|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
1-470 |
0e+00 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 835.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 1 MGIARWLNRTVGFFVFALLDIADFLLCYTYKTLDYFLESERKPCYCSSPPEAKAKTEKIIVSERGGYSKVVSLTRSKIHF 80
Cdd:PLN03087 11 MGAGRALNEAVSFVVFSLLDILDFLLCFVYKVADYFFEAEWKPCYCSSAKEAIAASGKILVSERGGESKVVSLSSTKLHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 81 DEISDTLYSRgPSLLTRLSKL-VRSVKCFNYKGLImrgnvVESCDHHESKKKISKGKkRLMTLNSTVIEK---------S 150
Cdd:PLN03087 91 EEISDTLYTR-PSLLSDASKLtVNELKKLKMEGKC-----VGSCEKTSNKRKRGTKK-STLTVNSTIVEMlrgkiggqqL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 151 STAPRWSDCHCSFCTSWLTSTNrDSLFVKVQQPKDNKkARDNVVFIHGFVSSSAFWTETLFPNFSDSAKSNYRFIAVDLL 230
Cdd:PLN03087 164 HPAPRWSDCDCKFCTSWLSSSN-ESLFVHVQQPKDNK-AKEDVLFIHGFISSSAFWTETLFPNFSDAAKSTYRLFAVDLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 231 GYGRSPKPNDSLYTLREHLEMIEKSVISKFKLKTFHIVAHSLGCILALALAVKHPGAIKSLTLLAPPYYKVPKGVQPAQY 310
Cdd:PLN03087 242 GFGRSPKPADSLYTLREHLEMIERSVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAPPYYPVPKGVQATQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 311 VMREVARKEVWPPMQFGASVLSWYEHLGRTIGLVLIKNHQLIEFVTRLLTLNRMRTYLIEGFLCHTHNGSFHTLHNIIFG 390
Cdd:PLN03087 322 VMRKVAPRRVWPPIAFGASVACWYEHISRTICLVICKNHRLWEFLTRLLTRNRMRTFLIEGFFCHTHNAAWHTLHNIICG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 391 SGAKLDSYLDHVRDHVDCDVAIFHGGKDELIPVECSYSVKSKVPRATVHVIPDKDHITIVVGRQKDFARELELIWQRTKS 470
Cdd:PLN03087 402 SGSKLDGYLDHVRDQLKCDVAIFHGGDDELIPVECSYAVKAKVPRARVKVIDDKDHITIVVGRQKEFARELEEIWRRSSG 481
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
193-462 |
1.16e-24 |
|
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: 101.62 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtLFPNFSDsaksNYRFIAVDLLGYGRSPKPnDSLYTLREHLEMIEKsVISKFKLKTFHIVAHSL 272
Cdd:COG0596 26 VVLLHGLPGSSYEWRP-LIPALAA----GYRVIAPDLRGHGRSDKP-AGGYTLDDLADDLAA-LLDALGLERVVLVGHSM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 273 GCILALALAVKHPGAIKSLTLLAPpyykvpkgvqpaqyvMREVARKEVWPPMQFGASVLSWYEHLGRTiglvliknhqli 352
Cdd:COG0596 99 GGMVALELAARHPERVAGLVLVDE---------------VLAALAEPLRRPGLAPEALAALLRALART------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 353 EFVTRLltlnrmrtyliegflchthngsfhtlhniifgsgakldsyldhvrDHVDCDVAIFHGGKDELIPVECSYSVKSK 432
Cdd:COG0596 152 DLRERL---------------------------------------------ARITVPTLVIWGEKDPIVPPALARRLAEL 186
|
250 260 270
....*....|....*....|....*....|
gi 15238212 433 VPRATVHVIPDKDHiTIVVGRQKDFARELE 462
Cdd:COG0596 187 LPNAELVVLPGAGH-FPPLEQPEAFAAALR 215
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
193-452 |
2.19e-23 |
|
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: 98.73 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtLFPNFsdsAKSNYRFIAVDLLGYGRSPKP-NDSLYTLREHLEMIEKsVISKFKLKTFHIVAHS 271
Cdd:pfam00561 3 VLLLHGLPGSSDLWRK-LAPAL---ARDGFRVIALDLRGFGKSSRPkAQDDYRTDDLAEDLEY-ILEALGLEKVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 272 LGCILALALAVKHPGAIKSLTLLAPPYYKvpkgvqpaqYVMREVARkevwppmQFGASVLSWYE---------HLGRTIG 342
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVLLGALDPP---------HELDEADR-------FILALFPGFFDgfvadfapnPLGRLVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 343 --LVLIKNHQLIEFVTRLLTLNRMRTYLIEGFLCHThNGSFHTLHNIIFGSGAKLDSYldhvrdhvDCDVAIFHGGKDEL 420
Cdd:pfam00561 142 klLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVT-GALLFIETWSTELRAKFLGRL--------DEPTLIIWGDQDPL 212
|
250 260 270
....*....|....*....|....*....|..
