|
Name |
Accession |
Description |
Interval |
E-value |
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
48-300 |
5.48e-95 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 282.16 E-value: 5.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLGH 127
Cdd:PHA02857 25 KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIKSTYPGVPVFLLGH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlaNPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLIC 207
Cdd:PHA02857 105 SMGATISILAAYKNPNLFTAMILMSPLV--NAEAVPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQYDPLVN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 RAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:PHA02857 183 HEKIKAGFASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NREIKIYEGAKHHLHKETDEVKKS 261
|
250
....*....|...
gi 1418205693 288 VFREINMWVSQRI 300
Cdd:PHA02857 262 VMKEIETWIFNRV 274
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
45-281 |
3.36e-92 |
|
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: 273.71 E-value: 3.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 45 QPLRALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFL 124
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 125 LGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSL-GPIDSSVLSRNKTEVDLYNSD 203
Cdd:pfam12146 81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLFPRLRVpNNLLPDSLSRDPEVVAAYAAD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418205693 204 PLICRaGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLHKEL 281
Cdd:pfam12146 161 PLVHG-GISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNEP 237
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
48-298 |
1.39e-43 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 148.61 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDyPGLPVFLLGH 127
Cdd:COG2267 28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRAR-PGLPVVLLGH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVLAAkvlnlvlpnmslgpidssvlsrnktevdlynsdplic 207
Cdd:COG2267 107 SMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWLRA------------------------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 raglkvcfgiqllnavTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAkSQDKTLKIYEGAYHVLHKELPEvtNS 287
Cdd:COG2267 150 ----------------LRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVLLPGARHELLNEPAR--EE 210
|
250
....*....|.
gi 1418205693 288 VFREINMWVSQ 298
Cdd:COG2267 211 VLAAILAWLER 221
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
41-299 |
4.03e-35 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 130.26 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 41 PRQTQPlRALIFVSHGAGEHCGRYDE-LAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQ--KDY 117
Cdd:PLN02385 81 PENSRP-KAAVCFCHGYGDTCTFFFEgIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDDLVDDVIEHYSKIKgnPEF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLV-----LANPESATTFKVLAAKVLnlvlPNMSLGP----IDSS 188
Cdd:PLN02385 160 RGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCkiaddVVPPPLVLQILILLANLL----PKAKLVPqkdlAELA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 189 VLSRNKTEVDLYNsdpLIC---RAGLKVcfGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDK 265
Cdd:PLN02385 236 FRDLKKRKMAEYN---VIAykdKPRLRT--AVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSVSKFLYEKASSSDK 310
|
250 260 270
....*....|....*....|....*....|....*
gi 1418205693 266 TLKIYEGAYH-VLHKELPEVTNSVFREINMWVSQR 299
Cdd:PLN02385 311 KLKLYEDAYHsILEGEPDEMIFQVLDDIISWLDSH 345
|
|
| PLN02298 |
PLN02298 |
hydrolase, alpha/beta fold family protein |
41-304 |
1.48e-34 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 165939 [Multi-domain] Cd Length: 330 Bit Score: 127.97 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 41 PRQTQPLRALIFVSHGAGEHCG-RYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKD--Y 117
Cdd:PLN02298 52 PSSSSPPRALIFMVHGYGNDISwTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVDLVVEDCLSFFNSVKQReeF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPESATTFKVlaAKVLNLV---LPNMSLGP----IDSSVL 190
Cdd:PLN02298 132 QGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPI--PQILTFVarfLPTLAIVPtadlLEKSVK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 191 SRNKTEVDLYNsdPLICRAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIY 270
Cdd:PLN02298 210 VPAKKIIAKRN--PMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSRALYEEAKSEDKTIKIY 287
|
250 260 270
....*....|....*....|....*....|....*
gi 1418205693 271 EGAYH-VLHKELPEVTNSVFREINMWVSQRIGAAA 304
Cdd:PLN02298 288 DGMMHsLLFGEPDENIEIVRRDILSWLNERCTGKA 322
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
47-307 |
8.40e-31 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 119.23 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 47 LRALIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHVFIRDVLQHVDFMQKDYPGLPVFLLG 126
Cdd:PLN02652 135 MRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLFG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 127 HSMGGAIaILTAAERPS---HFSGMVLISPLVLANPESATTFKVlaAKVLNLVLPNMSLGPIDSS--VLSRNKTEVDLYN 201
Cdd:PLN02652 215 HSTGGAV-VLKAASYPSiedKLEGIVLTSPALRVKPAHPIVGAV--APIFSLVAPRFQFKGANKRgiPVSRDPAALLAKY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 202 SDPLICRAGLKVCFGIQLLNAVTRVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLHKEl 281
Cdd:PLN02652 292 SDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLFE- 370
|
250 260
....*....|....*....|....*.
