|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02211 |
PLN02211 |
methyl indole-3-acetate methyltransferase |
2-259 |
4.19e-47 |
|
methyl indole-3-acetate methyltransferase
Pssm-ID: 215128 Cd Length: 273 Bit Score: 157.74 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 2 EKNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILV 81
Cdd:PLN02211 14 PNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSL-PENEKVILV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 82 AHSMGGIPAALASDIFPSKIATIVFLTAFMpdtRNLPAYVYQKLIRSVPQEGWLDTV----FGTyGKHECPLEfALFGPK 157
Cdd:PLN02211 93 GHSAGGLSVTQAIHRFPKKICLAVYVAATM---LKLGFQTDEDMKDGVPDLSEFGDVyelgFGL-GPDQPPTS-AIIKKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 158 FMAKNLYQLSPVQDLELAKMLVRVNPIITnnLAGTRsFSEEG--YGTVTRIYIVCGEDMAVPEDYQWWMIKNFPPKEVME 235
Cdd:PLN02211 168 FRRKILYQMSPQEDSTLAAMLLRPGPILA--LRSAR-FEEETgdIDKVPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYE 244
|
250 260
....*....|....*....|....
gi 15227859 236 IKcADHMAMFSKPHKLCALLVEIA 259
Cdd:PLN02211 245 LE-SDHSPFFSTPFLLFGLLIKAA 267
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
7-248 |
2.06e-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: 89.87 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 7 KRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQ-TLKDYCKPLLELLNSLGsdDDKVILVAHSM 85
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALG--LEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 86 GGIPAALASDIFPSKIATIVFLTAFMPDTRNLPAYVYQKLIrsvpQEGWLDtvfGTYGKHEcPLEFALFGPKFMAKNLYQ 165
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL----FPGFFD---GFVADFA-PNPLGRLVAKLLALLLLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 166 LSPVQDL-ELAKMLVRVNPIITNNLAGTRSFSEEGYGTVTR----------IYIVCGE-DMAVPEDYQWWMIKNFPPKEV 233
Cdd:pfam00561 151 LRLLKALpLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgrldepTLIIWGDqDPLVPPQALEKLAQLFPNARL 230
|
250
....*....|....*
gi 15227859 234 MEIKCADHMAMFSKP 248
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
10-257 |
1.70e-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: 70.42 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 10 VLVHGLCHGAWCWYKVKTHLEAvGHCVTAVDLAASGiNMTRLEEIQTLKDYCKPLLELLNSLGsdDDKVILVAHSMGGIP 89
Cdd:COG0596 27 VLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALG--LERVVLVGHSMGGMV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 90 AALASDIFPSKIATIVFLTAfmpdtrnlpayVYQKLIRSVPQEGWLDTVFGTygkhecplefalfgpkfmaknlyQLSPV 169
Cdd:COG0596 103 ALELAARHPERVAGLVLVDE-----------VLAALAEPLRRPGLAPEALAA-----------------------LLRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 170 QDLELAKMLVRVNpiitnnlagtrsfseegygtvTRIYIVCGE-DMAVPEDYQWWMIKNFPPKEVMEIKCADHMAMFSKP 248
Cdd:COG0596 149 ARTDLRERLARIT---------------------VPTLVIWGEkDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207
|
....*....
gi 15227859 249 HKLCALLVE 257
Cdd:COG0596 208 EAFAAALRD 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02211 |
PLN02211 |
methyl indole-3-acetate methyltransferase |
2-259 |
4.19e-47 |
|
methyl indole-3-acetate methyltransferase
Pssm-ID: 215128 Cd Length: 273 Bit Score: 157.74 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 2 EKNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILV 81
Cdd:PLN02211 14 PNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSL-PENEKVILV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 82 AHSMGGIPAALASDIFPSKIATIVFLTAFMpdtRNLPAYVYQKLIRSVPQEGWLDTV----FGTyGKHECPLEfALFGPK 157
Cdd:PLN02211 93 GHSAGGLSVTQAIHRFPKKICLAVYVAATM---LKLGFQTDEDMKDGVPDLSEFGDVyelgFGL-GPDQPPTS-AIIKKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 158 FMAKNLYQLSPVQDLELAKMLVRVNPIITnnLAGTRsFSEEG--YGTVTRIYIVCGEDMAVPEDYQWWMIKNFPPKEVME 235
Cdd:PLN02211 168 FRRKILYQMSPQEDSTLAAMLLRPGPILA--LRSAR-FEEETgdIDKVPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYE 244
|
250 260
....*....|....*....|....
