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Conserved domains on  [gi|15233203|ref|NP_191079|]
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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, ...
 11-297 4.65e-98

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 PLN02298:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 330  Bit Score: 292.45  E-value: 4.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   11 SEEFIENSRGMQLLTCKWFPVNQE-PRALIFFCHGYAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFD 89
Cdd:PLN02298  33 SKSFFTSPRGLSLFTRSWLPSSSSpPRALIFMVHGYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   90 LLIDDVSSHFSKISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEEMKPSRMVISMINMVTNLI 169
Cdd:PLN02298 113 LVVEDCLSFFNSVKQREEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIPQILTFVARFL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  170 PSWkSIIHGPDILNSAIKLPEKRHEIRTNPNCYNGWPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSK 249
Cdd:PLN02298 193 PTL-AIVPTADLLEKSVKVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSR 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15233203  250 LLYEVALSNDKTLKLYPEMWHSLLFGEPPENSEIVFNDIVQWMQTRIT 297
Cdd:PLN02298 272 ALYEEAKSEDKTIKIYDGMMHSLLFGEPDENIEIVRRDILSWLNERCT 319
 
Name Accession Description Interval E-value
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 11-297 4.65e-98

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 292.45  E-value: 4.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   11 SEEFIENSRGMQLLTCKWFPVNQE-PRALIFFCHGYAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFD 89
Cdd:PLN02298  33 SKSFFTSPRGLSLFTRSWLPSSSSpPRALIFMVHGYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   90 LLIDDVSSHFSKISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEEMKPSRMVISMINMVTNLI 169
Cdd:PLN02298 113 LVVEDCLSFFNSVKQREEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIPQILTFVARFL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  170 PSWkSIIHGPDILNSAIKLPEKRHEIRTNPNCYNGWPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSK 249
Cdd:PLN02298 193 PTL-AIVPTADLLEKSVKVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSR 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15233203  250 LLYEVALSNDKTLKLYPEMWHSLLFGEPPENSEIVFNDIVQWMQTRIT 297
Cdd:PLN02298 272 ALYEEAKSEDKTIKIYDGMMHSLLFGEPDENIEIVRRDILSWLNERCT 319
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 33-277 1.23e-65

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: 206.30  E-value: 1.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    33 QEPRALIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFDLLIDDVSSHFSKISEmgDNTKKK 112
Cdd:pfam12146   1 GEPRAVVVLVHGLG-EHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIRE--EHPGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   113 RFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEeMKPSRMVISMINMVTNLIPSWKsiIHGPDILNSAIKLPEKR 192
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKP-YLAPPILKLLAKLLGKLFPRLR--VPNNLLPDSLSRDPEVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   193 HEIRTNPNCYNGwPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLYEVALSNDKTLKLYPEMWHSL 272
Cdd:pfam12146 155 AAYAADPLVHGG-ISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHEL 233


                  ....*
gi 15233203   273 LFgEP 277
Cdd:pfam12146 234 LN-EP 237
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-293 3.57e-34

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 124.34  E-value: 3.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  12 EEFIENSRGMQLLTCKWFPvNQEPRALIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFDLL 91
Cdd:COG2267   5 LVTLPTRDGLRLRGRRWRP-AGSPRGTVVLVHGLG-EHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  92 IDDVsSHFskISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPmckiaeemkpsrmvisminmvtnlips 171
Cdd:COG2267  83 VDDL-RAA--LDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP--------------------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 172 wkSIIHGPDILNSAiklpekrheirtnpncynGWPRmktmselfriSLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLL 251
Cdd:COG2267 133 --AYRADPLLGPSA------------------RWLR----------ALRLAEALARIDVPVLVLHGGADRVVPPEAARRL 182

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15233203 252 YEvALSNDKTLKLYPEMWHSLLFGeppENSEIVFNDIVQWMQ 293
Cdd:COG2267 183 AA-RLSPDVELVLLPGARHELLNE---PAREEVLAAILAWLE 220
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 59-293 3.48e-11

