|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
44-305 |
4.76e-54 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 176.84 E-value: 4.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 44 LPLSYRLLDGE---AALPaVVFLHGLFGSKTNFNSIAKILaqQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQ 120
Cdd:PRK10673 1 MKLNIRAQTAQnphNNSP-IVLVHGLFGSLDNLGVLARDL--VNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 121 LGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTgVSHFATYVAAMRAINIADELPRSRARKLADEQlssv 200
Cdd:PRK10673 78 LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYH-VRRHDEIFAAINAVSEAGATTRQQAAAIMRQH---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 201 IQDMAVRQHLLTNLVEVDgrfvWRVNLDALTQHLDKILAFpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQ 280
Cdd:PRK10673 153 LNEEGVIQFLLKSFVDGE----WRFNVPVLWDQYPHIVGW-EKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAH 227
|
250 260
....*....|....*....|....*
gi 1887096812 281 TVPNAGHWIHADRPQDFIAAIRGFL 305
Cdd:PRK10673 228 VIAGAGHWVHAEKPDAVLRAIRRYL 252
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
58-305 |
3.98e-40 |
|
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: 139.75 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 58 PAVVFLHGLFGSKTNFNSIAKILAQqtGRRVLTVDARNHGDSPHSP-DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGK 136
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAA--GYRVIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 137 TAMLLALQRPELVERLIAVDispvestgvSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVrqhlltnlve 216
Cdd:COG0596 102 VALELAARHPERVAGLVLVD---------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITV---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 217 vdgrfvwrvnldaltqhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQD 296
Cdd:COG0596 163 ---------------------------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEA 209
|
....*....
gi 1887096812 297 FIAAIRGFL 305
Cdd:COG0596 210 FAAALRDFL 218
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
58-294 |
2.15e-28 |
|
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: 109.52 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP---DMSYEIMSQDLQDLLPQLGLVPCVVVGHSMG 134
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGKSSRPKaqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 135 GKTAMLLALQRPELVERLIAVD-ISPVESTG--VSHFATYVAAMRAINIADELPRSRARKLADEQLSSViqdmaVRQHLL 211
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLLGaLDPPHELDeaDRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLL-----LRLRLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 212 TNLVEVDGRFvWRVNLDA----LTQHLDKILAFPQRQE-----SYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTV 282
Cdd:pfam00561 155 KALPLLNKRF-PSGDYALakslVTGALLFIETWSTELRakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233
|
250
....*....|..
gi 1887096812 283 PNAGHWIHADRP 294
Cdd:pfam00561 234 PDAGHFAFLEGP 245
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
48-305 |
1.05e-18 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 82.74 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 48 YRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDM--SYEIMSQDLQ---DLLPQLG 122
Cdd:COG2267 19 RRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRaalDALRARP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 123 LVPCVVVGHSMGGKTAMLLALQRPELVERLIAvdISPvestgvshfatyvaamraINIADELPRSRARKLADEQLSSVIQ 202
Cdd:COG2267 98 GLPVVLLGHSMGGLIALLYAARYPDRVAGLVL--LAP------------------AYRADPLLGPSARWLRALRLAEALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 203 DMAVrqhlltnlvevdgrfvwrvnldaltqhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIM-RLFPRAQMQT 281
Cdd:COG2267 158 RIDV-------------------------------------------PVLVLHGGADRVVPPEAARRLAaRLSPDVELVL 194
|
250 260
....*....|....*....|....*
gi 1887096812 282 VPNAGHWIHADRPQD-FIAAIRGFL 305
Cdd:COG2267 195 LPGARHELLNEPAREeVLAAILAWL 219
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
58-305 |
1.40e-13 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 68.81 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 58 PAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHS-PDMSYEIMSQDLQDLLPQL--GLVPCVVVGHSMG 134
Cdd:COG1647 16 KGVLLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 135 GKTAMLLALQRPElVERLIAvdISPV-----ESTGVSHFATYVAA-MRAINIADELPRSRARKLADEQLSSVIQdmavrq 208
Cdd:COG1647 95 GLLALLLAARYPD-VAGLVL--LSPAlkiddPSAPLLPLLKYLARsLRGIGSDIEDPEVAEYAYDRTPLRALAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 209 hlLTNLVEvdgrfVWRVNLDALTQhldkilafpqrqesylgPTLFLLGGNSQFVHPSHHPEIMRLF--PRAQMQTVPNAG 286
Cdd:COG1647 166 --LQRLIR-----EVRRDLPKITA-----------------PTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSG 221
|
250 260
....*....|....*....|
gi 1887096812 287 HWIHADRPQDFIA-AIRGFL 305
Cdd:COG1647 222 HVITLDKDREEVAeEILDFL 241
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
60-300 |
4.26e-13 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 67.11 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 60 VVFLHGLFGSKTNFNSiakilAQQTGRRVLTVDARNHGDSPHSPDMSYEImsQDLQDLLPQLGLV-PCVVVGHSMGGKTA 138
Cdd:pfam12697 1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSSSPPPLDLADL--ADLAALLDELGAArPVVLVGHSLGGAVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 139 MLLALqrpelVERLIAVDISPVeSTGVSHFATYVAAMRAINIADELPRSRARKLADEQLSSviqdmavrqhlltnlvEVD 218
Cdd:pfam12697 74 LAAAA-----AALVVGVLVAPL-AAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD----------------DLP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 219 GRFVWRVNLDALTQHLDKILAFPQRQESYLGPTLFLLGGNSQFVHPsHHPEIMRLFPRAQMQTVPNAGHWIHaDRPQDFI 298
Cdd:pfam12697 132 ADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPE-LAQRLLAALAGARLVVLPGAGHLPL-DDPEEVA 209
|
..
