|
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 |
9.28e-113 |
|
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: 340.01 E-value: 9.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520 1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984567 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 |
2.71e-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: 2.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930 81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324
|
410 420
....*....|....*....|....*...
gi 767984567 570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 super family |
cl47529 |
Prolyl oligopeptidase family; |
687-806 |
1.32e-45 |
|
Prolyl oligopeptidase family; The actual alignment was detected with superfamily member pfam00326:
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 162.78 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767984567 767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY 806
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGY 129
|
|
|
|
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 |
9.28e-113 |
|
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: 340.01 E-value: 9.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520 1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984567 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 |
2.71e-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: 2.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930 81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324
|
410 420
....*....|....*....|....*...
gi 767984567 570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
687-806 |
1.32e-45 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 162.78 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767984567 767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY 806
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGY 129
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
637-817 |
5.73e-41 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 150.17 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 637 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKfEG 716
Cdd:COG1506 1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGES-AG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 717 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 793
Cdd:COG1506 68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180
....*....|....*....|....
gi 767984567 794 RYMGHPDQNEQGYYLGSVAMQAEK 817
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADK 166
|
|
|
|
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 |
9.28e-113 |
|
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: 340.01 E-value: 9.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 8 MKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVK 87
Cdd:pfam19520 1 MSVPSTACNMAAAMETEQLGLEIFETAECEENVESEDSPKLEPFYVERYSWSQLKKLLTDTRKYHGYMMAKAPHDFMFVK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984567 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 |
2.71e-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: 2.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 175 SGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPN--IRMDPKLCPaDPDWIAFIHSNDIWISNIVTREERRLTYv 252
Cdd:pfam00930 3 DGKYLLLATNYTKNWRHSYTADYYIYDLETNRVEPLPPGegKIQDAKWSP-DGDRLAFVRDNNLYVRELATGKEIQITS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 253 hnelanMEEDARSAGVATFVLQEE-FDRYSGYWWCPKAEttpsggkilRILYEENDESEVEIIHVTSPMLETR--RADSF 329
Cdd:pfam00930 81 ------DGSDGIFNGVADWVYEEEvLGSNSAVWWSPDGS---------RLAFLRFDESEVPIITLPYYTDEGPgpEVREI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 330 RYPKTGTANPKVTFKMSEImidAEGRIIdvidkeLIQPFEILFEGVEYIARAGWTPEGKyAWSILLDRSQTRLQIVLISP 409
Cdd:pfam00930 146 KYPKAGAPNPTVELFVYDL---ASGKTV------EVVPPDDLSDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 410 ElfipveddvmerqrliesvpdSVTPLIIYEETTDIWINIHDIFHVFPQSHEEeieFIFASEcKTGFRHLYKITSIlkes 489
Cdd:pfam00930 216 E---------------------TGRTVVILEETSDGWVELHQDPHFIKRDGSG---FLWISE-RDGYNHLYLYDLD---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 490 kykrssGGLPapsdfkcpikeeIAITSGEWEVlgrhGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDR 569
Cdd:pfam00930 267 ------GKSP------------IQLTSGNWEV----TSILGVDETRDLVYFTATEDSPTERHLYSVSLDSGGEPTCLTDD 324
|
410 420
....*....|....*....|....*...
gi 767984567 570 GYSH--SCCISQHCDFFISKYSNQKNPH 595
Cdd:pfam00930 325 SGDHdySASFSPNGSYYVLTYSGPDTPP 352
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
687-806 |
1.32e-45 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 162.78 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 687 FRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYdFIDLDRVGIHGWSYGGYLSLMALM 766
Cdd:pfam00326 5 WNAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQG-YTDPDRLAIWGGSYGGYLTGAALN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767984567 767 QRSDIFRVAIAGAPVTLWIFYDTG----YTERYMGH--PDQNEQGY 806
Cdd:pfam00326 84 QRPDLFKAAVAHVPVVDWLAYMSDtslpFTERYMEWgnPWDNEEGY 129
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
637-817 |
5.73e-41 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 150.17 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 637 SFESTTGFTLYGMLYKPHDlqpGKKYPTVLFIYGGPQVQLVNNRFkgvkyfRLNTLASLGYVVVVIDNRGschRGLKfEG 716
Cdd:COG1506 1 TFKSADGTTLPGWLYLPAD---GKKYPVVVYVHGGPGSRDDSFLP------LAQALASRGYAVLAPDYRG---YGES-AG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 717 afkyKMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTG---YTE 793
Cdd:COG1506 68 ----DWGGDEVDDVLAAIDYLAAR-PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTtreYTE 142
|
170 180
....*....|....*....|....
