|
Name |
Accession |
Description |
Interval |
E-value |
| DPPIV_N |
pfam00930 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
99-426 |
4.44e-113 |
|
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: 345.07 E-value: 4.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 99 TQGGLVGFDMLARKVTYLFDTNEETASLDFSPVGDRVAYVRNHNLYIArggKLGEGmsRAIAVTIDGTETLVYGQA--VH 176
Cdd:pfam00930 21 YTADYYIYDLETNRVEPLPPGEGKIQDAKWSPDGDRLAFVRDNNLYVR---ELATG--KEIQITSDGSDGIFNGVAdwVY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 177 QRE-FGIEKGTFWSPKGSCLAFYRMDQSMVKPTPIVDYHPLEA--ESKPLYYPMAGTPSHHVTVGIYHLATGKTVYLQTG 253
Cdd:pfam00930 96 EEEvLGSNSAVWWSPDGSRLAFLRFDESEVPIITLPYYTDEGPgpEVREIKYPKAGAPNPTVELFVYDLASGKTVEVVPP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 254 E---PKEKFLTNLSWSPDENiLYVAEVNRAQNECKVNAYDAETGRfVRTLFVETDKHYVEPLHPLTFLPGSNNQFIWQSR 330
Cdd:pfam00930 176 DdlsDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDAETGR-TVVILEETSDGWVELHQDPHFIKRDGSGFLWISE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 331 RDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAGFDPKGTRLYFESTEASPLERHFYCIDIK-GGKTKDLTPESGMHR--TQ 407
Cdd:pfam00930 254 RDGYNHLYLYDLDGKSPIQLTSGNWEVTSILGVDETRDLVYFTATEDSPTERHLYSVSLDsGGEPTCLTDDSGDHDysAS 333
|
330
....*....|....*....
2DCM_A 408 LSPDGSAIIDIFQSPTVPR 426
Cdd:pfam00930 334 FSPNGSYYVLTYSGPDTPP 352
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
462-706 |
1.15e-59 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 200.63 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 462 AADGqTPLYYKLTMPlhfDPAKKYPVIVYVYGGPHAQLVTKTWRSSvggwdiYMAQKGYAVFTVDSRGsanRGAAFeqvi 541
Cdd:COG1506 4 SADG-TTLPGWLYLP---ADGKKYPVVVYVHGGPGSRDDSFLPLAQ------ALASRGYAVLAPDYRG---YGESA---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 542 hRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDVFKVGVAGGPVIDWNRY---EIMYGERYF 618
Cdd:COG1506 67 -GDWGGDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYygtTREYTERLM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 619 DAPQENPEGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNVMGPDRVHLYETI 698
Cdd:COG1506 146 GGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERI 225
|
....*...
2DCM_A 699 TRYFTDHL 706
Cdd:COG1506 226 LDFLDRHL 233
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
514-706 |
1.66e-48 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 169.72 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 514 YMAQKGYAVFTVDSRGSANRGAAFEQVIHRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDV 593
Cdd:pfam00326 9 LLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 594 FKVGVAGGPVIDWNRY----EIMYGERYFD--APQENPEGYDAANLLKRAGDLK--GRLMLIHGAIDPVVVWQHSLLFLD 665
Cdd:pfam00326 89 FKAAVAHVPVVDWLAYmsdtSLPFTERYMEwgNPWDNEEGYDYLSPYSPADNVKvyPPLLLIHGLLDDRVPPWQSLKLVA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
2DCM_A 666 ACVKARTYPDYYVYPSHEHNVMGPD-RVHLYETITRYFTDHL 706
Cdd:pfam00326 169 ALQRKGVPFLLLIFPDEGHGIGKPRnKVEEYARELAFLLEYL 210
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
326-416 |
1.07e-09 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 57.76 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 326 IWQSRRDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAgFDPKGTRLYFESTEASPleRHFYCIDIKGGKTKDLTPESGMHR 405
Cdd:COG0823 2 AFTLSRDGNSDIYVVDLDGGEPRRLTNSPGIDTSPA-WSPDGRRIAFTSDRGGG--PQIYVVDADGGEPRRLTFGGGYNA 78
|
90
....*....|..
