|
Name |
Accession |
Description |
Interval |
E-value |
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
346-596 |
2.95e-52 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 179.06 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 346 DLDFEAILLQPsnsPDKSQVPMVVMPHGGPHSSFvTAWMLFPAMLCKMGFAVLLVNYRGstgFGQDSilslpGNVGHQDV 425
Cdd:COG1506 7 GTTLPGWLYLP---ADGKKYPVVVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRG---YGESA-----GDWGGDEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 426 KDVQFAVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDipdwcmvetgfPYSND 505
Cdd:COG1506 75 DDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTR-----------EYTER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 506 YLPDLNVLEEMLDK-SPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTHALSevEVESDSF 584
Cdd:COG1506 144 LMGGPWEDPEAYAArSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS--GAGAPDY 221
|
250
....*....|...
gi 1720431501 585 MNTVL-WLHTHLG 596
Cdd:COG1506 222 LERILdFLDRHLK 234
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
375-572 |
1.58e-35 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 132.74 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 375 PHSSFVTAWmlfpamLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVQQVLQEEHFDARRVALMGGSHG 454
Cdd:pfam00326 1 PSFSWNAQL------LADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 455 GFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDIP---DWCmvETGFPYSNdylpdlnvLEEMLDKSPIKYIPQVK-- 529
Cdd:pfam00326 75 GYLTGAALNQRPDLFKAAVAHVPVVDWLAYMSDTSLPfteRYM--EWGNPWDN--------EEGYDYLSPYSPADNVKvy 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720431501 530 TPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTH 572
Cdd:pfam00326 145 PPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGH 187
|
|
| APEH_N |
pfam19283 |
Acylamino-acid-releasing enzyme, N-terminal domain; This entry represents the N-terminal ... |
19-150 |
2.89e-28 |
|
Acylamino-acid-releasing enzyme, N-terminal domain; This entry represents the N-terminal region from the Acylamino-acid-releasing enzyme (EC:3.4.19.1). The protein is involved in removing the N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. This domain does not represent the catalytic domain which is found at the C-terminus of these proteins.
Pssm-ID: 466026 Cd Length: 274 Bit Score: 114.27 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 19 SWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDEEMARPKkpdqaIKGDqfvFYEDWGETMVSKSIPVLCVLDIESGN 98
Cdd:pfam19283 140 SWNSDETLIAYVAEEPSPSKPTFGDLGYKKGGSSEKDCGSWK-----GQGD---WEEDWGETYAGKRQPALFVIDINSGE 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720431501 99 ISVLEGVPENVSPGQAFWAP----GDTGVVFVGWWHEPFRLGIRYCTNRRSALYYV 150
Cdd:pfam19283 212 VQAVKGIPKSLSVGQVVWAPssegSDQYLVFVGWSSDPRKLGIKYCYNRPCALYAV 267
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
142-275 |
1.53e-08 |
|
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: 53.91 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 142 NRRSALYYVDLSGGKCELLSDESLAVCSPRLSPDQCRVVYLQYpslapHHQCSQLFLYDwytkvtslVVDIVPRQLgeSF 221
Cdd:COG0823 8 DGNSDIYVVDLDGGEPRRLTNSPGIDTSPAWSPDGRRIAFTSD-----RGGGPQIYVVD--------ADGGEPRRL--TF 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720431501 222 SGIYCSllpLGCWSADSQRVVFDSVQRSRQDLFAVDTQTGSVTSLTAGGSAGSW 275
Cdd:COG0823 73 GGGYNA---SPSWSPDGKRLAFVSRSDGRFDIYVLDLDGGAPRRLTDGPGSPSW 123
|
|
| PRK10115 |
PRK10115 |
protease 2; Provisional |
362-491 |
2.33e-03 |
|
protease 2; Provisional
Pssm-ID: 182247 [Multi-domain] Cd Length: 686 Bit Score: 41.03 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 362 KSQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGStgfgqdsilslpGNVGHQDVKDVQFAVQQVLQEEHF 441
Cdd:PRK10115 442 KGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGG------------GELGQQWYEDGKFLKKKNTFNDYL 509
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720431501 442 DARRVAL------------MGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDIP 491
Cdd:PRK10115 510 DACDALLklgygspslcygMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIP 571
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
356-465 |
