|
Name |
Accession |
Description |
Interval |
E-value |
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
76-317 |
1.11e-53 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 176.64 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 76 LYVPMPtGIPHENIFIRTKDGIRLNLILIRYTGDNSPYsPTIIYFHGNAGNIGHRLP----------NALLMlvnlkvnl 145
Cdd:COG1073 1 IFPPSD-KVNKEDVTFKSRDGIKLAGDLYLPAGASKKY-PAVVVAHGNGGVKEQRALyaqrlaelgfNVLAF-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 146 llvDYRGYGKSEGEASEEGLY--LDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVAIHLASENsHRISAIMVENTFLSIP 223
Cdd:COG1073 71 ---DYRGYGESEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 224 HMASTLFSFFPMRYLPLWCYK----------NKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIF 293
Cdd:COG1073 147 DLAAQRAKEARGAYLPGVPYLpnvrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP-KELLIV 225
|
250 260
....*....|....*....|....*.
gi 49355781 294 PDGTHNDT-WQCQG-YFTALEQFIKE 317
Cdd:COG1073 226 PGAGHVDLyDRPEEeYFDKLAEFFKK 251
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
149-298 |
2.32e-13 |
|
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: 68.78 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTR-PDLdktKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIP 223
Cdd:pfam12146 38 DHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 224 H---------MASTLFSFFPMRYLPlWCYKNKFLS--------YRKISQC--------------------------RMPS 260
Cdd:pfam12146 115 PylappilklLAKLLGKLFPRLRVP-NNLLPDSLSrdpevvaaYAADPLVhggisartlyelldagerllrraaaiTVPL 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 49355781 261 LFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:pfam12146 194 LLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
149-298 |
1.04e-03 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 40.51 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVA--IHLASENSH----------RISA 212
Cdd:PLN02385 122 DYPGFGLSEGLhgyiPSFDDLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVAlkVHLKQPNAWdgailvapmcKIAD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 213 IMVEN-TFLSIPHMASTLF---SFFPMRYLPLWCY----KNKFLSYRKIS---QCRM----------------------P 259
Cdd:PLN02385 202 DVVPPpLVLQILILLANLLpkaKLVPQKDLAELAFrdlkKRKMAEYNVIAykdKPRLrtavellrttqeiemqleevslP 281
|
170 180 190
....*....|....*....|....*....|....*....
gi 49355781 260 SLFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:PLN02385 282 LLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYH 320
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
76-317 |
1.11e-53 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 176.64 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 76 LYVPMPtGIPHENIFIRTKDGIRLNLILIRYTGDNSPYsPTIIYFHGNAGNIGHRLP----------NALLMlvnlkvnl 145
Cdd:COG1073 1 IFPPSD-KVNKEDVTFKSRDGIKLAGDLYLPAGASKKY-PAVVVAHGNGGVKEQRALyaqrlaelgfNVLAF-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 146 llvDYRGYGKSEGEASEEGLY--LDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVAIHLASENsHRISAIMVENTFLSIP 223
Cdd:COG1073 71 ---DYRGYGESEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 224 HMASTLFSFFPMRYLPLWCYK----------NKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIF 293
Cdd:COG1073 147 DLAAQRAKEARGAYLPGVPYLpnvrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP-KELLIV 225
|
250 260
....*....|....*....|....*.
