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Conserved domains on  [gi|300797479|ref|NP_001178767|]
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protein phosphatase methylesterase 1 [Rattus norvegicus]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-229 3.38e-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: 85.44  E-value: 3.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNSEDLSAETMAKDVGNVVEAMYGD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479 146 lppPVMLIGHSMGGAIAVHTAAANlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   90 ---RVVLVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 300797479 225 ESARV 229
Cdd:COG0596  158 ARITV 162
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-229 3.38e-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: 85.44  E-value: 3.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNSEDLSAETMAKDVGNVVEAMYGD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479 146 lppPVMLIGHSMGGAIAVHTAAANlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   90 ---RVVLVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 300797479 225 ESARV 229
Cdd:COG0596  158 ARITV 162
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-356 1.64e-14

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: 72.54  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNSEDLSAETMAKDVGNVVEAmYGDlpPPVMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  156 SMGGAIAVHTAA------ANLVpsLLGLCMIDVVEGTAMD-ALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESAR 228
Cdd:pfam00561  77 SMGGLIALAYAAkypdrvKALV--LLGALDPPHELDEADRfILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  229 VSMvgqvkqcegitspessksivegiieeeeedeegsESVNKRKKEDDMETKKdHPYTWRIelakteKYWDGWF-RGLSN 307
Cdd:pfam00561 155 KAL----------------------------------PLLNKRFPSGDYALAK-SLVTGAL------LFIETWStELRAK 193

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300797479  308 LFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 356
Cdd:pfam00561 194 FLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-178 3.97e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 60.73  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNSEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300797479 140 EAMYgdlPPPVMLIGHSMGGAIAVHTAAA--NLVPSLLGLC 178
Cdd:PRK14875 192 DALG---IERAHLVGHSMGGAVALRLAARapQRVASLTLIA 229
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 127-176 8.39e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 8.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300797479 127 SAETMAKDVGNVVEAMYGDLPP-PVMLIGHSMGGAIAVHtAAANLVPSLLG 176
Cdd:cd00741    6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALAGL-AGLDLRGRGLG 55
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-229 3.38e-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: 85.44  E-value: 3.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNSEDLSAETMAKDVGNVVEAMYGD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479 146 lppPVMLIGHSMGGAIAVHTAAANlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   90 ---RVVLVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 300797479 225 ESARV 229
Cdd:COG0596  158 ARITV 162
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-169 2.76e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 74.27  E-value: 2.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  72 SGSEGPVLLLLHGGGHSALSWAVFTAAIISRvQCRIVALDLRSHGETKVKNSEDLSAETMAKDVGNVVEAMYGDLPPPVM 151
Cdd:COG2267   24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGLPVV 102

                         90
                 ....*....|....*...
gi 300797479 152 LIGHSMGGAIAVHTAAAN 169
Cdd:COG2267  103 LLGHSMGGLIALLYAARY 120
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-356 1.64e-14

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: 72.54  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNSEDLSAETMAKDVGNVVEAmYGDlpPPVMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  156 SMGGAIAVHTAA------ANLVpsLLGLCMIDVVEGTAMD-ALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESAR 228
Cdd:pfam00561  77 SMGGLIALAYAAkypdrvKALV--LLGALDPPHELDEADRfILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  229 VSMvgqvkqcegitspessksivegiieeeeedeegsESVNKRKKEDDMETKKdHPYTWRIelakteKYWDGWF-RGLSN 307
Cdd:pfam00561 155 KAL----------------------------------PLLNKRFPSGDYALAK-SLVTGAL------LFIETWStELRAK 193