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: 63.26  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    59 KFAKEGFAVHGIEYEGHGRSSG---LSVYIDNFDLLIDDVSSHFSKISE---------MGD------NTKKKR---FLMG 117
Cdd:TIGR01607  69 NFNKNGYSVYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetkSDDesydivNTKENRlpmYIIG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   118 ESMGGAVVLL---LHRKKPEFWD-----GGILIAPMCKIAE-----EMKPSRMVISMINMV-----TNLIPSWKSIIHGP 179
Cdd:TIGR01607 149 LSMGGNIALRlleLLGKSNENNDklnikGCISLSGMISIKSvgsddSFKFKYFYLPVMNFMsrvfpTFRISKKIRYEKSP 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   180 DIlNSAIKLPEKRheirtnpncYNGWPRMKTMSELFRISLDLENRLNEV--TMPFIVLHGEDDKVTDKGGSKLLYEVALS 257
Cdd:TIGR01607 229 YV-NDIIKFDKFR---------YDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSI 298

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15233203   258 NDKTLKLYPEMWHSLLFgEPpeNSEIVFNDIVQWMQ 293
Cdd:TIGR01607 299 SNKELHTLEDMDHVITI-EP--GNEEVLKKIIEWIS 331
 
Name Accession Description Interval E-value
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 11-297 4.65e-98

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 292.45  E-value: 4.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   11 SEEFIENSRGMQLLTCKWFPVNQE-PRALIFFCHGYAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFD 89
Cdd:PLN02298  33 SKSFFTSPRGLSLFTRSWLPSSSSpPRALIFMVHGYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   90 LLIDDVSSHFSKISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEEMKPSRMVISMINMVTNLI 169
Cdd:PLN02298 113 LVVEDCLSFFNSVKQREEFQGLPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCKISDKIRPPWPIPQILTFVARFL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  170 PSWkSIIHGPDILNSAIKLPEKRHEIRTNPNCYNGWPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSK 249
Cdd:PLN02298 193 PTL-AIVPTADLLEKSVKVPAKKIIAKRNPMRYNGKPRLGTVVELLRVTDYLGKKLKDVSIPFIVLHGSADVVTDPDVSR 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15233203  250 LLYEVALSNDKTLKLYPEMWHSLLFGEPPENSEIVFNDIVQWMQTRIT 297
Cdd:PLN02298 272 ALYEEAKSEDKTIKIYDGMMHSLLFGEPDENIEIVRRDILSWLNERCT 319
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 8-297 3.95e-96

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 288.19  E-value: 3.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    8 VGYSEEFIENSRGMQLLTCKWFPVNQEPRALIFFCHGYAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDN 87
Cdd:PLN02385  59 IKTEESYEVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   88 FDLLIDDVSSHFSKISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEEMKPSRMVISMINMVTN 167
Cdd:PLN02385 139 FDDLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPNAWDGAILVAPMCKIADDVVPPPLVLQILILLAN 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  168 LIPSWKsIIHGPDILNSAIKLPEKRHEIRTNPNCYNGWPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGG 247
Cdd:PLN02385 219 LLPKAK-LVPQKDLAELAFRDLKKRKMAEYNVIAYKDKPRLRTAVELLRTTQEIEMQLEEVSLPLLILHGEADKVTDPSV 297

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15233203  248 SKLLYEVALSNDKTLKLYPEMWHSLLFGEPPENSEIVFNDIVQWMQTRIT 297
Cdd:PLN02385 298 SKFLYEKASSSDKKLKLYEDAYHSILEGEPDEMIFQVLDDIISWLDSHST 347
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 33-277 1.23e-65

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: 206.30  E-value: 1.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    33 QEPRALIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFDLLIDDVSSHFSKISEmgDNTKKK 112
Cdd:pfam12146   1 GEPRAVVVLVHGLG-EHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIRE--EHPGLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   113 RFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEeMKPSRMVISMINMVTNLIPSWKsiIHGPDILNSAIKLPEKR 192
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKP-YLAPPILKLLAKLLGKLFPRLR--VPNNLLPDSLSRDPEVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   193 HEIRTNPNCYNGwPRMKTMSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLYEVALSNDKTLKLYPEMWHSL 272
Cdd:pfam12146 155 AAYAADPLVHGG-ISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHEL 233


                  ....*
gi 15233203   273 LFgEP 277
Cdd:pfam12146 234 LN-EP 237
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 1-296 1.44e-34