gi 15227859 236 IKcADHMAMFSKPHKLCALLVEIA 259
Cdd:PLN02211 245 LE-SDHSPFFSTPFLLFGLLIKAA 267
|
|
| PLN02965 |
PLN02965 |
Probable pheophorbidase |
9-259 |
2.63e-40 |
|
Probable pheophorbidase
Pssm-ID: 178549 [Multi-domain] Cd Length: 255 Bit Score: 139.67 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 9 FVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILVAHSMGGI 88
Cdd:PLN02965 6 FVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDL-PPDHKVILVGHSIGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 89 PAALASDIFPSKIATIVFLTAFMPDTRNLPAYVYQKLIrsVPQEGWLDTVFGTyGKHECPLEFaLFGPKFMAKNLYQLSP 168
Cdd:PLN02965 85 SVTEALCKFTDKISMAIYVAAAMVKPGSIISPRLKNVM--EGTEKIWDYTFGE-GPDKPPTGI-MMKPEFVRHYYYNQSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 169 VQDLELAKMLVRVNPIIT-NNLAGTRSFSEEGYgtVTRIYIVCGEDMAVPEDYQWWMIKNFPPKEVMEIKCADHMAMFSK 247
Cdd:PLN02965 161 LEDYTLSSKLLRPAPVRAfQDLDKLPPNPEAEK--VPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSDHSAFFSV 238
|
250
....*....|..
gi 15227859 248 PHKLCALLVEIA 259
Cdd:PLN02965 239 PTTLFQYLLQAV 250
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
7-248 |
2.06e-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: 89.87 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 7 KRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQ-TLKDYCKPLLELLNSLGsdDDKVILVAHSM 85
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALG--LEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 86 GGIPAALASDIFPSKIATIVFLTAFMPDTRNLPAYVYQKLIrsvpQEGWLDtvfGTYGKHEcPLEFALFGPKFMAKNLYQ 165
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL----FPGFFD---GFVADFA-PNPLGRLVAKLLALLLLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 166 LSPVQDL-ELAKMLVRVNPIITNNLAGTRSFSEEGYGTVTR----------IYIVCGE-DMAVPEDYQWWMIKNFPPKEV 233
Cdd:pfam00561 151 LRLLKALpLLNKRFPSGDYALAKSLVTGALLFIETWSTELRakflgrldepTLIIWGDqDPLVPPQALEKLAQLFPNARL 230
|
250
....*....|....*
gi 15227859 234 MEIKCADHMAMFSKP 248
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
10-257 |
1.70e-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: 70.42 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 10 VLVHGLCHGAWCWYKVKTHLEAvGHCVTAVDLAASGiNMTRLEEIQTLKDYCKPLLELLNSLGsdDDKVILVAHSMGGIP 89
Cdd:COG0596 27 VLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALG--LERVVLVGHSMGGMV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 90 AALASDIFPSKIATIVFLTAfmpdtrnlpayVYQKLIRSVPQEGWLDTVFGTygkhecplefalfgpkfmaknlyQLSPV 169
Cdd:COG0596 103 ALELAARHPERVAGLVLVDE-----------VLAALAEPLRRPGLAPEALAA-----------------------LLRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 170 QDLELAKMLVRVNpiitnnlagtrsfseegygtvTRIYIVCGE-DMAVPEDYQWWMIKNFPPKEVMEIKCADHMAMFSKP 248
Cdd:COG0596 149 ARTDLRERLARIT---------------------VPTLVIWGEkDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207
|
....*....
