|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02211 |
PLN02211 |
methyl indole-3-acetate methyltransferase |
2-182 |
7.99e-31 |
|
methyl indole-3-acetate methyltransferase
Pssm-ID: 215128 Cd Length: 273 Bit Score: 113.45 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 2 EKNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILV 81
Cdd:PLN02211 14 PNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSL-PENEKVILV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 82 AHSMGGIPAALASDIFPSKIATIVFLTAFMpdtRNLPAYVYQKLIRSVPQEGWLDTV----FGTyGKHECPLEfALFGPK 157
Cdd:PLN02211 93 GHSAGGLSVTQAIHRFPKKICLAVYVAATM---LKLGFQTDEDMKDGVPDLSEFGDVyelgFGL-GPDQPPTS-AIIKKE 167
|
170 180
....*....|....*....|....*...
gi 334184394 158 FMAKNLYQLSPVQGQ---EALVRKGTVP 182
Cdd:PLN02211 168 FRRKILYQMSPQEDStlaAMLLRPGPIL 195
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
7-113 |
8.19e-16 |
|
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: 73.31 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 7 KRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQ-TLKDYCKPLLELLNSLGsdDDKVILVAHSM 85
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALG--LEKVNLVGHSM 78
|
90 100
....*....|....*....|....*...
gi 334184394 86 GGIPAALASDIFPSKIATIVFLTAFMPD 113
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPP 106
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
10-107 |
6.49e-13 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 62.15 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 10 VLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIqtLKDYCKPLLELlnslgSDDDKVILVAHSMGGIP 89
Cdd:COG1075 9 VLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQ--LAAFVDAVLAA-----TGAEKVDLVGHSMGGLV 81
|
90 100
....*....|....*....|
gi 334184394 90 A--ALASDIFPSKIATIVFL 107
Cdd:COG1075 82 AryYLKRLGGAAKVARVVTL 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02211 |
PLN02211 |
methyl indole-3-acetate methyltransferase |
2-182 |
7.99e-31 |
|
methyl indole-3-acetate methyltransferase
Pssm-ID: 215128 Cd Length: 273 Bit Score: 113.45 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 2 EKNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILV 81
Cdd:PLN02211 14 PNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSL-PENEKVILV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 82 AHSMGGIPAALASDIFPSKIATIVFLTAFMpdtRNLPAYVYQKLIRSVPQEGWLDTV----FGTyGKHECPLEfALFGPK 157
Cdd:PLN02211 93 GHSAGGLSVTQAIHRFPKKICLAVYVAATM---LKLGFQTDEDMKDGVPDLSEFGDVyelgFGL-GPDQPPTS-AIIKKE 167
|
170 180
....*....|....*....|....*...
gi 334184394 158 FMAKNLYQLSPVQGQ---EALVRKGTVP 182
Cdd:PLN02211 168 FRRKILYQMSPQEDStlaAMLLRPGPIL 195
|
|
| PLN02965 |
PLN02965 |
Probable pheophorbidase |
9-170 |
1.14e-28 |
|
Probable pheophorbidase
Pssm-ID: 178549 [Multi-domain] Cd Length: 255 Bit Score: 107.70 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 9 FVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLgSDDDKVILVAHSMGGI 88
Cdd:PLN02965 6 FVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDL-PPDHKVILVGHSIGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 89 PAALASDIFPSKIATIVFLTAFMPDTRNLPAYVYQKLIrsVPQEGWLDTVFGTyGKHECPLEFaLFGPKFMAKNLYQLSP 168
Cdd:PLN02965 85 SVTEALCKFTDKISMAIYVAAAMVKPGSIISPRLKNVM--EGTEKIWDYTFGE-GPDKPPTGI-MMKPEFVRHYYYNQSP 160
|
..
gi 334184394 169 VQ 170
Cdd:PLN02965 161 LE 162
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
7-113 |
8.19e-16 |
|
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: 73.31 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 7 KRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQ-TLKDYCKPLLELLNSLGsdDDKVILVAHSM 85
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALG--LEKVNLVGHSM 78
|
90 100
....*....|....*....|....*...