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 130.01  E-value: 1.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    1 MAHVDGQVGYSEEFIENSRGMQLLTCKWFPVNQEPRALIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSG 80
Cdd:PLN02652 101 MVEDGEGTRWATSLFYGARRNALFCRSWAPAAGEMRGILIIIHGLN-EHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   81 LSVYIDNFDLLIDDVSSHFSKIseMGDNTKKKRFLMGESMGGAVVL--LLHRKKPEFWDGGILIAPmckiAEEMKPSRMV 158
Cdd:PLN02652 180 LHGYVPSLDYVVEDTEAFLEKI--RSENPGVPCFLFGHSTGGAVVLkaASYPSIEDKLEGIVLTSP----ALRVKPAHPI 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  159 ISMINMVTNLI-PSWKsiIHGPDILNSAI-KLPEKRHEIRTNPNCYNGWPRMKTMSELFRISLDLENRLNEVTMPFIVLH 236
Cdd:PLN02652 254 VGAVAPIFSLVaPRFQ--FKGANKRGIPVsRDPAALLAKYSDPLVYTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLH 331

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  237 GEDDKVTDKGGSKLLYEVALSNDKTLKLYPEMWHSLLFgePPENSEIVfNDIVQWMQTRI 296
Cdd:PLN02652 332 GTADRVTDPLASQDLYNEAASRHKDIKLYDGFLHDLLF--EPEREEVG-RDIIDWMEKRL 388
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-293 3.57e-34

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 124.34  E-value: 3.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  12 EEFIENSRGMQLLTCKWFPvNQEPRALIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFDLL 91
Cdd:COG2267   5 LVTLPTRDGLRLRGRRWRP-AGSPRGTVVLVHGLG-EHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  92 IDDVsSHFskISEMGDNTKKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPmckiaeemkpsrmvisminmvtnlips 171
Cdd:COG2267  83 VDDL-RAA--LDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP--------------------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 172 wkSIIHGPDILNSAiklpekrheirtnpncynGWPRmktmselfriSLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLL 251
Cdd:COG2267 133 --AYRADPLLGPSA------------------RWLR----------ALRLAEALARIDVPVLVLHGGADRVVPPEAARRL 182

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15233203 252 YEvALSNDKTLKLYPEMWHSLLFGeppENSEIVFNDIVQWMQ 293
Cdd:COG2267 183 AA-RLSPDVELVLLPGARHELLNE---PAREEVLAAILAWLE 220
PHA02857 PHA02857
monoglyceride lipase; Provisional
 24-296 1.83e-21

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 91.87  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   24 LTCKWFPVNQEPRALIFFCHGyAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFDLLIDDVSSHFSKIS 103
Cdd:PHA02857  13 IYCKYWKPITYPKALVFISHG-AGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVRDVVQHVVTIK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  104 EMGDNTKKkrFLMGESMGGAVVLLLHRKKPEFWDGGILIAPMCKiAEEMkpSRMVISMINMVTNLIPSwkSIIHGpdiLN 183
Cdd:PHA02857  92 STYPGVPV--FLLGHSMGATISILAAYKNPNLFTAMILMSPLVN-AEAV--PRLNLLAAKLMGIFYPN--KIVGK---LC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  184 SAIKLPEKRHEIRTNPNCYNGWPRMKT--MSELFRISLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLYEVALSnDKT 261
Cdd:PHA02857 162 PESVSRDMDEVYKYQYDPLVNHEKIKAgfASQVLKATNKVRKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANC-NRE 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15233203  262 LKLYPEMWHSlLFGEPPENSEIVFNDIVQWMQTRI 296
Cdd:PHA02857 241 IKIYEGAKHH-LHKETDEVKKSVMKEIETWIFNRV 274
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
30-292 7.18e-21

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 89.31  E-value: 7.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  30 PVNQEPRALIFFCHGYAIDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGlsvyiDNFDLLIDDVSSHFSKISEMGDNT 109
Cdd:COG1506  17 PADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAG-----DWGGDEVDDVLAAIDYLAARPYVD 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 110 KKKRFLMGESMGGAVVLLLHRKKPEFWDGGILIAPmckiaeemkpsrmvisminmVTNlipsWKSIIHGPDILNSAiklp 189
Cdd:COG1506  92 PDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG--------------------VSD----LRSYYGTTREYTER---- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 190 ekrheirtnpncYNGWPRmkTMSELFRiSLDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLYEVALSN--DKTLKLYPE 267
Cdd:COG1506 144 ------------LMGGPW--EDPEAYA-ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkPVELLVYPG 208

