|
Name |
Accession |
Description |
Interval |
E-value |
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
78-314 |
1.82e-95 |
|
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: 283.34 E-value: 1.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 78 GPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMKSRHPDLPVFI 157
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 158 VGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGT-MDSRWVSRDKTKVEAYDTD 236
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453008 237 ELNfHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHDL 314
Cdd:pfam12146 161 PLV-HGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
61-329 |
5.63e-82 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 250.19 E-value: 5.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 61 LVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSL 140
Cdd:PHA02857 5 MFNLDNDYIYCKYWKPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 141 QHIDLMKSRHPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSLTLGTMDS 220
Cdd:PHA02857 85 QHVVTIKSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 221 RWVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApSSDKKL 300
Cdd:PHA02857 163 ESVSRDMDEVYKYQYDPLVNHEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHA-NCNREI 241
|
250 260
....*....|....*....|....*....
gi 1879453008 301 KVYEGGYHALHHDLPEVAESTLKEVTSWI 329
Cdd:PHA02857 242 KIYEGAKHHLHKETDEVKKSVMKEIETWI 270
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
56-331 |
1.96e-46 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 157.09 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 56 SELRHLVNADGLHLFCRYWEPAGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVY 135
Cdd:COG2267 3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 136 IRDSLQHIDLMKSRhPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFkvflakvlnhllpsltl 215
Cdd:COG2267 83 VDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSA----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 216 gtmdsRWVsrdktkveaydtdelnfhgglrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNApS 295
Cdd:COG2267 145 -----RWL-------------------------------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-S 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 1879453008 296 SDKKLKVYEGGYHALHHDlpEVAESTLKEVTSWITE 331
Cdd:COG2267 188 PDVELVLLPGARHELLNE--PAREEVLAAILAWLER 221
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
62-332 |
2.53e-46 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 160.69 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 62 VNADGLHLFCRYWEP-AGPPRALVFIAHGAGEHCGPYDE-IAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDS 139
Cdd:PLN02385 67 VNSRGVEIFSKSWLPeNSRPKAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 140 LQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATP-----FKVFLAKVL--NHLL 210
Cdd:PLN02385 147 IEHYSKIKGNpeFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPplvlqILILLANLLpkAKLV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 211 PSLTLGTMdsrwVSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 290
Cdd:PLN02385 227 PQKDLAEL----AFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLY 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1879453008 291 KNAPSSDKKLKVYEGGYHALHHDLPEVAEST-LKEVTSWITEH 332
Cdd:PLN02385 303 EKASSSDKKLKLYEDAYHSILEGEPDEMIFQvLDDIISWLDSH 345
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
66-339 |
7.72e-37 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 135.29 E-value: 7.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 66 GLHLFCRYWEP--AGPPRALVFIAHGAGEHCG-PYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQH 142
Cdd:PLN02298 42 GLSLFTRSWLPssSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 143 IDLMKSR--HPDLPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQMNPESATPFKV-----FLAKvlnhLLPslTL 215
Cdd:PLN02298 122 FNSVKQReeFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIpqiltFVAR----FLP--TL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 216 GTMDSRWVSRDKTKVEAY----DTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFK 291
Cdd:PLN02298 196 AIVPTADLLEKSVKVPAKkiiaKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYE 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1879453008 292 NAPSSDKKLKVYEGGYHALHHDLP-EVAESTLKEVTSWITEHLPAKKSP 339
Cdd:PLN02298 276 EAKSEDKTIKIYDGMMHSLLFGEPdENIEIVRRDILSWLNERCTGKATP 324
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
69-333 |
3.30e-35 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 132.32 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 69 LFCRYWEP-AGPPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNIKNFQVYIRDSLQHIDLMK 147
Cdd:PLN02652 123 LFCRSWAPaAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 148 SRHPDLPVFIVGHSMGGAIsILTACERPS---DFAGVVLIAPMVQMNPesATPFKVFLAKVLNHLLPSLTLGTMDSRW-- 222
Cdd:PLN02652 203 SENPGVPCFLFGHSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKP--AHPIVGAVAPIFSLVAPRFQFKGANKRGip 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 223 VSRDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKV 302
Cdd:PLN02652 280 VSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKL 359
|
250 260 270
....*....|....*....|....*....|.