gi 15238212 421 IPVECSYSVKSKVPRATVHVIPDKDHITIVVG 452
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEG 244
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
193-307 |
9.69e-04 |
|
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273783 [Multi-domain] Cd Length: 245 Bit Score: 40.96 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTETLfpnfsDSAKSNYRFIAVDLLGYGRSP--KPNDSLYTLREHLEMIEKSVIskfklktfhIVAH 270
Cdd:TIGR01738 7 LVLIHGWGMNAEVFRCLD-----EELSAHFTLHLVDLPGHGRSRgfGPLSLADMAEAIAAQAPDPAI---------WLGW 72
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15238212 271 SLGCILALALAVKHPGAIKSLTLLAP-PYYKV----PKGVQP 307
Cdd:TIGR01738 73 SLGGLVALHIAATHPDRVRALVTVASsPCFSAredwPEGIKP 114
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
1-470 |
0e+00 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 835.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 1 MGIARWLNRTVGFFVFALLDIADFLLCYTYKTLDYFLESERKPCYCSSPPEAKAKTEKIIVSERGGYSKVVSLTRSKIHF 80
Cdd:PLN03087 11 MGAGRALNEAVSFVVFSLLDILDFLLCFVYKVADYFFEAEWKPCYCSSAKEAIAASGKILVSERGGESKVVSLSSTKLHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 81 DEISDTLYSRgPSLLTRLSKL-VRSVKCFNYKGLImrgnvVESCDHHESKKKISKGKkRLMTLNSTVIEK---------S 150
Cdd:PLN03087 91 EEISDTLYTR-PSLLSDASKLtVNELKKLKMEGKC-----VGSCEKTSNKRKRGTKK-STLTVNSTIVEMlrgkiggqqL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 151 STAPRWSDCHCSFCTSWLTSTNrDSLFVKVQQPKDNKkARDNVVFIHGFVSSSAFWTETLFPNFSDSAKSNYRFIAVDLL 230
Cdd:PLN03087 164 HPAPRWSDCDCKFCTSWLSSSN-ESLFVHVQQPKDNK-AKEDVLFIHGFISSSAFWTETLFPNFSDAAKSTYRLFAVDLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 231 GYGRSPKPNDSLYTLREHLEMIEKSVISKFKLKTFHIVAHSLGCILALALAVKHPGAIKSLTLLAPPYYKVPKGVQPAQY 310
Cdd:PLN03087 242 GFGRSPKPADSLYTLREHLEMIERSVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAPPYYPVPKGVQATQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 311 VMREVARKEVWPPMQFGASVLSWYEHLGRTIGLVLIKNHQLIEFVTRLLTLNRMRTYLIEGFLCHTHNGSFHTLHNIIFG 390
Cdd:PLN03087 322 VMRKVAPRRVWPPIAFGASVACWYEHISRTICLVICKNHRLWEFLTRLLTRNRMRTFLIEGFFCHTHNAAWHTLHNIICG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 391 SGAKLDSYLDHVRDHVDCDVAIFHGGKDELIPVECSYSVKSKVPRATVHVIPDKDHITIVVGRQKDFARELELIWQRTKS 470
Cdd:PLN03087 402 SGSKLDGYLDHVRDQLKCDVAIFHGGDDELIPVECSYAVKAKVPRARVKVIDDKDHITIVVGRQKEFARELEEIWRRSSG 481
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
193-462 |
1.16e-24 |
|
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: 101.62 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtLFPNFSDsaksNYRFIAVDLLGYGRSPKPnDSLYTLREHLEMIEKsVISKFKLKTFHIVAHSL 272
Cdd:COG0596 26 VVLLHGLPGSSYEWRP-LIPALAA----GYRVIAPDLRGHGRSDKP-AGGYTLDDLADDLAA-LLDALGLERVVLVGHSM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 273 GCILALALAVKHPGAIKSLTLLAPpyykvpkgvqpaqyvMREVARKEVWPPMQFGASVLSWYEHLGRTiglvliknhqli 352
