|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
53-249 |
3.61e-73 |
|
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: 224.02 E-value: 3.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATT 132
Cdd:pfam12146 41 GHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 FKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGS 211
Cdd:pfam12146 121 ILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGG 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 1918877125 212 ADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 249
Cdd:pfam12146 200 ADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
52-268 |
2.90e-72 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 223.22 E-value: 2.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 52 VGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESAT 131
Cdd:PHA02857 61 IGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 132 TFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGS 211
Cdd:PHA02857 139 RLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1918877125 212 ADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 268
Cdd:PHA02857 219 NNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
53-266 |
5.53e-31 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 115.10 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATT 132
Cdd:COG2267 65 GHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 FKVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSA 212
Cdd:COG2267 144 ARWLRA-----------------------------------------------------LRLAEALARIDVPVLVLHGGA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1918877125 213 DRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 266
Cdd:COG2267 171 DRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
89-122 |
1.29e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214008 Cd Length: 280 Bit Score: 45.68 E-value: 1.29e-05
10 20 30
....*....|....*....|....*....|....
gi 1918877125 89 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 122
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
53-248 |
6.66e-05 |
|
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.
Pssm-ID: 162444 [Multi-domain] Cd Length: 332 Bit Score: 43.62 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIAiLTAAER 109
Cdd:TIGR01607 84 GHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA-LRLLEL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 110 PGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLI 174
Cdd:TIGR01607 163 LGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDIIKFDKFR 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1918877125 175 CRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKE 248
Cdd:TIGR01607 241 YDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVITIE 316
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
69-159 |
7.49e-03 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 36.82 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 69 VFVRDVLQHVDsmqkdypGLPVFLLGHSMGGAIAILTAA--ERPGHF-AGMVLISPLVLANPESATTFKVLAAKVLNLVl 145
Cdd:smart00824 52 AQAEAVLRAAG-------GRPFVLVGHSSGGLLAHAVAArlEARGIPpAAVVLLDTYPPGDPAPEGWLPELLRGVFERE- 123
|
90
....*....|....
gi 1918877125 146 pnLSLGPIDSSVLS 159
Cdd:smart00824 124 --DSFVPMDDARLT 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
53-249 |
3.61e-73 |
|
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: 224.02 E-value: 3.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATT 132
Cdd:pfam12146 41 GHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 FKVLAAKVLNLVLPNLSL-GPIDSSVLSRNKTEVDIYNSDPLICRaGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGS 211
Cdd:pfam12146 121 ILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAADPLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGG 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 1918877125 212 ADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKEL 249
Cdd:pfam12146 200 ADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
52-268 |
2.90e-72 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 223.22 E-value: 2.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 52 VGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlaNPESAT 131
Cdd:PHA02857 61 IGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 132 TFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGS 211
Cdd:PHA02857 139 RLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1918877125 212 ADRLCDSKGAYLLMELAKSqDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRT 268
Cdd:PHA02857 219 NNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKSVMKEIETWIFNRV 274
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
53-266 |
5.53e-31 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 115.10 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDyPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATT 132
Cdd:COG2267 65 GHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 FKVLAAkvlnlvlpnlslgpidssvlsrnktevdiynsdplicraglkvcfgiqllnavSRVERALPKLTVPFLLLQGSA 212
Cdd:COG2267 144 ARWLRA-----------------------------------------------------LRLAEALARIDVPVLVLHGGA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1918877125 213 DRLCDSKGAYLLMELAkSQDKTLKIYEGAYHVLHKELPEvtNSVFHEINMWVSQ 266
Cdd:COG2267 171 DRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EEVLAAILAWLER 221
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
53-275 |
1.19e-28 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 111.41 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQKD--YPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESA 130
Cdd:PLN02298 97 GHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 131 TTFKVlaAKVLNLV---LPNLSLGP----IDSSVLSRNKTEVDIYNsdPLICRAGLKVCFGIQLLNAVSRVERALPKLTV 203
Cdd:PLN02298 177 PPWPI--PQILTFVarfLPTLAIVPtadlLEKSVKVPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSI 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918877125 204 PFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQRTATAGTAS 275
Cdd:PLN02298 253 PFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIYDGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKATPS 325
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
53-267 |
