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Conserved domains on  [gi|7706645|ref|NP_057231|]
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protein phosphatase methylesterase 1 isoform a [Homo sapiens]

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 5.14e-18

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: 81.97  E-value: 5.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596  13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645  146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596  88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                ....*
gi 7706645  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 5.14e-18

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: 81.97  E-value: 5.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596  13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645  146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596  88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                ....*
gi 7706645  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 9.05e-15

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: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    156 SMGGAIAVHTAS--SNLVPS--LLGLCMIDVVEGTAMD-ALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVS 230
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKAlvLLGALDPPHELDEADRfILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    231 MVGQVKQCEGITSPEGSksivegiieeeeedeegsesiskrkkeddmetkkdHPYTWRIelakteKYWDGWF-RGLSNLF 309
Cdd:pfam00561 157 LPLLNKRFPSGDYALAK-----------------------------------SLVTGAL------LFIETWStELRAKFL 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 7706645    310 LSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 356
Cdd:pfam00561 196 GRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 5.10e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.26  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100
                 ....*....|....*....|....*..
gi 7706645   140 EAMYgdlPPPIMLIGHSMGGAIAVHTA 166
Cdd:PRK14875 192 DALG---IERAHLVGHSMGGAVALRLA 215
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-229 5.14e-18

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: 81.97  E-value: 5.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596  13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645  146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596  88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                ....*
gi 7706645  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 9.05e-15

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: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    156 SMGGAIAVHTAS--SNLVPS--LLGLCMIDVVEGTAMD-ALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVS 230
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKAlvLLGALDPPHELDEADRfILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    231 MVGQVKQCEGITSPEGSksivegiieeeeedeegsesiskrkkeddmetkkdHPYTWRIelakteKYWDGWF-RGLSNLF 309
Cdd:pfam00561 157 LPLLNKRFPSGDYALAK-----------------------------------SLVTGAL------LFIETWStELRAKFL 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 7706645    310 LSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 356
Cdd:pfam00561 196 GRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-166 9.52e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.73  E-value: 9.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   72 SGSEGPVLLLLHGGGHSALSWAVFTAAIISRvQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIM 151
Cdd:COG2267  24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGLPVV 102

                        90
                ....*....|....*
gi 7706645  152 LIGHSMGGAIAVHTA 166
Cdd:COG2267 103 LLGHSMGGLIALLYA 117
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-362 1.64e-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: 69.04  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     79 LLLLHGGGHSALSWAVFTAAiisrvQCRIVALDLRSHGETkVKNPEDLSAetmAKDVGNVVEAmYGDLPPPImLIGHSMG 158
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA-----GVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDE-LGAARPVV-LVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    159 GAIAVHTASSNLVPSLLglcmIDvvegtAMDALNSMQNFLRGRPKTFKSLENAIEWsvksgqiRNLESARVSMVGQVkqc 238
Cdd:pfam12697  70 GAVALAAAAAALVVGVL----VA-----PLAAPPGLLAALLALLARLGAALAAPAW-------LAAESLARGFLDDL--- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    239 egitspegsksivegiieeeeedeegsesiskrkkeddmetkkDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPkLL 318
Cdd:pfam12697 131 -------------------------------------------PADAEWAAALARLAALLAALALLPLAAWRDLPVP-VL 166

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 7706645    319 LLAGVDRLDKDLT--IGQMQGKFQMQVLPQCGHAVHEDaPDKVAEA 362
Cdd:pfam12697 167 VLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 5.10e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.26  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100
                 ....*....|....*....|....*..
gi 7706645   140 EAMYgdlPPPIMLIGHSMGGAIAVHTA 166
Cdd:PRK14875 192 DALG---IERAHLVGHSMGGAVALRLA 215
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
77-167 5.59e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.02  E-value: 5.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETkvknpEDLSAETMAKDVGNVVEAM----YGDlPPPIML 152
Cdd:COG1506  24 PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAIDYLaarpYVD-PDRIGI 97