gi 49355781 294 PDGTHNDT-WQCQG-YFTALEQFIKE 317
Cdd:COG1073 226 PGAGHVDLyDRPEEeYFDKLAEFFKK 251
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
91-320 |
2.08e-28 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 110.11 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 91 IRTKDGIRLNLILIRYTgDNSPYsPTIIYFHGNAGNI-GHRLPNA----------LLMlvnlkvnlllvDYRGYGKSEGE 159
Cdd:COG1506 2 FKSADGTTLPGWLYLPA-DGKKY-PVVVYVHGGPGSRdDSFLPLAqalasrgyavLAP-----------DYRGYGESAGD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 160 ASEEGLYlDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIPHMASTLFSFFPMRYLP 239
Cdd:COG1506 69 WGGDEVD-DVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 240 LWcykNKFLSYRKIS------QCRMPSLFISGLSDQLIPPVMMKQLYE--LSPSRTKRLAIFPDGTHNDTWQCQ-GYFTA 310
Cdd:COG1506 148 PW---EDPEAYAARSplayadKLKTPLLLIHGEADDRVPPEQAERLYEalKKAGKPVELLVYPGEGHGFSGAGApDYLER 224
|
250
....*....|
gi 49355781 311 LEQFIKEVVK 320
Cdd:COG1506 225 ILDFLDRHLK 234
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
85-317 |
9.05e-22 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 91.60 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 85 PHENIFIRTKDGIRLNLIliRYTGDNSPySPTIIYFHGNAGNIG--HRLPNAL-------LMLvnlkvnlllvDYRGYGK 155
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGR--RWRPAGSP-RGTVVLVHGLGEHSGryAELAEALaaagyavLAF----------DLRGHGR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 156 SEGE----ASEEGLYLDSEAVLDYVMTRPDLdktKIFLFGRSLGGAVAIHLASENSHRISAIMventfLSIPHMASTLFS 231
Cdd:COG2267 69 SDGPrghvDSFDDYVDDLRAALDALRARPGL---PVVLLGHSMGGLIALLYAARYPDRVAGLV-----LLAPAYRADPLL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 232 FFPMRYLplwcykNKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIFPDGTH---NDTWQCQgYF 308
Cdd:COG2267 141 GPSARWL------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPD-VELVLLPGARHellNEPAREE-VL 212
|
....*....
gi 49355781 309 TALEQFIKE 317
Cdd:COG2267 213 AAILAWLER 221
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
149-298 |
2.32e-13 |
|
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: 68.78 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTR-PDLdktKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIP 223
Cdd:pfam12146 38 DHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 224 H---------MASTLFSFFPMRYLPlWCYKNKFLS--------YRKISQC--------------------------RMPS 260
Cdd:pfam12146 115 PylappilklLAKLLGKLFPRLRVP-NNLLPDSLSrdpevvaaYAADPLVhggisartlyelldagerllrraaaiTVPL 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 49355781 261 LFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:pfam12146 194 LLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
149-318 |
2.40e-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: 68.10 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGEASEEGLYLDSEAVLDyVMTRpdLDKTKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIPHMAST 228
Cdd:COG0596 56 DLRGHGRSDKPAGGYTLDDLADDLAA-LLDA--LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 229 LFSFFPMRYLPLWCYKNKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPsrTKRLAIFPDGTHNDTWQCQGYF 308
Cdd:COG0596 133 RPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAF 210
|
170
....*....|.
gi 49355781 309 T-ALEQFIKEV 318
Cdd:COG0596 211 AaALRDFLARL 221
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
149-320 |
9.40e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 52.25 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGEASE---EGLYLDSEAVLDYVMTRPDldktKIFLFGRSLGGAVAIHLASENSHrISAIMVENTFLSIPHM 225
