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Conserved domains on  [gi|1039011896|gb|ANM61727|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 5-221 1.44e-78

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


The actual alignment was detected with superfamily member PLN02385:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 349  Bit Score: 240.42  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   5 EEDFVLNSRGMKLFTCVWKPVKQEPKALLFLCHGYAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDD 84
Cdd:PLN02385   62 EESYEVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  85 LVDDVSNHYSTICEREENKGKMRFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEIKPHPVVISILIKLAKFIP 164
Cdd:PLN02385  142 LVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILILLANLLP 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896 165 TWKIVPGNDIIDIAIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNLHQV 221
Cdd:PLN02385  222 KAKLVPQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEV 278
 
Name Accession Description Interval E-value
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 5-221 1.44e-78

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 240.42  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   5 EEDFVLNSRGMKLFTCVWKPVKQEPKALLFLCHGYAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDD 84
Cdd:PLN02385   62 EESYEVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  85 LVDDVSNHYSTICEREENKGKMRFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEIKPHPVVISILIKLAKFIP 164
Cdd:PLN02385  142 LVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILILLANLLP 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896 165 TWKIVPGNDIIDIAIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNLHQV 221
Cdd:PLN02385  222 KAKLVPQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEV 278
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 27-224 4.64e-54

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: 173.94  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  27 QEPKALLFLCHGYAmESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDDLVDDVSNHYSTIceREENKGKM 106
Cdd:pfam12146   1 GEPRAVVVLVHGLG-EHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKI--REEHPGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 107 RFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEiKPHPVVISILIKLAKFIPTWKiVPGNDIIDIAIKEPHIRN 186
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY-LAPPILKLLAKLLGKLFPRLR-VPNNLLPDSLSRDPEVVA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039011896 187 QVRENKYCyKGRPRLNTAYQLLLVSLDLEKNLHQ----VLIF 224
Cdd:pfam12146 156 AYAADPLV-HGGISARTLYELLDAGERLLRRAAAitvpLLLL 196
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-138 1.35e-29

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 110.48  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   3 MYEEDFVLNSR-GMKLFTCVWKPvKQEPKALLFLCHGYAmESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISN 81
Cdd:COG2267     1 MTRRLVTLPTRdGLRLRGRRWRP-AGSPRGTVVLVHGLG-EHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896  82 FDDLVDDVSNHYSTICEREENKgkmRFLLGESMGGAVVLLLARKKPDFWDGAVLVAP 138
Cdd:COG2267    79 FDDYVDDLRAALDALRARPGLP---VVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 53-218 7.71e-12

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 64.03  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  53 RLANAGFAVYGMDYEGHGKSEG---LNGYISNFDDLVDDV-------------------SNHYSTICEREENKGKMrFLL 110
Cdd:TIGR01607  69 NFNKNGYSVYGLDLQGHGESDGlqnLRGHINCFDDLVYDViqymnrindsiilenetksDDESYDIVNTKENRLPM-YII 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 111 GESMGGAVVL----LLARKKPDFWD----GAVLVAPMCKLA-----DEIKPHPVVISILIKLAKFIPTWKIVPGNDIidi 177
Cdd:TIGR01607 148 GLSMGGNIALrlleLLGKSNENNDKlnikGCISLSGMISIKsvgsdDSFKFKYFYLPVMNFMSRVFPTFRISKKIRY--- 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039011896 178 aIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNL 218
Cdd:TIGR01607 225 -EKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDI 264
 
Name Accession Description Interval E-value
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 5-221 1.44e-78

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 240.42  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   5 EEDFVLNSRGMKLFTCVWKPVKQEPKALLFLCHGYAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDD 84
Cdd:PLN02385   62 EESYEVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  85 LVDDVSNHYSTICEREENKGKMRFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEIKPHPVVISILIKLAKFIP 164
Cdd:PLN02385  142 LVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILILLANLLP 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896 165 TWKIVPGNDIIDIAIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNLHQV 221
Cdd:PLN02385  222 KAKLVPQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEV 278
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 5-223 1.90e-68

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 213.87  E-value: 1.90e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   5 EEDFVLNSRGMKLFTCVWKPVKQE-PKALLFLCHGYAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFD 83
Cdd:PLN02298   33 SKSFFTSPRGLSLFTRSWLPSSSSpPRALIFMVHGYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  84 DLVDDVSNHYSTICEREENKGKMRFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEIKPHPVVISILIKLAKFI 163
Cdd:PLN02298  113 LVVEDCLSFFNSVKQREEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIPQILTFVARFL 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 164 PTWKIVPGNDIIDIAIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNLHQVLI 223
Cdd:PLN02298  193 PTLAIVPTADLLEKSVKVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSI 252
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 27-224 4.64e-54