gi 15227859 249 HKLCALLVE 257
Cdd:COG0596 208 EAFAAALRD 216
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
10-107 |
2.43e-13 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 64.47 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 10 VLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIqtLKDYCKPLLELlnslgSDDDKVILVAHSMGGIP 89
Cdd:COG1075 9 VLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQ--LAAFVDAVLAA-----TGAEKVDLVGHSMGGLV 81
|
90 100
....*....|....*....|
gi 15227859 90 A--ALASDIFPSKIATIVFL 107
Cdd:COG1075 82 AryYLKRLGGAAKVARVVTL 101
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
9-254 |
1.51e-12 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 64.80 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 9 FVLVHGLCHGAWCWykvkTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYckplLELLNSLGsDDDKVILVAHSMGGi 88
Cdd:pfam12697 1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL----AALLDELG-AARPVVLVGHSLGG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 89 paALASDIFPSKIATIVFLTAFMPDTRNLPAY--VYQKLIRSVPQEGWLDTVFgtygkhecplefalFGPKFMAKnlyql 166
Cdd:pfam12697 71 --AVALAAAAAALVVGVLVAPLAAPPGLLAALlaLLARLGAALAAPAWLAAES--------------LARGFLDD----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 167 sPVQDLELAKMLVRVNPIitnnLAGTRSFSEEGY-GTVTRIYIVCGEDMAVPEDYQWWMiKNFPPKEVMEIKCADHMAMF 245
Cdd:pfam12697 130 -LPADAEWAAALARLAAL----LAALALLPLAAWrDLPVPVLVLAEEDRLVPELAQRLL-AALAGARLVVLPGAGHLPLD 203
|
....*....
gi 15227859 246 SkPHKLCAL 254
Cdd:pfam12697 204 D-PEEVAEA 211
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
10-120 |
3.09e-10 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 58.47 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 10 VLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLGSD-DDKVILVAHSMGGI 88
Cdd:COG2267 32 VLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARpGLPVVLLGHSMGGL 111
|
90 100 110
....*....|....*....|....*....|...
gi 15227859 89 PAALASDIFPSKIATIVFL-TAFMPDTRNLPAY 120
Cdd:COG2267 112 IALLYAARYPDRVAGLVLLaPAYRADPLLGPSA 144
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
3-133 |
2.67e-04 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 41.47 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 3 KNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIqTLKDYCKPLLELLNSLGSDDDKVILVA 82
Cdd:COG1647 12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKT-TWEDWLEDVEEAYEILKAGYDKVIVIG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15227859 83 HSMGGIPAALASDIFPSkIATIVFL--TAFMPDTRNLPAYVYQKLIRSVPQEG 133
Cdd:COG1647 91 LSMGGLLALLLAARYPD-VAGLVLLspALKIDDPSAPLLPLLKYLARSLRGIG 142
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
9-134 |
1.99e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 38.82 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227859 9 FVLVHGLCHGAWCWYKVKTHLEAVGHCVtAVDLaasgINMTR---LEEIQTLKDYCKPLLELLNSLGSDDdkVILVAHSM 85
Cdd:PRK03592 30 IVFLHGNPTSSYLWRNIIPHLAGLGRCL-APDL----IGMGAsdkPDIDYTFADHARYLDAWFDALGLDD--VVLVGHDW 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15227859 86 GGipaALASDI---FPSKIATIVFLTAFM--PDTRNLPAYVYQ--KLIRSvPQEGW 134
Cdd:PRK03592 103 GS---ALGFDWaarHPDRVRGIAFMEAIVrpMTWDDFPPAVRElfQALRS-PGEGE 154
|
|
| PRK10673 |
PRK10673 |
esterase; |
34-105 |
3.00e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 38.17 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227859 34 HCVTAVDLAASGINmTRLEEIqTLKDYCKPLLELLNSLGSDddKVILVAHSMGGIPAALASDIFPSKIATIV 105
Cdd:PRK10673 43 HDIIQVDMRNHGLS-PRDPVM-NYPAMAQDLLDTLDALQIE--KATFIGHSMGGKAVMALTALAPDRIDKLV 110
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
49-109 |
4.87e-03 |
|
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: 37.34 E-value: 4.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227859 49 TRLEEIQTLKDYCKPLLELLNSLGSDDDKVILVAHSMGGIPAALA---SDIFPSKIATIVFLTA 109
Cdd:pfam07819 64 TLLDQAEYLNDAIRYILSLYASGRPGPTSVILIGHSMGGIVARAAltlPNYIPQSVNTIITLSS 127
|
|
| |