2.86e-03 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 40.39 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 356 PSNSPDKSQVPMVVMPHGGphsSFV--TAWMLFPAMLCKMGFAVLLV--NYR-GSTGFGQDSILSLPGNVGHQDvkdvQF 430
Cdd:cd00312 86 PKNTKPGNSLPVMVWIHGG---GFMfgSGSLYPGDGLAREGDNVIVVsiNYRlGVLGFLSTGDIELPGNYGLKD----QR 158
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720431501 431 AVQQVLQE--EHF--DARRVALMGGSHGGFL-SCHLIGQY 465
Cdd:cd00312 159 LALKWVQDniAAFggDPDSVTIFGESAGGASvSLLLLSPD 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
346-596 |
2.95e-52 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 179.06 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 346 DLDFEAILLQPsnsPDKSQVPMVVMPHGGPHSSFvTAWMLFPAMLCKMGFAVLLVNYRGstgFGQDSilslpGNVGHQDV 425
Cdd:COG1506 7 GTTLPGWLYLP---ADGKKYPVVVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRG---YGESA-----GDWGGDEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 426 KDVQFAVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDipdwcmvetgfPYSND 505
Cdd:COG1506 75 DDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTR-----------EYTER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 506 YLPDLNVLEEMLDK-SPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTHALSevEVESDSF 584
Cdd:COG1506 144 LMGGPWEDPEAYAArSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFS--GAGAPDY 221
|
250
....*....|...
gi 1720431501 585 MNTVL-WLHTHLG 596
Cdd:COG1506 222 LERILdFLDRHLK 234
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
375-572 |
1.58e-35 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 132.74 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 375 PHSSFVTAWmlfpamLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVQQVLQEEHFDARRVALMGGSHG 454
Cdd:pfam00326 1 PSFSWNAQL------LADRGYVVAIANGRGSGGYGEAFHDAGKGDLGQNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 455 GFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDIP---DWCmvETGFPYSNdylpdlnvLEEMLDKSPIKYIPQVK-- 529
Cdd:pfam00326 75 GYLTGAALNQRPDLFKAAVAHVPVVDWLAYMSDTSLPfteRYM--EWGNPWDN--------EEGYDYLSPYSPADNVKvy 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720431501 530 TPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTH 572
Cdd:pfam00326 145 PPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGH 187
|
|
| APEH_N |
pfam19283 |
Acylamino-acid-releasing enzyme, N-terminal domain; This entry represents the N-terminal ... |
19-150 |
2.89e-28 |
|
Acylamino-acid-releasing enzyme, N-terminal domain; This entry represents the N-terminal region from the Acylamino-acid-releasing enzyme (EC:3.4.19.1). The protein is involved in removing the N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. This domain does not represent the catalytic domain which is found at the C-terminus of these proteins.
Pssm-ID: 466026 Cd Length: 274 Bit Score: 114.27 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 19 SWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDEEMARPKkpdqaIKGDqfvFYEDWGETMVSKSIPVLCVLDIESGN 98
Cdd:pfam19283 140 SWNSDETLIAYVAEEPSPSKPTFGDLGYKKGGSSEKDCGSWK-----GQGD---WEEDWGETYAGKRQPALFVIDINSGE 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720431501 99 ISVLEGVPENVSPGQAFWAP----GDTGVVFVGWWHEPFRLGIRYCTNRRSALYYV 150
Cdd:pfam19283 212 VQAVKGIPKSLSVGQVVWAPssegSDQYLVFVGWSSDPRKLGIKYCYNRPCALYAV 267
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
351-595 |
8.70e-17 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 80.34 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 351 AILLQPSNSPDKSqvPMVVMPHGGphSSFVTAWMLFPAMLCKMGFAVLLVNYRG---STGFgqdsilslPGNVGHQDVKD 427
Cdd:COG1073 25 GDLYLPAGASKKY--PAVVVAHGN--GGVKEQRALYAQRLAELGFNVLAFDYRGygeSEGE--------PREEGSPERRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 428 VQFAVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPEtysaciarnpVINIVSMMGTTDIPDWC------MVETGFP 501
Cdd:COG1073 93 ARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPR----------VKAVILDSPFTSLEDLAaqrakeARGAYLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 502 YSnDYLPDLNVLEEMLDK-SPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKArnvPVRLLLYPKSTHALSEVEVE 580
Cdd:COG1073 163 GV-PYLPNVRLASLLNDEfDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAE---PKELLIVPGAGHVDLYDRPE 238
|
250
....*....|....*
gi 1720431501 581 SDSFMNTVLWLHTHL 595
Cdd:COG1073 239 EEYFDKLAEFFKKNL 253