6.02e-27 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 107.15 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDFHVFVRDVLQHVDSMQ--KDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLV-----LA 125
Cdd:PLN02385 125 GFGLSEGLHGYIPSFDDLVDDVIEHYSKIKgnPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 126 NPESATTFKVLAAKVLnlvlPNLSLGP----IDSSVLSRNKTEVDIYNsdpLIC---RAGLKVcfGIQLLNAVSRVERAL 198
Cdd:PLN02385 205 PPPLVLQILILLANLL----PKAKLVPqkdlAELAFRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQL 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 199 PKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYH-VLHKELPEVTNSVFHEINMWVSQR 267
Cdd:PLN02385 276 EEVSLPLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
49-256 |
2.38e-25 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 100.79 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 49 LLPvGHGQSEGErMVVSDFHVFVRDVLQHVDSMQKDYPglPVFLLGHSMGGAIAILTAAERPgHFAGMVLISPLVLANPE 128
Cdd:COG1647 49 RLP-GHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 129 SAttfkvLAAKVLNLVLPNLSLGPIDssvLSRNKTEVDIYNSDPLICraglkvcfGIQLLNAVSRVERALPKLTVPFLLL 208
Cdd:COG1647 124 SA-----PLLPLLKYLARSLRGIGSD---IEDPEVAEYAYDRTPLRA--------LAELQRLIREVRRDLPKITAPTLII 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1918877125 209 QGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 256
Cdd:COG1647 188 QSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
52-267 |
5.49e-22 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 94.19 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 52 VGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIaILTAAERP---GHFAGMVLISPLVLANPE 128
Cdd:PLN02652 172 IGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFGHSTGGAV-VLKAASYPsieDKLEGIVLTSPALRVKPA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 129 SATTFKVlaAKVLNLVLPNLSLGPIDSS--VLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFL 206
Cdd:PLN02652 251 HPIVGAV--APIFSLVAPRFQFKGANKRgiPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFM 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918877125 207 LLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKElPEvTNSVFHEINMWVSQR 267
Cdd:PLN02652 329 VLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE-PE-REEVGRDIIDWMEKR 387
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
53-259 |
1.89e-15 |
|
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: 73.50 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSdFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVlanpesatt 132
Cdd:COG0596 59 GHGRSDKPAGGYT-LDDLADDLAALLDALGLE----RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVL--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 fKVLAAkvlNLVLPNLSLGPIDSSVLSRNKTEvdiynsdplicraglkvcfgiqllnavsrVERALPKLTVPFLLLQGSA 212
Cdd:COG0596 125 -AALAE---PLRRPGLAPEALAALLRALARTD-----------------------------LRERLARITVPTLVIWGEK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1918877125 213 DRLCDSKGAYLLMELAKsqDKTLKIYEGAYHVLHKELPEVTNSVFHE 259
Cdd:COG0596 172 DPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAAALRD 216
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
53-244 |
5.61e-12 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 64.17 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGE-RMVVS----DFHVFVRDVLQhvdsmQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLISPlvLANP 127
Cdd:COG1073 74 GYGESEGEpREEGSperrDARAAVDYLRT-----LPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVILDSP--FTSL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 128 ESAttFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKtEVDIYNsdplicraglkvcfgiqllnavsrverALPKLTVPFLL 207
Cdd:COG1073 146 EDL--AAQRAKEARGAYLPGVPYLPNVRLASLLND-EFDPLA---------------------------KIEKISRPLLF 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 1918877125 208 LQGSADRLCDSKGAYLLMELAkSQDKTLKIYEGAYHV 244
Cdd:COG1073 196 IHGEKDEAVPFYMSEDLYEAA-AEPKELLIVPGAGHV 231
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
53-248 |
1.28e-11 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 62.73 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERmvvsdFHVFVRDVLQHVDSM--QKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvlanpesa 130
Cdd:COG1506 61 GYGESAGDW-----GGDEVDDVLAAIDYLaaRPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 131 ttfkvlaakVLNLVlpnlslgpidsSVLSRNKTEVDIYNSDPLICRAGLKvcfgiqllnAVSRVERAlPKLTVPFLLLQG 210
Cdd:COG1506 127 ---------VSDLR-----------SYYGTTREYTERLMGGPWEDPEAYA---------ARSPLAYA-DKLKTPLLLIHG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1918877125 211 SADRLCDSKGAYLLMELAKSQ--DKTLKIYEGAYHVLHKE 248
Cdd:COG1506 177 EADDRVPPEQAERLYEALKKAgkPVELLVYPGEGHGFSGA 216
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
53-248 |
3.66e-10 |
|
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: 58.67 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGeRMVVSDFHV--FVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLAN---- 126
Cdd:pfam00561 37 GFGKSSR-PKAQDDYRTddLAEDLEYILEALGLE----KVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHelde 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 127 ---------PESATTFKVLAAKVLNLVLPNLSLGPI---DSSVLSRNKTEVDIYNSDPLIcrAGLKVCFGIQLLNAVSRV 194
Cdd:pfam00561 112 adrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLLKALPLLNKRFPSGDYAL--AKSLVTGALLFIETWSTE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1918877125 195 ERA--LPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSqdKTLKIYEGAYHVLHKE 248
Cdd:pfam00561 190 LRAkfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPN--ARLVVIPDAGHFAFLE 243
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
53-246 |
6.58e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 49.01 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGERMVVSDfhvfVRDVLQHVDSMQKDYPglpVFLLGHSMGGAIAiLTAAERPGHFAgmVLISPLVLANPESATT 132
Cdd:pfam12697 31 GHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSLGGAVA-LAAAAAALVVG--VLVAPLAAPPGLLAAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 133 FKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLlnavsrveRALPKLTVPFLLLqGSA 212
Cdd:pfam12697 101 LALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPL--------AAWRDLPVPVLVL-AEE 171
|
170 180 190
....*....|....*....|....*....|....