2DCM_A 406 T-QLSPDGSAII 416
Cdd:COG0823 79 SpSWSPDGKRLA 90
|
|
| Esterase_713 |
cd12807 |
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ... |
482-547 |
1.57e-03 |
|
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214006 Cd Length: 315 Bit Score: 41.16 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 482 AKKYPvIVYVYGGPHAqlvTKTWRSSVGG---WDIYMAQKGYAVFTVDSRGsanRG-AAFEQVIHRRLGQ 547
Cdd:cd12807 51 KKKYP-IVLVHGCCLT---GKTWETTPDGrmgWDEYFVRKGHPVYVVDQVG---RGrSGFDPTIINAVKL 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DPPIV_N |
pfam00930 |
Dipeptidyl peptidase IV (DPP IV) N-terminal region; This family is an alignment of the region ... |
99-426 |
4.44e-113 |
|
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: 345.07 E-value: 4.44e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 99 TQGGLVGFDMLARKVTYLFDTNEETASLDFSPVGDRVAYVRNHNLYIArggKLGEGmsRAIAVTIDGTETLVYGQA--VH 176
Cdd:pfam00930 21 YTADYYIYDLETNRVEPLPPGEGKIQDAKWSPDGDRLAFVRDNNLYVR---ELATG--KEIQITSDGSDGIFNGVAdwVY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 177 QRE-FGIEKGTFWSPKGSCLAFYRMDQSMVKPTPIVDYHPLEA--ESKPLYYPMAGTPSHHVTVGIYHLATGKTVYLQTG 253
Cdd:pfam00930 96 EEEvLGSNSAVWWSPDGSRLAFLRFDESEVPIITLPYYTDEGPgpEVREIKYPKAGAPNPTVELFVYDLASGKTVEVVPP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 254 E---PKEKFLTNLSWSPDENiLYVAEVNRAQNECKVNAYDAETGRfVRTLFVETDKHYVEPLHPLTFLPGSNNQFIWQSR 330
Cdd:pfam00930 176 DdlsDADYYITRVKWVPDGK-LLVQWLNRDQNRLKVVLCDAETGR-TVVILEETSDGWVELHQDPHFIKRDGSGFLWISE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 331 RDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAGFDPKGTRLYFESTEASPLERHFYCIDIK-GGKTKDLTPESGMHR--TQ 407
Cdd:pfam00930 254 RDGYNHLYLYDLDGKSPIQLTSGNWEVTSILGVDETRDLVYFTATEDSPTERHLYSVSLDsGGEPTCLTDDSGDHDysAS 333
|
330
....*....|....*....
2DCM_A 408 LSPDGSAIIDIFQSPTVPR 426
Cdd:pfam00930 334 FSPNGSYYVLTYSGPDTPP 352
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
462-706 |
1.15e-59 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 200.63 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 462 AADGqTPLYYKLTMPlhfDPAKKYPVIVYVYGGPHAQLVTKTWRSSvggwdiYMAQKGYAVFTVDSRGsanRGAAFeqvi 541
Cdd:COG1506 4 SADG-TTLPGWLYLP---ADGKKYPVVVYVHGGPGSRDDSFLPLAQ------ALASRGYAVLAPDYRG---YGESA---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 542 hRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDVFKVGVAGGPVIDWNRY---EIMYGERYF 618
Cdd:COG1506 67 -GDWGGDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYygtTREYTERLM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 619 DAPQENPEGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNVMGPDRVHLYETI 698
Cdd:COG1506 146 GGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERI 225
|
....*...