gi 1879453008 303 YEGGYHALHHDlPEvAESTLKEVTSWITEHL 333
Cdd:PLN02652 360 YDGFLHDLLFE-PE-REEVGRDIIDWMEKRL 388
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
77-332 |
1.30e-27 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 108.49 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 77 AGPPRALVFIaHGAGehCGPYD--EIAQRLKELSLLVFAHDHVGHGQSEGDrMNIKNFQVYIRDSLQHIDLMKSRHPdlP 154
Cdd:COG1647 12 EGGRKGVLLL-HGFT--GSPAEmrPLAEALAKAGYTVYAPRLPGHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 155 VFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESAtpfkvFLAKVLNHLlpsltlgtmdSRWVSRDKTKVEAYD 234
Cdd:COG1647 86 VIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-----PLLPLLKYL----------ARSLRGIGSDIEDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 235 TDELNFHGgLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGGYHALHHD- 313
Cdd:COG1647 150 VAEYAYDR-TPLRALAELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDk 228
|
250 260
....*....|....*....|
gi 1879453008 314 -LPEVAEstlkEVTSWITEH 332
Cdd:COG1647 229 dREEVAE----EILDFLERL 244
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
52-333 |
2.68e-20 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 88.43 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 52 GVPYSELrHLVNADGLHLFCRYWEPAG--PPRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGDRMNI 129
Cdd:COG1073 7 KVNKEDV-TFKSRDGIKLAGDLYLPAGasKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 130 KNFQvyIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVLIAPMVQMNPESATPFKVFLAKVLN 207
Cdd:COG1073 86 GSPE--RRDARAAVDYLRTLpgVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 208 H--LLPSLTLgtmdsrwvsrdktkveaydtdelnfhgglrVSFGMQLMGAATRIEReipsINWPFLLLHGDADKLCDIGG 285
Cdd:COG1073 163 GvpYLPNVRL------------------------------ASLLNDEFDPLAKIEK----ISRPLLFIHGEKDEAVPFYM 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1879453008 286 SKMMFKNAPsSDKKLKVYEGGYHALHHDLPEvaESTLKEVTSWITEHL 333
Cdd:COG1073 209 SEDLYEAAA-EPKELLIVPGAGHVDLYDRPE--EEYFDKLAEFFKKNL 253
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
63-334 |
2.95e-20 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 88.15 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 63 NADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGP-YDEIAQRLKELSLLVFAHDHVGHGQSEGDRmniknFQVYIRDSL 140
Cdd:COG1506 4 SADGTTLPGWLYLPADGkKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 141 QHIDLMKSRhPDLP---VFIVGHSMGGAISILTACERPSDFAGVVLIAPMVqmNPESATPFKVFLAKVLNHLLPSltlgt 217
Cdd:COG1506 79 AAIDYLAAR-PYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSYYGTTREYTERLMGGPWE----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 218 mdsrwvsrdktKVEAYDTdelnfhgglrvsfgMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPSS- 296
Cdd:COG1506 151 -----------DPEAYAA--------------RSPLAYADKLKT-------PLLLIHGEADDRVPPEQAERLYEALKKAg 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 1879453008 297 -DKKLKVYEGGYHALhhdLPEVAESTLKEVTSWITEHLP 334
Cdd:COG1506 199 kPVELLVYPGEGHGF---SGAGAPDYLERILDFLDRHLK 234
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
59-332 |
3.59e-18 |
|
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: 81.97 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 59 RHLVNADGLHLFCRYWEPAGPPraLVFIaHGAGEHCGPYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIkNFQVYIRD 138
Cdd:COG0596 4 PRFVTVDGVRLHYREAGPDGPP--VVLL-HGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGY-TLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 139 slqHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIAPMVQmnpesatpfkvFLAKVLNHllpsltlgtm 218
Cdd:COG0596 79 ---LAALLDALGLE-RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-----------ALAEPLRR---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 219 dsrwvsrdktkveaYDTDELNFHGGLRVSFGMQLMGAATRIEReipsinwPFLLLHGDADKLCDIGGSKMMFKNAPssDK 298
Cdd:COG0596 134 --------------PGLAPEALAALLRALARTDLRERLARITV-------PTLVIWGEKDPIVPPALARRLAELLP--NA 190
|
250 260 270
....*....|....*....|....*....|....
gi 1879453008 299 KLKVYEGGYHALHHDLPEVaesTLKEVTSWITEH 332
Cdd:COG0596 191 ELVVLPGAGHFPPLEQPEA---FAAALRDFLARL 221
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
60-328 |
3.48e-11 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 62.29 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 60 HLVNADGLHLFCRYWEPAGP-PRALVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGD------RMNIKNF 132
Cdd:COG0412 7 TIPTPDGVTLPGYLARPAGGgPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDDpdearaLMGALDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 133 QVYIRDSLQHIDLMKSR--HPDLPVFIVGHSMGGAISILTACERPsDFAGVVliapmvqmnpesatpfkvflakvlnhll 210
Cdd:COG0412 87 ELLAADLRAALDWLKAQpeVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAV---------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 211 psltlgtmdsrwvsrdktkveaydtdelNFHGGLrvsfgmqlmgAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMF 290
Cdd:COG0412 138 ----------------------------SFYGGL----------PADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALE 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1879453008 291 K--NAPSSDKKLKVYEGGYHALHHDL-----PEVAESTLKEVTSW 328
Cdd:COG0412 180 AalAAAGVDVELHVYPGAGHGFTNPGrprydPAAAEDAWQRTLAF 224
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
83-313 |
1.00e-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: 60.98 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 83 LVFIAHGAGEHCGPYDEIAQRLKELSLLVFAHDHVGHGQSEGdRMNIKNFQVYirDSLQHIDLMKSRHPDLPVFIVGHSM 162
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 163 GGAISILTACERPSDFAGVVLIAPMvqMNPESATPFKVFLAKVL-------------NHLLPSL-----TLGTMDSRWVS 224
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFpgffdgfvadfapNPLGRLVakllaLLLLRLRLLKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 225 RDKTKVEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDADKLCDIGGSKMMfkNAPSSDKKLKVYE 304
Cdd:pfam00561 157 LPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVIP 234
|
....*....
