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Conserved domains on  [gi|409971401|ref|NP_001258522|]
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protein phosphatase methylesterase 1 isoform b [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 4.97e-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: 82.36  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 409971401 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 4.97e-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: 82.36  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 409971401 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.
 77-370 1.53e-13

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: 69.84  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  156 SMGGAIAVHTAS--SNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAiewsvKSGQIRNLESARVsmvg 233
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPN-----PLGRLVAKLLALL---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  234 qvkqcegitspegsksivegiieeeeedeeGSESISKRKKEDDMEGLPSETQNLllflqtkKDHPYTWRIelakteKYWD 313
Cdd:pfam00561 148 ------------------------------LLRLRLLKALPLLNKRFPSGDYAL-------AKSLVTGAL------LFIE 184

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 409971401  314 GWF-RGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 370
Cdd:pfam00561 185 TWStELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 4.76e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.65  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100
                 ....*....|....*....|....*..
gi 409971401 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 4.97e-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: 82.36  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  66 TFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKvKNPEDLSAETMAKDVGNVVEAMygD 145
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDAL--G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401 146 LPPPImLIGHSMGGAIAVHTASSNlvPSLL-GLCMIDvvegtamDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNL 224
Cdd:COG0596   88 LERVV-LVGHSMGGMVALELAARH--PERVaGLVLVD-------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL 157


                 ....*
gi 409971401 225 ESARV 229
Cdd:COG0596  158 ARITV 162
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-166 8.78e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.11  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  72 SGSEGPVLLLLHGGGHSALSWAVFTAAIISRvQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIM 151
Cdd:COG2267   24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRARPGLPVV 102

                         90
                 ....*....|....*
gi 409971401 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.
 77-370 1.53e-13

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: 69.84  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   77 PVLLLLHGGGHSALSWAVFTAAIiSRVQCRIVALDLRSHGETKV-KNPEDLSAETMAKDVGNVVEAmYGDlpPPIMLIGH 155
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAL-ARDGFRVIALDLRGFGKSSRpKAQDDYRTDDLAEDLEYILEA-LGL--EKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  156 SMGGAIAVHTAS--SNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAiewsvKSGQIRNLESARVsmvg 233
Cdd:pfam00561  77 SMGGLIALAYAAkyPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPN-----PLGRLVAKLLALL---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  234 qvkqcegitspegsksivegiieeeeedeeGSESISKRKKEDDMEGLPSETQNLllflqtkKDHPYTWRIelakteKYWD 313
Cdd:pfam00561 148 ------------------------------LLRLRLLKALPLLNKRFPSGDYAL-------AKSLVTGAL------LFIE 184

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 409971401  314 GWF-RGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKF---QMQVLPQCGHAVHEDAP 370
Cdd:pfam00561 185 TWStELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpnaRLVVIPDAGHFAFLEGP 245
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-376 1.04e-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: 64.03  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   79 LLLLHGGGHSALSWAVFTAAiisrvQCRIVALDLRSHGETkVKNPEDLSAetmAKDVGNVVEAmYGDLPPPImLIGHSMG 158
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA-----GVAVLAPDLPGHGSS-SPPPLDLAD---LADLAALLDE-LGAARPVV-LVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  159 GAIAVHTASSNLVPSLLglcmIDvvegtAMDALNSMQNFLRGRPKTFKSLENAIEWsvksgqiRNLESARVSMVGQVkqc 238
Cdd:pfam12697  70 GAVALAAAAAALVVGVL----VA-----PLAAPPGLLAALLALLARLGAALAAPAW-------LAAESLARGFLDDL--- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  239 egitspegsksivegiieeeeedeegsesiskrkkeddmeglpsetqnlllflqtkkDHPYTWRIELAKTEKYWDGWFRG 318
Cdd:pfam12697 131 ---------------------------------------------------------PADAEWAAALARLAALLAALALL 153