Cdd:COG0596 99 GGMVALELAARHPERVAGLVLVDE---------------VLAALAEPLRRPGLAPEALAALLRALART------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 353 EFVTRLltlnrmrtyliegflchthngsfhtlhniifgsgakldsyldhvrDHVDCDVAIFHGGKDELIPVECSYSVKSK 432
Cdd:COG0596 152 DLRERL---------------------------------------------ARITVPTLVIWGEKDPIVPPALARRLAEL 186
|
250 260 270
....*....|....*....|....*....|
gi 15238212 433 VPRATVHVIPDKDHiTIVVGRQKDFARELE 462
Cdd:COG0596 187 LPNAELVVLPGAGH-FPPLEQPEAFAAALR 215
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
193-452 |
2.19e-23 |
|
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: 98.73 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtLFPNFsdsAKSNYRFIAVDLLGYGRSPKP-NDSLYTLREHLEMIEKsVISKFKLKTFHIVAHS 271
Cdd:pfam00561 3 VLLLHGLPGSSDLWRK-LAPAL---ARDGFRVIALDLRGFGKSSRPkAQDDYRTDDLAEDLEY-ILEALGLEKVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 272 LGCILALALAVKHPGAIKSLTLLAPPYYKvpkgvqpaqYVMREVARkevwppmQFGASVLSWYE---------HLGRTIG 342
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVLLGALDPP---------HELDEADR-------FILALFPGFFDgfvadfapnPLGRLVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 343 --LVLIKNHQLIEFVTRLLTLNRMRTYLIEGFLCHThNGSFHTLHNIIFGSGAKLDSYldhvrdhvDCDVAIFHGGKDEL 420
Cdd:pfam00561 142 klLALLLLRLRLLKALPLLNKRFPSGDYALAKSLVT-GALLFIETWSTELRAKFLGRL--------DEPTLIIWGDQDPL 212
|
250 260 270
....*....|....*....|....*....|..
gi 15238212 421 IPVECSYSVKSKVPRATVHVIPDKDHITIVVG 452
Cdd:pfam00561 213 VPPQALEKLAQLFPNARLVVIPDAGHFAFLEG 244
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
165-311 |
4.30e-16 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 76.96 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 165 TSWLTSTNRDSLFVKVQQPKDnkKARDNVVFIHGFVSSSAFWTEtLFPNFsdsAKSNYRFIAVDLLGYGRSPKPN---DS 241
Cdd:COG2267 5 LVTLPTRDGLRLRGRRWRPAG--SPRGTVVLVHGLGEHSGRYAE-LAEAL---AAAGYAVLAFDLRGHGRSDGPRghvDS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 242 LYTLREHLEMIEKSVISKFKLKTFhIVAHSLGCILALALAVKHPGAIKSLTLLAPPYYKVPKGVQPAQYV 311
Cdd:COG2267 79 FDDYVDDLRAALDALRARPGLPVV-LLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL 147
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
193-446 |
4.42e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.44 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWtetLFpNFSDSAkSNYRFIAVDLLGYGRSPKPNDslytlREHLEMIEKSVI---SKFKLKTFHIVA 269
Cdd:PRK14875 134 VVLIHGFGGDLNNW---LF-NHAALA-AGRPVIALDLPGHGASSKAVG-----AGSLDELAAAVLaflDALGIERAHLVG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 270 HSLGCILALALAVKHPGAIKSLTLLAppyykvPKGVQP---AQYVMREVA---RKEVWPpmqfgasvlsWYEHLGRTIGL 343
Cdd:PRK14875 204 HSMGGAVALRLAARAPQRVASLTLIA------PAGLGPeinGDYIDGFVAaesRRELKP----------VLELLFADPAL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 344 VlikNHQLIEFVTRLLTLNRMRTYLiegflchthngsfHTLHNIIFGSGAKLDSYLDHVRDHvDCDVAIFHGGKDELIPV 423
Cdd:PRK14875 268 V---TRQMVEDLLKYKRLDGVDDAL-------------RALADALFAGGRQRVDLRDRLASL-AIPVLVIWGEQDRIIPA 330
|
250 260
....*....|....*....|...
