|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
53-304 |
2.86e-43 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 152.76 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 53 NFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSH 131
Cdd:PLN02894 124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 132 LILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 200
Cdd:PLN02894 204 LILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 201 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIPVSVIFGARSCIDgNSGTSIQSLRPKSYVKTIA 280
Cdd:PLN02894 282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIR 358
|
250 260
....*....|....*....|....
gi 564366316 281 ILGAGHYVYADQPEEFNQKVKEIC 304
Cdd:PLN02894 359 VPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
50-293 |
1.36e-19 |
|
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: 86.02 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 128
Cdd:pfam00561 16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 129 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 204
Cdd:pfam00561 94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 205 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 283
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235
|
250
....*....|
gi 564366316 284 AGHYVYADQP 293
Cdd:pfam00561 236 AGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
50-302 |
6.82e-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: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 130 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 209
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 210 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 288
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 564366316 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 |
3.76e-06 |
|
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: 47.62 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 62 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 138
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222
|
90 100
....*....|....*....|.
gi 564366316 139 GFPERPDLADqERPIP---VW 156
Cdd:cd12808 223 GAPDPAEAAP-LADVPhllVW 242
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
53-304 |
2.86e-43 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 152.76 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 53 NFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSH 131
Cdd:PLN02894 124 NFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 132 LILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYS-----SMFE 200
Cdd:PLN02894 204 LILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKIIRGLGPWGPNLVRRYTTARFGAHStgdilSEEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 201 DDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIPVSVIFGARSCIDgNSGTSIQSLRPKSYVKTIA 280
Cdd:PLN02894 282 SKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVPTTFIYGRHDWMN-YEGAVEARKRMKVPCEIIR 358
|
250 260
....*....|....*....|....
gi 564366316 281 ILGAGHYVYADQPEEFNQKVKEIC 304
Cdd:PLN02894 359 VPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
50-293 |
1.36e-19 |
|
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: 86.02 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 128
Cdd:pfam00561 16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 129 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 204
Cdd:pfam00561 94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 205 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 283
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235
|
250
....*....|
gi 564366316 284 AGHYVYADQP 293
Cdd:pfam00561 236 AGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
50-302 |
6.82e-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: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 130 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 209
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 210 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 288
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 564366316 289 YADQPEEFNQKVKE 302
Cdd:COG0596 203 PLEQPEAFAAALRD 216
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
63-163 |
5.02e-13 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 66.95 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 63 VYAFDLLGFGRSSRPRFDSDAEEvenQFVESIEEWRCALRLD---KMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWg 139
Cdd:COG2267 58 VLAFDLRGHGRSDGPRGHVDSFD---DYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA- 133
|
90 100
....*....|....*....|....*
gi 564366316 140 fperpDLADQERPIPV-WIRALGAA 163
Cdd:COG2267 134 -----YRADPLLGPSArWLRALRLA 153
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
63-195 |
1.29e-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: 66.08 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 63 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlrldKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEP 137
Cdd:pfam12146 34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564366316 138 WgfperpdLADQERPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 195
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
35-140 |
1.17e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 55.72 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 35 TPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALRLDKMILLGHNLG 114
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207
|
90 100
....*....|....*....|....*.
gi 564366316 115 GFLAAAYSLKYPSRVSHLILVEPWGF 140
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
|
|
| PLN02578 |
PLN02578 |
hydrolase |
50-139 |
3.22e-07 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 50.99 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLRLDKMILLGHNLGGFLAAAYSLKYPSRV 129
Cdd:PLN02578 102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177
|
90
....*....|
gi 564366316 130 SHLILVEPWG 139
Cdd:PLN02578 178 AGVALLNSAG 187
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
57-298 |
4.05e-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: 49.78 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 57 LSTDRPVYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlrldkmILLGHNLGGFLAAAYSlkyPSRVSHLILV 135
Cdd:pfam12697 18 LAAGVAVLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAAA---AAALVVGVLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 136 EPWGFPerpdlADQERPIPVWIRALGAALtpfnplaglriaGPFGLSLVQRLRPDFKrkyssmfeDDTVTEYIYHCNVQT 215
Cdd:pfam12697 88 APLAAP-----PGLLAALLALLARLGAAL------------AAPAWLAAESLARGFL--------DDLPADAEWAAALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 216 PSGETAFKNMTIPYGWakrpmlqrigglhPDIPVSVIFGARSciDGNSGTSIQ-SLRPKSYVKTIAILGAGHYVYaDQPE 294
Cdd:pfam12697 143 LAALLAALALLPLAAW-------------RDLPVPVLVLAEE--DRLVPELAQrLLAALAGARLVVLPGAGHLPL-DDPE 206
|
....