gi 767984567 794 RYMGHPDQNEQGYYLGSVAMQAEK 817
Cdd:COG1506 143 RLMGGPWEDPEAYAARSPLAYADK 166
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
634-771 |
1.05e-12 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 68.79 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 634 EIFSFESTTGFTLYGMLYKPHDlqPGKKYPTVLFIYGgpqvqlvnnrFKGVKYFRL---NTLASLGYVVVVIDNRG---S 707
Cdd:COG1073 11 EDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHG----------NGGVKEQRAlyaQRLAELGFNVLAFDYRGygeS 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984567 708 chrglkfEGAFKYkMGQIEIDDQVEGLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDI 771
Cdd:COG1073 79 -------EGEPRE-EGSPERRDARAAVDYLRTL-PGVDPERIGLLGISLGGGYALNAAATDPRV 133
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
634-782 |
7.16e-11 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 63.06 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 634 EIFSFESTTGFTLYGMLYKPHDlqpGKKYPTVLFI--YGGpqvqlVNNRFKGVkyfrLNTLASLGYVVVVID--NRGSch 709
Cdd:COG0412 4 ETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLheIFG-----LNPHIRDV----ARRLAAAGYVVLAPDlyGRGG-- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984567 710 RGLKFEGAFKYkMGQIEIDDQVE----GLQYLASRyDFIDLDRVGIHGWSYGGYLSLMALMQRSDIfR--VAIAGAPVT 782
Cdd:COG0412 70 PGDDPDEARAL-MGALDPELLAAdlraALDWLKAQ-PEVDAGRVGVVGFCFGGGLALLAAARGPDL-AaaVSFYGGLPA 145
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
650-786 |
7.37e-08 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 54.20 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 650 LYKPHDLQPGKKYPTVLFIYGG------PQVQLVNnrfKGVKYFRLNTLASLGYVVVVidnrGSCHRGlkfegafKYKMG 723
Cdd:COG4099 37 LYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTH---GAPKFINPENQAKFPAIVLA----PQCPED-------DYWSD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984567 724 QIEIDDQVEGLQYLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFR--VAIAGAP----------VTLWIF 786
Cdd:COG4099 103 TKALDAVLALLDDLIAEYR-IDPDRIYLTGLSMGGYGTWDLAARYPDLFAaaVPICGGGdpanaanlkkVPVWIF 176
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
650-764 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 650 LYKPhdLQPGKKYPTVLFIYGGPQvqlvnnrFKGVKY----FRLNTLASL---GYVVVVIDNRGSCHRglKFEGAfkykm 722
Cdd:pfam20434 3 IYLP--KNAKGPYPVVIWIHGGGW-------NSGDKEadmgFMTNTVKALlkaGYAVASINYRLSTDA--KFPAQ----- 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767984567 723 gqieIDDQVEGLQYL---ASRYDfIDLDRVGIHGWSYGGYLSLMA 764
Cdd:pfam20434 67 ----IQDVKAAIRFLranAAKYG-IDTNKIALMGFSAGGHLALLA 106
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
692-775 |
1.50e-05 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 47.79 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 692 LASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEI------D-----DQVEGLQYLASRY-DFIDLDRVGIHGWSYGGY 759
Cdd:COG4188 85 LASHGYVVAAPDHPGSNAADLSAALDGLADALDPEElwerplDlsfvlDQLLALNKSDPPLaGRLDLDRIGVIGHSLGGY 164
|
90
....*....|....*.