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300797479  308 LFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 356
Cdd:pfam00561 194 FLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-362 1.02e-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: 69.42  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   79 LLLLHGGGHSALSWAVFTAAiisrvQCRIVALDLRSHGETkVKNSEDLSAetmAKDVGNVVEAMygDLPPPVMLIGHSMG 158
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA-----GVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDEL--GAARPVVLVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  159 GAIAVHTAAANLVPSLLglcmIDvvegtAMDALNSMQNFLRGRPKTFKSLENAIEWsvksgqiRNLESARVSMVGQVkqc 238
Cdd:pfam12697  70 GAVALAAAAAALVVGVL----VA-----PLAAPPGLLAALLALLARLGAALAAPAW-------LAAESLARGFLDDL--- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  239 egitspessksivegiieeeeedeegsesvnkrkkeddmetkkDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPkLL 318
Cdd:pfam12697 131 -------------------------------------------PADAEWAAALARLAALLAALALLPLAAWRDLPVP-VL 166

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 300797479  319 LLAGVDRLDKDLT--IGQMQGKFQMQVLPQCGHAVHEDaPDKVAEA 362
Cdd:pfam12697 167 VLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-178 3.97e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 60.73  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNSEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300797479 140 EAMYgdlPPPVMLIGHSMGGAIAVHTAAA--NLVPSLLGLC 178
Cdd:PRK14875 192 DALG---IERAHLVGHSMGGAVALRLAARapQRVASLTLIA 229
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
77-167 1.11e-07

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.33  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGEtkvknSEDLSAETMAKDVGNVVEAM----YGDlPPPVML 152
Cdd:COG1506   24 PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGE-----SAGDWGGDEVDDVLAAIDYLaarpYVD-PDRIGI 97

                         90
                 ....*....|....*
gi 300797479 153 IGHSMGGAIAVHTAA 167
Cdd:COG1506   98 YGHSYGGYMALLAAA 112
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 39-166 1.92e-06

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 50.24  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   39 RDFTPVPWSQYfesmeDVEVENETGKDTFRVYKSG--SEGPVLLLLHGGGHSALSWAVFTAAIISRVQCriVALDLRSHG 116
Cdd:PLN02980 1337 RTFKEEQVRTY-----ELRVDVDGFSCLIKVHEVGqnAEGSVVLFLHGFLGTGEDWIPIMKAISGSARC--ISIDLPGHG 1409

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300797479  117 ETKVKNSEDLSAETMAKDVGNVVEAMYGDL----PPPVMLIGHSMGGAIAVHTA 166
Cdd:PLN02980 1410 GSKIQNHAKETQTEPTLSVELVADLLYKLIehitPGKVTLVGYSMGARIALYMA 1463
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 77-162 1.17e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.66  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  77 PVLLLlHGGGHSALSWAVFTAAIISRVQCrIVALDLrshgetkvkNSEDLSAETMAKDVGNVVEAMYGDLP-PPVMLIGH 155
Cdd:COG1075    7 PVVLV-HGLGGSAASWAPLAPRLRAAGYP-VYALNY---------PSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGH 75


                 ....*..
gi 300797479 156 SMGGAIA 162
Cdd:COG1075   76 SMGGLVA 82
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-169 2.40e-05

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: 45.28  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   78 VLLLLHGGG-HS-----------ALSWAVFtaaiisrvqcrivALDLRSHGEtkvknSEDLSA-----ETMAKDVGNVVE 140
Cdd:pfam12146   6 VVVLVHGLGeHSgryahladalaAQGFAVY-------------AYDHRGHGR-----SDGKRGhvpsfDDYVDDLDTFVD 67

                          90       100       110
                  ....*....|....*....|....*....|
gi 300797479  141 AMYGDLP-PPVMLIGHSMGGAIAVHTAAAN 169
Cdd:pfam12146  68 KIREEHPgLPLFLLGHSMGGLIAALYALRY 97
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 72-168 1.66e-04

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 42.53  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  72 SGSEGPVLLLLH--GGGHSA-LSWAVFTAAiisrvQCRIVALDLRSHgetkvknsEDLSAETMAKDVGNVVEAMYGDLPP 148
Cdd:COG3208    2 RPDARLRLFCFPyaGGSASAyRPWAAALPP-----DIEVLAVQLPGR--------GDRLGEPPLTSLEELADDLAEELAP 68