2DCM_A 699 TRYFTDHL 706
Cdd:COG1506 226 LDFLDRHL 233
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
514-706 |
1.66e-48 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 169.72 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 514 YMAQKGYAVFTVDSRGSANRGAAFEQVIHRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDV 593
Cdd:pfam00326 9 LLADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 594 FKVGVAGGPVIDWNRY----EIMYGERYFD--APQENPEGYDAANLLKRAGDLK--GRLMLIHGAIDPVVVWQHSLLFLD 665
Cdd:pfam00326 89 FKAAVAHVPVVDWLAYmsdtSLPFTERYMEwgNPWDNEEGYDYLSPYSPADNVKvyPPLLLIHGLLDDRVPPWQSLKLVA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
2DCM_A 666 ACVKARTYPDYYVYPSHEHNVMGPD-RVHLYETITRYFTDHL 706
Cdd:pfam00326 169 ALQRKGVPFLLLIFPDEGHGIGKPRnKVEEYARELAFLLEYL 210
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
459-691 |
1.54e-13 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 70.38 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 459 TIMAADGQT-PLYykLTMPlhfDPAKKYPVIVYVYG----GPHAQLVTKTWrssvggwdiymAQKGYAVFTVDSRGSANR 533
Cdd:COG0412 7 TIPTPDGVTlPGY--LARP---AGGGPRPGVVVLHEifglNPHIRDVARRL-----------AAAGYVVLAPDLYGRGGP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 534 GAAFEQVIHRRLGQTE---MADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMtTNLMLTHGDVFKVGVAggpvidwnrye 610
Cdd:COG0412 71 GDDPDEARALMGALDPellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGL-ALLAAARGPDLAAAVS----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 611 iMYGeryfdapqenpeGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNVMGPD 690
Cdd:COG0412 139 -FYG------------GLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHGFTNPG 205
|
.
2DCM_A 691 R 691
Cdd:COG0412 206 R 206
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
450-706 |
5.24e-13 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 69.56 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 450 YAMPEIRTGTIMAADGqtplyYKLTMPLHF--DPAKKYPVIVYVYGGPHaqlvTKTWRSSVGGWdiyMAQKGYAVFTVDS 527
Cdd:COG1073 5 SDKVNKEDVTFKSRDG-----IKLAGDLYLpaGASKKYPAVVVAHGNGG----VKEQRALYAQR---LAELGFNVLAFDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 528 RGS-ANRGAAFEQVIHRRLgqtemaDQMCGVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDVfK-----VGVAGG 601
Cdd:COG1073 73 RGYgESEGEPREEGSPERR------DARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRV-KavildSPFTSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 602 PVIDWNRYEIMYGERYFDAPQENPEGY-----DAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARtypDY 676
Cdd:COG1073 146 EDLAAQRAKEARGAYLPGVPYLPNVRLasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPK---EL 222
|
250 260 270
....*....|....*....|....*....|..
2DCM_A 677 YVYPSHEHNvMGPDRVHL--YETITRYFTDHL 706
Cdd:COG1073 223 LIVPGAGHV-DLYDRPEEeyFDKLAEFFKKNL 253
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
326-416 |
1.07e-09 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 57.76 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 326 IWQSRRDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAgFDPKGTRLYFESTEASPleRHFYCIDIKGGKTKDLTPESGMHR 405
Cdd:COG0823 2 AFTLSRDGNSDIYVVDLDGGEPRRLTNSPGIDTSPA-WSPDGRRIAFTSDRGGG--PQIYVVDADGGEPRRLTFGGGYNA 78
|
90
....*....|..