gi 1418205693 282 PEvTNSVFREINMWVSQRIGAAAGTG 307
Cdd:PLN02652 371 PE-REEVGRDIIDWMEKRLDLVNGSA 395
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
85-288 |
1.34e-24 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 99.63 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 85 GHGQSEGErMVVSDFHVFIRDVLQHVDFMQKDYPglPVFLLGHSMGGAIAILTAAERPsHFSGMVLISPLVLANPESAtt 164
Cdd:COG1647 52 GHGTSPED-LLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 165 fkvLAAKVLNLVLPnmSLGPIDSSVLSRNKTEVDlYNSDPLICraglkvcfGIQLLNAVTRVERALPKLTLPFLLLQGSA 244
Cdd:COG1647 126 ---PLLPLLKYLAR--SLRGIGSDIEDPEVAEYA-YDRTPLRA--------LAELQRLIREVRRDLPKITAPTLIIQSRK 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1418205693 245 DRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVLH--KELPEVTNSV 288
Cdd:COG1647 192 DEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEI 237
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
40-276 |
4.22e-19 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 84.58 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 40 PPRQTQPLRALIfVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGERMVVSDFHvfIRDVLQHVDFM--QKDY 117
Cdd:COG1073 30 PAGASKKYPAVV-VAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE--RRDARAAVDYLrtLPGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPsHFSGMVLISPlvLANPESAttFKVLAAKVLNLVLPNMSLGPidssvlsrNKTEV 197
Cdd:COG1073 107 DPERIGLLGISLGGGYALNAAATDP-RVKAVILDSP--FTSLEDL--AAQRAKEARGAYLPGVPYLP--------NVRLA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418205693 198 DLYNSDplicraglkvcfgiqlLNAVTRVEralpKLTLPFLLLQGSADRLCDSKGAYLLMEsAKSQDKTLKIYEGAYHV 276
Cdd:COG1073 174 SLLNDE----------------FDPLAKIE----KISRPLLFIHGEKDEAVPFYMSEDLYE-AAAEPKELLIVPGAGHV 231
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
41-301 |
3.35e-17 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 78.91 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 41 PRQTQPLRALIFVsHGAGEH-CGRYDELAQMLVGLELLVFAHDHVGHGQSEGERmvvsdFHVFIRDVLQHVDFM--QKDY 117
Cdd:COG1506 17 PADGKKYPVVVYV-HGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDW-----GGDEVDDVLAAIDYLaaRPYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 118 PGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPlvLANPESATTFKVLAAKVLNLVLPNMslgpidssvlsrnktEV 197
Cdd:COG1506 91 DPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--VSDLRSYYGTTREYTERLMGGPWED---------------PE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 198 DLYNSDPLicraglkvcfgiqllnavtrveRALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKSQ--DKTLKIYEGAYH 275
Cdd:COG1506 154 AYAARSPL----------------------AYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkPVELLVYPGEGH 211
|
250 260
....*....|....*....|....*.
