|
Name |
Accession |
Description |
Interval |
E-value |
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
27-345 |
2.81e-84 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 258.11 E-value: 2.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 27 GFRTATIETPERPHPLTLAIWYPAADDgaprlvgdnpvfqgvavreAATPLSGRHPLVVLSHGFGGNRFNQAWLAVQLAD 106
Cdd:COG4188 27 GVQTLTLRDPSRDRPLPVDVWYPATAP-------------------ADAPAGGPFPLVVLSHGLGGSREGYAYLAEHLAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 107 AGYVVAATDHPGTSTFDRDP--------DQAAALWRRPADLSRVIDHLTG----AADLSAMVDPTRIAVIGHSLGGWTSV 174
Cdd:COG4188 88 HGYVVAAPDHPGSNAADLSAaldgladaLDPEELWERPLDLSFVLDQLLAlnksDPPLAGRLDLDRIGVIGHSLGGYTAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 175 EIAGGRFDADAFTRNCAETTSIACTILArigrlsdpdwRSHMGADLVDPRVSAVIALDPGGIGGFTQASLKGITIPVLVI 254
Cdd:COG4188 168 ALAGARLDFAALRQYCGKNPDLQCRALD----------LPRLAYDLRDPRIKAVVALAPGGSGLFGEEGLAAITIPVLLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 255 AAGVDRIhLPAETEARRLAGLLPDRSTDFHELPDAAHFSFIGLCKPGAATILEreqpgdgilcRDGDGRDRPALHAETTT 334
Cdd:COG4188 238 AGSADDV-TPAPDEQIRPFDLLPGADKYLLTLEGATHFSFLDPCTPGAAILPE----------PDPPGPDRAAIHEYLNA 306
|
330
....*....|.
gi 504560870 335 LVLEALATVWP 345
Cdd:COG4188 307 LSLAFFDAYLK 317
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
78-291 |
1.61e-17 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 80.40 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTFDRDPDQAAAL------WRRPADLSRVIDHLTGAAD 151
Cdd:COG0412 26 GGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEARALmgaldpELLAADLRAALDWLKAQPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 152 lsamVDPTRIAVIGHSLGGWTSVEIAGGRfdadaftrncaettsiactilarigrlsdpdwrshmgadlvdPRVSAVIAL 231
Cdd:COG0412 106 ----VDAGRVGVVGFCFGGGLALLAAARG------------------------------------------PDLAAAVSF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504560870 232 DPGGIGGFTQASLKGITIPVLVIAAGVDRIHLPAETEA--RRLAGLLPDrsTDFHELPDAAH 291
Cdd:COG0412 140 YGGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAAleAALAAAGVD--VELHVYPGAGH 199
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
78-291 |
3.03e-17 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 79.68 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPLVVLSHGFGGNRFNQ-AWLAVQLADAGYVVAATDHPGTSTFDRDPDQAAAlwrrpADLSRVIDHLTGAADlsamV 156
Cdd:COG1506 20 GKKYPVVVYVHGGPGSRDDSfLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEV-----DDVLAAIDYLAARPY----V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 157 DPTRIAVIGHSLGGWTSVEIAGgrFDADAFTrnCAETTSiACTILARIGRLSDPDWRSHMGADLVDPRvsAVIALDPggi 236
Cdd:COG1506 91 DPDRIGIYGHSYGGYMALLAAA--RHPDRFK--AAVALA-GVSDLRSYYGTTREYTERLMGGPWEDPE--AYAARSP--- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504560870 237 ggftQASLKGITIPVLVIAAGVDRIHLPAETEARRLAGLLPDRSTDFHELPDAAH 291
Cdd:COG1506 161 ----LAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGH 211
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
78-292 |
4.27e-16 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 76.88 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTFDRDPDQAAALWRRpaDLSRVIDHLTGAADlsamVD 157
Cdd:COG1073 34 SKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERR--DARAAVDYLRTLPG----VD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 158 PTRIAVIGHSLGGWTSVEIAGGRFDADAFtrnCAET--TSIACTILARIGRlsdpDWRSHMGADLVDPRVSAVIAL---- 231
Cdd:COG1073 108 PERIGLLGISLGGGYALNAAATDPRVKAV---ILDSpfTSLEDLAAQRAKE----ARGAYLPGVPYLPNVRLASLLndef 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504560870 232 DPggiggFTQASLkgITIPVLVIAAGVDRIHLPAETEarRLAGLLPDRsTDFHELPDAAHF 292
Cdd:COG1073 181 DP-----LAKIEK--ISRPLLFIHGEKDEAVPFYMSE--DLYEAAAEP-KELLIVPGAGHV 231
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
75-308 |
4.64e-16 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 76.19 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 75 TPLSGRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTFDRDPDQAAALWRRPADLSRVIDHLTGAADLsa 154
Cdd:COG2267 22 RPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 155 mvdptRIAVIGHSLGGWTSVEIA---GGRFDAdaftrncaettsiactiLArigrLSDPDWRSHmgaDLVDPRVSAVIAL 231