gi 334184394 86 GGIPAALASDIFPSKIATIVFLTAFMPD 113
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPP 106
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
10-107 |
6.49e-13 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 62.15 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 10 VLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIqtLKDYCKPLLELlnslgSDDDKVILVAHSMGGIP 89
Cdd:COG1075 9 VLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSAEQ--LAAFVDAVLAA-----TGAEKVDLVGHSMGGLV 81
|
90 100
....*....|....*....|
gi 334184394 90 A--ALASDIFPSKIATIVFL 107
Cdd:COG1075 82 AryYLKRLGGAAKVARVVTL 101
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
10-107 |
9.46e-12 |
|
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: 61.56 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 10 VLVHGLCHGAWCWYKVKTHLEAvGHCVTAVDLAASGiNMTRLEEIQTLKDYCKPLLELLNSLGsdDDKVILVAHSMGGIP 89
Cdd:COG0596 27 VLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALG--LERVVLVGHSMGGMV 102
|
90
....*....|....*...
gi 334184394 90 AALASDIFPSKIATIVFL 107
Cdd:COG0596 103 ALELAARHPERVAGLVLV 120
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
10-120 |
4.38e-10 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 56.93 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 10 VLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLGSD-DDKVILVAHSMGGI 88
Cdd:COG2267 32 VLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARpGLPVVLLGHSMGGL 111
|
90 100 110
....*....|....*....|....*....|...
gi 334184394 89 PAALASDIFPSKIATIVFL-TAFMPDTRNLPAY 120
Cdd:COG2267 112 IALLYAARYPDRVAGLVLLaPAYRADPLLGPSA 144
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
9-139 |
8.57e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 50.55 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 9 FVLVHGLCHGAWCWykvkTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYckplLELLNSLGsDDDKVILVAHSMGGi 88
Cdd:pfam12697 1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL----AALLDELG-AARPVVLVGHSLGG- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 334184394 89 paALASDIFPSKIATIVFLTAFMPDTRNLPAY--VYQKLIRSVPQEGWLDTVF 139
Cdd:pfam12697 71 --AVALAAAAAALVVGVLVAPLAAPPGLLAALlaLLARLGAALAAPAWLAAES 121
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
3-133 |
2.31e-04 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 40.70 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 3 KNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIqTLKDYCKPLLELLNSLGSDDDKVILVA 82
Cdd:COG1647 12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKT-TWEDWLEDVEEAYEILKAGYDKVIVIG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 334184394 83 HSMGGIPAALASDIFPSkIATIVFL--TAFMPDTRNLPAYVYQKLIRSVPQEG 133
Cdd:COG1647 91 LSMGGLLALLLAARYPD-VAGLVLLspALKIDDPSAPLLPLLKYLARSLRGIG 142
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
9-134 |
1.21e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 38.82 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184394 9 FVLVHGLCHGAWCWYKVKTHLEAVGHCVtAVDLaasgINMTR---LEEIQTLKDYCKPLLELLNSLGSDDdkVILVAHSM 85
Cdd:PRK03592 30 IVFLHGNPTSSYLWRNIIPHLAGLGRCL-APDL----IGMGAsdkPDIDYTFADHARYLDAWFDALGLDD--VVLVGHDW 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 334184394 86 GGipaALASDI---FPSKIATIVFLTAFM--PDTRNLPAYVYQ--KLIRSvPQEGW 134
Cdd:PRK03592 103 GS---ALGFDWaarHPDRVRGIAFMEAIVrpMTWDDFPPAVRElfQALRS-PGEGE 154
|
|
| PRK10673 |
PRK10673 |
esterase; |
34-105 |
1.77e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 38.17 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334184394 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 |
3.80e-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: 36.96 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184394 49 TRLEEIQTLKDYCKPLLELLNSLGSDDDKVILVAHSMGGIPAALA---SDIFPSKIATIVFLTA 109
Cdd:pfam07819 64 TLLDQAEYLNDAIRYILSLYASGRPGPTSVILIGHSMGGIVARAAltlPNYIPQSVNTIITLSS 127
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
31-104 |
7.02e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 36.46 E-value: 7.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334184394 31 AVGHCVTAVDLAASGINMTRLEEiQTLKDYCKPLLELLNSLGSDddKVILVAHSMGG-IPAALASDIfPSKIATI 104
Cdd:PRK14875 155 AAGRPVIALDLPGHGASSKAVGA-GSLDELAAAVLAFLDALGIE--RAHLVGHSMGGaVALRLAARA-PQRVASL 225
|
|
| |
