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Conserved domains on  [gi|42562323|ref|NP_173960|]
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methyl esterase 13 [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
190-434 6.22e-62

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PLN02965:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 255  Bit Score: 201.30  E-value: 6.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  190 FVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYSKPLLHFFESLKPTEKVILVGHDFGGAC 269
Cdd:PLN02965   6 FVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  270 MSYAMEMFPTKIAKAVFISAAMLANGQ-STLDLFNQQLGSNDLMQqaqiFLYANGKKNPPTAVDFDRSLLRDFLFNQSPP 348
Cdd:PLN02965  86 VTEALCKFTDKISMAIYVAAAMVKPGSiISPRLKNVMEGTEKIWD----YTFGEGPDKPPTGIMMKPEFVRHYYYNQSPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  349 KDLALASVSIRP-----------IPFAPVSEKVhvseknygsiRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKGSD 417
Cdd:PLN02965 162 EDYTLSSKLLRPapvrafqdldkLPPNPEAEKV----------PRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSD 231
                        250
                 ....*....|....*..
gi 42562323  418 HAPFFSRPQSLNKILVE 434
Cdd:PLN02965 232 HSAFFSVPTTLFQYLLQ 248
 
Name Accession Description Interval E-value
PLN02965 PLN02965
Probable pheophorbidase
190-434 6.22e-62

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 201.30  E-value: 6.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  190 FVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYSKPLLHFFESLKPTEKVILVGHDFGGAC 269
Cdd:PLN02965   6 FVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  270 MSYAMEMFPTKIAKAVFISAAMLANGQ-STLDLFNQQLGSNDLMQqaqiFLYANGKKNPPTAVDFDRSLLRDFLFNQSPP 348
Cdd:PLN02965  86 VTEALCKFTDKISMAIYVAAAMVKPGSiISPRLKNVMEGTEKIWD----YTFGEGPDKPPTGIMMKPEFVRHYYYNQSPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  349 KDLALASVSIRP-----------IPFAPVSEKVhvseknygsiRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKGSD 417
Cdd:PLN02965 162 EDYTLSSKLLRPapvrafqdldkLPPNPEAEKV----------PRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSD 231
                        250
                 ....*....|....*..
gi 42562323  418 HAPFFSRPQSLNKILVE 434
Cdd:PLN02965 232 HSAFFSVPTTLFQYLLQ 248
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
188-425 7.93e-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: 82.55  E-value: 7.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   188 KRFVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSS----IDTNNITSLAHYskplLHFFESLKPTEKVILVGH 263
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSrpkaQDDYRTDDLAED----LEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   264 DFGGACMSYAMEMFPTKIAKAVFISAamLANGQSTLDLFNQQLGSNDLMQQAQIFLYANGKKNPPTAVDFDRSLLRDFLF 343
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   344 NQSPPKDLALASVSIRPIPFAPVSEKVHVSE---------KNYGSIRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLK 414
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETwstelrakfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
                         250
                  ....*....|.
gi 42562323   415 GSDHAPFFSRP 425
Cdd:pfam00561 235 DAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
181-434 1.00e-15

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: 75.81  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 181 KVEGSETKRFVLVHGGGFGAWCWYKTITLLEKHgFQVDAVELTGSGVSSIDTNNITsLAHYSKPLLHFFESLKPtEKVIL 260
Cdd:COG0596  17 REAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGL-ERVVL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 261 VGHDFGGACMSYAMEMFPTKIAKAVFISAAMlangqstlDLFNQQLGSNDLMQQAqiflyangkknpptavdfdrsLLRD 340
Cdd:COG0596  94 VGHSMGGMVALELAARHPERVAGLVLVDEVL--------AALAEPLRRPGLAPEA---------------------LAAL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 341 FLFNQSPPKDLALASVSIrpipfaPVsekvhvseknygsirrFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKGSDHAP 420
Cdd:COG0596 145 LRALARTDLRERLARITV------PT----------------LVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
                       250
                ....*....|....
gi 42562323 421 FFSRPQSLNKILVE 434
Cdd:COG0596 203 PLEQPEAFAAALRD 216
 
Name Accession Description Interval E-value
PLN02965 PLN02965
Probable pheophorbidase
190-434 6.22e-62

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 201.30  E-value: 6.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  190 FVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYSKPLLHFFESLKPTEKVILVGHDFGGAC 269
Cdd:PLN02965   6 FVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  270 MSYAMEMFPTKIAKAVFISAAMLANGQ-STLDLFNQQLGSNDLMQqaqiFLYANGKKNPPTAVDFDRSLLRDFLFNQSPP 348
Cdd:PLN02965  86 VTEALCKFTDKISMAIYVAAAMVKPGSiISPRLKNVMEGTEKIWD----YTFGEGPDKPPTGIMMKPEFVRHYYYNQSPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  349 KDLALASVSIRP-----------IPFAPVSEKVhvseknygsiRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKGSD 417
Cdd:PLN02965 162 EDYTLSSKLLRPapvrafqdldkLPPNPEAEKV----------PRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSD 231
                        250
                 ....*....|....*..
gi 42562323  418 HAPFFSRPQSLNKILVE 434
Cdd:PLN02965 232 HSAFFSVPTTLFQYLLQ 248
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
190-434 1.81e-58