gi 15238212 424 ECSYSVKskvPRATVHVIPDKDH 446
Cdd:PRK14875 331 AHAQGLP---DGVAVHVLPGAGH 350
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
184-456 |
3.29e-12 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 66.12 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 184 KDNKKArdnVVFIHGFVSSSA---FWTETLfpnfsdsAKSNYRFIAVDLLGYGRSP------KPNDSLYTLREHLEMIEK 254
Cdd:COG1647 12 EGGRKG---VLLLHGFTGSPAemrPLAEAL-------AKAGYTVYAPRLPGHGTSPedllktTWEDWLEDVEEAYEILKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 255 SViskfklKTFHIVAHSLGCILALALAVKHPgAIKSLTLLAPPYYkvpkgvqpaqyvmrevarkeVWPPMQFGASVLSWy 334
Cdd:COG1647 82 GY------DKVIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALK--------------------IDDPSAPLLPLLKY- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 335 ehlgrtiglvliknhqliefVTRLLTLNRMRTYLIEGFLCHTHNGSFHTLHNiifgsgakLDSYLDHVR---DHVDCDVA 411
Cdd:COG1647 134 --------------------LARSLRGIGSDIEDPEVAEYAYDRTPLRALAE--------LQRLIREVRrdlPKITAPTL 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15238212 412 IFHGGKDELIPVECSYSVKSKV--PRATVHVIPDKDHItIVVGRQKD 456
Cdd:COG1647 186 IIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHV-ITLDKDRE 231
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
193-331 |
1.17e-11 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 64.03 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFwtetlfpnFSDSAKSNYRFIAVDLLGYGRSPKPNDSLYTLREHLEMIEKSVISkfklKTFHIVAHSL 272
Cdd:pfam12697 1 VVLVHGAGLSAAP--------LAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAA----RPVVLVGHSL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15238212 273 GCILALALAvkhPGAIKSLTLLAPPYYKVPKGVQPAQYVMR--EVARKEVWPPMQFGASVL 331
Cdd:pfam12697 69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARlgAALAAPAWLAAESLARGF 126
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
165-296 |
6.60e-11 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 63.78 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 165 TSWLTSTNRDSLFVKVQQpKDNKKARDNVVFIHGFVSSSAFWtetlFPNFsDSAKSNYRFIAVDLLGYGRSPKPNdslYT 244
Cdd:PLN02894 81 VRWFRSASNEPRFINTVT-FDSKEDAPTLVMVHGYGASQGFF----FRNF-DALASRFRVIAIDQLGWGGSSRPD---FT 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15238212 245 LREHlEMIEKSVISKFK-------LKTFHIVAHSLGCILALALAVKHPGAIKSLTLLAP 296
Cdd:PLN02894 152 CKST-EETEAWFIDSFEewrkaknLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGP 209
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
191-297 |
3.87e-10 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 60.78 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 191 DNVVFIHGFVSSSAFWtETLFPNFSDSAksnyRFIAVDLLGYGRSPKPNDSlYTLREHLEMIEKsVISKFKLKTFHIVAH 270
Cdd:PRK03592 28 DPIVFLHGNPTSSYLW-RNIIPHLAGLG----RCLAPDLIGMGASDKPDID-YTFADHARYLDA-WFDALGLDDVVLVGH 100
|
90 100 110
....*....|....*....|....*....|.