gi 767984567 760 LSLMALMQRSDIFRVA 775
Cdd:COG4188 165 TALALAGARLDFAALR 180
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
632-780 |
2.16e-05 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 46.53 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 632 PPEIFSFESTTGFTLYGMLYKPHDlQPGkkyPTVLFIYGGpqvqlvnnRFKGVKYFRL-NTLASLGYVVVVIDNRG---S 707
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRPAG-SPR---GTVVLVHGL--------GEHSGRYAELaEALAAAGYAVLAFDLRGhgrS 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984567 708 CHRGLKFEGAFKYkmgqieIDDQVEGLQYLASRYDfidlDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAP 780
Cdd:COG2267 70 DGPRGHVDSFDDY------VDDLRAALDALRARPG----LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
|
|
| Peptidase_S15 |
pfam02129 |
X-Pro dipeptidyl-peptidase (S15 family); |
650-790 |
4.14e-05 |
|
X-Pro dipeptidyl-peptidase (S15 family);
Pssm-ID: 396621 [Multi-domain] Cd Length: 264 Bit Score: 46.18 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 650 LYKPhdLQPGKKYPTVLFI--YGGPqvqlvNNRFKGVKYFRLN-TLASLGYVVVVIDNRGSchRGLkfEGAFKYKMGQiE 726
Cdd:pfam02129 9 IYRP--TKTGGPVPALLTRspYGAR-----RDGASDLALAHPEwEFAARGYAVVYQDVRGT--GGS--EGVFTVGGPQ-E 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984567 727 IDDQVEGLQYLASRYDFIDldRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLW--IFYDTG 790
Cdd:pfam02129 77 AADGKDVIDWLAGQPWCNG--KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLydYYREGG 140
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
645-768 |
3.05e-04 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 44.15 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 645 TLYGMLYKPHDLQpgKKYPTVLFI--YGgpqvqlVNNRFKGVKYFRLNTLASLGYVVVVIDNRG---SchrglkfEGAFk 719
Cdd:COG2936 24 RLAADIYRPKDAE--GPVPVILERtpYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGtggS-------EGEF- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767984567 720 YKMGQIEIDDQVEGLQYLAsrydfiDLD----RVGIHGWSYGGYLSLMALMQR 768
Cdd:COG2936 88 DPYRVDEQTDGYDTIDWLA------KQPwsngKVGMIGISYGGFTQLAAAADR 134
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
650-782 |
6.61e-04 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 41.78 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 650 LYKPHDlqPGKKYPTVLFIYGGpqvqlvnnrfkgvkYFRLNTL-----------ASLGYVVVVIDNRgschrgL----KF 714
Cdd:COG0657 3 VYRPAG--AKGPLPVVVYFHGG--------------GWVSGSKdthdplarrlaARAGAAVVSVDYR------LapehPF 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984567 715 EGAfkykmgqieIDDQVEGLQYLASRYDF--IDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGA----PVT 782
Cdd:COG0657 61 PAA---------LEDAYAALRWLRANAAElgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQvliyPVL 125
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
736-784 |
1.87e-03 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 40.74 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767984567 736 YLASRYDfIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPvTLW 784
Cdd:COG2819 120 YIDKRYR-TDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP-SLW 166
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
650-777 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 650 LYKPHD-LQPGKKYPTVLFIYGGPQVQlvnNRFkgVKYFRLNT-LASL-------GYVVVVIDNRGSCHRGLKFEGAFKY 720
Cdd:COG2382 99 VYLPPGyDNPGKKYPVLYLLDGGGGDE---QDW--FDQGRLPTiLDNLiaagkipPMIVVMPDGGDGGDRGTEGPGNDAF 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767984567 721 kmgQIEIDDQVegLQYLASRYDFI-DLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIA 777
Cdd:COG2382 174 ---ERFLAEEL--IPFVEKNYRVSaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
691-786 |
2.46e-03 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 40.15 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 691 TLASLGYVVVVIDNRG---SchrglkfEGAFKYkmGQIEIDDQVEGLQYLASRYdfidLDRVGIHGWSYGGYLSLMALMQ 767
Cdd:COG2945 50 ALVAAGFAVLRFNFRGvgrS-------EGEFDE--GRGELDDAAAALDWLRAQN----PLPLWLAGFSFGAYVALQLAMR 116
|
90
....*....|....*....
gi 767984567 768 RSDIFRVAIAGAPVTLWIF 786
Cdd:COG2945 117 LPEVEGLILVAPPVNRYDF 135
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
663-789 |
2.72e-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: 40.18 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984567 663 PTVLFIYGGPQVqlvnnrfkGVKYFRL-NTLASLGYVVVVIDNRGSCH-RGLKFEGAFkykmgqiEIDDQVEGLQYLASR 740
Cdd:pfam00561 1 PPVLLLHGLPGS--------SDLWRKLaPALARDGFRVIALDLRGFGKsSRPKAQDDY-------RTDDLAEDLEYILEA 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767984567 741 YDfidLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDT 789
Cdd:pfam00561 66 LG---LEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDE 111
|
|
|