gi 1879453008 305 GGYHALHHD 313
Cdd:pfam00561 235 DAGHFAFLE 243
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
111-329 |
9.12e-09 |
|
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: 55.94 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 111 VFAHDHVGHGQSEG---DRMNIKNFQVYIRDSLQHI--------------------DLMKSRHPDLPVFIVGHSMGGAIS 167
Cdd:TIGR01607 77 VYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 168 -----ILTACERPSD---FAGVVLIAPMVQM----NPESATpFKVFLAKVLNHL-------LPSLTLGTMDSRWVSrdkt 228
Cdd:TIGR01607 157 lrlleLLGKSNENNDklnIKGCISLSGMISIksvgSDDSFK-FKYFYLPVMNFMsrvfptfRISKKIRYEKSPYVN---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 229 kvEAYDTDELNFHGGLRVSFGMQLMGAATRIEREIPSI--NWPFLLLHGDADKLCDIGGSKMMFKNAPSSDKKLKVYEGG 306
Cdd:TIGR01607 232 --DIIKFDKFRYDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDM 309
|
250 260
....*....|....*....|...
gi 1879453008 307 YHALhhDLPEVAESTLKEVTSWI 329
Cdd:TIGR01607 310 DHVI--TIEPGNEEVLKKIIEWI 330
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
83-319 |
3.16e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 53.25 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 83 LVFIaHGAGEHcgpYDEIAQRLKElSLLVFAHDHVGHGQSEGDRMNIknfqvyiRDSLQHIDLMKSRHPDLPVFIVGHSM 162
Cdd:pfam12697 1 VVLV-HGAGLS---AAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDL-------ADLADLAALLDELGAARPVVLVGHSL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 163 GGAISILTAcerPSDFAGVVLIAPMVQMNPESATPFKVFLAKVLNHLLPSLTLGTMDSRWVSRDKTKVEAYDTdelnfhg 242
Cdd:pfam12697 69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1879453008 243 gLRVSFGMQLMGAATRIEREIPSINWPFLLLHGDaDKLCDIGGSKMMfknAPSSDKKLKVYEGGYHALHHDLPEVAE 319
Cdd:pfam12697 139 -ALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLL---AALAGARLVVLPGAGHLPLDDPEEVAE 210
|
|
| PRK10749 |
PRK10749 |
lysophospholipase L2; Provisional |
97-187 |
1.14e-07 |
|
lysophospholipase L2; Provisional
Pssm-ID: 182697 Cd Length: 330 Bit Score: 52.69 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 97 YDEIAQRLKELSLLVFAHDHVGHGQS-----EGDRMNIKNFQVYIRDS----LQHIDLMKSRHpdlpVFIVGHSMGGAIS 167
Cdd:PRK10749 70 YAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLaafwQQEIQPGPYRK----RYALAHSMGGAIL 145
|
90 100
....*....|....*....|
gi 1879453008 168 ILTACERPSDFAGVVLIAPM 187
Cdd:PRK10749 146 TLFLQRHPGVFDAIALCAPM 165
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
138-187 |
1.17e-04 |
|
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: 43.37 E-value: 1.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1879453008 138 DSLQHIDLMKSRHPDL-----PVFIVGHSMGGAISILTACERPSDFAGVVLIAPM 187
Cdd:cd12809 151 NLAEQEALVRAAGCALldiigPAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
143-197 |
1.32e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 43.07 E-value: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 143 IDLMKSRH---PDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA--PMVQMNPESATP 197
Cdd:COG3509 122 VDDLAARYgidPK-RVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglPYGAASDAACAP 180
|
|
| Abhydrolase_11 |
pfam20408 |
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ... |
80-183 |
1.40e-04 |
|
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.