gi 1887096812 299 AA 300
Cdd:pfam12697 210 EA 211
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
52-305 |
4.29e-13 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 67.35 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 52 DGEAALPAVVFLHGLFGSKTN-FNSIAKILAQQtGRRVLTVDARNHGDSPHSPdmsYEIMSQDLQ---DLLPQLGLVP-- 125
Cdd:COG1506 18 ADGKKYPVVVYVHGGPGSRDDsFLPLAQALASR-GYAVLAPDYRGYGESAGDW---GGDEVDDVLaaiDYLAARPYVDpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 126 -CVVVGHSMGGKTAMLLALQRPELVERLIAVDispvestGVSHFATYVAAMRAIN-IADELPRSRARKLADeqlSSVIqd 203
Cdd:COG1506 94 rIGIYGHSYGGYMALLAAARHPDRFKAAVALA-------GVSDLRSYYGTTREYTeRLMGGPWEDPEAYAA---RSPL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 204 mavrqhlltnlvevdgrfvwrvnldaltQHLDKIlafpqrqesyLGPTLFLLGGNSQFVHPSHhpeIMRLF-------PR 276
Cdd:COG1506 162 ----------------------------AYADKL----------KTPLLLIHGEADDRVPPEQ---AERLYealkkagKP 200
|
250 260
....*....|....*....|....*....
gi 1887096812 277 AQMQTVPNAGHWIHADRPQDFIAAIRGFL 305
Cdd:COG1506 201 VELLVYPGEGHGFSGAGAPDYLERILDFL 229
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
53-305 |
9.38e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 68.05 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 53 GEAALPAVVFLHGLFGSKTN--FNsiakILAQQTGRRVLTVDARNHGDS-PHSPDMSYEIMSQDLQDLLPQLGLVPCVVV 129
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNwlFN----HAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 130 GHSMGGKTAMLLALQRPELVERLiavdiSPVESTGVShfatyvaamRAINIA--DELPRSRARKladeQLSSVIQDMAVR 207
Cdd:PRK14875 203 GHSMGGAVALRLAARAPQRVASL-----TLIAPAGLG---------PEINGDyiDGFVAAESRR----ELKPVLELLFAD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 208 QHLLTN-LVEVDGRFvwrVNLDALTQHLDKILA--FPQ-RQESYLG--------PTLFLLGGNSQFVhPSHHPEimRLFP 275
Cdd:PRK14875 265 PALVTRqMVEDLLKY---KRLDGVDDALRALADalFAGgRQRVDLRdrlaslaiPVLVIWGEQDRII-PAAHAQ--GLPD 338
|
250 260 270
....*....|....*....|....*....|
gi 1887096812 276 RAQMQTVPNAGHWIHADRPQDFIAAIRGFL 305
Cdd:PRK14875 339 GVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
59-293 |
4.99e-12 |
|
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: 64.54 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 59 AVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSP----HSPdmSYEIMSQDLQDLLPQL----GLVPCVVVG 130
Cdd:pfam12146 6 VVVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIreehPGLPLFLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 131 HSMGGKTAMLLALQRPELVERLI----AVDISPVESTGVSHFATYVAAMRAiniadelPRSRARKLADeqLSSVIQDMAV 206
Cdd:pfam12146 83 HSMGGLIAALYALRYPDKVDGLIlsapALKIKPYLAPPILKLLAKLLGKLF-------PRLRVPNNLL--PDSLSRDPEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 207 RQhLLTNLVEVDGRFVWRVNLDALtQHLDKILafpQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRA--QMQTVPN 284
Cdd:pfam12146 154 VA-AYAADPLVHGGISARTLYELL-DAGERLL---RRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPG 228
|
....*....