2DCM_A 406 T-QLSPDGSAII 416
Cdd:COG0823 79 SpSWSPDGKRLA 90
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
239-395 |
6.66e-07 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 49.67 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 239 IYHLATGKTVYLQTGEPKEkflTNLSWSPDEN-ILYVAEVNRAQNeckVNAYDAETGRFVRTLFveTDKHYVEPlhplTF 317
Cdd:COG0823 15 VVDLDGGEPRRLTNSPGID---TSPAWSPDGRrIAFTSDRGGGPQ---IYVVDADGGEPRRLTF--GGGYNASP----SW 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2DCM_A 318 LPgSNNQFIWQSRRDGWNHLYLYDTTGRLIRQVTKGEWEVTnfagFDPKGTRLYFESTEASplERHFYCIDIKGGKTK 395
Cdd:COG0823 83 SP-DGKRLAFVSRSDGRFDIYVLDLDGGAPRRLTDGPGSPS----WSPDGRRIVFSSDRGG--RPDLYVVDLDGRKRR 153
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
452-702 |
8.87e-07 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 50.39 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 452 MPEiRTGTIMAADGQTpLYYKLTMPLhfDPAKkyPVIVYVYG-GPHAqlvtKTWRSSVGgwdiYMAQKGYAVFTVD---- 526
Cdd:COG2267 1 MTR-RLVTLPTRDGLR-LRGRRWRPA--GSPR--GTVVLVHGlGEHS----GRYAELAE----ALAAAGYAVLAFDlrgh 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 527 --SRGSANRGAAFEQVIhrrlgqtEMADQMcgVDFLKSQSwvdADRIGVHGWAYGGFMTTNLMLTHGDVFKVGVAGGPvi 604
Cdd:COG2267 67 grSDGPRGHVDSFDDYV-------DDLRAA--LDALRARP---GLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 605 dwnryeimygeRYFDAPQENP--EGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTypdYYVYPSH 682
Cdd:COG2267 133 -----------AYRADPLLGPsaRWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVE---LVLLPGA 198
|
250 260
....*....|....*....|.
2DCM_A 683 EHNVMG-PDRVHLYETITRYF 702
Cdd:COG2267 199 RHELLNePAREEVLAAILAWL 219
|
|
| Axe1 |
COG3458 |
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ... |
465-706 |
1.33e-06 |
|
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442681 [Multi-domain] Cd Length: 318 Bit Score: 50.96 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 465 GQTPLYYKLTMPLHfdpAKKYPVIVYV--YGGphaqlvtktwRSSVGGWDIYMAQKGYAVFTVDSRG-SANRGAAFEQVI 541
Cdd:COG3458 65 GGARIYGWLLRPKG---EGPLPAVVEFhgYGG----------GRGLPHEDLDWAAAGYAVLVMDTRGqGSSWGDTPDPGG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 542 ---------------------HRRLgqteMADQMCGVDFLKSQSWVDADRIGVHGWAYGGFMT----------TNLMLTH 590
Cdd:COG3458 132 ysggalpgymtrgiddpdtyyYRRV----YLDAVRAVDALRSLPEVDGKRIGVTGGSQGGGLAlaaaaldprvKAAAADV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 591 ---GD---VFKVGVAGGpvidwnryeimYGE--RYFDAPQENPEG-------YDAANLLKRAgdlKGRLMLIHGAIDPVV 655
Cdd:COG3458 208 pflCDfrrALELGRAGP-----------YPEirRYLRRHREREPEvfetlsyFDAVNFARRI---KAPVLFSVGLMDPVC 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
2DCM_A 656 ----VWQ--HSLlfldACVKartypDYYVYPSHEHNVMGPDRVhlyETITRYFTDHL 706
Cdd:COG3458 274 ppstVFAayNAL----AGPK-----EILVYPFNGHEGGGPEQQ---DRQLAFLRELL 318
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
459-686 |
5.14e-06 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 48.43 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 459 TIMAADGQTPLYYKLTMPLHFDPAKKYPVIVYVYGG------PHAQLVTKTWRssvggWDIYMAQKGYAVFTVDSRGSAN 532
Cdd:COG4099 23 TFTDPSDGDTLPYRLYLPKGYDPGKKYPLVLFLHGAgergtdNEKQLTHGAPK-----FINPENQAKFPAIVLAPQCPED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 533 RGAAFEqvihrrlGQTEMADQMcgVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDVFkvgVAGGPVidwnryeim 612
Cdd:COG4099 98 DYWSDT-------KALDAVLAL--LDDLIAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPI--------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DCM_A 613 ygeryfdAPQENPEgyDAANLLKRAgdlkgrLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNV 686