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
340-573 |
1.19e-14 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 73.46 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 340 ENVQYADLD---FEAILLQPsnsPDKSQVPMVVMPHGgphsSF-VTAWMLFPA-MLCKMGFAVLLVN--YRGSTGFGQDS 412
Cdd:COG0412 4 ETVTIPTPDgvtLPGYLARP---AGGGPRPGVVVLHE----IFgLNPHIRDVArRLAAAGYVVLAPDlyGRGGPGDDPDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 413 ILSLPGNVG-HQDVKDVQFAVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPEtYSACIARNPVinivsmmgttdip 491
Cdd:COG0412 77 ARALMGALDpELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGG------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 492 dwcmvetgfpysndylpdlnvleeMLDKSPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKST 571
Cdd:COG0412 143 ------------------------LPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAG 198
|
..
gi 1720431501 572 HA 573
Cdd:COG0412 199 HG 200
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
360-592 |
2.33e-12 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 66.56 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 360 PDKSQVPMVVMPHG-GPHSSfvtAWMLFPAMLCKMGFAVLLVNYRGstgFGQDsilslPGNVGHQD-----VKDVQFAVQ 433
Cdd:COG2267 23 PAGSPRGTVVLVHGlGEHSG---RYAELAEALAAAGYAVLAFDLRG---HGRS-----DGPRGHVDsfddyVDDLRAALD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 434 QVLQEEHfdaRRVALMGGSHGGFLSCHLIGQYPETYSACIArnpvinivsmMGTTDIPDwcmveTGFPYSNDYLPDLNVL 513
Cdd:COG2267 92 ALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVL----------LAPAYRAD-----PLLGPSARWLRALRLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 514 EemldkspikYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARnvpVRLLLYPKSTHALSeVEVESDSFMNTVL-WLH 592
Cdd:COG2267 154 E---------ALARIDVPVLVLHGGADRVVPPEAARRLAARLSPD---VELVLLPGARHELL-NEPAREEVLAAILaWLE 220
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
360-596 |
1.50e-11 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 360 PDKSQVPMVVMPHGGphsSFV-----TAWMLFPAMLCKMGFAVLLVNYRgstgfgqdsilsLPGNVGHQD-VKDVQFAVQ 433
Cdd:COG0657 8 GAKGPLPVVVYFHGG---GWVsgskdTHDPLARRLAARAGAAVVSVDYR------------LAPEHPFPAaLEDAYAALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 434 QVLQ---EEHFDARRVALMGGSHGGFLSCHLigqypeTYSACIARNPVIN-IVSMMGTTDipdwcmvetgfpysndylPD 509
Cdd:COG0657 73 WLRAnaaELGIDPDRIAVAGDSAGGHLAAAL------ALRARDRGGPRPAaQVLIYPVLD------------------LT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 510 LNVLEEMLDKSPikyipqvktPVLLMLGQEDRRVPfkQGLEYYHALKARNVPVRLLLYPKSTHA---LSEVEVESDSFMN 586
Cdd:COG0657 129 ASPLRADLAGLP---------PTLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGfglLAGLPEARAALAE 197
|
250
....*....|
gi 1720431501 587 TVLWLHTHLG 596
Cdd:COG0657 198 IAAFLRRALA 207
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
356-555 |
5.24e-11 |
|
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: 62.58 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 356 PSNSpdKSQVPMVVMPHGGphssfvtAWML------------FPAMLCKMGFAVLLVNYRGSTgfgqDSILslPGNVghQ 423
Cdd:pfam20434 6 PKNA--KGPYPVVIWIHGG-------GWNSgdkeadmgfmtnTVKALLKAGYAVASINYRLST----DAKF--PAQI--Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 424 DVKD-VQFAVQQVlQEEHFDARRVALMGGSHGGFLSC---------HLIGQYPETYSACIARNPVIN-IVSMMGTTDIPD 492
Cdd:pfam20434 69 DVKAaIRFLRANA-AKYGIDTNKIALMGFSAGGHLALlaglsnnnkEFEGNVGDYTPESSKESFKVNaVVDFYGPTDLLD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720431501 493 WcmvetgfpYSNDYLPDLNVLEEML---------DK----SPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHAL 555
Cdd:pfam20434 148 M--------DSCGTHNDAKSPETLLlgapplenpDLaksaSPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
415-596 |
2.14e-09 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 57.61 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 415 SLPGNVGHQDVKDVQFAVQQV-------LQEEHFDARRVALMGGSHGGFLSCHLIGQYPETYSAciarnpvinIVSMMGt 487
Cdd:COG0400 53 DLSFLEGREDEEGLAAAAEALaafidelEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAG---------VVALSG- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 488 tdipdwcmvetgfpysndYLPDLNVLEEMLDKSPikyipqvKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLY 567
Cdd:COG0400 123 ------------------YLPGEEALPAPEAALA-------GTPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREY 177
|
170 180
....*....|....*....|....*....