gi 1418205693 276 VLHKelpEVTNSVFREINMWVSQRIG 301
Cdd:COG1506 212 GFSG---AGAPDYLERILDFLDRHLK 234
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
48-291 |
1.71e-16 |
|
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: 76.96 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 48 RALIFVsHGAGEHCGRYDELAQMLvGLELLVFAHDHVGHGQSEGERMVVSdFHVFIRDVLQHVDFMQKDypglPVFLLGH 127
Cdd:COG0596 24 PPVVLL-HGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGLE----RVVLVGH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 128 SMGGAIAILTAAERPSHFSGMVLISPLVlanpesattfKVLAAkvlNLVLPNMSLGPIDSSVLSRNKTEvdlynsdplic 207
Cdd:COG0596 97 SMGGMVALELAARHPERVAGLVLVDEVL----------AALAE---PLRRPGLAPEALAALLRALARTD----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 208 raglkvcfgiqllnavtrVERALPKLTLPFLLLQGSADRLCDSKGAYLLMESAKsqDKTLKIYEGAYHVLHKELPEVTNS 287
Cdd:COG0596 153 ------------------LRERLARITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAA 212
|
....
gi 1418205693 288 VFRE 291
Cdd:COG0596 213 ALRD 216
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
49-280 |
6.04e-13 |
|
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: 67.14 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 49 ALIFVsHGAGEHCGRYDELAQMLVGLELLVFAHDHVGHGQSEGeRMVVSDFHVFirDVLQHVDFMQKDYPGLPVFLLGHS 128
Cdd:pfam00561 2 PVLLL-HGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTD--DLAEDLEYILEALGLEKVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 129 MGGAIAILTAAERPSHFSGMVLISPLVLAN-------------PESATTFKVLAAKVLNLVLPNMSLGPI---DSSVLSR 192
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVLLGALDPPHeldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLllrLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 193 NKTEVDLYNSDPLIcrAGLKVCFGIQLLNAVTRVERA--LPKLTLPFLLLQGSADRLCDSKGAYLLmeSAKSQDKTLKIY 270
Cdd:pfam00561 158 PLLNKRFPSGDYAL--AKSLVTGALLFIETWSTELRAkfLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARLVVI 233
|
250
....*....|
gi 1418205693 271 EGAYHVLHKE 280
Cdd:pfam00561 234 PDAGHFAFLE 243
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
50-278 |
2.51e-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: 50.55 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 50 LIFVsHGAGEHcgrYDELAQmLVGLELLVFAHDHVGHGQSEGERMVVSDfhvfIRDVLQHVDFMQKDYPglpVFLLGHSM 129
Cdd:pfam12697 1 VVLV-HGAGLS---AAPLAA-LLAAGVAVLAPDLPGHGSSSPPPLDLAD----LADLAALLDELGAARP---VVLVGHSL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 130 GGAIAiLTAAERPSHFSgmVLISPLVLANPESATTFKVLAAKVLNLVLPNMSLGPIDSSVLSRNKTEVDLYNSDPLICRA 209
Cdd:pfam12697 69 GGAVA-LAAAAAALVVG--VLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418205693 210 GLKVCFGIQLlnavtrveRALPKLTLPFLLLqGSADRLCDskgAYLLMESAKSQDKTLKIYEGAYHVLH 278
Cdd:pfam12697 146 LLAALALLPL--------AAWRDLPVPVLVL-AEEDRLVP---ELAQRLLAALAGARLVVLPGAGHLPL 202
|
|
| PRK10749 |
PRK10749 |
lysophospholipase L2; Provisional |
63-275 |
6.94e-06 |
|
lysophospholipase L2; Provisional
Pssm-ID: 182697 Cd Length: 330 Bit Score: 46.91 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 63 RYDELAQMLVGLELLVFAHDHVGHGQS-----EGERMVVSDFHVFIRDVLQhvdFMQKDYPGLPV---FLLGHSMGGAIA 134
Cdd:PRK10749 69 KYAELAYDLFHLGYDVLIIDHRGQGRSgrlldDPHRGHVERFNDYVDDLAA---FWQQEIQPGPYrkrYALAHSMGGAIL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 135 ILTAAERPSHFSGMVLISPL---VLANPESATTFKVLAAKVLNLVLPNMSLG-------PIDSSVLS----RNKTEVDLY 200
