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Conserved domains on  [gi|1034574201|ref|XP_016873402|]
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protein phosphatase methylesterase 1 isoform X2 [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 6.67e-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: 82.74  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596    88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                  ....*
gi 1034574201 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 6.67e-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: 82.74  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596    88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                  ....*
gi 1034574201 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.
 77-200 7.03e-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: 69.46  E-value: 7.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034574201 156 SMGGAIAVHTAS--SNLVPS--LLGLCMIDVVEGTAMD-ALNSMQNFLRG 200
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKAlvLLGALDPPHELDEADRfILALFPGFFDG 126
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 3.66e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875  115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                          90       100
                  ....*....|....*....|....*..
gi 1034574201 140 EAMYgdlPPPIMLIGHSMGGAIAVHTA 166
Cdd:PRK14875  192 DALG---IERAHLVGHSMGGAVALRLA 215
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 127-162 8.82e-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: 35.94  E-value: 8.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034574201 127 SAETMAKDVGNVVEAMYGDLPP-PIMLIGHSMGGAIA 162
Cdd:cd00741     6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALA 42
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-229 6.67e-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: 82.74  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596    13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596    88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                  ....*
gi 1034574201 225 ESARV 229
Cdd:COG0596   158 ARITV 162
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-166 1.83e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.50  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  72 SGSEGPVLLLLHGGGHSALSWAVFTAAIISRvQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIM 151
Cdd:COG2267    24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGLPVV 102

                          90
                  ....*....|....*
gi 1034574201 152 LIGHSMGGAIAVHTA 166
Cdd:COG2267   103 LLGHSMGGLIALLYA 117
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 77-200 7.03e-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: 69.46  E-value: 7.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034574201 156 SMGGAIAVHTAS--SNLVPS--LLGLCMIDVVEGTAMD-ALNSMQNFLRG 200
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKAlvLLGALDPPHELDEADRfILALFPGFFDG 126
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-175 7.60e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 60.18  E-value: 7.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  79 LLLLHGGGHSALSWAVFTAAiisrvQCRIVALDLRSHGETkVKNPEDLSAetmAKDVGNVVEAmYGDLPPPImLIGHSMG 158
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA-----GVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDE-LGAARPVV-LVGHSLG 69

                          90
                  ....*....|....*..
gi 1034574201 159 GAIAVHTASSNLVPSLL 175
Cdd:pfam12697  70 GAVALAAAAAALVVGVL 86
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 3.66e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875  115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                          90       100
                  ....*....|....*....|....*..
gi 1034574201 140 EAMYgdlPPPIMLIGHSMGGAIAVHTA 166
Cdd:PRK14875  192 DALG---IERAHLVGHSMGGAVALRLA 215
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
77-167 2.20e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.40  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETkvknpEDLSAETMAKDVGNVVEAM----YGDlPPPIML 152
Cdd:COG1506    24 PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAIDYLaarpYVD-PDRIGI 97

                          90
                  ....*....|....*
gi 1034574201 153 IGHSMGGAIAVHTAS 167
Cdd:COG1506    98 YGHSYGGYMALLAAA 112
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 39-166 3.05e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 48.31  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201   39 RDFSPVPWSQYfesmeDVEVENETGKDTFRVYKSG--SEGPVLLLLHGGGHSALSWAVFTAAIISRVQCriVALDLRSHG 116
Cdd:PLN02980  1337 RTFKEEQVRTY-----ELRVDVDGFSCLIKVHEVGqnAEGSVVLFLHGFLGTGEDWIPIMKAISGSARC--ISIDLPGHG 1409

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034574201  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 8.60e-06

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: 8.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  78 VLLLLHGGG-HS-----------ALSWAVFtaaiisrvqcrivALDLRSHGETK-----VKNPEDlsaetMAKDVGNVVE 140
Cdd:pfam12146   6 VVVLVHGLGeHSgryahladalaAQGFAVY-------------AYDHRGHGRSDgkrghVPSFDD-----YVDDLDTFVD 67

                          90       100
                  ....*....|....*....|....*..
gi 1034574201 141 AMYGDLP-PPIMLIGHSMGGAIAVHTA 166
Cdd:pfam12146  68 KIREEHPgLPLFLLGHSMGGLIAALYA 94
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 77-162 1.52e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 42.89  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLlHGGGHSALSWAVFTAAIISRVQCrIVALDLrshgetkvkNPEDLSAETMAKDVGNVVEAMYGDLP-PPIMLIGH 155
Cdd:COG1075     7 PVVLV-HGLGGSAASWAPLAPRLRAAGYP-VYALNY---------PSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGH 75


                  ....*..
gi 1034574201 156 SMGGAIA 162
Cdd:COG1075    76 SMGGLVA 82
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
80-214 3.96e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.78  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  80 LLLHG-GG--HSALSWAVFTAAIisrvQCRIVALDLRSHGEtkvkNPEDLSAETmAKDVGNVVEAMYGDL---PPPIMLI 153
Cdd:COG1647    19 LLLHGfTGspAEMRPLAEALAKA----GYTVYAPRLPGHGT----SPEDLLKTT-WEDWLEDVEEAYEILkagYDKVIVI 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574201 154 GHSMGGAIAVHTASSNlvPSLLGLCMID---VVEGTAM---DALNSMQNFLRGRPKTFKSLENAIEW 214
Cdd:COG1647    90 GLSMGGLLALLLAARY--PDVAGLVLLSpalKIDDPSApllPLLKYLARSLRGIGSDIEDPEVAEYA 154
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-166 4.32e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 43.32  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  68 RVY---KSGSEGPVLLLLHGGGHSALSWAVFT---AAIISRVQCRIVALDLRSHGETKvknpedlsAETMAKDVGNVVEA 141
Cdd:COG0657     2 DVYrpaGAKGPLPVVVYFHGGGWVSGSKDTHDplaRRLAARAGAAVVSVDYRLAPEHP--------FPAALEDAYAALRW 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034574201 142 M------YGDLPPPIMLIGHSMGGAIAVHTA 166
Cdd:COG0657    74 LranaaeLGIDPDRIAVAGDSAGGHLAAALA 104
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 72-166 7.44e-05