gi 1887096812 285 AGHWIHADR 293
Cdd:pfam12146 229 LYHELLNEP 237
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
52-305 |
4.53e-11 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 61.85 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSP--DMSYEImsQDLQDLLPQLGLVPCV-- 127
Cdd:COG1073 32 GASKKYPAVVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEGEPreEGSPER--RDARAAVDYLRTLPGVdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 128 ----VVGHSMGGKTAMLLALQRPelveRLIAVdispVESTGVSHFATyVAAMRAINIADE-------LPRSRARKLADEQ 196
Cdd:COG1073 109 erigLLGISLGGGYALNAAATDP----RVKAV----ILDSPFTSLED-LAAQRAKEARGAylpgvpyLPNVRLASLLNDE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 197 LSSViqdmavrqhlltnlvevdgrfvwrvnldaltQHLDKIlafpqrqesyLGPTLFLLGGNSQFvHPSHHPEimRLFPR 276
Cdd:COG1073 180 FDPL-------------------------------AKIEKI----------SRPLLFIHGEKDEA-VPFYMSE--DLYEA 215
|
250 260 270
....*....|....*....|....*....|....
gi 1887096812 277 A----QMQTVPNAGHWIHADRPQD-FIAAIRGFL 305
Cdd:COG1073 216 AaepkELLIVPGAGHVDLYDRPEEeYFDKLAEFF 249
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
58-144 |
1.26e-10 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 60.24 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 58 PAVVFLHGLFGSKTNFNSIAKILAQqtgRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKT 137
Cdd:PRK11126 3 PWLVFLHGLLGSGQDWQPVGEALPD---YPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79
|
....*..
gi 1887096812 138 AMLLALQ 144
Cdd:PRK11126 80 AMYYACQ 86
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
60-155 |
8.54e-09 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 52.52 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 60 VVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTA- 138
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLRAA-GYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVAr 83
|
90
....*....|....*...
gi 1887096812 139 -MLLALQRPELVERLIAV 155
Cdd:COG1075 84 yYLKRLGGAAKVARVVTL 101
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
52-148 |
1.03e-08 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 54.59 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 52 DGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVDARNHGDSPHSPDMSYEIMSQ--------DLQ---DLLPQ 120
Cdd:COG0412 24 AGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA-GYVVLAPDLYGRGGPGDDPDEARALMGAldpellaaDLRaalDWLKA 102
|
90 100 110
....*....|....*....|....*....|.
gi 1887096812 121 LGLV---PCVVVGHSMGGKTAMLLALQRPEL 148
Cdd:COG0412 103 QPEVdagRVGVVGFCFGGGLALLAAARGPDL 133
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
48-160 |
2.29e-07 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 48 YRLLDGEAALPAVVFLHG---LFGSKTNFNSIAKILAQQTGRRVLTVDARnhgdspHSPDMSYEIMSQDLQDLL------ 118
Cdd:COG0657 4 YRPAGAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR------LAPEHPFPAALEDAYAALrwlran 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1887096812 119 -PQLGLVP--CVVVGHSMGGKTAMLLALQRPELVERLIA--VDISPV 160
Cdd:COG0657 78 aAELGIDPdrIAVAGDSAGGHLAAALALRARDRGGPRPAaqVLIYPV 124
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
60-160 |
1.20e-06 |
|
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.