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  319 LSNLFLSCPIPkLLLLAGVDRLDKDLT--IGQMQGKFQMQVLPQCGHAVHEDaPDKVAEA 376
Cdd:pfam12697 154 PLAAWRDLPVP-VLVLAEEDRLVPELAqrLLAALAGARLVVLPGAGHLPLDD-PEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 61-166 4.76e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.65  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  61 ETGKDTFRVYKSGSE-GPVLLLLHGGGHSALSWaVFTAAIISRVQcRIVALDLRSHGETkVKNPEDLSAETMAKDVGNVV 139
Cdd:PRK14875 115 RIGGRTVRYLRLGEGdGTPVVLIHGFGGDLNNW-LFNHAALAAGR-PVIALDLPGHGAS-SKAVGAGSLDELAAAVLAFL 191

                         90       100
                 ....*....|....*....|....*..
gi 409971401 140 EAMYgdlPPPIMLIGHSMGGAIAVHTA 166
Cdd:PRK14875 192 DALG---IERAHLVGHSMGGAVALRLA 215
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
77-167 4.90e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.40  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETkvknpEDLSAETMAKDVGNVVEAM----YGDlPPPIML 152
Cdd:COG1506   24 PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGES-----AGDWGGDEVDDVLAAIDYLaarpYVD-PDRIGI 97

                         90
                 ....*....|....*
gi 409971401 153 IGHSMGGAIAVHTAS 167
Cdd:COG1506   98 YGHSYGGYMALLAAA 112
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 39-166 5.31e-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: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   39 RDFSPVPWSQYfesmeDVEVENETGKDTFRVYKSG--SEGPVLLLLHGGGHSALSWAVFTAAIISRVQCriVALDLRSHG 116
Cdd:PLN02980 1337 RTFKEEQVRTY-----ELRVDVDGFSCLIKVHEVGqnAEGSVVLFLHGFLGTGEDWIPIMKAISGSARC--ISIDLPGHG 1409

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 409971401  117 ETKVKNPEDLSAETMAKDVGNVVEAMYGDL----PPPIMLIGHSMGGAIAVHTA 166
Cdd:PLN02980 1410 GSKIQNHAKETQTEPTLSVELVADLLYKLIehitPGKVTLVGYSMGARIALYMA 1463
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 77-162 1.82e-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: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  77 PVLLLlHGGGHSALSWAVFTAAIISRVQCrIVALDLrshgetkvkNPEDLSAETMAKDVGNVVEAMYGDLP-PPIMLIGH 155
Cdd:COG1075    7 PVVLV-HGLGGSAASWAPLAPRLRAAGYP-VYALNY---------PSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGH 75


                 ....*..
gi 409971401 156 SMGGAIA 162
Cdd:COG1075   76 SMGGLVA 82
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-166 1.87e-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: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   78 VLLLLHGGG-HS-----------ALSWAVFtaaiisrvqcrivALDLRSHGETK-----VKNPEDlsaetMAKDVGNVVE 140
Cdd:pfam12146   6 VVVLVHGLGeHSgryahladalaAQGFAVY-------------AYDHRGHGRSDgkrghVPSFDD-----YVDDLDTFVD 67

                          90       100
                  ....*....|....*....|....*..
gi 409971401  141 AMYGDLP-PPIMLIGHSMGGAIAVHTA 166
Cdd:pfam12146  68 KIREEHPgLPLFLLGHSMGGLIAALYA 94
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
68-166 9.45e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 43.32  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  68 RVY---KSGSEGPVLLLLHGGGHSALSWAVFT---AAIISRVQCRIVALDLRSHGETKvknpedlsAETMAKDVGNVVEA 141
Cdd:COG0657    2 DVYrpaGAKGPLPVVVYFHGGGWVSGSKDTHDplaRRLAARAGAAVVSVDYRLAPEHP--------FPAALEDAYAALRW 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 409971401 142 M------YGDLPPPIMLIGHSMGGAIAVHTA 166
Cdd:COG0657   74 LranaaeLGIDPDRIAVAGDSAGGHLAAALA 104
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
80-214 1.03e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.39  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  80 LLLHG-GG--HSALSWAVFTAAIisrvQCRIVALDLRSHGETkvknPEDLSAETmAKDVGNVVEAMYGDL---PPPIMLI 153
Cdd:COG1647   19 LLLHGfTGspAEMRPLAEALAKA----GYTVYAPRLPGHGTS----PEDLLKTT-WEDWLEDVEEAYEILkagYDKVIVI 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409971401 154 GHSMGGAIAVHTASSNlvPSLLGLCMID---VVEGTAM---DALNSMQNFLRGRPKTFKSLENAIEW 214
Cdd:COG1647   90 GLSMGGLLALLLAARY--PDVAGLVLLSpalKIDDPSApllPLLKYLARSLRGIGSDIEDPEVAEYA 154
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 72-166 2.30e-04