Cdd:COG1647 49 RLPGHGTSPEDLLKttwEDWLEDVEEAYEILKAGYD----KVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 226 ASTLFSFFPM----------------------RYLPLWCYKN--KFLSY--RKISQCRMPSLFISGLSDQLIPPVMMKQL 279
Cdd:COG1647 124 SAPLLPLLKYlarslrgigsdiedpevaeyayDRTPLRALAElqRLIREvrRDLPKITAPTLIIQSRKDEVVPPESARYI 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 49355781 280 YELSPSRTKRLAIFPDGTHNDT--WQCQGYFTALEQFIKEVVK 320
Cdd:COG1647 204 YERLGSPDKELVWLEDSGHVITldKDREEVAEEILDFLERLAA 246
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
84-298 |
1.18e-07 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 51.89 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 84 IPHENIFIRTKDGIRLNLILIRYTGDnSPYsPTIIYFHGNAG------NIGHRL---------PNALlmlvnlkvnlllv 148
Cdd:COG0412 1 MTTETVTIPTPDGVTLPGYLARPAGG-GPR-PGVVVLHEIFGlnphirDVARRLaaagyvvlaPDLY------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGEASEEGLYLDSE-------AVLDYVMTRPDLDKTKIFLFGRSLGGAVAIHLASENsHRISAImventfls 221
Cdd:COG0412 66 GRGGPGDDPDEARALMGALDPEllaadlrAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARG-PDLAAA-------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49355781 222 iphmastlFSFFPMRYLPlwcyknkfLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYEL--SPSRTKRLAIFPDGTH 298
Cdd:COG0412 137 --------VSFYGGLPAD--------DLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAAlaAAGVDVELHVYPGAGH 199
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
115-238 |
2.03e-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: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 115 PTIIYFHGNAGNIG--HRLPNALLmlvNLKVNLLLVDYRGYGKSEGEASEEGLYLDS-EAVLDYVMTRpdLDKTKIFLFG 191
Cdd:pfam00561 1 PPVLLLHGLPGSSDlwRKLAPALA---RDGFRVIALDLRGFGKSSRPKAQDDYRTDDlAEDLEYILEA--LGLEKVNLVG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 49355781 192 RSLGGAVAIHLASENSHRISAIMVENTFLSiPHMASTLFSFFPMRYL 238
Cdd:pfam00561 76 HSMGGLIALAYAAKYPDRVKALVLLGALDP-PHELDEADRFILALFP 121
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
150-298 |
2.38e-07 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 50.55 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 150 YRGYGKSEGEASE-EGLYLDSEAVLDYVMTRPDLdktKIFLFGRSLGGAVAIHLASEnSHRISAimventFLSIphmaST 228
Cdd:COG2945 63 FRGVGRSEGEFDEgRGELDDAAAALDWLRAQNPL---PLWLAGFSFGAYVALQLAMR-LPEVEG------LILV----AP 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49355781 229 LFSFFPMRYLPLwcyknkflsyrkisqCRMPSLFISGLSDQLIPPVMMKQLYE-LSPsrTKRLAIFPDGTH 298
Cdd:COG2945 129 PVNRYDFSFLAP---------------CPAPTLVIHGEQDEVVPPAEVLDWARpLSP--PLPVVVVPGADH 182
|
|
| Axe1 |
COG3458 |
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ... |
78-298 |
3.23e-05 |
|
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442681 [Multi-domain] Cd Length: 318 Bit Score: 45.18 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 78 VPMPTGIPHENIF---IRTKDGIRLNLILIRYTGDNsPYsPTIIYFHGNAGNIGHRLPN---------ALLMlvnlkvnl 145
Cdd:COG3458 45 TPVETGLPGVEVYdvtFTGFGGARIYGWLLRPKGEG-PL-PAVVEFHGYGGGRGLPHEDldwaaagyaVLVM-------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 146 llvDYRGYGKSEGEASEE-------------------------GLYLDseAV--LDYVMTRPDLDKTKIFLFGRSLGGAV 198
Cdd:COG3458 115 ---DTRGQGSSWGDTPDPggysggalpgymtrgiddpdtyyyrRVYLD--AVraVDALRSLPEVDGKRIGVTGGSQGGGL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 199 AIhLASENSHRISAIMVENTFLS-IP---HMAST-----LFSFFPMRYLPlwcYKNKF--LSY-------RKIsqcRMPS 260
Cdd:COG3458 190 AL-AAAALDPRVKAAAADVPFLCdFRralELGRAgpypeIRRYLRRHRER---EPEVFetLSYfdavnfaRRI---KAPV 262
|
250 260 270
....*....|....*....|....*....|....*...