gi 1720431501 568 PkSTHALSEVEVESdsfmnTVLWLHTHLG 596
Cdd:COG0400 178 P-GGHEISPEELAD-----ARAWLAERLA 200
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
366-574 |
2.84e-09 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 57.70 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 366 PMVVMPHGGPHSSFVtaWMLFPAMLCKmGFAVLLVNYRGstgFGQDSILSLPGNVGHQdVKDVQfavqQVLqeEHFDARR 445
Cdd:COG0596 24 PPVVLLHGLPGSSYE--WRPLIPALAA-GYRVIAPDLRG---HGRSDKPAGGYTLDDL-ADDLA----ALL--DALGLER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 446 VALMGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDipdwcmvetgfpySNDYLPDLNVLEEMLDKSPIKYI 525
Cdd:COG0596 91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRP-------------GLAPEALAALLRALARTDLRERL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720431501 526 PQVKTPVLLMLGQEDRRVPFKQGLEYYHALKArnvpVRLLLYPKSTHAL 574
Cdd:COG0596 158 ARITVPTLVIWGEKDPIVPPALARRLAELLPN----AELVVLPGAGHFP 202
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
424-572 |
5.32e-09 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 56.90 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 424 DVKDVQFAVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPETYSAciarnpvinIVSMMGTTDIPDWCmvetgfpys 503
Cdd:COG4099 105 ALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAA---------AVPICGGGDPANAA--------- 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720431501 504 ndylpdlnvleemldksPIKyipqvKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTH 572
Cdd:COG4099 167 -----------------NLK-----KVPVWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGH 213
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
142-275 |
1.53e-08 |
|
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: 53.91 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 142 NRRSALYYVDLSGGKCELLSDESLAVCSPRLSPDQCRVVYLQYpslapHHQCSQLFLYDwytkvtslVVDIVPRQLgeSF 221
Cdd:COG0823 8 DGNSDIYVVDLDGGEPRRLTNSPGIDTSPAWSPDGRRIAFTSD-----RGGGPQIYVVD--------ADGGEPRRL--TF 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720431501 222 SGIYCSllpLGCWSADSQRVVFDSVQRSRQDLFAVDTQTGSVTSLTAGGSAGSW 275
Cdd:COG0823 73 GGGYNA---SPSWSPDGKRLAFVSRSDGRFDIYVLDLDGGAPRRLTDGPGSPSW 123
|
|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
91-269 |
4.48e-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: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 91 VLDIESGNISVL-EGVPENVSPgqaFWAPGDTGVVFVgwwhepfrlgirycTNR--RSALYYVDLSGGKCELLSDESLAV 167
Cdd:COG0823 15 VVDLDGGEPRRLtNSPGIDTSP---AWSPDGRRIAFT--------------SDRggGPQIYVVDADGGEPRRLTFGGGYN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 168 CSPRLSPDQCRVVYLQYPSLAphhqcSQLFLYDWYTKvtslvvdiVPRQLGESFSGiycsllplGCWSADSQRVVFDSVQ 247
Cdd:COG0823 78 ASPSWSPDGKRLAFVSRSDGR-----FDIYVLDLDGG--------APRRLTDGPGS--------PSWSPDGRRIVFSSDR 136
|
170 180
....*....|....*....|..
