

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 44.53  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 602 TLYGMLYKPHDLQpgKKYPTVLFI--YGgpqvqlVNNRFKGVKYFRLNTLASLGYVVVVIDNRG---SchrglkfEGAFk 676
Cdd:COG2936   24 RLAADIYRPKDAE--GPVPVILERtpYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGtggS-------EGEF- 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767984563 677 YKMGQIEIDDQVEGLQYLAsrydfiDLD----RVGIHGWSYGGYLSLMALMQR 725
Cdd:COG2936   88 DPYRVDEQTDGYDTIDWLA------KQPwsngKVGMIGISYGGFTQLAAAADR 134
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
693-823 9.73e-04

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: 9.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 693 YLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvTLWIfydtgyterymghpdqnEQGYYLGSVAmQA 772
Cdd:COG2819  120 YIDKRYR-TDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP-SLWW-----------------DDGALLDEAE-AL 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767984563 773 EKFPSEPNRLLLLHGFLDE---NVHFAHTSILLSFLVRAGKP---YDLQIYPQERHS 823
Cdd:COG2819  180 LKRSPLPKRLYLSVGTLEGdsmDGMVDDARRLAEALKAKGYPglnVKFEVFPGETHG 236
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 620-792 1.69e-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: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  620 PTVLFIYGGPQVqlvnnrfkGVKYFRL-NTLASLGYVVVVIDNRGSCH-RGLKFEGAFkykmgqiEIDDQVEGLQYLASR 697
Cdd:pfam00561   1 PPVLLLHGLPGS--------SDLWRKLaPALARDGFRVIALDLRGFGKsSRPKAQDDY-------RTDDLAEDLEYILEA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563  698 YDfidLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPS 777
Cdd:pfam00561  66 LG---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAK 142

                         170
                  ....*....|....*
gi 767984563  778 EPNRLLLLHGFLDEN 792
Cdd:pfam00561 143 LLALLLLRLRLLKAL 157
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
607-734 2.14e-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: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 607 LYKPHD-LQPGKKYPTVLFIYGGPQVQlvnNRFkgVKYFRLNT-LASL-------GYVVVVIDNRGSCHRGLKFEGAFKY 677
Cdd:COG2382   99 VYLPPGyDNPGKKYPVLYLLDGGGGDE---QDW--FDQGRLPTiLDNLiaagkipPMIVVMPDGGDGGDRGTEGPGNDAF 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767984563 678 kmgQIEIDDQVegLQYLASRYDFI-DLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIA 734
Cdd:COG2382  174 ---ERFLAEEL--IPFVEKNYRVSaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
648-743 2.55e-03

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 40.15  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984563 648 TLASLGYVVVVIDNRG---SchrglkfEGAFKYkmGQIEIDDQVEGLQYLASRYdfidLDRVGIHGWSYGGYLSLMALMQ 724
Cdd:COG2945   50 ALVAAGFAVLRFNFRGvgrS-------EGEFDE--GRGELDDAAAALDWLRAQN----PLPLWLAGFSFGAYVALQLAMR 116

                         90
                 ....*....|....*....
gi 767984563 725 RSDIFRVAIAGAPVTLWIF 743
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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