Pssm-ID: 369540 Cd Length: 233 Bit Score: 48.51 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 60 VVFLHGLFGSKTNFNSIAKILAQQtgRRVLTVDARNHGDSP---HSPDMSYEIMSQDLQDLLPQLGLV------------ 124
Cdd:pfam07819 7 VLFIPGNAGSYKQVRSIASVAANL--YQVLRKLLQNDNGFHldfFSVDFNEELSAFHGRTLLDQAEYLndairyilslya 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1887096812 125 -------PCVVVGHSMGGKTA---MLLALQRPELVERLIAVDiSPV 160
Cdd:pfam07819 85 sgrpgptSVILIGHSMGGIVAraaLTLPNYIPQSVNTIITLS-SPH 129
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
60-305 |
2.08e-06 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 49.08 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 60 VVFLHGLFGSKTNFNSIAKILAQQTgrRVLTVDARNHGDSP---------HSPDMSYEIMSQDLQDLLPQLGLVPCVVVG 130
Cdd:PLN02980 1374 VLFLHGFLGTGEDWIPIMKAISGSA--RCISIDLPGHGGSKiqnhaketqTEPTLSVELVADLLYKLIEHITPGKVTLVG 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 131 HSMGGKTAMLLALQRPELVERLIAVDISPVESTGVShfatyvaamRAINIADElpRSRARKLADEQLSSVIQDM------ 204
Cdd:PLN02980 1452 YSMGARIALYMALRFSDKIEGAVIISGSPGLKDEVA---------RKIRSAKD--DSRARMLIDHGLEIFLENWysgelw 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 205 -AVRQH---------------------LLTNLVEVDGRFVWRvNLDALTQHLdkILAFPQRQESY--LGPTLFLLGGNSQ 260
Cdd:PLN02980 1521 kSLRNHphfnkivasrllhkdvpslakLLSDLSIGRQPSLWE-DLKQCDTPL--LLVVGEKDVKFkqIAQKMYREIGKSK 1597
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1887096812 261 FVHPSHHPEIMrlfpraQMQTVPNAGHWIHADRPQDFIAAIRGFL 305
Cdd:PLN02980 1598 ESGNDKGKEII------EIVEIPNCGHAVHLENPLPVIRALRKFL 1636
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
45-155 |
3.11e-06 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 47.96 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 45 PLSYRLLDGEAALPAVVFLHGLFGSKTNF-NSIAKILAQQtGRRVLTVDARNHGDS-PHSP---DMSY-EIMSQD----- 113
Cdd:COG4757 19 PLAARLFPPAGPPRAVVLINPATGVPQRFyRPFARYLAER-GFAVLTYDYRGIGLSrPGSLrgfDAGYrDWGELDlpavl 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1887096812 114 --LQDLLPQLglvPCVVVGHSMGGKtaMLLALQRPELVERLIAV 155
Cdd:COG4757 98 daLRARFPGL---PLLLVGHSLGGQ--LLGLAPNAERVDRLVTV 136
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
41-146 |
1.80e-05 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 45.48 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 41 PRPLPLSYRL-------LDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVD-----------ARNHGDSPHS 102
Cdd:COG4188 39 DRPLPVDVWYpatapadAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASH-GYVVAAPDhpgsnaadlsaALDGLADALD 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1887096812 103 P--------DMSY-----EIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRP 146
Cdd:COG4188 118 PeelwerplDLSFvldqlLALNKSDPPLAGRLDLDRIGVIGHSLGGYTALALAGARL 174
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
114-155 |
2.23e-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: 214007 Cd Length: 309 Bit Score: 45.31 E-value: 2.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1887096812 114 LQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 155
Cdd:cd12808 180 YDALLDRVG--PCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| PRK10566 |
PRK10566 |
esterase; Provisional |
56-148 |
1.37e-04 |
|
esterase; Provisional
Pssm-ID: 182555 [Multi-domain] Cd Length: 249 Bit Score: 42.67 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 56 ALPAVVFLHGLFGSKTNFNSIAKILAqQTGRRVLTVDARNH-----GDSPHSPDMSYEIMSQDLQDL------LPQLGLV 124
Cdd:PRK10566 26 PLPTVFFYHGFTSSKLVYSYFAVALA-QAGFRVIMPDAPMHgarfsGDEARRLNHFWQILLQNMQEFptlraaIREEGWL 104
|
90 100
....*....|....*....|....*..
gi 1887096812 125 P---CVVVGHSMGGKTAMLLALQRPEL 148
Cdd:PRK10566 105 LddrLAVGGASMGGMTALGIMARHPWV 131
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
107-155 |
1.58e-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: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1887096812 107 YEIMSQD-LQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 155
Cdd:cd12809 155 QEALVRAaGCALLDIIG--PAILITHSQGGPFGWLAADARPDLVKAIVAI 202
|
|
| Chlorophyllase |
pfam07224 |
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ... |
39-171 |
7.21e-04 |
|
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.