                         90       100
                 ....*....|....*....|....
gi 300797479 149 ----PVMLIGHSMGGAIAVHTAAA 168
Cdd:COG3208   69 lldrPFALFGHSMGALLAFELARR 92
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-168 2.27e-04

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 41.78  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  68 RVY---KSGSEGPVLLLLHGGGHSALSWAVFT---AAIISRVQCRIVALDLRSHGETKVknsedlsaETMAKDVGNVVEA 141
Cdd:COG0657    2 DVYrpaGAKGPLPVVVYFHGGGWVSGSKDTHDplaRRLAARAGAAVVSVDYRLAPEHPF--------PAALEDAYAALRW 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 300797479 142 M------YGDLPPPVMLIGHSMGGAIAVHTAAA 168
Cdd:COG0657   74 LranaaeLGIDPDRIAVAGDSAGGHLAAALALR 106
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
80-214 3.11e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 41.85  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  80 LLLHG-GG--HSALSWAVFTAAIisrvQCRIVALDLRSHGETKvknsEDLSAETmAKDVGNVVEAMYGDL---PPPVMLI 153
Cdd:COG1647   19 LLLHGfTGspAEMRPLAEALAKA----GYTVYAPRLPGHGTSP----EDLLKTT-WEDWLEDVEEAYEILkagYDKVIVI 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300797479 154 GHSMGGAIAVHTAAANlvPSLLGLCMID---VVEGTAM---DALNSMQNFLRGRPKTFKSLENAIEW 214
Cdd:COG1647   90 GLSMGGLLALLLAARY--PDVAGLVLLSpalKIDDPSApllPLLKYLARSLRGIGSDIEDPEVAEYA 154
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 77-182 1.07e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 40.06  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNSEDLSAEtmakdvgnVVEAMYGDLPP-PVMLIGH 155
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADE--------YAEALRQIQPEgPYALFGH 72