                       250       260
                ....*....|....*....|....*
gi 15233203 268 MWHSLLFGEPPEnseiVFNDIVQWM 292
Cdd:COG1506 209 EGHGFSGAGAPD----YLERILDFL 229
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 3-294 1.48e-18

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 83.43  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   3 HVDGQVGYSEEFIENSRGMQLLTCKWFPVN-QEPRALIFFCHGYAIDCSTTFkDIAPKFAKEGFAVHGIEYEGHGRSSGL 81
Cdd:COG1073   3 PPSDKVNKEDVTFKSRDGIKLAGDLYLPAGaSKKYPAVVVAHGNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  82 SVYIDNFDllIDDVSSHFSKISEMGDNTKKKRFLMGESMGGAVVLLLhrkkpefwdggiliapmckiAEEMKPSRMVISm 161
Cdd:COG1073  82 PREEGSPE--RRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNA--------------------AATDPRVKAVIL- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 162 INMVTNLipswksiihgPDILNSAIKLPEKRHeirTNPNCYngWPRMkTMSELFRISLDLENRLNEVTMPFIVLHGEDDK 241
Cdd:COG1073 139 DSPFTSL----------EDLAAQRAKEARGAY---LPGVPY--LPNV-RLASLLNDEFDPLAKIEKISRPLLFIHGEKDE 202

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233203 242 VTDKGGSKLLYEvALSNDKTLKLYPEMWHSLLFGEPPensEIVFNDIVQWMQT 294
Cdd:COG1073 203 AVPFYMSEDLYE-AAAEPKELLIVPGAGHVDLYDRPE---EEYFDKLAEFFKK 251
PST-A TIGR01607
Plasmodium subtelomeric family (PST-A); This model represents a paralogous family of genes in ...
 59-293 3.48e-11

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: 63.26  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    59 KFAKEGFAVHGIEYEGHGRSSG---LSVYIDNFDLLIDDVSSHFSKISE---------MGD------NTKKKR---FLMG 117
Cdd:TIGR01607  69 NFNKNGYSVYGLDLQGHGESDGlqnLRGHINCFDDLVYDVIQYMNRINDsiilenetkSDDesydivNTKENRlpmYIIG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   118 ESMGGAVVLL---LHRKKPEFWD-----GGILIAPMCKIAE-----EMKPSRMVISMINMV-----TNLIPSWKSIIHGP 179
Cdd:TIGR01607 149 LSMGGNIALRlleLLGKSNENNDklnikGCISLSGMISIKSvgsddSFKFKYFYLPVMNFMsrvfpTFRISKKIRYEKSP 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   180 DIlNSAIKLPEKRheirtnpncYNGWPRMKTMSELFRISLDLENRLNEV--TMPFIVLHGEDDKVTDKGGSKLLYEVALS 257
Cdd:TIGR01607 229 YV-NDIIKFDKFR---------YDGGITFNLASELIKATDTLDCDIDYIpkDIPILFIHSKGDCVCSYEGTVSFYNKLSI 298

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15233203   258 NDKTLKLYPEMWHSLLFgEPpeNSEIVFNDIVQWMQ 293
Cdd:TIGR01607 299 SNKELHTLEDMDHVITI-EP--GNEEVLKKIIEWIS 331
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 39-289 2.59e-09

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: 56.55  E-value: 2.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203  39 IFFCHGYAiDCSTTFKDIAPKFAkEGFAVHGIEYEGHGRSSGLSVYIDnFDLLIDDVSSHfskISEMGDntkkKRF-LMG 117
Cdd:COG0596  26 VVLLHGLP-GSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYT-LDDLADDLAAL---LDALGL----ERVvLVG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 118 ESMGGAVVLLLHRKKPEFWDGGILIAPMCKIAEEMkpsrmvisminmvtnlipsWKSIIHGPDILNSAIKLPEKRheirt 197
Cdd:COG0596  96 HSMGGMVALELAARHPERVAGLVLVDEVLAALAEP-------------------LRRPGLAPEALAALLRALART----- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203 198 npncyngwprmktmselfrislDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLYEvaLSNDKTLKLYPEMWHSLLFGEP 277
Cdd:COG0596 152 ----------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLAE--LLPNAELVVLPGAGHFPPLEQP 207