Pssm-ID: 254111 Cd Length: 307 Bit Score: 40.59 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 39 AEPRPLPLSYRLLDGEaaLPAVVFLHGLFGSKTN----FNSIAK----ILAQQTGRRVLTVDARNHGDSPHSpdmSYEIM 110
Cdd:pfam07224 30 PPPKPLIIITPKEAGT--YPVVLFLHGTMLSNEFyslfFNHIAShgfiVVAPQLYRLFPPPSQQDEIDSAAE---VANWL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887096812 111 SQDLQDLLP---QLGLVPCVVVGHSMGGKTAMLLALQ-RPEL-VERLIAVDisPVESTGVS-----HFATY 171
Cdd:pfam07224 105 PLGLQVVLPtgvEANLSKLALSGHSRGGKTAFALALGySLDVtFSALIGVD--PVAGTSKDdrtdpHVLTY 173
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
53-154 |
2.41e-03 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 38.35 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 53 GEAALPAVVFLHGLFGSKTNFNSIAKILAQQtGRRVLTVdarnHGDSPHSPDM--------------------SYEIMSQ 112
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALP-GAAVLAP----RAPVPEGPGGrawfdlsflegredeeglaaAAEALAA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1887096812 113 DLQDLLPQLGLVPC--VVVGHSMGGKTAMLLALQRPELVERLIA 154
Cdd:COG0400 76 FIDELEARYGIDPEriVLAGFSQGAAMALSLALRRPELLAGVVA 119
|
|
| Lipase_3 |
pfam01764 |
Lipase (class 3); |
107-186 |
2.56e-03 |
|
Lipase (class 3);
Pssm-ID: 396362 [Multi-domain] Cd Length: 139 Bit Score: 37.63 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 107 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLAL----QRPELVERLIAVDI-SPveSTGVSHFATYVAAM------ 175
Cdd:pfam01764 46 REQVLAELKRLLEKYPDYSIVVTGHSLGGALASLAALdlveNGLRLSSRVTVVTFgQP--RVGNLEFAKLHDSQgpkfsy 123
|
90
....*....|.
gi 1887096812 176 RAINIADELPR 186
Cdd:pfam01764 124 RVVHQRDIVPR 134
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
51-155 |
2.69e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 39.12 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 51 LDGEAALPAVVFLHGLFGSK----TNFNSIAKILaqqtgrRVLTVDARNHGDSPHsPDMSYEIMSQ-------DLQDLLP 119
Cdd:PLN02894 99 FDSKEDAPTLVMVHGYGASQgfffRNFDALASRF------RVIAIDQLGWGGSSR-PDFTCKSTEEteawfidSFEEWRK 171
|
90 100 110
....*....|....*....|....*....|....*.
gi 1887096812 120 QLGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAV 155
Cdd:PLN02894 172 AKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILV 207
|
|
| Esterase_713 |
cd12807 |
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family ... |
112-155 |
4.11e-03 |
|
Novel bacterial esterase 713 that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (esterase 713) with the alpha/beta hydrolase fold that cleaves esters on halogenated cyclic compounds. This Alcaligenes esterase, however, does not contain the GXSXXG pentapeptide around the active site serine residue as seen in other esterase families. This enzyme is active as a dimer though its natural substrate is unknown. It has two distinct disulfide bridges; one formed between adjacent cysteines appears to facilitate the correct formation of the oxyanion cleft in the catalytic site. Esterase 713 also resembles human pancreatic lipase in its location of the acidic residue of the catalytic triad. It is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.
Pssm-ID: 214006 Cd Length: 315 Bit Score: 38.46 E-value: 4.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1887096812 112 QDLQDLLPQLGlvPCVVVGHSMGGKTAMLLALQRPELVERLIAV 155
Cdd:cd12807 179 NALAALADKLG--GAVLLGHSQSGPFPLEAALLRPAGVKGIVSV 220
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
124-154 |
4.92e-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: 37.83 E-value: 4.92e-03
10 20 30
....*....|....*....|....*....|.
gi 1887096812 124 VPCVVVGHSMGGKTAMLLALQRPELVERLIA 154
Cdd:pfam00756 110 DGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
45-148 |
6.41e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 37.25 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887096812 45 PLSYRLL-----DGEAALPAVVFLHGLFGSKTNfnsIAKILAQQTGRRVLTVDARNHGD---SPHSPDMSY---EIMSQD 113
Cdd:COG4099 32 TLPYRLYlpkgyDPGKKYPLVLFLHGAGERGTD---NEKQLTHGAPKFINPENQAKFPAivlAPQCPEDDYwsdTKALDA 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1887096812 114 LQDLLPQLglvpcV-----------VVGHSMGGKTAMLLALQRPEL 148
Cdd:COG4099 109 VLALLDDL-----IaeyridpdriyLTGLSMGGYGTWDLAARYPDL 149
|
|
| Lipase_3 |
cd00519 |
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ... |
107-157 |
9.71e-03 |
|
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: 36.69 E-value: 9.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1887096812 107 YEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALqrpELVERLIAVDI 157
Cdd:cd00519 111 YNQVLPELKSALKQYPDYKIIVTGHSLGGALASLLAL---DLRLRGPGSDV 158
|
|
| |