Cdd:COG2267 100 -----PVVLLGHSMGGLIALLYAaryPDRVAG-----------------LV----LLAPAYRAD---PLLGPSARWLRAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504560870 232 dpggiggFTQASLKGITIPVLVIAAGVDRIhLPAEtEARRLAGLLPDRSTdFHELPDAAHFSFIGLCKPGAATILER 308
Cdd:COG2267 151 -------RLAEALARIDVPVLVLHGGADRV-VPPE-AARRLAARLSPDVE-LVLLPGARHELLNEPAREEVLAAILA 217
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
82-295 |
4.91e-13 |
|
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: 67.33 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 82 PLVVLSHGFGGNRFNQAWLAVQLADaGYVVAATDHPGTSTFDRdPDQAAALWRRPADLSRVIDHLtgaadlsamvDPTRI 161
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDAL----------GLERV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 162 AVIGHSLGGWTSVEIA---GGRFDA--------DAFTRNCAETTSIACTILARIGRLSDPDWRshmgadlvdprvsavia 230
Cdd:COG0596 92 VLVGHSMGGMVALELAarhPERVAGlvlvdevlAALAEPLRRPGLAPEALAALLRALARTDLR----------------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504560870 231 ldpggiggftqASLKGITIPVLVIAAGVDRIHLPAetEARRLAGLLPDrsTDFHELPDAAHFSFI 295
Cdd:COG0596 155 -----------ERLARITVPTLVIWGEKDPIVPPA--LARRLAELLPN--AELVVLPGAGHFPPL 204
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
77-291 |
6.15e-10 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 58.80 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 77 LSGRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTfdrdpdqaaalwrRPADLSRV-----IDHL-TGAA 150
Cdd:COG1647 11 LEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGT-------------SPEDLLKTtwedwLEDVeEAYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 151 DLSAMVDptRIAVIGHSLGGWTSVEIAGGRFDADA--------FTRNCAettsiacTILARIGRLSDPDWRShMGADLVD 222
Cdd:COG1647 78 ILKAGYD--KVIVIGLSMGGLLALLLAARYPDVAGlvllspalKIDDPS-------APLLPLLKYLARSLRG-IGSDIED 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504560870 223 PRVSAvIALDPGGIGGF---------TQASLKGITIPVLVIAAGVDRIhLPAETeARRLAGLLPDRSTDFHELPDAAH 291
Cdd:COG1647 148 PEVAE-YAYDRTPLRALaelqrlireVRRDLPKITAPTLIIQSRKDEV-VPPES-ARYIYERLGSPDKELVWLEDSGH 222
|
|
| DLH |
pfam01738 |
Dienelactone hydrolase family; |
73-205 |
1.03e-08 |
|
Dienelactone hydrolase family;
Pssm-ID: 396343 [Multi-domain] Cd Length: 213 Bit Score: 54.67 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 73 AATPLSGRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTFDRDPDQAAALWR---RPADLSRVIDHLTGA 149
Cdd:pfam01738 4 LATPKNPPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLYFRQGDPNDEADAARAMFelvSKRVMEKVLDDLEAA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504560870 150 AD-LSAM--VDPTRIAVIGHSLGGWTSVEIA--GGRFDADA------FTRNCAETTSIACTILARIG 205
Cdd:pfam01738 84 VNyLKSQpeVSPKKVGVVGYCMGGALAVLLAakGPLVDAAVgfygvgPEPPLIEAPDIKAPILFHFG 150
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
83-291 |
7.53e-08 |
|
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: 52.60 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 83 LVVLSHGFG--GNRFNQawLAVQLADAGYVVAATDHPG--TStfdrdpDQAAALWRrpaDLSRVIDhltgaaDLSAMVDP 158
Cdd:pfam12146 6 VVVLVHGLGehSGRYAH--LADALAAQGFAVYAYDHRGhgRS------DGKRGHVP---SFDDYVD------DLDTFVDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 159 TR-------IAVIGHSLGGWTSVEIA---GGRFD-----ADAFTRNCAETTSIACTILARIGRL---------SDPDWRS 214
Cdd:pfam12146 69 IReehpglpLFLLGHSMGGLIAALYAlryPDKVDglilsAPALKIKPYLAPPILKLLAKLLGKLfprlrvpnnLLPDSLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 215 H-------MGAD-LVDPRVSAVIALDPGGIGGFTQASLKGITIPVLVIAAGVDRIHLPAETeaRRLAGLLPDRSTDFHEL 286
Cdd:pfam12146 149 RdpevvaaYAADpLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGS--REFYERAGSTDKTLKLY 226
|
....*
gi 504560870 287 PDAAH 291
Cdd:pfam12146 227 PGLYH 231
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
78-173 |
3.69e-07 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 47.90 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPlVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPgtsTFDRDPDQAAalwrrpADLSRVIDHL---TGAAdlsa 154
Cdd:COG1075 3 ATRYP-VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYP---STNGSIEDSA------EQLAAFVDAVlaaTGAE---- 68
|
90
....*....|....*....