                       250
                ....*....|..
gi 15233203 278 PEnseivFNDIV 289
Cdd:COG0596 208 EA-----FAAAL 214
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 38-277 3.19e-08

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: 53.66  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    38 LIFFCHGYAiDCSTTFKDIAPKFAKEGFAVHGIEYEGHGRSSGLsvyIDNFDLLIDDVSSHFSKISEMGDNTKKkrFLMG 117
Cdd:pfam00561   2 PVLLLHGLP-GSSDLWRKLAPALARDGFRVIALDLRGFGKSSRP---KAQDDYRTDDLAEDLEYILEALGLEKV--NLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   118 ESMGGAVVLLLHRKKPEFWDGGILIAPmckIAEEMKPSRMVISMIN---MVTNLIPSWKSIIHGPDILNSAIKLPEKRHE 194
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALVLLGA---LDPPHELDEADRFILAlfpGFFDGFVADFAPNPLGRLVAKLLALLLLRLR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   195 I-----RTNPNCYNGWPRMKTMSELFRIS-------LDLENRLNEVTMPFIVLHGEDDKVTDKGGSKLLyeVALSNDKTL 262
Cdd:pfam00561 153 LlkalpLLNKRFPSGDYALAKSLVTGALLfietwstELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKL--AQLFPNARL 230

                         250
                  ....*....|....*
gi 15233203   263 KLYPEMWHSLLFGEP 277
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
PRK10749 PRK10749
lysophospholipase L2; Provisional
 64-163 2.03e-06

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 48.84  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203   64 GFAVHGIEYEGHGRSSGL-----SVYIDNFDLLIDDVSSHFSKISEMGDNTKkkRFLMGESMGGAVVLLLHRKKPEFWDG 138
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGRLlddphRGHVERFNDYVDDLAAFWQQEIQPGPYRK--RYALAHSMGGAILTLFLQRHPGVFDA 158

                         90       100
                 ....*....|....*....|....*
gi 15233203  139 GILIAPMCKIAEEMkPSRMVISMIN 163
Cdd:PRK10749 159 IALCAPMFGIVLPL-PSWMARRILN 182
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 39-145 2.13e-03

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 38.61  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    39 IFFCHGYaidcSTTFKDIAPKFAkEGFAVHGIEYEGHGRSSGLSVYIDNFDLLIDDVSSHFskisemgdnTKKKRFLMGE 118
Cdd:pfam12697   1 VVLVHGA----GLSAAPLAALLA-AGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELG---------AARPVVLVGH 66

                          90       100
                  ....*....|....*....|....*..
gi 15233203   119 SMGGAVVLLLHRKKPefwDGGILIAPM 145
Cdd:pfam12697  67 SLGGAVALAAAAAAL---VVGVLVAPL 90
RimP_N pfam02576
RimP N-terminal domain; This entry represents the N-terminal domain of the ribosome maturation ...
 56-121 3.39e-03

RimP N-terminal domain; This entry represents the N-terminal domain of the ribosome maturation factor RimP (also known as yhbC). RimP facilitates the maturation of the 30S ribosomal subunit. The N-terminal domain contains two alpha-helices and a three-stranded beta-sheet. It is suggested that the N-terminal domain of SP14.3 (RimP orthologue) could function as a protein module that binds to other proteins, especially those that contain highly positively charged surfaces..


Pssm-ID: 460600  Cd Length: 73  Bit Score: 35.65  E-value: 3.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233203    56 IAPKFAKEGFAVHGIEYEGHGRSSGLSVYIDNFD-LLIDD---VSSHFSKISEMGDNTKKKRFLMGESMG 121
Cdd:pfam02576   2 IEPVVESLGFELVDVEFVKEGGGWTLRIYIDKDGgVTIDDcakVSRAISAVLDVEDPISGEYTLEVSSPG 71
 
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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