gi 49355781 261 LFISGLSDQLIPPVMMKQLYELSPSrTKRLAIFPDGTH 298
Cdd:COG3458 263 LFSVGLMDPVCPPSTVFAAYNALAG-PKEILVYPFNGH 299
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
115-282 |
5.35e-05 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 115 PTIIYFHGNAGN------IGHRL---------PNALLMLvnlkvnlllvDYRGYG-----KSEGEASEEGL-----YLDs 169
Cdd:COG0400 6 PLVVLLHGYGGDeedllpLAPELalpgaavlaPRAPVPE----------GPGGRAwfdlsFLEGREDEEGLaaaaeALA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 170 eAVLDYVMTRPDLDKTKIFLFGRSLGGAVAIHLASENSHRISAIMventflsiphmastLFS-FFPMRylPLWCYKNKFL 248
Cdd:COG0400 75 -AFIDELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVV--------------ALSgYLPGE--EALPAPEAAL 137
|
170 180 190
....*....|....*....|....*....|....
gi 49355781 249 SYRKIsqcrmpsLFISGLSDQLIPPVMMKQLYEL 282
Cdd:COG0400 138 AGTPV-------FLAHGTQDPVIPVERAREAAEA 164
|
|
| AXE1 |
pfam05448 |
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ... |
164-300 |
6.87e-05 |
|
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.
Pssm-ID: 398876 [Multi-domain] Cd Length: 316 Bit Score: 43.93 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 164 GLYLDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVAIhLASENSHRISAIMVENTFLS---------IPHMASTLFSFFP 234
Cdd:pfam05448 153 RVFLDAVRAVEIVMSFPEVDEERIVVTGGSQGGALAL-AAAALSPRIKAVVADYPFLSdfrrawemdLEHPYDELNRYFK 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49355781 235 -----------MRYLPLWCYKNkfLSYRkisqCRMPSLFISGLSDQLIPPVMMKQLYElSPSRTKRLAIFPDGTHND 300
Cdd:pfam05448 232 rdphhereeeaFRTLSYFDIKN--LAHR----VKGPVLMAIGLIDDVCPPSTVFAAYN-HLTTEKEIRVYPYFAHEY 301
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
149-298 |
1.04e-03 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 40.51 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTRPDLDKTKIFLFGRSLGGAVA--IHLASENSH----------RISA 212
Cdd:PLN02385 122 DYPGFGLSEGLhgyiPSFDDLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVAlkVHLKQPNAWdgailvapmcKIAD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 213 IMVEN-TFLSIPHMASTLF---SFFPMRYLPLWCY----KNKFLSYRKIS---QCRM----------------------P 259
Cdd:PLN02385 202 DVVPPpLVLQILILLANLLpkaKLVPQKDLAELAFrdlkKRKMAEYNVIAykdKPRLrtavellrttqeiemqleevslP 281
|
170 180 190
....*....|....*....|....*....|....*....
gi 49355781 260 SLFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:PLN02385 282 LLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYH 320
|
|
| Abhydrolase_2 |
pfam02230 |
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ... |
111-298 |
6.84e-03 |
|
Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.
Pssm-ID: 396693 [Multi-domain] Cd Length: 217 Bit Score: 37.36 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 111 SPYSPTIIYFHG---------NAGNIGHRLPNALLMLVNLKVNLLLVDYRG--------YGKSEGEASEEGLYLDS---- 169
Cdd:pfam02230 11 DPAQATVIFLHGlgdsghgwaDAAKTEAPLPNIKFIFPHGPEIPVTLNGGMrmpawfdlVGLSPNAKEDEAGIKNSaeti 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355781 170 EAVLDYVMTRPdLDKTKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFLsIPHMAstlfsfFPmrylplwcyKNKFLS 249
Cdd:pfam02230 91 EELIDAEQKKG-IPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFL-PLPTK------FP---------SHPNLV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 49355781 250 YRKISQCRmpslfISGLSDQLIPPVMMKQLYELSPSRTKR--LAIFPDGTH 298
Cdd:pfam02230 154 TKKTPIFL-----IHGEEDPVVPLALGKLAKEYLKTSLNKveLKIYEGLAH 199
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
182-220 |
8.62e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 37.64 E-value: 8.62e-03
10 20 30
....*....|....*....|....*....|....*....
gi 49355781 182 LDKTKIFLFGRSLGGAVAIHLASENSHRISAIMVENTFL 220
Cdd:PRK00870 112 LDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTGL 150
|
|
| |