gi 1720431501 248 RSRQDLFAVDTqTGSVTSLTAG 269
Cdd:COG0823 137 GGRPDLYVVDL-DGRKRRLTPA 157
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
366-493 |
4.63e-07 |
|
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: 51.35 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 366 PMVVMPHGGPHSSFVtaWM-LFPAmLCKMGFAVLLVNYRGstgFGQDSILSLPGNVGHQDVKDVqfaVQQVLqeEHFDAR 444
Cdd:pfam00561 1 PPVLLLHGLPGSSDL--WRkLAPA-LARDGFRVIALDLRG---FGKSSRPKAQDDYRTDDLAED---LEYIL--EALGLE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720431501 445 RVALMGGSHGGFLSCHLIGQYPEtysaciarnPVINIVSMMGTTDIPDW 493
Cdd:pfam00561 70 KVNLVGHSMGGLIALAYAAKYPD---------RVKALVLLGALDPPHEL 109
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
355-572 |
5.42e-06 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 48.56 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 355 QPSNSPDKSQVPMVVMPHGGPHSSFVTAWMLfpAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGH-----QDVKDVQ 429
Cdd:COG4188 52 APADAPAGGPFPLVVLSHGLGGSREGYAYLA--EHLASHGYVVAAPDHPGSNAADLSAALDGLADALDpeelwERPLDLS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 430 FAVQQVLQEE--------HFDARRVALMGGSHGGflschligqypetYSAciarnpvinIVSMMGTTDIPDWCMVETGFP 501
Cdd:COG4188 130 FVLDQLLALNksdpplagRLDLDRIGVIGHSLGG-------------YTA---------LALAGARLDFAALRQYCGKNP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 502 YSNDYLPDLNVLEEMLDKSPIKYI----------------PQVKTPVLLMLGQEDRRVPF-KQGLEYYHALKArnVPVRL 564
Cdd:COG4188 188 DLQCRALDLPRLAYDLRDPRIKAVvalapggsglfgeeglAAITIPVLLVAGSADDVTPApDEQIRPFDLLPG--ADKYL 265
|
....*...
gi 1720431501 565 LLYPKSTH 572
Cdd:COG4188 266 LTLEGATH 273
|
|
| Axe1 |
COG3458 |
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ... |
342-458 |
1.73e-05 |
|
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442681 [Multi-domain] Cd Length: 318 Bit Score: 47.11 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 342 VQYADLDFE--------AILLQPSNSPDksqVPMVVMPHG-GPHSSFVTAWMLFPAMlckmGFAVLLVNYRG---STGFG 409
Cdd:COG3458 54 VEVYDVTFTgfggariyGWLLRPKGEGP---LPAVVEFHGyGGGRGLPHEDLDWAAA----GYAVLVMDTRGqgsSWGDT 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720431501 410 QDSILSLPGNV-GHQ----DVKD-----------VQfAVQQVLQEEHFDARRVALMGGSHGGFLS 458
Cdd:COG3458 127 PDPGGYSGGALpGYMtrgiDDPDtyyyrrvyldaVR-AVDALRSLPEVDGKRIGVTGGSQGGGLA 190
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
356-471 |
5.04e-05 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 45.38 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 356 PSNSPDKSQVPMVVMPHG--GPHSSFVTAWMlFPAMLCKMGFAVLLVNyrGSTGFGQDSILSLPGNVGHQDVKDVQF--- 430
Cdd:COG3509 44 PAGYDGGAPLPLVVALHGcgGSAADFAAGTG-LNALADREGFIVVYPE--GTGRAPGRCWNWFDGRDQRRGRDDVAFiaa 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720431501 431 AVQQVLQEEHFDARRVALMGGSHGGFLSCHLIGQYPETYSA 471
Cdd:COG3509 121 LVDDLAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAA 161
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
368-574 |
7.99e-05 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 44.51 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 368 VVMPHG-GPHSSF---VTAWmlfpamLCKMGFAVLLVNYRGstgFGQdsilSlPGNVGHQD-----VKDVQFAVQQVLQE 438
Cdd:pfam12146 7 VVLVHGlGEHSGRyahLADA------LAAQGFAVYAYDHRG---HGR----S-DGKRGHVPsfddyVDDLDTFVDKIREE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 439 EHFdaRRVALMGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMgttdIPDWCMVETGF--------PYSNDYLPD- 509
Cdd:pfam12146 73 HPG--LPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYL----APPILKLLAKLlgklfprlRVPNNLLPDs 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 510 ----------------------LNVLEEMLDKSpiKYI----PQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARNvpVR 563
Cdd:pfam12146 147 lsrdpevvaayaadplvhggisARTLYELLDAG--ERLlrraAAITVPLLLLHGGADRVVDPAGSREFYERAGSTD--KT 222
|
250
....*....|.
