|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
53-304 |
9.02e-44 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 154.30 E-value: 9.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 53 NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNH 131
Cdd:PLN02894 124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 132 LILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 200
Cdd:PLN02894 204 LILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 201 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGkmHPDIPVSVIFGARSCIDGNSGtsiQSLRPHSYV--KT 278
Cdd:PLN02894 282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMNYEGA---VEARKRMKVpcEI 356
|
250 260
....*....|....*....|....*.
gi 1475409105 279 IAILGAGHYVYADQPEEFNQKVKEIC 304
Cdd:PLN02894 357 IRVPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
63-293 |
7.53e-21 |
|
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: 89.49 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 63 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 141
Cdd:pfam00561 30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 142 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtvteyiyhcnVQTPSG 218
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD-------------YALAKS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409105 219 ETAFKNMTIPYgWAKRPMLQRIGKmhPDIPVSVIFGARSCIDGNSGT-SIQSLRPHSYVKTIAilGAGHYVYADQP 293
Cdd:pfam00561 175 LVTGALLFIET-WSTELRAKFLGR--LDEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--DAGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
50-302 |
6.68e-19 |
|
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: 83.51 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 50 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 130 NHLILVepwgfperpdladqdrpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 209
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 210 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgkmhpDIPVSVIFGARS-CIDGNSGTSIQSLRPHSYVKTIAilGAGHYV 288
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 1475409105 289 YADQPEEFNQKVKE 302
Cdd:COG0596 203 PLEQPEAFAAALRD 216
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
62-156 |
1.40e-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: 46.08 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 62 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 137
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
|
90 100
....*....|....*....|..
gi 1475409105 138 WGFPERPDLADqDRPIP---VW 156
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
53-304 |
9.02e-44 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 154.30 E-value: 9.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 53 NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNH 131
Cdd:PLN02894 124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 132 LILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 200
Cdd:PLN02894 204 LILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 201 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGkmHPDIPVSVIFGARSCIDGNSGtsiQSLRPHSYV--KT 278
Cdd:PLN02894 282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMNYEGA---VEARKRMKVpcEI 356
|
250 260
....*....|....*....|....*.
gi 1475409105 279 IAILGAGHYVYADQPEEFNQKVKEIC 304
Cdd:PLN02894 357 IRVPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
63-293 |
7.53e-21 |
|
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: 89.49 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 63 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 141
Cdd:pfam00561 30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 142 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtvteyiyhcnVQTPSG 218
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD-------------YALAKS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409105 219 ETAFKNMTIPYgWAKRPMLQRIGKmhPDIPVSVIFGARSCIDGNSGT-SIQSLRPHSYVKTIAilGAGHYVYADQP 293
Cdd:pfam00561 175 LVTGALLFIET-WSTELRAKFLGR--LDEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--DAGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
50-302 |
6.68e-19 |
|
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: 83.51 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 50 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 130 NHLILVepwgfperpdladqdrpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 209
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 210 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgkmhpDIPVSVIFGARS-CIDGNSGTSIQSLRPHSYVKTIAilGAGHYV 288
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 1475409105 289 YADQPEEFNQKVKE 302
Cdd:COG0596 203 PLEQPEAFAAALRD 216
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
63-195 |
8.11e-13 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 66.85 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 63 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlgldKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 137
Cdd:pfam12146 34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1475409105 138 WgfperpdLADQDRPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 195
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
63-163 |
1.81e-12 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 65.41 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 63 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESIEewrcALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPW 138
Cdd:COG2267 58 VLAFDLRGHGRSDGPRghVDSFDDYVDdlRAALDALR----ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
|
90 100
....*....|....*....|....*.
gi 1475409105 139 gfperpDLADQDRPIPV-WIRALGAA 163
Cdd:COG2267 134 ------YRADPLLGPSArWLRALRLA 153
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
35-140 |
9.59e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 52.64 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 35 TPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALGLDKMILLGHNLG 114
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207
|
90 100
....*....|....*....|....*.
gi 1475409105 115 GFLAAAYSLKYPSRVNHLILVEPWGF 140
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
63-298 |
5.57e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 49.39 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 63 VYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlgldkmILLGHNLGGFLAAAYSlkyPSRVNHLILVEPWGFP 141
Cdd:pfam12697 24 VLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAAA---AAALVVGVLVAPLAAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 142 erpdlADQDRPIPVWIRALGAALtpfnplaglriaGPFGLSLVQRLRPDFKrkyssmfeDDTVTEYIYHCNVQTPSGETA 221
Cdd:pfam12697 94 -----PGLLAALLALLARLGAAL------------AAPAWLAAESLARGFL--------DDLPADAEWAAALARLAALLA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475409105 222 FKNMTIPYGWakrpmlqrigkmhPDIPVSVIFGARSciDGNSGTSIQ-SLRPHSYVKTIAILGAGHYVYaDQPEEFNQ 298
Cdd:pfam12697 149 ALALLPLAAW-------------RDLPVPVLVLAEE--DRLVPELAQrLLAALAGARLVVLPGAGHLPL-DDPEEVAE 210
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
59-141 |
9.10e-07 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 49.81 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 59 TNRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---GLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV 135
Cdd:PLN03087 231 STYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305
|
....*.
gi 1475409105 136 EPWGFP 141
Cdd:PLN03087 306 APPYYP 311
|
|
| PLN02578 |
PLN02578 |
hydrolase |
50-139 |
1.71e-06 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 49.07 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 50 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLGLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:PLN02578 102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177
|
90
....*....|
gi 1475409105 130 NHLILVEPWG 139
Cdd:PLN02578 178 AGVALLNSAG 187
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
62-156 |
1.40e-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: 46.08 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 62 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 137
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
|
90 100
....*....|....*....|..
gi 1475409105 138 WGFPERPDLADqDRPIP---VW 156
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
65-153 |
6.12e-05 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 43.83 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 65 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGF 140
Cdd:PRK03592 58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129
|
90
....*....|....
gi 1475409105 141 PER-PDLADQDRPI 153
Cdd:PRK03592 130 PMTwDDFPPAVREL 143
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
66-165 |
1.18e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 66 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV------EPW 138
Cdd:COG0400 52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALsgylpgEEA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1475409105 139 GFPERPDLA---------DQDRPIPV--------WIRALGAALT 165
Cdd:COG0400 130 LPAPEAALAgtpvflahgTQDPVIPVerareaaeALEAAGADVT 173
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
57-137 |
1.67e-04 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 42.95 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 57 LCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHnlGGFLAAA--YSLKYPSRVNHLIL 134
Cdd:PLN03084 150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227
|
...
gi 1475409105 135 VEP 137
Cdd:PLN03084 228 LNP 230
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
62-135 |
1.78e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 40.20 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409105 62 PVYAFDLLGFGRSSRPRfdsdAEEVENQfvesIEEWRCALGLDKMILLGHNLGGFLAAAY--SLKYPSRVNHLILV 135
Cdd:COG1075 34 PVYALNYPSTNGSIEDS----AEQLAAF----VDAVLAATGAEKVDLVGHSMGGLVARYYlkRLGGAAKVARVVTL 101
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
50-135 |
5.80e-03 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 37.69 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409105 50 WALNFG-------DLCTNRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalGLDKMILLGHNLGGFLAA 119
Cdd:PRK10349 22 WGLNAEvwrcideELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVAS 89
|
90
....*....|....*.
gi 1475409105 120 AYSLKYPSRVNHLILV 135
Cdd:PRK10349 90 QIALTHPERVQALVTV 105
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