gi 504560870 155 mvdptRIAVIGHSLGGWTS 173
Cdd:COG1075 69 -----KVDLVGHSMGGLVA 82
|
|
| PAF-AH_p_II |
pfam03403 |
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ... |
54-175 |
3.76e-07 |
|
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.
Pssm-ID: 397462 [Multi-domain] Cd Length: 372 Bit Score: 51.29 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 54 GAPRLVGdNPVFQgVAVREAATPLS--------GRHPLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDH----PGTST 121
Cdd:pfam03403 67 GTSSWLG-NRLFA-LLVGSLTLPASwnspfktgEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHrdrsASATY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 122 FDRDPDQAA---ALW--------------RRPADLSRV------------IDH-------LTGAADLSAM---VDPTRIA 162
Cdd:pfam03403 145 FFKDKPAAEeeqKSWiylrkvkeeeefhlRNEQVQQRAqecskalslildINLgtpvenvLDSDFDWQQLkgnLDMSKIA 224
|
170
....*....|...
gi 504560870 163 VIGHSLGGWTSVE 175
Cdd:pfam03403 225 VIGHSFGGATVIQ 237
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
82-295 |
1.10e-06 |
|
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: 49.04 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 82 PLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPGTSTFDRDPDQAA-ALWRRPADLSRVIDHLtgaadlsamvDPTR 160
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEAL----------GLEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 161 IAVIGHSLGGWTSVEIAgGRFD--ADAFTRNCAETTSIACTILARIGRLSDPDW---------RSHMGADL------VDP 223
Cdd:pfam00561 71 VNLVGHSMGGLIALAYA-AKYPdrVKALVLLGALDPPHELDEADRFILALFPGFfdgfvadfaPNPLGRLVakllalLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 224 RVSAVIALDP------------------GGIGGFTQASLKG-------ITIPVLVIAAGVDRIhLPAETeARRLAGLLPd 278
Cdd:pfam00561 150 RLRLLKALPLlnkrfpsgdyalakslvtGALLFIETWSTELrakflgrLDEPTLIIWGDQDPL-VPPQA-LEKLAQLFP- 226
|
250
....*....|....*..
gi 504560870 279 rSTDFHELPDAAHFSFI 295
Cdd:pfam00561 227 -NARLVVIPDAGHFAFL 242
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
78-170 |
4.52e-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: 41.01 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPLVVLSHG---FGGNRFNQA----WLAVQLADAGYVVAATDH--PGTSTFdrdPDQ-----AAALWrrpadlsrVI 143
Cdd:pfam20434 10 KGPYPVVIWIHGggwNSGDKEADMgfmtNTVKALLKAGYAVASINYrlSTDAKF---PAQiqdvkAAIRF--------LR 78
|
90 100
....*....|....*....|....*..