Cdd:PRK10749 146 TLFLQRHPGVFDAIALCAPMfgiVLPLPSWMARRILNWAEGHPRIRDGYAIGtgrwrplPFAINVLThsreRYRRNLRFY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 201 NSDPLI---------CRAGLKVcfGIQLLNAVtrveralPKLTLPFLLLQGSADRLCDSKG------AYLLMESAKSQDK 265
Cdd:PRK10749 226 ADDPELrvggptyhwVRESILA--GEQVLAGA-------GDITTPLLLLQAEEERVVDNRMhdrfceARTAAGHPCEGGK 296
|
250
....*....|
gi 1418205693 266 TLKIyEGAYH 275
Cdd:PRK10749 297 PLVI-KGAYH 305
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
102-153 |
1.61e-05 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 45.36 E-value: 1.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1418205693 102 FIRDVLQhvDFMQKDYPGLPVF--LLGHSMGGAIAILTAAERPSHFSGMVLISP 153
Cdd:COG2819 112 FLEEELK--PYIDKRYRTDPERtgLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| PLN02578 |
PLN02578 |
hydrolase |
78-297 |
1.81e-05 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 45.60 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 78 VFAHDHVGHGQSEgERMVVSDFHVFIRDVlqhVDFMqKDYPGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPL--- 154
Cdd:PLN02578 115 VYALDLLGFGWSD-KALIEYDAMVWRDQV---ADFV-KEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqf 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 155 ---------VLANPESA-TTFKVLAAK------VLNLVLPNMSLGPIDSSVLS---RNKTEVDLY--------NSDP--- 204
Cdd:PLN02578 190 gsesrekeeAIVVEETVlTRFVVKPLKewfqrvVLGFLFWQAKQPSRIESVLKsvyKDKSNVDDYlvesitepAADPnag 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 205 -----LICRAglkvcfgiqLLNAVT-RVERALPKLTLPFLLLQGSADRLCDSKGAYLLmeSAKSQDKTLkIYEGAYHVLH 278
Cdd:PLN02578 270 evyyrLMSRF---------LFNQSRyTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKI--KAFYPDTTL-VNLQAGHCPH 337
|
250
....*....|....*....
gi 1418205693 279 KELPEVTNSVFREinmWVS 297
Cdd:PLN02578 338 DEVPEQVNKALLE---WLS 353
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
41-142 |
2.04e-05 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 44.96 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 41 PRQTQPLRALIFVsHGAGEHCGRYDELAQMLVGLELLVFA---HDHVGHGQSEGE---RMVVSDFHVFIRDVLQHVDFM- 113
Cdd:COG0412 23 PAGGGPRPGVVVL-HEIFGLNPHIRDVARRLAAAGYVVLApdlYGRGGPGDDPDEaraLMGALDPELLAADLRAALDWLk 101
|
90 100 110
....*....|....*....|....*....|
gi 1418205693 114 -QKDYPGLPVFLLGHSMGGAIAILTAAERP 142
Cdd:COG0412 102 aQPEVDAGRVGVVGFCFGGGLALLAAARGP 131
|
|
| PST-A |
TIGR01607 |
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ... |
78-280 |
2.79e-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: 45.16 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 78 VFAHDHVGHGQSEGE---RMVVSDFHVFIRDVLQHV--------------------DFMQKDYPGLPVFLLGHSMGGAIA 134
Cdd:TIGR01607 77 VYGLDLQGHGESDGLqnlRGHINCFDDLVYDVIQYMnrindsiilenetksddesyDIVNTKENRLPMYIIGLSMGGNIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 135 ILT------AAERPSH--------FSGMVLISPLVLANPESATTFKVLAAKVLNLVLPNMSLGPIDSsvLSRNKTEVDLY 200
Cdd:TIGR01607 157 LRLlellgkSNENNDKlnikgcisLSGMISIKSVGSDDSFKFKYFYLPVMNFMSRVFPTFRISKKIR--YEKSPYVNDII 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 201 NSDPLICRAGLKVCFGIQLLNAVTRVE---RALPKlTLPFLLLQGSADRLCDSKGAYLLMESAKSQDKTLKIYEGAYHVL 277
Cdd:TIGR01607 235 KFDKFRYDGGITFNLASELIKATDTLDcdiDYIPK-DIPILFIHSKGDCVCSYEGTVSFYNKLSISNKELHTLEDMDHVI 313
|
...