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 193.18  E-value: 1.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  190 FVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYSKPLLHFFESLKPTEKVILVGHDFGGAC 269
Cdd:PLN02211  21 FVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGLS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  270 MSYAMEMFPTKIAKAVFISAAMLANGQSTLDLFNQqlGSNDLMQQAQIFL--YANGKKNPPTAVDFDRSLLRDFLFNQSP 347
Cdd:PLN02211 101 VTQAIHRFPKKICLAVYVAATMLKLGFQTDEDMKD--GVPDLSEFGDVYElgFGLGPDQPPTSAIIKKEFRRKILYQMSP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  348 PKDLALASVSIRPIPF-APVSEKVHVSEKNYGSIRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKgSDHAPFFSRPQ 426
Cdd:PLN02211 179 QEDSTLAAMLLRPGPIlALRSARFEEETGDIDKVPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELE-SDHSPFFSTPF 257

                 ....*...
gi 42562323  427 SLNKILVE 434
Cdd:PLN02211 258 LLFGLLIK 265
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
188-425 7.93e-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: 82.55  E-value: 7.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   188 KRFVLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSS----IDTNNITSLAHYskplLHFFESLKPTEKVILVGH 263
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSrpkaQDDYRTDDLAED----LEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   264 DFGGACMSYAMEMFPTKIAKAVFISAamLANGQSTLDLFNQQLGSNDLMQQAQIFLYANGKKNPPTAVDFDRSLLRDFLF 343
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   344 NQSPPKDLALASVSIRPIPFAPVSEKVHVSE---------KNYGSIRRFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLK 414
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETwstelrakfLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
                         250
                  ....*....|.
gi 42562323   415 GSDHAPFFSRP 425
Cdd:pfam00561 235 DAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
181-434 1.00e-15

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: 75.81  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 181 KVEGSETKRFVLVHGGGFGAWCWYKTITLLEKHgFQVDAVELTGSGVSSIDTNNITsLAHYSKPLLHFFESLKPtEKVIL 260
Cdd:COG0596  17 REAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAALLDALGL-ERVVL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 261 VGHDFGGACMSYAMEMFPTKIAKAVFISAAMlangqstlDLFNQQLGSNDLMQQAqiflyangkknpptavdfdrsLLRD 340
Cdd:COG0596  94 VGHSMGGMVALELAARHPERVAGLVLVDEVL--------AALAEPLRRPGLAPEA---------------------LAAL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 341 FLFNQSPPKDLALASVSIrpipfaPVsekvhvseknygsirrFYIKTMEDYAVPVLLQEAMIKLNPPEQVFQLKGSDHAP 420
Cdd:COG0596 145 LRALARTDLRERLARITV------PT----------------LVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
                       250
                ....*....|....
gi 42562323 421 FFSRPQSLNKILVE 434
Cdd:COG0596 203 PLEQPEAFAAALRD 216
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
190-423 1.22e-13

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 69.81  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   190 FVLVHGGGFGawcwYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYskplLHFFESLKPTEKVILVGHDFGGAc 269
Cdd:pfam12697   1 VVLVHGAGLS----AAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL----AALLDELGAARPVVLVGHSLGGA- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323   270 msYAMEMFPTKIAKAVFISAAMLANGQSTldlfnqqlgsnDLMQQAQIFLYANGKKNPPTAVDFDRSLLRDFLFNQSPPK 349
Cdd:pfam12697  72 --VALAAAAAALVVGVLVAPLAAPPGLLA-----------ALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAA 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42562323   350 DLALASVSIRPIPFAPVSEKVHVseknygsIRRFYIKTMEDYAVPVLLQEAMIKLnPPEQVFQLKGSDHAPFFS 423
Cdd:pfam12697 139 ALARLAALLAALALLPLAAWRDL-------PVPVLVLAEEDRLVPELAQRLLAAL-AGARLVVLPGAGHLPLDD 204
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
191-294 9.27e-13

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 67.33  E-value: 9.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 191 VLVHGGGFGAWCWYKTITLLEKHGFQVDAVELTGSGVSSIDTNNITSLAHYSKPLLHFFESLK--PTEKVILVGHDFGGA 268
Cdd:COG2267  32 VLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRarPGLPVVLLGHSMGGL 111
                        90       100
                ....*....|....*....|....*.
gi 42562323 269 CMSYAMEMFPTKIAKAVFISAAMLAN 294
Cdd:COG2267 112 IALLYAARYPDRVAGLVLLAPAYRAD 137
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
191-289 1.85e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 46.36  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323 191 VLVHG-GGFgAWCWYKTITLLEKHGFQVDAVELtGSGVSSIDTNnitslahySKPLLHFFESLK---PTEKVILVGHDFG 266
Cdd:COG1075   9 VLVHGlGGS-AASWAPLAPRLRAAGYPVYALNY-PSTNGSIEDS--------AEQLAAFVDAVLaatGAEKVDLVGHSMG 78
                        90       100
                ....*....|....*....|....*
gi 42562323 267 GACMSYAMEMF--PTKIAKAVFISA 289
Cdd:COG1075  79 GLVARYYLKRLggAAKVARVVTLGT 103
PLN00413 PLN00413
triacylglycerol lipase
201-268 3.16e-04

triacylglycerol lipase


Pssm-ID: 165792  Cd Length: 479  Bit Score: 43.08  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562323  201 WC------WYKTITLLEKHGFQVDAVELTGSG----VSSIDTNNITSLAHYSKPLLHFFESLK--PTEKVILVGHDFGGA 268
Cdd:PLN00413 217 WCtdldlsWHEVKNVGKIHGGFMKALGLPKEGwpeeINLDETQNATSLLAYYTILRHLKEIFDqnPTSKFILSGHSLGGA 296
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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