                        90
                ....*....|....*
gi 7706645  153 IGHSMGGAIAVHTAS 167
Cdd:COG1506  98 YGHSYGGYMALLAAA 112
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 39-166 4.96e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 48.70  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     39 RDFSPVPWSQYfesmeDVEVENETGKDTFRVYKSG--SEGPVLLLLHGGGHSALSWAVFTAAIISRVQCriVALDLRSHG 116
Cdd:PLN02980 1337 RTFKEEQVRTY-----ELRVDVDGFSCLIKVHEVGqnAEGSVVLFLHGFLGTGEDWIPIMKAISGSARC--ISIDLPGHG 1409

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7706645    117 ETKVKNPEDLSAETMAKDVGNVVEAMYGDL----PPPIMLIGHSMGGAIAVHTA 166
Cdd:PLN02980 1410 GSKIQNHAKETQTEPTLSVELVADLLYKLIehitPGKVTLVGYSMGARIALYMA 1463
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-166 1.86e-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: 45.67  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     78 VLLLLHGGG-HS-----------ALSWAVFtaaiisrvqcrivALDLRSHGETK-----VKNPEDlsaetMAKDVGNVVE 140
Cdd:pfam12146   6 VVVLVHGLGeHSgryahladalaAQGFAVY-------------AYDHRGHGRSDgkrghVPSFDD-----YVDDLDTFVD 67

                          90       100
                  ....*....|....*....|....*..
gi 7706645    141 AMYGDLP-PPIMLIGHSMGGAIAVHTA 166
Cdd:pfam12146  68 KIREEHPgLPLFLLGHSMGGLIAALYA 94
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 77-162 1.94e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.28  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   77 PVLLLlHGGGHSALSWAVFTAAIISRVQCrIVALDLrshgetkvkNPEDLSAETMAKDVGNVVEAMYGDLP-PPIMLIGH 155
Cdd:COG1075   7 PVVLV-HGLGGSAASWAPLAPRLRAAGYP-VYALNY---------PSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGH 75


                ....*..
gi 7706645  156 SMGGAIA 162
Cdd:COG1075  76 SMGGLVA 82
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
80-214 9.90e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.39  E-value: 9.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   80 LLLHG-GG--HSALSWAVFTAAIisrvQCRIVALDLRSHGETkvknPEDLSAETmAKDVGNVVEAMYGDL---PPPIMLI 153
Cdd:COG1647  19 LLLHGfTGspAEMRPLAEALAKA----GYTVYAPRLPGHGTS----PEDLLKTT-WEDWLEDVEEAYEILkagYDKVIVI 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706645  154 GHSMGGAIAVHTASSNlvPSLLGLCMID---VVEGTAM---DALNSMQNFLRGRPKTFKSLENAIEW 214
Cdd:COG1647  90 GLSMGGLLALLLAARY--PDVAGLVLLSpalKIDDPSApllPLLKYLARSLRGIGSDIEDPEVAEYA 154
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-166 1.08e-04

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 42.94  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   68 RVY---KSGSEGPVLLLLHGGGHSALSWAVFT---AAIISRVQCRIVALDLRSHGETKVknpedlsaETMAKDVGNVVEA 141
Cdd:COG0657   2 DVYrpaGAKGPLPVVVYFHGGGWVSGSKDTHDplaRRLAARAGAAVVSVDYRLAPEHPF--------PAALEDAYAALRW 73

                        90       100       110
                ....*....|....*....|....*....|.
gi 7706645  142 M------YGDLPPPIMLIGHSMGGAIAVHTA 166
Cdd:COG0657  74 LranaaeLGIDPDRIAVAGDSAGGHLAAALA 104
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 72-166 1.96e-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: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   72 SGSEGPVLLLLH--GGGHSA-LSWAVFTAAiisrvQCRIVALDLRSHgetkvknpEDLSAETMAKDVGNVVEAMYGDLPP 148
Cdd:COG3208   2 RPDARLRLFCFPyaGGSASAyRPWAAALPP-----DIEVLAVQLPGR--------GDRLGEPPLTSLEELADDLAEELAP 68

                        90       100
                ....*....|....*....|..
gi 7706645  149 ----PIMLIGHSMGGAIAVHTA 166
Cdd:COG3208  69 lldrPFALFGHSMGALLAFELA 90
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 76-185 9.45e-04