gi 1418205693 278 HKE 280
Cdd:TIGR01607 314 TIE 316
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
78-153 |
4.19e-05 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 44.55 E-value: 4.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418205693 78 VFAHDHVGHGQSeGERMVVSDFHVFIRDVLqhvDFMqkDYPGLP-VFLLGHSMGGAIAILTAAERPSHFSGMVLISP 153
Cdd:PRK14875 160 VIALDLPGHGAS-SKAVGAGSLDELAAAVL---AFL--DALGIErAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
41-166 |
6.07e-05 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 43.42 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 41 PRQTQPLraLIFVsHGAGEhcgRYDEL-AQMLVGLELLVFAHDHVGHG------Q-SEGERMVVSDFHvfiRDVLQHVDF 112
Cdd:COG4099 45 PGKKYPL--VLFL-HGAGE---RGTDNeKQLTHGAPKFINPENQAKFPaivlapQcPEDDYWSDTKAL---DAVLALLDD 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 113 MQKDYPGLP--VFLLGHSMGGAIAILTAAERPSHFSGMVLISPlvLANPESATTFK 166
Cdd:COG4099 116 LIAEYRIDPdrIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG--GGDPANAANLK 169
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
121-154 |
1.74e-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: 42.60 E-value: 1.74e-04
10 20 30
....*....|....*....|....*....|....
gi 1418205693 121 PVFLLGHSMGGAIAILTAAERPSHFSGMVLISPL 154
Cdd:cd12809 172 PAILITHSQGGPFGWLAADARPDLVKAIVAIEPS 205
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
99-140 |
3.16e-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: 41.31 E-value: 3.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1418205693 99 FHVFIRDVLQHVDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:cd00519 107 YKSLYNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLALD 148
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
48-160 |
5.97e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 40.28 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 48 RALIFVSHGAGEHCGRYDELAQMLVGLELLVFA------HDHVGHG-----------QSEGERMVVSDFHVFIRDVLQHV 110
Cdd:COG0400 5 APLVVLLHGYGGDEEDLLPLAPELALPGAAVLAprapvpEGPGGRAwfdlsflegreDEEGLAAAAEALAAFIDELEARY 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1418205693 111 DFmqkdyPGLPVFLLGHSMGGAIAILTAAERPSHFSGMVLISPLVLANPE 160
Cdd:COG0400 85 GI-----DPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEA 129
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
50-275 |
7.37e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 40.86 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 50 LIFVSHGAGEHCGRYDELAQMLVGLELLVFAHDHVGH--GQSEGERMVVSDFHVF---------IRDVLQHVDFMQKDYP 118
Cdd:COG4188 64 LVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSnaADLSAALDGLADALDPeelwerpldLSFVLDQLLALNKSDP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 119 GLP-------VFLLGHSMGGAIAILTAAERPshfsgmvlisplvlanpeSATTFKVLAAKVLNLVLPNMSLGPIDSSVls 191
Cdd:COG4188 144 PLAgrldldrIGVIGHSLGGYTALALAGARL------------------DFAALRQYCGKNPDLQCRALDLPRLAYDL-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 192 rnktevdlynSDPLIcRAGLkvcfgiqLLNAVTR---VERALPKLTLPFLLLQGSADRlcDSKGAY---LLMESAKSQDK 265
Cdd:COG4188 204 ----------RDPRI-KAVV-------ALAPGGSglfGEEGLAAITIPVLLVAGSADD--VTPAPDeqiRPFDLLPGADK 263