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: 173.94  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  27 QEPKALLFLCHGYAmESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDDLVDDVSNHYSTIceREENKGKM 106
Cdd:pfam12146   1 GEPRAVVVLVHGLG-EHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKI--REEHPGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 107 RFLLGESMGGAVVLLLARKKPDFWDGAVLVAPMCKLADEiKPHPVVISILIKLAKFIPTWKiVPGNDIIDIAIKEPHIRN 186
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY-LAPPILKLLAKLLGKLFPRLR-VPNNLLPDSLSRDPEVVA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039011896 187 QVRENKYCyKGRPRLNTAYQLLLVSLDLEKNLHQ----VLIF 224
Cdd:pfam12146 156 AYAADPLV-HGGISARTLYELLDAGERLLRRAAAitvpLLLL 196
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-138 1.35e-29

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 110.48  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   3 MYEEDFVLNSR-GMKLFTCVWKPvKQEPKALLFLCHGYAmESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISN 81
Cdd:COG2267     1 MTRRLVTLPTRdGLRLRGRRWRP-AGSPRGTVVLVHGLG-EHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896  82 FDDLVDDVSNHYSTICEREENKgkmRFLLGESMGGAVVLLLARKKPDFWDGAVLVAP 138
Cdd:COG2267    79 FDDYVDDLRAALDALRARPGLP---VVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 9-223 2.93e-22

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 94.19  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   9 VLNSRGMKLFTCVWKPVKQEPKALLFLCHGYAmESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDDLVDD 88
Cdd:PLN02652  115 FYGARRNALFCRSWAPAAGEMRGILIIIHGLN-EHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVED 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  89 VSNHYSTIceREENKGKMRFLLGESMGGAVVlLLARKKP---DFWDGAVLVAPmcklADEIKP-HPVVISILIKLAKFIP 164
Cdd:PLN02652  194 TEAFLEKI--RSENPGVPCFLFGHSTGGAVV-LKAASYPsieDKLEGIVLTSP----ALRVKPaHPIVGAVAPIFSLVAP 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039011896 165 TWKIVPGNDIIDIAIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNLHQVLI 223
Cdd:PLN02652  267 RFQFKGANKRGIPVSRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTV 325
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
29-221 8.27e-18

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 79.60  E-value: 8.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  29 PKALLfLCHGYaMESSITMNSAATRLANAGFAVYGMDYEGHGKS-EGLNGyiSNFDDLVDDVSNHYSTICEReenkGKMR 107
Cdd:COG1647    15 RKGVL-LLHGF-TGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSpEDLLK--TTWEDWLEDVEEAYEILKAG----YDKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 108 FLLGESMGGAVVLLLARKKPDFwDGAVLVAPMCKLADeikPHPVVISILIKLAKFIPTWkivpGNDIIDIAIKEphirnq 187
Cdd:COG1647    87 IVIGLSMGGLLALLLAARYPDV-AGLVLLSPALKIDD---PSAPLLPLLKYLARSLRGI----GSDIEDPEVAE------ 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039011896 188 vrenkYCYKGRPrLNTAYQLLLVSLDLEKNLHQV 221
Cdd:COG1647   153 -----YAYDRTP-LRALAELQRLIREVRRDLPKI 180
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
11-139 1.56e-16

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 75.82  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  11 NSRGMKLFTCVWKPVKQEPKALLFLCHGYAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGyisnfDDLVDDVS 90
Cdd:COG1506     4 SADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWG-----GDEVDDVL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039011896  91 NHYSTICEREE-NKGKMrFLLGESMGGAVVLLLARKKPDFWDGAVLVAPM 139
Cdd:COG1506    79 AAIDYLAARPYvDPDRI-GIYGHSYGGYMALLAAARHPDRFKAAVALAGV 127
PHA02857 PHA02857
monoglyceride lipase; Provisional
 10-139 1.11e-15

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 74.54  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  10 LNSRGMKLFTCVWKPVKQePKALLFLCHGyAMESSITMNSAATRLANAGFAVYGMDYEGHGKSEGLNGYISNFDDLVDDV 89
Cdd:PHA02857    6 FNLDNDYIYCKYWKPITY-PKALVFISHG-AGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDV 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039011896  90 SNHYSTIceREENKGKMRFLLGESMGGAVVLLLARKKPDFWDGAVLVAPM 139
Cdd:PHA02857   84 VQHVVTI--KSTYPGVPVFLLGHSMGATISILAAYKNPNLFTAMILMSPL 131
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 1-147 5.08e-14

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 69.56  E-value: 5.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896   1 MVMYEEDFVLNSRGMKLFTCVWKPVKQEPK-ALLFLCHGYAMESSITMNSAAtRLANAGFAVYGMDYEGHGKSEGLNGYI 79
Cdd:COG1073     7 KVNKEDVTFKSRDGIKLAGDLYLPAGASKKyPAVVVAHGNGGVKEQRALYAQ-RLAELGFNVLAFDYRGYGESEGEPREE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011896  80 SNFDDLvdDVSNHYSTICEREENKGKMRFLLGESMGGAVVLLLARKKPDFwDGAVLVAPMCKLADEIK 147
Cdd:COG1073    86 GSPERR--DARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRV-KAVILDSPFTSLEDLAA 150
PRK10749 PRK10749
lysophospholipase L2; Provisional
 58-186 2.37e-12