gi 564366316 295 EFNQ 298
Cdd:pfam12697 207 EVAE 210
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
53-141 |
1.19e-06 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 49.81 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 53 NFEDLS-TDRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---RLDKMILLGHNLGGFLAAAYSLKYPSR 128
Cdd:PLN03087 224 NFSDAAkSTYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGA 298
|
90
....*....|...
gi 564366316 129 VSHLILVEPWGFP 141
Cdd:PLN03087 299 VKSLTLLAPPYYP 311
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
62-156 |
3.76e-06 |
|
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: 47.62 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 62 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 138
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222
|
90 100
....*....|....*....|.
gi 564366316 139 GFPERPDLADqERPIP---VW 156
Cdd:cd12808 223 GAPDPAEAAP-LADVPhllVW 242
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
57-137 |
8.26e-05 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 43.72 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 57 LSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHnlGGFLAAA--YSLKYPSRVSHLIL 134
Cdd:PLN03084 150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227
|
...
gi 564366316 135 VEP 137
Cdd:PLN03084 228 LNP 230
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
50-135 |
3.63e-04 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 41.16 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 50 WALNF-------EDLSTDRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalRLDKMILLGHNLGGFLAA 119
Cdd:PRK10349 22 WGLNAevwrcidEELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVAS 89
|
90
....*....|....*.
gi 564366316 120 AYSLKYPSRVSHLILV 135
Cdd:PRK10349 90 QIALTHPERVQALVTV 105
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
66-157 |
6.02e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 40.28 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 66 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPwGFPERP 144
Cdd:COG0400 52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSG-YLPGEE 128
|
90
....*....|....*.
gi 564366316 145 DLADQE---RPIPVWI 157
Cdd:COG0400 129 ALPAPEaalAGTPVFL 144
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
65-153 |
1.93e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 39.21 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 65 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGF 140
Cdd:PRK03592 58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129
|
90
....*....|....
gi 564366316 141 PER-PDLADQERPI 153
Cdd:PRK03592 130 PMTwDDFPPAVREL 143
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
57-188 |
2.33e-03 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 39.69 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 57 LSTDRPVYAFDLLGFGRSSRPrfdsdaeevenqfVESIEEwRCALRLDKM---------ILLGHNLGGFLA--AAYSLKy 125
Cdd:COG3319 624 LGPDRPVYGLQAPGLDGGEPP-------------PASVEE-MAARYVEAIravqpegpyHLLGWSFGGLVAyeMARQLE- 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564366316 126 pSR---VSHLILVEPWGfPERPDLADQERPIPVWIRALGAALTPFNPLAGLRiagpfGLSLVQRLR 188
Cdd:COG3319 689 -AQgeeVALLVLLDSYA-PGALARLDEAELLAALLRDLARGVDLPLDAEELR-----ALDPEERLA 747
|
|
| PRK10673 |
PRK10673 |
esterase; |
56-136 |
9.77e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 37.02 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366316 56 DLSTDRPVYAFDLLGFGRSSR-PRFDSDAeeVENQFVESIEEwrcaLRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLIL 134
Cdd:PRK10673 38 DLVNDHDIIQVDMRNHGLSPRdPVMNYPA--MAQDLLDTLDA----LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVA 111
|
..
gi 564366316 135 VE 136
Cdd:PRK10673 112 ID 113
|
|
|