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 40.59  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    76 GPVLLLLHGGGHSALSWAvftaAIISRV-QCRIVALDLRSHGEtkvknpedlSAETMAKDVGNVVE------AMYGDLPp 148
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQ----PVGEALpDYPRLYIDLPGHGG---------SAAISVDGFADVSRllsqtlQSYNILP- 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 7706645   149 pIMLIGHSMGGAIAVHTASSNLVPSLLGLCmidvVEG 185
Cdd:PRK11126  68 -YWLVGYSLGGRIAMYYACQGLAGGLCGLI----VEG 99
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 68-182 3.20e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 38.95  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    68 RVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKVKNPEDLSA------ETMAKDVGNVVEA 141
Cdd:PLN02824  21 RYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKS--HRVYAIDLLGYGYSDKPNPRSAPPnsfytfETWGEQLNDFCSD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 7706645   142 MYGDlppPIMLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDV 182
Cdd:PLN02824  99 VVGD---PAFVICNSVGGVVGLQAAVDA--PELVrGVMLINI 135
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 77-167 3.55e-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: 38.52  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645     77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAEtmakdvgnVVEAMYGDLPP-PIMLIGH 155
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADE--------YAEALRQIQPEgPYALFGH 72

                          90
                  ....*....|..
gi 7706645    156 SMGGAIAVHTAS 167
Cdd:pfam00975  73 SMGGMLAFEVAR 84
PRK10673 PRK10673
esterase;
107-182 4.61e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 38.56  E-value: 4.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706645   107 IVALDLRSHGETKVKNPEDLSAetMAKDVGNVVEAMygDLPPPImLIGHSMGGAIAVhtASSNLVPSLL-GLCMIDV 182
Cdd:PRK10673  45 IIQVDMRNHGLSPRDPVMNYPA--MAQDLLDTLDAL--QIEKAT-FIGHSMGGKAVM--ALTALAPDRIdKLVAIDI 114
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 53-167 4.76e-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: 4.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   53 MEDVEVENETGKD---TFRVYKSGSEG-PVLLLLHGGG----HSALSWAVFTAAIISrvqcrIVALDLRSHGE-----TK 119
Cdd:COG1073  10 KEDVTFKSRDGIKlagDLYLPAGASKKyPAVVVAHGNGgvkeQRALYAQRLAELGFN-----VLAFDYRGYGEsegepRE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 7706645  120 VKNPEDLSAETMAKDVGNvveamYGDLPP-PIMLIGHSMGGAIAVHTAS 167
Cdd:COG1073  85 EGSPERRDARAAVDYLRT-----LPGVDPeRIGLLGISLGGGYALNAAA 128
PRK05855 PRK05855
SDR family oxidoreductase;
69-158 5.22e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 38.81  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645    69 VYKSG-SEGPVLLLLHGGGHSALSW-AVftAAIISRvQCRIVALDLRSHGETKVknPEDLSAETMAK---DVGNVVEAMY 143
Cdd:PRK05855  17 VYEWGdPDRPTVVLVHGYPDNHEVWdGV--APLLAD-RFRVVAYDVRGAGRSSA--PKRTAAYTLARladDFAAVIDAVS 91

                         90
                 ....*....|....*
gi 7706645   144 GDlpPPIMLIGHSMG 158
Cdd:PRK05855  92 PD--RPVHLLAHDWG 104
YpfH COG0400
Predicted esterase [General function prediction only];
77-166 5.58e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 5.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706645   77 PVLLLLHGGGHSALSWAVFtAAIISRVQCRIVALD------------LRSHGETKVKNPEDLSAEtmAKDVGNVVEAM-- 142
Cdd:COG0400   6 PLVVLLHGYGGDEEDLLPL-APELALPGAAVLAPRapvpegpggrawFDLSFLEGREDEEGLAAA--AEALAAFIDELea 82

                        90       100
                ....*....|....*....|....*
gi 7706645  143 -YGDLPPPIMLIGHSMGGAIAVHTA 166
Cdd:COG0400  83 rYGIDPERIVLAGFSQGAAMALSLA 107
 
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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