gi 504560870 144 DHltgAADLSamVDPTRIAVIGHSLGG 170
Cdd:pfam20434 79 AN---AAKYG--IDTNKIALMGFSAGG 100
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
84-294 |
5.13e-04 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 40.92 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 84 VVLSHGFGgnrFNQAWLAvQLADAGYVVAATDHPGTSTFDRDPDQaaalWRRPADLSRVIDHLtgaadlsamVDPTRIAV 163
Cdd:pfam12697 1 VVLVHGAG---LSAAPLA-ALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDEL---------GAARPVVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 164 IGHSLGGWTSVEIAGGRFDA----DAFTRNCAETTSIACTILARIGRLSDPDWRSHMG----------ADLVDPRVSAVI 229
Cdd:pfam12697 64 VGHSLGGAVALAAAAAALVVgvlvAPLAAPPGLLAALLALLARLGAALAAPAWLAAESlargflddlpADAEWAAALARL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504560870 230 ALDPGGIGGFTQASLKGITIPVLVIAAGVDRIHLPAETEARRLAGllpdrsTDFHELPDAAHFSF 294
Cdd:pfam12697 144 AALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAALAG------ARLVVLPGAGHLPL 202
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
94-183 |
6.22e-04 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 40.68 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 94 RFNQAWLAvqlaDAGYVVAATDHPGTSTFDRDPDQAaaLWRRPADlsRVIDHLTGAAD-LSAM--VDPTRIAVIGHSLGG 170
Cdd:pfam00326 4 SWNAQLLA----DRGYVVAIANGRGSGGYGEAFHDA--GKGDLGQ--NEFDDFIAAAEyLIEQgyTDPDRLAIWGGSYGG 75
|
90
....*....|....*.
gi 504560870 171 WTS---VEIAGGRFDA 183
Cdd:pfam00326 76 YLTgaaLNQRPDLFKA 91
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
79-308 |
2.84e-03 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 38.32 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 79 GRHPLVVLSHG---FGGNRFNQAWLAVQLAD-AGYVVAATDH--PGTSTFDRDPDQAAALWRRpadlsrVIDHltgAADL 152
Cdd:COG0657 11 GPLPVVVYFHGggwVSGSKDTHDPLARRLAArAGAAVVSVDYrlAPEHPFPAALEDAYAALRW------LRAN---AAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 153 SamVDPTRIAVIGHSlggwtsveiAGGrfdadaftrncaeTTSIACTILARigrlsdpdwrshmgaDLVDPRVSAVIALD 232
Cdd:COG0657 82 G--IDPDRIAVAGDS---------AGG-------------HLAAALALRAR---------------DRGGPRPAAQVLIY 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 233 PggIGGFT----QASLKGiTIPVLVIAAGVDRIHLPAETEARRL--AGllpdRSTDFHELPDAAHFSFIGLCKPGAATIL 306
Cdd:COG0657 123 P--VLDLTasplRADLAG-LPPTLIVTGEADPLVDESEALAAALraAG----VPVELHVYPGGGHGFGLLAGLPEARAAL 195
|
..
gi 504560870 307 ER 308
Cdd:COG0657 196 AE 197
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
78-170 |
3.18e-03 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 38.83 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 78 SGRHPLVVLSHGFGGN--------RFNQawlavqLADA-GYVVAA---TDHPGTSTFDrdpdqaaalWRRPADLSRVIDH 145
Cdd:COG3509 50 GAPLPLVVALHGCGGSaadfaagtGLNA------LADReGFIVVYpegTGRAPGRCWN---------WFDGRDQRRGRDD 114
|
90 100 110
....*....|....*....|....*....|....
gi 504560870 146 ltgAADLSAM---------VDPTRIAVIGHSLGG 170
Cdd:COG3509 115 ---VAFIAALvddlaarygIDPKRVYVTGLSAGG 145
|
|
| PRK10566 |
PRK10566 |
esterase; Provisional |
74-172 |
3.65e-03 |
|
esterase; Provisional
Pssm-ID: 182555 [Multi-domain] Cd Length: 249 Bit Score: 38.43 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 74 ATPLSGRH---PLVVLSHGFGGNRFNQAWLAVQLADAGYVVAATDHPG-TSTFDRDpdqAAALWRRPAD-LSRVIDHLTG 148
Cdd:PRK10566 17 AFPAGQRDtplPTVFFYHGFTSSKLVYSYFAVALAQAGFRVIMPDAPMhGARFSGD---EARRLNHFWQiLLQNMQEFPT 93
|
90 100
....*....|....*....|....*..
gi 504560870 149 ---AADLSAMVDPTRIAVIGHSLGGWT 172
Cdd:PRK10566 94 lraAIREEGWLLDDRLAVGGASMGGMT 120
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
84-170 |
9.23e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 37.62 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504560870 84 VVLSHGFGGN----RFNQAWLAvqladAGYVVAATDHP--GTSTFDRDPDQAAALwrrPADLSRVIDHLtgaadlsamvD 157
Cdd:PRK14875 134 VVLIHGFGGDlnnwLFNHAALA-----AGRPVIALDLPghGASSKAVGAGSLDEL---AAAVLAFLDAL----------G 195
|
90
....*....|...
gi 504560870 158 PTRIAVIGHSLGG 170
Cdd:PRK14875 196 IERAHLVGHSMGG 208
|
|
| |