gi 1720431501 564 LLLYPKSTHAL 574
Cdd:pfam12146 223 LKLYPGLYHEL 233
|
|
| DLH |
pfam01738 |
Dienelactone hydrolase family; |
519-573 |
9.81e-05 |
|
Dienelactone hydrolase family;
Pssm-ID: 396343 [Multi-domain] Cd Length: 213 Bit Score: 43.88 E-value: 9.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720431501 519 KSPIKYIPQVKTPVLLMLGQEDRRVPFKQGLEYYHALKARNVPVRLLLYPKSTHA 573
Cdd:pfam01738 132 EPPLIEAPDIKAPILFHFGEEDHFVPADSRELIEEALKAANVDHQIHSYPGAGHA 186
|
|
| PRK10115 |
PRK10115 |
protease 2; Provisional |
362-491 |
2.33e-03 |
|
protease 2; Provisional
Pssm-ID: 182247 [Multi-domain] Cd Length: 686 Bit Score: 41.03 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 362 KSQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGStgfgqdsilslpGNVGHQDVKDVQFAVQQVLQEEHF 441
Cdd:PRK10115 442 KGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGG------------GELGQQWYEDGKFLKKKNTFNDYL 509
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720431501 442 DARRVAL------------MGGSHGGFLSCHLIGQYPETYSACIARNPVINIVSMMGTTDIP 491
Cdd:PRK10115 510 DACDALLklgygspslcygMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIP 571
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
356-465 |
2.86e-03 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 40.39 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 356 PSNSPDKSQVPMVVMPHGGphsSFV--TAWMLFPAMLCKMGFAVLLV--NYR-GSTGFGQDSILSLPGNVGHQDvkdvQF 430
Cdd:cd00312 86 PKNTKPGNSLPVMVWIHGG---GFMfgSGSLYPGDGLAREGDNVIVVsiNYRlGVLGFLSTGDIELPGNYGLKD----QR 158
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720431501 431 AVQQVLQE--EHF--DARRVALMGGSHGGFL-SCHLIGQY 465
Cdd:cd00312 159 LALKWVQDniAAFggDPDSVTIFGESAGGASvSLLLLSPD 198
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
356-568 |
3.04e-03 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 40.22 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 356 PSNSPDKSQVPMVVMPHGGP--HSSFVTAWMLFPAM--LCKMG----FAVLLVNYRGSTGFGQDsilsLPGNVGHQD--V 425
Cdd:COG2382 103 PGYDNPGKKYPVLYLLDGGGgdEQDWFDQGRLPTILdnLIAAGkippMIVVMPDGGDGGDRGTE----GPGNDAFERflA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431501 426 KDVqfaVQQVlqEEHF----DARRVALMGGSHGGFLSCHLIGQYPETYSaciarnpviNIVSMMGTTDIPDWcmvetgfp 501
Cdd:COG2382 179 EEL---IPFV--EKNYrvsaDPEHRAIAGLSMGGLAALYAALRHPDLFG---------YVGSFSGSFWWPPG-------- 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720431501 502 ySNDYLPDLNVLEEMLDKSPIKyipqvktpVLLMLGQEDRRVPfkQGLEYYHALKARNVPVRLLLYP 568
Cdd:COG2382 237 -DADRGGWAELLAAGAPKKPLR--------FYLDVGTEDDLLE--ANRALAAALKAKGYDVEYREFP 292
|
|
| |
