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Conserved domains on  [gi|15235567|ref|NP_195463|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

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, ...
 9-265 3.09e-30

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: 112.79  E-value: 3.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   9 NVKVIGSGEATIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAG--TTNPDYFDFDRYSNlegysfDLIAILEDLKI 86
Cdd:COG0596  15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGrsDKPAGGYTLDDLAD------DLAALLDALGL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  87 ESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISASPRYVNDVDYQGGFEQEDLNQLFEAIRsnykawclgfaplavggdm 166
Cdd:COG0596  89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALA------------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567 167 dsiavqefsrtlfnmrpdialsvgqtifQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGcESVVEVIPSDGH 246
Cdd:COG0596 150 ----------------------------RTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP-NAELVVLPGAGH 200

                       250
                ....*....|....*....
gi 15235567 247 LPQLSSPDSVIPVILRHIR 265
Cdd:COG0596 201 FPPLEQPEAFAAALRDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 9-265 3.09e-30

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: 112.79  E-value: 3.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   9 NVKVIGSGEATIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAG--TTNPDYFDFDRYSNlegysfDLIAILEDLKI 86
Cdd:COG0596  15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGrsDKPAGGYTLDDLAD------DLAALLDALGL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  87 ESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISASPRYVNDVDYQGGFEQEDLNQLFEAIRsnykawclgfaplavggdm 166
Cdd:COG0596  89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALA------------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567 167 dsiavqefsrtlfnmrpdialsvgqtifQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGcESVVEVIPSDGH 246
Cdd:COG0596 150 ----------------------------RTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP-NAELVVLPGAGH 200

                       250
                ....*....|....*....
gi 15235567 247 LPQLSSPDSVIPVILRHIR 265
Cdd:COG0596 201 FPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 19-253 3.02e-15

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 73.31  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    19 TIVLGHGFGTDQSVWKHLVPHLVDD-YRVVLYDNMGAGTTnpdyfdfDRYSNLEGYSFDLIA-----ILEDLKIESCIFV 92
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKS-------SRPKAQDDYRTDDLAedleyILEALGLEKVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    93 GHSVSAMIGVLASLNRPDLFSKIVMISASP--------RYVNDVDYQGGFE---QEDLNQLFEAIRSNYKAWCLGF-APL 160
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDppheldeaDRFILALFPGFFDgfvADFAPNPLGRLVAKLLALLLLRlRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   161 AVGGDMDSIAVQEFsRTLFNMRPDIALSVGQTIFQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGCESVVEV 240
Cdd:pfam00561 155 KALPLLNKRFPSGD-YALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|...
gi 15235567   241 IPSdGHLPQLSSP 253
Cdd:pfam00561 234 PDA-GHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-266 2.56e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    6 EAHNVKVIGSGEA---TIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTTNPDYFDfdrySNLEGYSFDLIAILE 82
Cdd:PRK14875 117 GGRTVRYLRLGEGdgtPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGA----GSLDELAAAVLAFLD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   83 DLKIESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISAS--PRYVNdVDYQGGF----EQEDLNQLFEAIrsnykawclg 156
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAglGPEIN-GDYIDGFvaaeSRRELKPVLELL---------- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  157 FA-PLAVGGDM-DSI-------AVQEFSRTLfnmrpdialsvGQTIF-----QSDMRQILPFVTVPCHILQSVKDLAVPV 222
Cdd:PRK14875 262 FAdPALVTRQMvEDLlkykrldGVDDALRAL-----------ADALFaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPA 330

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15235567  223 VvseylHA-NLGCESVVEVIPSDGHLPQLSSPDSVIPVILRHIRN 266
Cdd:PRK14875 331 A-----HAqGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 9-265 3.09e-30

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: 112.79  E-value: 3.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   9 NVKVIGSGEATIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAG--TTNPDYFDFDRYSNlegysfDLIAILEDLKI 86
Cdd:COG0596  15 HYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGrsDKPAGGYTLDDLAD------DLAALLDALGL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  87 ESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISASPRYVNDVDYQGGFEQEDLNQLFEAIRsnykawclgfaplavggdm 166
Cdd:COG0596  89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALA------------------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567 167 dsiavqefsrtlfnmrpdialsvgqtifQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGcESVVEVIPSDGH 246
Cdd:COG0596 150 ----------------------------RTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLP-NAELVVLPGAGH 200