gi 1918877125 213 DRLCDskgAYLLMELAKSQDKTLKIYEGAYHVLH 246
Cdd:pfam12697 172 DRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
50-121 |
1.23e-06 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 49.17 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1918877125 50 LPvGHGQSeGERMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 121
Cdd:PRK14875 165 LP-GHGAS-SKAVGAGSLDELAAAVLAFLDALGIE----RAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
71-134 |
8.65e-06 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 45.73 E-value: 8.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1918877125 71 VRDVLQHVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLISPlvLANPESATTFK 134
Cdd:COG4099 106 LDAVLALLDDLIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
89-122 |
1.29e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214008 Cd Length: 280 Bit Score: 45.68 E-value: 1.29e-05
10 20 30
....*....|....*....|....*....|....
gi 1918877125 89 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISPL 122
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
67-108 |
1.32e-05 |
|
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238287 [Multi-domain] Cd Length: 229 Bit Score: 45.16 E-value: 1.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1918877125 67 FHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 108
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
71-128 |
2.07e-05 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 44.51 E-value: 2.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918877125 71 VRDVLQHVDSMQKDYpGLP---VFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPE 128
Cdd:COG0400 70 AEALAAFIDELEARY-GIDperIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
73-122 |
2.14e-05 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 442792 [Multi-domain] Cd Length: 202 Bit Score: 44.49 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1918877125 73 DVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGhFAGMVLIS-PL 122
Cdd:COG3571 65 AWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAEGGG-AAGLVCLGyPF 114
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
72-108 |
5.74e-05 |
|
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238382 [Multi-domain] Cd Length: 153 Bit Score: 42.49 E-value: 5.74e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1918877125 72 RDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAE 108
Cdd:cd00741 12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAGLD 48
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
53-248 |
6.66e-05 |
|
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.
Pssm-ID: 162444 [Multi-domain] Cd Length: 332 Bit Score: 43.62 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 53 GHGQSEGE---RMVVSDFHVFVRDVLQHVDSMQK-------------DY-------PGLPVFLLGHSMGGAIAiLTAAER 109
Cdd:TIGR01607 84 GHGESDGLqnlRGHINCFDDLVYDVIQYMNRINDsiilenetksddeSYdivntkeNRLPMYIIGLSMGGNIA-LRLLEL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 110 PGH---------------FAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSsvLSRNKTEVDIYNSDPLI 174
Cdd:TIGR01607 163 LGKsnenndklnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDIIKFDKFR 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1918877125 175 CRAGLKVCFGIQLLNAVSRVE---RALPKlTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKE 248
Cdd:TIGR01607 241 YDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVITIE 316
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
70-131 |
1.30e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 42.68 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1918877125 70 FVRDVlqhVDSMQKDYPGLP--VFLLGHSMGGAIAILTAAERPGHFAGMVLIS--PLVLANPESAT 131
Cdd:COG3509 117 FIAAL---VDDLAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACA 179
|
|
| PRK10749 |
PRK10749 |
lysophospholipase L2; Provisional |
91-260 |
1.37e-04 |
|
lysophospholipase L2; Provisional
Pssm-ID: 182697 Cd Length: 330 Bit Score: 42.68 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 91 FLLGHSMGGAIAILTAAERPGHFAGMVLISPL---VLANPESATTFKVLAAKVLNLVLPNLSLG-------PIDSSVLS- 159
Cdd:PRK10749 134 YALAHSMGGAILTLFLQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLTh 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 160 ---RNKTEVDIYNSDPLI---------CRAGLKVcfGIQLLNAVsrveralPKLTVPFLLLQGSADRLCDSkgayllmel 227
Cdd:PRK10749 214 sreRYRRNLRFYADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEERVVDN--------- 275
|
170 180 190
....*....|....*....|....*....|...