gi 15238212 271 SLGCILALALAVKHPGAIKSL----TLLAPP 297
Cdd:PRK03592 101 DWGSALGFDWAARHPDRVRGIafmeAIVRPM 131
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
187-299 |
2.00e-09 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 54.84 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 187 KKARDNVVFIHGFVSSSAFWtETLFPNFsdsAKSNYRFIAVDLLGYGRSPkpNDSLYTLREHLEmiekSVISKFKLKTFH 266
Cdd:COG1075 2 AATRYPVVLVHGLGGSAASW-APLAPRL---RAAGYPVYALNYPSTNGSI--EDSAEQLAAFVD----AVLAATGAEKVD 71
|
90 100 110
....*....|....*....|....*....|....*
gi 15238212 267 IVAHSLGCILALALAVKHPGA--IKSLTLLAPPYY 299
Cdd:COG1075 72 LVGHSMGGLVARYYLKRLGGAakVARVVTLGTPHH 106
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
193-297 |
1.09e-08 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 56.81 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFvSSSAFWTETLFPNFSDsaksNYRFIAVDLLGYGRSPKP---NDSLYTLREHLEMIEkSVISKFKLKTFHIVA 269
Cdd:PLN03084 130 VLLIHGF-PSQAYSYRKVLPVLSK----NYHAIAFDWLGFGFSDKPqpgYGFNYTLDEYVSSLE-SLIDELKSDKVSLVV 203
|
90 100
....*....|....*....|....*...
gi 15238212 270 HSLGCILALALAVKHPGAIKSLTLLAPP 297
Cdd:PLN03084 204 QGYFSPPVVKYASAHPDKIKKLILLNPP 231
|
|
| YdeN |
COG3545 |
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; |
236-298 |
7.73e-08 |
|
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
Pssm-ID: 442766 [Multi-domain] Cd Length: 170 Bit Score: 51.78 E-value: 7.73e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238212 236 PKPNDSLYTLREHLEMIEKSVIskfklktfhIVAHSLGCILALALAVKHPGAIKSLTLLAPPY 298
Cdd:COG3545 36 PDLDDWLAALDAAVAAADGPVV---------LVAHSLGCLAVAHWAARLPRKVAGALLVAPPD 89
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
193-294 |
3.07e-07 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 52.05 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtlfpNFSDSAKSnYRFIAVDLLGYGRSPKPN------DSLYTLREHLEMIEKSVISKFKLKTFh 266
Cdd:PLN02824 32 LVLVHGFGGNADHWRK----NTPVLAKS-HRVYAIDLLGYGYSDKPNprsappNSFYTFETWGEQLNDFCSDVVGDPAF- 105
|
90 100
....*....|....*....|....*...
gi 15238212 267 IVAHSLGCILALALAVKHPGAIKSLTLL 294
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLI 133
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
193-332 |
3.31e-07 |
|
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: 51.06 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAfWTETLFPNFsdsAKSNYRFIAVDLLGYGRSPK-----PNDSLYT--LREHLEMIeksvISKFKLKTF 265
Cdd:pfam12146 7 VVLVHGLGEHSG-RYAHLADAL---AAQGFAVYAYDHRGHGRSDGkrghvPSFDDYVddLDTFVDKI----REEHPGLPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15238212 266 HIVAHSLGCILALALAVKHPGAIKSLTLLAPPYYKVPKGVQPAQYVMREVARKeVWPPMQFGASVLS 332
Cdd:pfam12146 79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGK-LFPRLRVPNNLLP 144
|
|
| Ser_hydrolase |
pfam06821 |
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ... |
236-297 |
1.47e-05 |
|
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a conserved serine hydrolase motif, GXSXG/A, where the serine is a putative nucleophile. This family has an alpha-beta hydrolase fold. Eukaryotic members of this family have a conserved LXCXE motif, which binds to retinoblastomas. This motif is absent from prokaryotic members of this family.