                       250
                ....*....|....*....
gi 15235567 247 LPQLSSPDSVIPVILRHIR 265
Cdd:COG0596 201 FPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 19-253 3.02e-15

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 73.31  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    19 TIVLGHGFGTDQSVWKHLVPHLVDD-YRVVLYDNMGAGTTnpdyfdfDRYSNLEGYSFDLIA-----ILEDLKIESCIFV 92
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKS-------SRPKAQDDYRTDDLAedleyILEALGLEKVNLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    93 GHSVSAMIGVLASLNRPDLFSKIVMISASP--------RYVNDVDYQGGFE---QEDLNQLFEAIRSNYKAWCLGF-APL 160
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDppheldeaDRFILALFPGFFDgfvADFAPNPLGRLVAKLLALLLLRlRLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   161 AVGGDMDSIAVQEFsRTLFNMRPDIALSVGQTIFQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGCESVVEV 240
Cdd:pfam00561 155 KALPLLNKRFPSGD-YALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|...
gi 15235567   241 IPSdGHLPQLSSP 253
Cdd:pfam00561 234 PDA-GHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
14-265 1.65e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 59.25  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  14 GSGEATIVLGHGFGTDQSVWKHLVPHLVD-DYRVVLYDNMGAGTT---NPDYFDFDRYSNlegysfDLIAILEDLKIES- 88
Cdd:COG2267  25 GSPRGTVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSdgpRGHVDSFDDYVD------DLRAALDALRARPg 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  89 --CIFVGHSVSAMIGVLASLNRPDLFSKIVMIsaSPRYVNDvdyqggfeqedlnqlfeairsnykawclgfaplavggdm 166
Cdd:COG2267  99 lpVVLLGHSMGGLIALLYAARYPDRVAGLVLL--APAYRAD--------------------------------------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567 167 dsiavqefsrtlfnmrPDIALSVGqTIFQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGCESVVEVIPSDGH 246
Cdd:COG2267 138 ----------------PLLGPSAR-WLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARH 200

                       250       260
                ....*....|....*....|
gi 15235567 247 LPQLSSP-DSVIPVILRHIR 265
Cdd:COG2267 201 ELLNEPArEEVLAAILAWLE 220
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-266 2.56e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    6 EAHNVKVIGSGEA---TIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTTNPDYFDfdrySNLEGYSFDLIAILE 82
Cdd:PRK14875 117 GGRTVRYLRLGEGdgtPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGA----GSLDELAAAVLAFLD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   83 DLKIESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISAS--PRYVNdVDYQGGF----EQEDLNQLFEAIrsnykawclg 156
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAglGPEIN-GDYIDGFvaaeSRRELKPVLELL---------- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  157 FA-PLAVGGDM-DSI-------AVQEFSRTLfnmrpdialsvGQTIF-----QSDMRQILPFVTVPCHILQSVKDLAVPV 222
Cdd:PRK14875 262 FAdPALVTRQMvEDLlkykrldGVDDALRAL-----------ADALFaggrqRVDLRDRLASLAIPVLVIWGEQDRIIPA 330