|
250
....*....|
gi 1418205693 266 TLKIYEGAYH 275
Cdd:COG4188 264 YLLTLEGATH 273
|
|
| COG3571 |
COG3571 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
103-140 |
7.44e-04 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 442792 [Multi-domain] Cd Length: 202 Bit Score: 39.86 E-value: 7.44e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1418205693 103 IRDVLQHVDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3571 63 DAAWRAVIAALRARLAGLPLVIGGKSMGGRVASMLAAE 100
|
|
| Lipase |
cd00741 |
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ... |
99-140 |
1.09e-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: 39.02 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1418205693 99 FHVFIRDVLQHVDFMQKD----YPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:cd00741 3 FYKAARSLANLVLPLLKSalaqYPDYKIHVTGHSLGGALAGLAGLD 48
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
78-163 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418205693 78 VFAHDHVGHGQSEgermvvsdfHVFIRDVLQHvdfMQKDYPGLP--VFLLGHSMGGAIAILTAAERPSHFSGMVLIS--P 153
Cdd:COG3509 102 WFDGRDQRRGRDD---------VAFIAALVDD---LAARYGIDPkrVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglP 169
|
90
....*....|
gi 1418205693 154 LVLANPESAT 163
Cdd:COG3509 170 YGAASDAACA 179
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
102-155 |
3.02e-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: 38.60 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 102 FIRDVLqhVDFMQKDYPGLPVF--LLGHSMGGAIAILTAAERPSHFSGMVLISPLV 155
Cdd:pfam00756 92 FLTQEL--PPLLDANFPTAPDGraLAGQSMGGLGALYLALKYPDLFGSVSSFSPIL 145
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
117-165 |
3.03e-03 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.24 E-value: 3.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1418205693 117 YPGLPVFLLGHSMGGAIAILTAAerpshfsgMVLISPLVLANPESATTF 165
Cdd:pfam01764 60 YPDYSIVVTGHSLGGALASLAAL--------DLVENGLRLSSRVTVVTF 100
|
|
| PRK10673 |
PRK10673 |
esterase; |
86-151 |
5.85e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 37.79 E-value: 5.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 86 HGQSEgeRMVVSDFHVFIRDVLQHVDFMQKDypglPVFLLGHSMGGAIAILTAAERPSHFSGMVLI 151
Cdd:PRK10673 53 HGLSP--RDPVMNYPAMAQDLLDTLDALQIE----KATFIGHSMGGKAVMALTALAPDRIDKLVAI 112
|
|
| Lip2 |
COG3675 |
Predicted lipase [Lipid transport and metabolism]; |
79-140 |
6.59e-03 |
|
Predicted lipase [Lipid transport and metabolism];
Pssm-ID: 442891 [Multi-domain] Cd Length: 266 Bit Score: 37.43 E-value: 6.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418205693 79 FAHDHVGHGQSEGerMVVSDFHVFIRDVLQH-VDFMQKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3675 48 AAQVPYPFAKTGG--KVHRGFYRALQSLRELlEDALRPLSPGKRLYVTGHSLGGALATLAAAD 108
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
85-140 |
9.73e-03 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 36.75 E-value: 9.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1418205693 85 GHGQSEGERMVvSDFHVFIRDVLQHVdfmqKDYPGLPVFLLGHSMGGAIAILTAAE 140
Cdd:COG3208 42 GRGDRLGEPPL-TSLEELADDLAEEL----APLLDRPFALFGHSMGALLAFELARR 92
|
|
|