Cdd:COG4099 157 -------CGGGDPA--NAANLKKVP------VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
236-370 |
6.24e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 46.06 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 236 TVGIYHLATGKTvyLQTGEPKEKFLTNLSWSPDENILYVAEVNRaqnecKVNAYDAETGRFVRTLfvetdKHYVEPLHPL 315
Cdd:COG2319 185 TVRLWDLATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADG-----TVRLWDLATGKLLRTL-----TGHSGSVRSV 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
2DCM_A 316 TFLPgsNNQFIWQSRRDGwnHLYLYDTTGRLIRQVTKGEWEVTNFAGFDPKGTRL 370
Cdd:COG2319 253 AFSP--DGRLLASGSADG--TVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
471-603 |
2.63e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 43.45 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 471 YKLTMPLHFDPAKKYPVIVYV--YGGPHAQLVTKTwrssvgGWDIYMAQKGYAVFTVD-SRGSANRGAAFEQVIHRRLGQ 547
Cdd:COG3509 39 YRLYVPAGYDGGAPLPLVVALhgCGGSAADFAAGT------GLNALADREGFIVVYPEgTGRAPGRCWNWFDGRDQRRGR 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
2DCM_A 548 TEMA--DQMcgVDFLKSQSWVDADRIGVHGWAYGGFMTTNLMLTHGDVFKvgvAGGPV 603
Cdd:COG3509 113 DDVAfiAAL--VDDLAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFA---AVAPV 165
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
483-663 |
3.62e-04 |
|
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: 42.55 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 483 KKYPVIVYVYGgphaqlvtktwrssvGGW--------DIYM-------AQKGYAVFTVDSRGSANrgAAFEQVIHrrlgq 547
Cdd:pfam20434 11 GPYPVVIWIHG---------------GGWnsgdkeadMGFMtntvkalLKAGYAVASINYRLSTD--AKFPAQIQ----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 548 temaDQMCGVDFLKSQSW---VDADRIGVHGWAYGGF------MTTNLMLTHGDVFKVGVAGGP-------VIDWnrY-- 609
Cdd:pfam20434 69 ----DVKAAIRFLRANAAkygIDTNKIALMGFSAGGHlallagLSNNNKEFEGNVGDYTPESSKesfkvnaVVDF--Ygp 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2DCM_A 610 ---EIMYGERYFD------------APQENPEGYDAANLLK--RAGDLKgrLMLIHGAIDPVVVWQHSLLF 663
Cdd:pfam20434 143 tdlLDMDSCGTHNdakspetlllgaPPLENPDLAKSASPITyvDKNDPP--FLIIHGDKDPLVPYCQSVLL 211
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
236-370 |
3.64e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 236 TVGIYHLATGKTvyLQTGEPKEKFLTNLSWSPDENILYVAEVNRaqnecKVNAYDAETGRFVRTLfvetdKHYVEPLHPL 315
Cdd:COG2319 143 TVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDGKLLASGSDDG-----TVRLWDLATGKLLRTL-----TGHTGAVRSV 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
2DCM_A 316 TFLPgsNNQFIWQSRRDGwnHLYLYD-TTGRLIRQVTKGEWEVTNFAgFDPKGTRL 370
Cdd:COG2319 211 AFSP--DGKLLASGSADG--TVRLWDlATGKLLRTLTGHSGSVRSVA-FSPDGRLL 261
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
478-704 |
8.48e-04 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 42.15 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 478 HFDPAKKYPVIVYVYGGPHAQlvtKTWRSSVGGWDIY--MAQKG----YAVFTVDSRGSANRG------AAFEQVIHRRL 545
Cdd:COG2382 105 YDNPGKKYPVLYLLDGGGGDE---QDWFDQGRLPTILdnLIAAGkippMIVVMPDGGDGGDRGtegpgnDAFERFLAEEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 546 gqtemadqmcgVDFLKSQ--SWVDADRIGVHGWAYGGFMTTNLMLTHGDVF-KVGVAGGpvidwnryeimygerYFDAPQ 622
Cdd:COG2382 182 -----------IPFVEKNyrVSADPEHRAIAGLSMGGLAALYAALRHPDLFgYVGSFSG---------------SFWWPP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 623 ENPEGYDAANLLKRAGDLKG-RLMLIHGAIDPvvVWQHSLLFLDACVKARTYPDYYVYPS-HEHNVmgpDRVHLYETITR 700
Cdd:COG2382 236 GDADRGGWAELLAAGAPKKPlRFYLDVGTEDD--LLEANRALAAALKAKGYDVEYREFPGgHDWAV---WRAALPDFLPW 310
|
....