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 65.40  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  58 GFAVYGMDYEGHGKSEGL-----NGYISNFDDLVDDVSnhysTICEREENKG--KMRFLLGESMGGAVV-LLLARkKPDF 129
Cdd:PRK10749   81 GYDVLIIDHRGQGRSGRLlddphRGHVERFNDYVDDLA----AFWQQEIQPGpyRKRYALAHSMGGAILtLFLQR-HPGV 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011896 130 WDGAVLVAPMCkladeikphpvviSILIKLAKFIPTWkivpgndIIDIAIKEPHIRN 186
Cdd:PRK10749  156 FDAIALCAPMF-------------GIVLPLPSWMARR-------ILNWAEGHPRIRD 192
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 53-218 7.71e-12

Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in Plasmodium falciparum and Plasmodium yoelii, which are closely related to various phospholipases and lysophospholipases of plants as well as generally being related to the alpha/beta-fold superfamily of hydrolases. These genes are preferentially located in the subtelomeric regions of the chromosomes of both P. falciparum and P. yoelii.


Pssm-ID: 162444 [Multi-domain]  Cd Length: 332  Bit Score: 64.03  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  53 RLANAGFAVYGMDYEGHGKSEG---LNGYISNFDDLVDDV-------------------SNHYSTICEREENKGKMrFLL 110
Cdd:TIGR01607  69 NFNKNGYSVYGLDLQGHGESDGlqnLRGHINCFDDLVYDViqymnrindsiilenetksDDESYDIVNTKENRLPM-YII 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896 111 GESMGGAVVL----LLARKKPDFWD----GAVLVAPMCKLA-----DEIKPHPVVISILIKLAKFIPTWKIVPGNDIidi 177
Cdd:TIGR01607 148 GLSMGGNIALrlleLLGKSNENNDKlnikGCISLSGMISIKsvgsdDSFKFKYFYLPVMNFMSRVFPTFRISKKIRY--- 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039011896 178 aIKEPHIRNQVRENKYCYKGRPRLNTAYQLLLVSLDLEKNL 218
Cdd:TIGR01607 225 -EKSPYVNDIIKFDKFRYDGGITFNLASELIKATDTLDCDI 264
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 33-137 3.36e-10

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: 58.09  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  33 LFLCHGYAMeSSITMNSAATRLAnAGFAVYGMDYEGHGKSEGLNGYISnFDDLVDDVSnhysTICEREENKgkmRF-LLG 111
Cdd:COG0596    26 VVLLHGLPG-SSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYT-LDDLADDLA----ALLDALGLE---RVvLVG 95

                          90       100
                  ....*....|....*....|....*.
gi 1039011896 112 ESMGGAVVLLLARKKPDFWDGAVLVA 137
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 32-166 8.29e-09

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: 54.43  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  32 LLFLCHGYAMESSITMNSAATrLANAGFAVYGMDYEGHGKSEG---LNGYIsnFDDLVDDVSnhystiCEREENKGKMRF 108
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPA-LARDGFRVIALDLRGFGKSSRpkaQDDYR--TDDLAEDLE------YILEALGLEKVN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011896 109 LLGESMGGAVVLLLARKKPDFWDGAVLVAPmckladeIKPHPVVISILIKLAKFIPTW 166
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGA-------LDPPHELDEADRFILALFPGF 123
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
26-138 3.18e-08

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 52.09  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  26 KQEPKALLFLCH-----GYAMESSITMNsAATRLANAGFAVYGMDYEGHGKSEGlngyisNFDDLV---DDVsnhySTIC 97
Cdd:COG2945    19 EGPPRGVALILHphplfGGTMDNKVVYT-LARALVAAGFAVLRFNFRGVGRSEG------EFDEGRgelDDA----AAAL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039011896  98 E--REENKGKmRFLLGESMGGAVVLLLARKKPDFwDGAVLVAP 138
Cdd:COG2945    88 DwlRAQNPLP-LWLAGFSFGAYVALQLAMRLPEV-EGLILVAP 128
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
21-144 1.59e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.57  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  21 VWKPVKQEPKALLFLCHGyAMESSITMNSAATRLANAGFAVYGMDYEGHGK----SEGLNGYISNFDD--LVDDVSNHYS 94
Cdd:COG0412    20 LARPAGGGPRPGVVVLHE-IFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGpgddPDEARALMGALDPelLAADLRAALD 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039011896  95 TICEREENKGKMRFLLGESMGGAVVLLLARKKPDFwDGAVLVAPMCKLAD 144
Cdd:COG0412    99 WLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDL-AAAVSFYGGLPADD 147
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 33-139 3.72e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 43.62  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011896  33 LFLCHGyAMESSITMnsaaTRLANAGFAVYGMDYEGHGKSEGLNGYISNFDDLVDDVsnhysticeREENKGKMRFLLGE 112
Cdd:pfam12697   1 VVLVHG-AGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALL---------DELGAARPVVLVGH 66

                          90       100
                  ....*....|....*....|....*..
gi 1039011896 113 SMGGAVVLLLARKKPDFwdgAVLVAPM 139
Cdd:pfam12697  67 SLGGAVALAAAAAALVV---GVLVAPL 90
 
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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