Pssm-ID: 466557 [Multi-domain] Cd Length: 193 Bit Score: 42.19 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 80 PRALVFIAHGAG---EHcgPY-DEIAQRLKELSLLVFAHD-------HVGHGQSEGDRMNIknFQVYIRDSLQHIdlmks 148
Cdd:pfam20408 1 PKARLLLAHGAGagmDS--PFmQAMAAALAARGIAVVRFNfpymqrrRRTGKRRPPDRAPK--LLEAFRAVIAAL----- 71
|
90 100 110
....*....|....*....|....*....|....*
gi 1879453008 149 RHPDLPVFIVGHSMGGAISILTACErpSDFAGVVL 183
Cdd:pfam20408 72 RGPDLPLFIGGKSMGGRVASLLADD--SGVKGVIA 104
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
138-171 |
1.86e-04 |
|
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: 42.08 E-value: 1.86e-04
10 20 30
....*....|....*....|....*....|....
gi 1879453008 138 DSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 171
Cdd:cd00519 113 QVLPELKSALKQYPDYKIIVTGHSLGGALASLLA 146
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
79-185 |
2.01e-04 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 442792 [Multi-domain] Cd Length: 202 Bit Score: 41.79 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 79 PPRALVFIAHGAGehcGPYD-----EIAQRLKELSLLVFAHDHVG--HGQSEGDRMniknfQVYIRDSLQHIDLMKSRHP 151
Cdd:COG3571 7 DPRATLLLAHGAG---AGMDspfmvALAEALAAAGIAVARFEFPYmvAGRRPPDRA-----PVLDAAWRAVIAALRARLA 78
|
90 100 110
....*....|....*....|....*....|....
gi 1879453008 152 DLPVFIVGHSMGGAISILTACErPSDFAGVVLIA 185
Cdd:COG3571 79 GLPLVIGGKSMGGRVASMLAAE-GGGAAGLVCLG 111
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
77-188 |
2.21e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 77 AGPPRALVFIAHGAGEHcgPYD--EIAQRLKELSLLVFA------HDHVGHGQSEGDRMNIKNFQVYIRDSLQHID---- 144
Cdd:COG0400 1 GGPAAPLVVLLHGYGGD--EEDllPLAPELALPGAAVLAprapvpEGPGGRAWFDLSFLEGREDEEGLAAAAEALAafid 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1879453008 145 -LMKSRHPDL-PVFIVGHSMGGAISILTACERPSDFAGVVLIAPMV 188
Cdd:COG0400 79 eLEARYGIDPeRIVLAGFSQGAAMALSLALRRPELLAGVVALSGYL 124
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
111-186 |
2.84e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.24 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 111 VFAHDHVGHGQSEGDrmniknfqvYIRDSLQH-----IDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFAGVVLIA 185
Cdd:PRK14875 160 VIALDLPGHGASSKA---------VGAGSLDElaaavLAFLDALGIE-RAHLVGHSMGGAVALRLAARAPQRVASLTLIA 229
|
.
gi 1879453008 186 P 186
Cdd:PRK14875 230 P 230
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
142-199 |
1.05e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 39.95 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1879453008 142 HIDlmKSRhpdlpVFIVGHSMGGAISILTACERPSDFAGVVLIAPmvQMNPESATPFK 199
Cdd:COG4099 121 RID--PDR-----IYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
147-171 |
1.13e-03 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 38.78 E-value: 1.13e-03
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
137-171 |
1.32e-03 |
|
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: 38.64 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 1879453008 137 RDSLQHIDLMKSRHPDLPVFIVGHSMGGAISILTA 171
Cdd:cd00741 12 NLVLPLLKSALAQYPDYKIHVTGHSLGGALAGLAG 46
|
|
| PLN02578 |
PLN02578 |
hydrolase |
31-194 |
1.50e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 40.21 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 31 VSVADPSSMPEPGAAPRR---SPQGVPYSELR----HLVNadglhlfcrywEPAGPPRALVfiaHGAGEHCGPY----DE 99
Cdd:PLN02578 43 VSVMGSSSASQSVQGLERlpfKKEGYNFWTWRghkiHYVV-----------QGEGLPIVLI---HGFGASAFHWryniPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879453008 100 IAQRLKelsllVFAHDHVGHGQSegDRMNIKNFQVYIRDslQHIDLMKSRHPDlPVFIVGHSMGGAISILTACERPSDFA 179
Cdd:PLN02578 109 LAKKYK-----VYALDLLGFGWS--DKALIEYDAMVWRD--QVADFVKEVVKE-PAVLVGNSLGGFTALSTAVGYPELVA 178
|
170
....*....|....*
gi 1879453008 180 GVVLIAPMVQMNPES 194
Cdd:PLN02578 179 GVALLNSAGQFGSES 193
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
157-186 |
3.68e-03 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 38.43 E-value: 3.68e-03
10 20 30
....*....|....*....|....*....|
gi 1879453008 157 IVGHSMGGAISILTACERPSDFAGVVLIAP 186
Cdd:COG2819 134 LIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| |