2DCM_A 701 YFTD 704
Cdd:COG2382 311 LFKD 314
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
228-390 |
1.55e-03 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 41.03 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 228 AGTPSHHVTVG-IYHLATGKTVylqtgepkEKFLTNLS------WSPDENILYVAEVNRaqneCKVNAYD-AETGRFV-R 298
Cdd:COG3386 108 FTDMGEYLPTGaLYRVDPDGSL--------RVLADGLTfpngiaFSPDGRTLYVADTGA----GRIYRFDlDADGTLGnR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 299 TLFVETDKhyvEPLHP--LTFLPGSNnqfIWQSRRDGWnHLYLYDTTGRLIRQVTKGEWEVTNFAgFD-PKGTRLYFEST 375
Cdd:COG3386 176 RVFADLPD---GPGGPdgLAVDADGN---LWVALWGGG-GVVRFDPDGELLGRIELPERRPTNVA-FGgPDLRTLYVTTA 247
|
170
....*....|....*
2DCM_A 376 EASPLERHFYCIDIK 390
Cdd:COG3386 248 RSLPLAGALFRVRVD 262
|
|
| Esterase_713 |
cd12807 |
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ... |
482-547 |
1.57e-03 |
|
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214006 Cd Length: 315 Bit Score: 41.16 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 482 AKKYPvIVYVYGGPHAqlvTKTWRSSVGG---WDIYMAQKGYAVFTVDSRGsanRG-AAFEQVIHRRLGQ 547
Cdd:cd12807 51 KKKYP-IVLVHGCCLT---GKTWETTPDGrmgWDEYFVRKGHPVYVVDQVG---RGrSGFDPTIINAVKL 113
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
267-413 |
6.94e-03 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 38.91 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 267 PDENILYVAevNRAQNecKVNAYDAETGRFVRTLFVETDKHYVEpLHPltflpgsNNQFIWQSRRDGwNHLYLYDT-TGR 345
Cdd:COG3391 77 ADGRRLYVA--NSGSG--RVSVIDLATGKVVATIPVGGGPRGLA-VDP-------DGGRLYVADSGN-GRVSVIDTaTGK 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2DCM_A 346 LIRQVTKGEWevTNFAGFDPKGTRLYFESTEASPLERHFYCIDIKGGKTKDLTPESGM-HRTQLSPDGS 413
Cdd:COG3391 144 VVATIPVGAG--PHGIAVDPDGKRLYVANSGSNTVSVIVSVIDTATGKVVATIPVGGGpVGVAVSPDGR 210
|
|
| COG2936 |
COG2936 |
Predicted acyl esterase [General function prediction only]; |
456-606 |
9.26e-03 |
|
Predicted acyl esterase [General function prediction only];
Pssm-ID: 442179 [Multi-domain] Cd Length: 555 Bit Score: 39.14 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DCM_A 456 RTGTIMAADgqtplyykLTMPLhfDPAKKYPVIVY--VYGgphaqlVTKTWRSSVGGWDIYMAQKGYAVFTVDSRGSANR 533
Cdd:COG2936 20 RDGVRLAAD--------IYRPK--DAEGPVPVILErtPYG------KRDGTAGRDLGPHPYFAERGYAVVVQDVRGTGGS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DCM_A 534 GAAFEqvihrRLGQTEMADqmcG---VDFLKSQSWVDaDRIGVHGWAYGGFMTTNLMLTHGDVFKVGVAGGPVIDW 606
Cdd:COG2936 84 EGEFD-----PYRVDEQTD---GydtIDWLAKQPWSN-GKVGMIGISYGGFTQLAAAADRPPALKAIVPQAPTSDR 150
|
|
| |