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 42.92  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  72 SGSEGPVLLLLH--GGGHSA-LSWAVFTAAiisrvQCRIVALDLRSHgetkvknpEDLSAETMAKDVGNVVEAMYGDLPP 148
Cdd:COG3208     2 RPDARLRLFCFPyaGGSASAyRPWAAALPP-----DIEVLAVQLPGR--------GDRLGEPPLTSLEELADDLAEELAP 68

                          90       100
                  ....*....|....*....|..
gi 1034574201 149 ----PIMLIGHSMGGAIAVHTA 166
Cdd:COG3208    69 lldrPFALFGHSMGALLAFELA 90
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 76-185 5.60e-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: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  76 GPVLLLLHGGGHSALSWAvftaAIISRV-QCRIVALDLRSHGEtkvknpedlSAETMAKDVGNVVE------AMYGDLPp 148
Cdd:PRK11126    2 LPWLVFLHGLLGSGQDWQ----PVGEALpDYPRLYIDLPGHGG---------SAAISVDGFADVSRllsqtlQSYNILP- 67

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034574201 149 pIMLIGHSMGGAIAVHTASSNLVPSLLGLCmidvVEG 185
Cdd:PRK11126   68 -YWLVGYSLGGRIAMYYACQGLAGGLCGLI----VEG 99
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 68-182 1.24e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 39.72  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  68 RVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKVKNPEDLSA------ETMAKDVGNVVEA 141
Cdd:PLN02824   21 RYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKS--HRVYAIDLLGYGYSDKPNPRSAPPnsfytfETWGEQLNDFCSD 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034574201 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 2.16e-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: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAEtmakdvgnVVEAMYGDLPP-PIMLIGH 155
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADE--------YAEALRQIQPEgPYALFGH 72

                          90
                  ....*....|..
gi 1034574201 156 SMGGAIAVHTAS 167
Cdd:pfam00975  73 SMGGMLAFEVAR 84
YpfH COG0400
Predicted esterase [General function prediction only];
77-166 2.39e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  77 PVLLLLHGGGHSALSWAVFtAAIISRVQCRIVALD------------LRSHGETKVKNPEDLSAEtmAKDVGNVVEAM-- 142
Cdd:COG0400     6 PLVVLLHGYGGDEEDLLPL-APELALPGAAVLAPRapvpegpggrawFDLSFLEGREDEEGLAAA--AEALAAFIDELea 82

                          90       100
                  ....*....|....*....|....*
gi 1034574201 143 -YGDLPPPIMLIGHSMGGAIAVHTA 166
Cdd:COG0400    83 rYGIDPERIVLAGFSQGAAMALSLA 107
PRK10673 PRK10673
esterase;
107-182 2.76e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 38.56  E-value: 2.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574201 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 2.85e-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: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  53 MEDVEVENETGKD---TFRVYKSGSEG-PVLLLLHGGG----HSALSWAVFTAAIISrvqcrIVALDLRSHGE-----TK 119
Cdd:COG1073    10 KEDVTFKSRDGIKlagDLYLPAGASKKyPAVVVAHGNGgvkeQRALYAQRLAELGFN-----VLAFDYRGYGEsegepRE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034574201 120 VKNPEDLSAETMAKDVGNvveamYGDLPP-PIMLIGHSMGGAIAVHTAS 167
Cdd:COG1073    85 EGSPERRDARAAVDYLRT-----LPGVDPeRIGLLGISLGGGYALNAAA 128
PRK05855 PRK05855
SDR family oxidoreductase;
69-158 3.70e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 38.42  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  69 VYKSG-SEGPVLLLLHGGGHSALSW-AVftAAIISRvQCRIVALDLRSHGETKVknPEDLSAETMAK---DVGNVVEAMY 143
Cdd:PRK05855   17 VYEWGdPDRPTVVLVHGYPDNHEVWdGV--APLLAD-RFRVVAYDVRGAGRSSA--PKRTAAYTLARladDFAAVIDAVS 91

                          90
                  ....*....|....*
gi 1034574201 144 GDlpPPIMLIGHSMG 158
Cdd:PRK05855   92 PD--RPVHLLAHDWG 104
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
54-169 7.40e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 36.87  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574201  54 EDVEVENETGkDTFRVY----KSGSEGPVLLLLHG-GGHSAlsWAVFTAAIISRVQCRIVALDLRSHGETkVKNPED--- 125
Cdd:COG0412     4 ETVTIPTPDG-VTLPGYlarpAGGGPRPGVVVLHEiFGLNP--HIRDVARRLAAAGYVVLAPDLYGRGGP-GDDPDEara 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034574201 126 ----LSAETMAKDVGNVVEAMYGDL---PPPIMLIGHSMGGAIAVHTASSN 169
Cdd:COG0412    80 lmgaLDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARG 130
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 127-162 8.82e-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: 35.94  E-value: 8.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034574201 127 SAETMAKDVGNVVEAMYGDLPP-PIMLIGHSMGGAIA 162
Cdd:cd00741     6 AARSLANLVLPLLKSALAQYPDyKIHVTGHSLGGALA 42
 
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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