Pssm-ID: 399658 [Multi-domain] Cd Length: 171 Bit Score: 45.40 E-value: 1.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238212 236 PKPNDSLYTLREHLEMIEKSVIskfklktfhIVAHSLGCIL-ALALAVKHPGAIKSLTLLAPP 297
Cdd:pfam06821 37 PVLDDWVAALSRAVAALPGPVI---------LVAHSLGCLAvAHWAALQLRAKVAGALLVAPA 90
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
218-285 |
1.99e-05 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 46.50 E-value: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238212 218 AKSNYRFIAVDLLGYGRSPKP-NDSLYTLREHLEMIeKSVISKFKLKTFHIVAHSLGCILALALAVKHP 285
Cdd:PRK00870 70 AAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWM-RSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHP 137
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
193-294 |
1.30e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 44.06 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtlfpNFSDSAKsNYRFIAVDLLGYGRSPKPNDSLYTLREHLEMIE---KSVISKFKLKTFHIVA 269
Cdd:PLN02679 91 VLLVHGFGASIPHWRR----NIGVLAK-NYTVYAIDLLGFGASDKPPGFSYTMETWAELILdflEEVVQKPTVLIGNSVG 165
|
90 100
....*....|....*....|....*
gi 15238212 270 hSLGCILALALAvkHPGAIKSLTLL 294
Cdd:PLN02679 166 -SLACVIAASES--TRDLVRGLVLL 187
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
175-289 |
2.17e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 44.08 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 175 SLFVKVQQPKDNkkARDNVV-FIHGFVSSSAFWTETLfPNFSDSAksnyRFIAVDLLGYGRSPKPNDSLYTLREHLEMIE 253
Cdd:PLN02980 1357 SCLIKVHEVGQN--AEGSVVlFLHGFLGTGEDWIPIM-KAISGSA----RCISIDLPGHGGSKIQNHAKETQTEPTLSVE 1429
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15238212 254 ksVISKFKLKTFH--------IVAHSLGCILALALAVKHPGAIK 289
Cdd:PLN02980 1430 --LVADLLYKLIEhitpgkvtLVGYSMGARIALYMALRFSDKIE 1471
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
183-298 |
2.35e-04 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 42.70 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 183 PKDNKKARDnVVFIHGFVSSSAFWTETLFPNFsdsAKSNYRFIAVDLLGYGRSPKpNDSLYTLREHL----EMIEKSVIS 258
Cdd:COG1506 17 PADGKKYPV-VVYVHGGPGSRDDSFLPLAQAL---ASRGYAVLAPDYRGYGESAG-DWGGDEVDDVLaaidYLAARPYVD 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15238212 259 KFKLktfHIVAHSLGCILALALAVKHPGAIKSLTLLAPPY 298
Cdd:COG1506 92 PDRI---GIYGHSYGGYMALLAAARHPDRFKAAVALAGVS 128
|
|
| COG4782 |
COG4782 |
Esterase/lipase superfamily enzyme [General function prediction only]; |
172-296 |
3.78e-04 |
|
Esterase/lipase superfamily enzyme [General function prediction only];
Pssm-ID: 443812 Cd Length: 357 Bit Score: 42.64 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 172 NRDSLFVKVQQPKDNKKARDNVVFIHGFVSSsafwtetlfpnFSDSAksnYRF--IAVDL-----------------LGY 232
Cdd:COG4782 105 DEAAFLAALAAALAASGKREVLVFVHGFNTS-----------FEDAV---YRAaqIVHDLgfpgvpvlfswpsrgslLGY 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238212 233 GRSpkpNDSLYTLREHLE-MIEKsVISKFKLKTFHIVAHSLGCILAL----ALAVKHPGA----IKSLTLLAP 296
Cdd:COG4782 171 VYD---RESATYSRDALEeLLRD-LARDPGAERIHIVAHSMGNWLTMealrQLAIRGRGRvlrkIGQVVLAAP 239
|
|
| PLN02578 |
PLN02578 |
hydrolase |
193-296 |
4.02e-04 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 42.52 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTEtlfpNFSDSAKSnYRFIAVDLLGYGRSPKpndslyTLREHLEMIEKSVISKFKLKTFH----IV 268
Cdd:PLN02578 89 IVLIHGFGASAFHWRY----NIPELAKK-YKVYALDLLGFGWSDK------ALIEYDAMVWRDQVADFVKEVVKepavLV 157
|
90 100
....*....|....*....|....*...
gi 15238212 269 AHSLGCILALALAVKHPGAIKSLTLLAP 296
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNS 185
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
193-307 |
9.69e-04 |
|
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273783 [Multi-domain] Cd Length: 245 Bit Score: 40.96 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238212 193 VVFIHGFVSSSAFWTETLfpnfsDSAKSNYRFIAVDLLGYGRSP--KPNDSLYTLREHLEMIEKSVIskfklktfhIVAH 270
Cdd:TIGR01738 7 LVLIHGWGMNAEVFRCLD-----EELSAHFTLHLVDLPGHGRSRgfGPLSLADMAEAIAAQAPDPAI---------WLGW 72
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15238212 271 SLGCILALALAVKHPGAIKSLTLLAP-PYYKV----PKGVQP 307
Cdd:TIGR01738 73 SLGGLVALHIAATHPDRVRALVTVASsPCFSAredwPEGIKP 114
|
|
| |