gi 1918877125 228 aKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEI 260
Cdd:PRK10749 276 -RMHDRFCEARTAAGHPCEGGKPLVIKGAYHEI 307
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
70-121 |
3.78e-04 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 41.12 E-value: 3.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1918877125 70 FVRDVLQ-HVDsmqKDYPGLPVF--LLGHSMGGAIAILTAAERPGHFAGMVLISP 121
Cdd:COG2819 112 FLEEELKpYID---KRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
34-108 |
1.03e-03 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 39.45 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1918877125 34 REWEKAGSEHVletHLLPV---GHGQSEGERMVvSDFHVFVRDVLQHVdsmqKDYPGLPVFLLGHSMGGAIAILTAAE 108
Cdd:COG3208 23 RPWAAALPPDI---EVLAVqlpGRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
|
|
| Abhydrolase_5 |
pfam12695 |
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ... |
78-167 |
1.87e-03 |
|
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase enzymes.
Pssm-ID: 315383 [Multi-domain] Cd Length: 164 Bit Score: 38.20 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 78 VDSMQKDYPGLPVFLL-GHSMGGAIAILTAAERpGHFAGMVLisplvLANPESATTFKVLAAKVLNLVLPNLSLGPIDSS 156
Cdd:pfam12695 46 ALSIIKAHPKIQKWVVgGHSLGGVMASRFAADN-ELIKGVVF-----LASYPDKDSLSNLSFPVLSIYGTNDGVLNWKSY 119
|
90
....*....|....*.
gi 1918877125 157 V-----LSRNKTEVDI 167
Cdd:pfam12695 120 QknkqfLPKDTTYVSI 135
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
85-133 |
2.93e-03 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.24 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1918877125 85 YPGLPVFLLGHSMGGAIAILTAAerpghfagMVLISPLVLANPESATTF 133
Cdd:pfam01764 60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
92-123 |
3.07e-03 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 38.21 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|..
gi 1918877125 92 LLGHSMGGAIAILTAAERPGHFAGMVLISPLV 123
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
|
|
| PRK10673 |
PRK10673 |
esterase; |
54-119 |
4.68e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 37.79 E-value: 4.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1918877125 54 HGQSEgeRMVVSDFHVFVRDVLQHVDSMQKDypglPVFLLGHSMGGAIAILTAAERPGHFAGMVLI 119
Cdd:PRK10673 53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
51-121 |
5.89e-03 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 37.50 E-value: 5.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918877125 51 PVGHGQSEgermvvsDFHVfvRDVLQHVDSMqkdYPGLP----VFLLGHSMGGAIAILTAAERPGHFAGMVLISP 121
Cdd:COG0627 84 PAGHYRWE-------TYLT--EELPPLIEAN---FPVSAdrerRAIAGLSMGGHGALTLALRHPDLFRAVAAFSG 146
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
89-121 |
7.25e-03 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 37.22 E-value: 7.25e-03
10 20 30
....*....|....*....|....*....|...
gi 1918877125 89 PVFLLGHSMGGAIAILTAAERPGHFAGMVLISP 121
Cdd:cd12808 189 PCIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
69-159 |
7.49e-03 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 36.82 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918877125 69 VFVRDVLQHVDsmqkdypGLPVFLLGHSMGGAIAILTAA--ERPGHF-AGMVLISPLVLANPESATTFKVLAAKVLNLVl 145
Cdd:smart00824 52 AQAEAVLRAAG-------GRPFVLVGHSSGGLLAHAVAArlEARGIPpAAVVLLDTYPPGDPAPEGWLPELLRGVFERE- 123
|
90
....*....|....
gi 1918877125 146 pnLSLGPIDSSVLS 159
Cdd:smart00824 124 --DSFVPMDDARLT 135
|
|
| |