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 42.15  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  72 SGSEGPVLLLLH--GGGHSA-LSWAVFTAAiisrvQCRIVALDLRSHgetkvknpEDLSAETMAKDVGNVVEAMYGDLPP 148
Cdd:COG3208    2 RPDARLRLFCFPyaGGSASAyRPWAAALPP-----DIEVLAVQLPGR--------GDRLGEPPLTSLEELADDLAEELAP 68

                         90       100
                 ....*....|....*....|..
gi 409971401 149 ----PIMLIGHSMGGAIAVHTA 166
Cdd:COG3208   69 lldrPFALFGHSMGALLAFELA 90
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 76-185 1.18e-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: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  76 GPVLLLLHGGGHSALSWAvftaAIISRV-QCRIVALDLRSHGEtkvknpedlSAETMAKDVGNVVE------AMYGDLPp 148
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQ----PVGEALpDYPRLYIDLPGHGG---------SAAISVDGFADVSRllsqtlQSYNILP- 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 409971401 149 pIMLIGHSMGGAIAVHTASSNLVPSLLGLCmidvVEG 185
Cdd:PRK11126  68 -YWLVGYSLGGRIAMYYACQGLAGGLCGLI----VEG 99
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 68-182 3.38e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 38.95  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  68 RVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRvqCRIVALDLRSHGETKVKNPEDLSA------ETMAKDVGNVVEA 141
Cdd:PLN02824  21 RYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKS--HRVYAIDLLGYGYSDKPNPRSAPPnsfytfETWGEQLNDFCSD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 409971401 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 3.98e-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: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401   77 PVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAEtmakdvgnVVEAMYGDLPP-PIMLIGH 155
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADE--------YAEALRQIQPEgPYALFGH 72

                          90
                  ....*....|..
gi 409971401  156 SMGGAIAVHTAS 167
Cdd:pfam00975  73 SMGGMLAFEVAR 84
PRK05855 PRK05855
SDR family oxidoreductase;
69-158 4.33e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 39.19  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  69 VYKSG-SEGPVLLLLHGGGHSALSW-AVftAAIISRvQCRIVALDLRSHGETKVknPEDLSAETMAK---DVGNVVEAMY 143
Cdd:PRK05855  17 VYEWGdPDRPTVVLVHGYPDNHEVWdGV--APLLAD-RFRVVAYDVRGAGRSSA--PKRTAAYTLARladDFAAVIDAVS 91

                         90
                 ....*....|....*
gi 409971401 144 GDlpPPIMLIGHSMG 158
Cdd:PRK05855  92 PD--RPVHLLAHDWG 104
PRK10673 PRK10673
esterase;
107-182 4.85e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 38.56  E-value: 4.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409971401 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 5.01e-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: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  53 MEDVEVENETGKD---TFRVYKSGSEG-PVLLLLHGGG----HSALSWAVFTAAIISrvqcrIVALDLRSHGE-----TK 119
Cdd:COG1073   10 KEDVTFKSRDGIKlagDLYLPAGASKKyPAVVVAHGNGgvkeQRALYAQRLAELGFN-----VLAFDYRGYGEsegepRE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 409971401 120 VKNPEDLSAETMAKDVGNvveamYGDLPP-PIMLIGHSMGGAIAVHTAS 167
Cdd:COG1073   85 EGSPERRDARAAVDYLRT-----LPGVDPeRIGLLGISLGGGYALNAAA 128
YpfH COG0400
Predicted esterase [General function prediction only];
77-166 5.96e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409971401  77 PVLLLLHGGGHSALSWAVFtAAIISRVQCRIVALD------------LRSHGETKVKNPEDLSAEtmAKDVGNVVEAM-- 142
Cdd:COG0400    6 PLVVLLHGYGGDEEDLLPL-APELALPGAAVLAPRapvpegpggrawFDLSFLEGREDEEGLAAA--AEALAAFIDELea 82

                         90       100
                 ....*....|....*....|....*
gi 409971401 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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