|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
1-251 |
1.02e-35 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 131.96 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 1 MAAEEEEVDSADTEERSGWlTGWLP---TWCPTSTLHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTP 77
Cdd:PLN02894 14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSKVRWFRSASNEPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 78 LVLLHGFGGGLGLWAL---------------NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCA 141
Cdd:PLN02894 93 FINTVTFDSKEDAPTLvmvhgygasqgfffrNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 142 LGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLR 215
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622901727 216 IAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYH 251
Cdd:PLN02894 251 GLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYH 291
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
104-240 |
2.28e-18 |
|
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: 81.78 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 182
Cdd:pfam00561 30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622901727 183 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMF 240
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD 168
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
83-219 |
2.94e-14 |
|
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: 70.03 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 83 GFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAY 162
Cdd:COG0596 31 GLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALEL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622901727 163 SLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALgAALTPFNPLAGL-RIAGP 219
Cdd:COG0596 107 AARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALL-RALARTDLRERLaRITVP 163
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
103-197 |
1.28e-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: 45.70 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 103 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
|
90 100
....*....|....*....|..
gi 1622901727 179 WGFPERPDLADqDRPIP---VW 197
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
1-251 |
1.02e-35 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 131.96 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 1 MAAEEEEVDSADTEERSGWlTGWLP---TWCPTSTLHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTP 77
Cdd:PLN02894 14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGPPGSKVRWFRSASNEPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 78 LVLLHGFGGGLGLWAL---------------NFGDLCTNRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCA 141
Cdd:PLN02894 93 FINTVTFDSKEDAPTLvmvhgygasqgfffrNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 142 LGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLAD----QDRpiPVWIRALGAAL--TPFNPLAGLR 215
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSewltKFR--ATWKGAVLNHLweSNFTPQKIIR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622901727 216 IAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYH 251
Cdd:PLN02894 251 GLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYH 291
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
104-240 |
2.28e-18 |
|
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: 81.78 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWG-FP 182
Cdd:pfam00561 30 VIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDpPH 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622901727 183 ERPDLADQDRPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMF 240
Cdd:pfam00561 108 ELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD 168
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
83-219 |
2.94e-14 |
|
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: 70.03 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 83 GFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALGLDKMILLGHNLGGFLAAAY 162
Cdd:COG0596 31 GLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALEL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622901727 163 SLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALgAALTPFNPLAGL-RIAGP 219
Cdd:COG0596 107 AARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALL-RALARTDLRERLaRITVP 163
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
104-236 |
5.77e-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: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlgldKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:pfam12146 34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622901727 179 WgfperpdLADQDRPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 236
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
104-204 |
9.39e-13 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 65.79 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESIEewrcALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPW 179
Cdd:COG2267 58 VLAFDLRGHGRSDGPRghVDSFDDYVDdlRAALDALR----ARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA 133
|
90 100
....*....|....*....|....*.
gi 1622901727 180 gfperpDLADQDRPIPV-WIRALGAA 204
Cdd:COG2267 134 ------YRADPLLGPSArWLRALRLA 153
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
76-181 |
8.71e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 52.64 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 76 TPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALGLDKMILLGHNLG 155
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207
|
90 100
....*....|....*....|....*.
gi 1622901727 156 GFLAAAYSLKYPSRVNHLILVEPWGF 181
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
100-182 |
6.38e-07 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 50.19 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 100 TNRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---GLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV 176
Cdd:PLN03087 231 STYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305
|
....*.
gi 1622901727 177 EPWGFP 182
Cdd:PLN03087 306 APPYYP 311
|
|
| PLN02578 |
PLN02578 |
hydrolase |
91-180 |
2.03e-06 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 48.30 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 91 WALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLGLDKMILLGHNLGGFLAAAYSLKYPSRV 170
Cdd:PLN02578 102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177
|
90
....*....|
gi 1622901727 171 NHLILVEPWG 180
Cdd:PLN02578 178 AGVALLNSAG 187
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
104-220 |
4.06e-06 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 46.70 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlgldkmILLGHNLGGFLAAAYSlkyPSRVNHLILVEPWGFP 182
Cdd:pfam12697 24 VLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAAA---AAALVVGVLVAPLAAP 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622901727 183 erpdlADQDRPIPVWIRALGAALTPFNPLAGLRIAGPF 220
Cdd:pfam12697 94 -----PGLLAALLALLARLGAALAAPAWLAAESLARGF 126
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
103-197 |
1.28e-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: 45.70 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 103 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCALgLDKM---ILLGHNLGGFLAAAYSLKYPSRVNHLILVEP 178
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDAL-LDRVgpcIVVAHSQGGGFAFEAARARPDLVRAVVALEP 221
|
90 100
....*....|....*....|..
gi 1622901727 179 WGFPERPDLADqDRPIP---VW 197
Cdd:cd12808 222 SGAPDPAEAAP-LADVPhllVW 242
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
106-194 |
7.47e-05 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 43.44 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 106 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGF 181
Cdd:PRK03592 58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129
|
90
....*....|....
gi 1622901727 182 PER-PDLADQDRPI 194
Cdd:PRK03592 130 PMTwDDFPPAVREL 143
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
107-206 |
1.00e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 107 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILV------EPW 179
Cdd:COG0400 52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALsgylpgEEA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622901727 180 GFPERPDLA---------DQDRPIPV--------WIRALGAALT 206
Cdd:COG0400 130 LPAPEAALAgtpvflahgTQDPVIPVerareaaeALEAAGADVT 173
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
98-178 |
1.33e-04 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 42.95 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 98 LCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHnlGGFLAAA--YSLKYPSRVNHLIL 175
Cdd:PLN03084 150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227
|
...
gi 1622901727 176 VEP 178
Cdd:PLN03084 228 LNP 230
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
103-176 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622901727 103 PVYAFDLLGFGRSSRPRfdsdAEEVENQfvesIEEWRCALGLDKMILLGHNLGGFLAAAY--SLKYPSRVNHLILV 176
Cdd:COG1075 34 PVYALNYPSTNGSIEDS----AEQLAAF----VDAVLAATGAEKVDLVGHSMGGLVARYYlkRLGGAAKVARVVTL 101
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
97-176 |
6.09e-03 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 37.30 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 97 DLCTNRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalGLDKMILLGHNLGGFLAAAYSLKYPSRVNHL 173
Cdd:PRK10349 35 ELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVASQIALTHPERVQAL 102
|
...
gi 1622901727 174 ILV 176
Cdd:PRK10349 103 VTV 105
|
|
| PLN02385 |
PLN02385 |
hydrolase; alpha/beta fold family protein |
104-178 |
9.21e-03 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215216 [Multi-domain] Cd Length: 349 Bit Score: 37.04 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622901727 104 VYAFDLLGFGRSSR-----PRFDSDAEEVENQF--VESIEEWRcalGLDKMiLLGHNLGGFLAAAYSLKYPSRVNHLILV 176
Cdd:PLN02385 118 VFAMDYPGFGLSEGlhgyiPSFDDLVDDVIEHYskIKGNPEFR---GLPSF-LFGQSMGGAVALKVHLKQPNAWDGAILV 193
|
..
gi 1622901727 177 EP 178
Cdd:PLN02385 194 AP 195
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
91-118 |
9.71e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 37.13 E-value: 9.71e-03
10 20
....*....|....*....|....*...
gi 1622901727 91 WALNFGDLCTNRPVYAFDLLGFGRSSRP 118
Cdd:PLN02679 104 WRRNIGVLAKNYTVYAIDLLGFGASDKP 131
|
|
| |