                          90       100
                  ....*....|....*....|....*....
gi 300797479  156 SMGGAIAVHTAAA--NLVPSLLGLCMIDV 182
Cdd:pfam00975  73 SMGGMLAFEVARRleRQGEAVRSLFLSDA 101
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 76-185 1.16e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 40.21  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  76 GPVLLLLHGGGHSALSWAvftaAIISRV-QCRIVALDLRSHGE---TKVKNSEDLS---AETMAKdvgnvveamYGDLPp 148
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQ----PVGEALpDYPRLYIDLPGHGGsaaISVDGFADVSrllSQTLQS---------YNILP- 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 300797479 149 pVMLIGHSMGGAIAVHTAAANLVPSLLGLCmidvVEG 185
Cdd:PRK11126  68 -YWLVGYSLGGRIAMYYACQGLAGGLCGLI----VEG 99
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 60-179 1.49e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 39.75  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479   60 NETGKD-TFRVY-----KSGSEGPVLLLLHGGGHSAL--SWAVFTAAIISRvQCRIVALDLRSHGETKVKNSEDLSAETM 131
Cdd:pfam00756   2 NSLGREmKVQVYlpedyPPGRKYPVLYLLDGTGWFQNgpAKEGLDRLAASG-EIPPVIIVGSPRGGEVSFYSDWDRGLNA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300797479  132 AKDVGN-------------VVEAMYGDLPPPVMLIGHSMGGAIAVHTAAANlvPSLLGLCM 179
Cdd:pfam00756  81 TEGPGAyayetfltqelppLLDANFPTAPDGRALAGQSMGGLGALYLALKY--PDLFGSVS 139
PRK10673 PRK10673
esterase;
107-182 1.89e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 39.71  E-value: 1.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300797479 107 IVALDLRSHGETKvkNSEDLSAETMAKDVGNVVEAMYgdlPPPVMLIGHSMGGAIAVHTAAanLVPSLL-GLCMIDV 182
Cdd:PRK10673  45 IIQVDMRNHGLSP--RDPVMNYPAMAQDLLDTLDALQ---IEKATFIGHSMGGKAVMALTA--LAPDRIdKLVAIDI 114
PLN02578 PLN02578
hydrolase
 75-216 3.06e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 39.44  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  75 EGPVLLLLHGGGHSALSWAVFTAAIISRVqcRIVALDLRSHGETKvKNSEDLSAETMAKDVGNVVEAMYGDlppPVMLIG 154
Cdd:PLN02578  85 EGLPIVLIHGFGASAFHWRYNIPELAKKY--KVYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVKE---PAVLVG 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300797479 155 HSMGGAIAVHTAAANlvPsllglcmiDVVEGTAMdaLNS---MQNFLRGRPKTFKSLENAIEWSV 216
Cdd:PLN02578 159 NSLGGFTALSTAVGY--P--------ELVAGVAL--LNSagqFGSESREKEEAIVVEETVLTRFV 211
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 53-167 4.31e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 38.36  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  53 MEDVEVENETGKD---TFRVYKSGSEG-PVLLLLHGGG----HSALSWAVFTAAIISrvqcrIVALDLRSHGETKVKNSE 124
Cdd:COG1073   10 KEDVTFKSRDGIKlagDLYLPAGASKKyPAVVVAHGNGgvkeQRALYAQRLAELGFN-----VLAFDYRGYGESEGEPRE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300797479 125 DLSAETmaKDVGNVVEAM----YGDlPPPVMLIGHSMGGAIAVHTAA 167
Cdd:COG1073   85 EGSPER--RDARAAVDYLrtlpGVD-PERIGLLGISLGGGYALNAAA 128
PRK05855 PRK05855
SDR family oxidoreductase;
69-158 4.31e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 39.19  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  69 VYKSG-SEGPVLLLLHGGGHSALSW-AVftAAIISRvQCRIVALDLRSHGETKV-KNSEDLSAETMAKDVGNVVEAMYGD 145
Cdd:PRK05855  17 VYEWGdPDRPTVVLVHGYPDNHEVWdGV--APLLAD-RFRVVAYDVRGAGRSSApKRTAAYTLARLADDFAAVIDAVSPD 93

                         90
                 ....*....|...
gi 300797479 146 lpPPVMLIGHSMG 158
Cdd:PRK05855  94 --RPVHLLAHDWG 104
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
54-169 5.43e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  54 EDVEVENETGkDTFRVY----KSGSEGPVLLLLHG-GGHSAlsWAVFTAAIISRVQCRIVALDLRSHGETKVKNSED--- 125
Cdd:COG0412    4 ETVTIPTPDG-VTLPGYlarpAGGGPRPGVVVLHEiFGLNP--HIRDVARRLAAAGYVVLAPDLYGRGGPGDDPDEAral 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 300797479 126 ---LSAETMAKDVGNVVEAMYGDL---PPPVMLIGHSMGGAIAVHTAAAN 169
Cdd:COG0412   81 mgaLDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARG 130
YpfH COG0400
Predicted esterase [General function prediction only];
77-169 6.23e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797479  77 PVLLLLHGGGHSALSWAVFtAAIISRVQCRIVALD------------LRSHGETKVKNSEDLSAEtmAKDVGNVVEAM-- 142
Cdd:COG0400    6 PLVVLLHGYGGDEEDLLPL-APELALPGAAVLAPRapvpegpggrawFDLSFLEGREDEEGLAAA--AEALAAFIDELea 82

                         90       100
                 ....*....|....*....|....*...
gi 300797479 143 -YGDLPPPVMLIGHSMGGAIAVHTAAAN 169
Cdd:COG0400   83 rYGIDPERIVLAGFSQGAAMALSLALRR 110
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 127-176 8.39e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 8.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300797479 127 SAETMAKDVGNVVEAMYGDLPP-PVMLIGHSMGGAIAVHtAAANLVPSLLG 176
Cdd:cd00741    6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALAGL-AGLDLRGRGLG 55
 
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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