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15235567  223 VvseylHA-NLGCESVVEVIPSDGHLPQLSSPDSVIPVILRHIRN 266
Cdd:PRK14875 331 A-----HAqGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
16-247 4.04e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 55.72  E-value: 4.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  16 GEATIVLGHGFGTDQSVWKHLVPHLVD-DYRVVLYDNMGAGTTNPDyfdfdrysnLEGYSF-----DLIAILEDLKiESC 89
Cdd:COG1647  14 GRKGVLLLHGFTGSPAEMRPLAEALAKaGYTVYAPRLPGHGTSPED---------LLKTTWedwleDVEEAYEILK-AGY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  90 --IFV-GHSVSAMIGVLASLNRPDLfSKIVMISASPRYVNDVDYQGGFeqedLNQLFEAIRSNYKAWCLGFAPLAVGGDM 166
Cdd:COG1647  84 dkVIViGLSMGGLLALLLAARYPDV-AGLVLLSPALKIDDPSAPLLPL----LKYLARSLRGIGSDIEDPEVAEYAYDRT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567 167 DSIAVQEFSRtlfnmrpdialsvgqtiFQSDMRQILPFVTVPCHILQSVKDLAVPVVVSEYLHANLGCESV-VEVIPSDG 245
Cdd:COG1647 159 PLRALAELQR-----------------LIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKeLVWLEDSG 221


                ..
gi 15235567 246 HL 247
Cdd:COG1647 222 HV 223
PRK05855 PRK05855
SDR family oxidoreductase;
19-82 6.35e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 56.14  E-value: 6.35e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   19 TIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAG-TTNPdyfdfdrySNLEGYSF-----DLIAILE 82
Cdd:PRK05855  27 TVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGrSSAP--------KRTAAYTLarladDFAAVID 88
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 14-262 3.31e-07

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 50.51  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   14 GSGEAtIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTT---NPDYFDFDRYSNLEGYSFDLIAILEDLKIESCI 90
Cdd:PLN02824  27 TSGPA-LVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSdkpNPRSAPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   91 FVGHSVSAMIGVLASLNRPDLFSKIVMISAS---------PRYVNDV--DYQGGFEQEDLNQLFeairsnykawclgFAP 159
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLINISlrglhikkqPWLGRPFikAFQNLLRETAVGKAF-------------FKS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567  160 LAVGGDMDSIAVQEFSRTlfnmrPDIALSVGQTIFQSDMR--------------------QILPFVTVPCHILQSVKDLA 219
Cdd:PLN02824 173 VATPETVKNILCQCYHDD-----SAVTDELVEAILRPGLEpgavdvfldfisysggplpeELLPAVKCPVLIAWGEKDPW 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15235567  220 VPVVVSEyLHANLgcESVVE--VIPSDGHLPQLSSPDSVIPVILR 262
Cdd:PLN02824 248 EPVELGR-AYANF--DAVEDfiVLPGVGHCPQDEAPELVNPLIES 289
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 20-259 1.81e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 47.47  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    20 IVLGHGFGTDqsvWKHLVPHLVDDYRVVLYDNMGAGTTNPDYFDFDRYSnlegysfDLIAILEDLKIES-CIFVGHSVSA 98
Cdd:pfam12697   1 VVLVHGAGLS---AAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLA-------DLAALLDELGAARpVVLVGHSLGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    99 MIGVLAslnRPDLFSKIVMISASPryvndvdYQGGFEQEDLNQLFEAIRSnykawcLGFAPLAVGGDMDSIAVQEFSRTL 178
Cdd:pfam12697  71 AVALAA---AAAALVVGVLVAPLA-------APPGLLAALLALLARLGAA------LAAPAWLAAESLARGFLDDLPADA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   179 FNMRPDIALSVGQTIFQSDMRQILPFVTVPCHILQSvKDLAVPVVVSEYLHANLGCEsvVEVIPSDGHLPqLSSPDSVIP 258
Cdd:pfam12697 135 EWAAALARLAALLAALALLPLAAWRDLPVPVLVLAE-EDRLVPELAQRLLAALAGAR--LVVLPGAGHLP-LDDPEEVAE 210


                  .
gi 15235567   259 V 259
Cdd:pfam12697 211 A 211
PLN02578 PLN02578
hydrolase
 8-158 2.65e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 44.83  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    8 HNVKVIGSGE-ATIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTTNPDYFDFDRYSnlegYSFDLIAILEDLKI 86
Cdd:PLN02578  76 HKIHYVVQGEgLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMV----WRDQVADFVKEVVK 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235567   87 ESCIFVGHSVSAMIGVLASLNRPDLFSKIVMISASPRYVNDVDYQGGFEQEDLNQL----FEAIRSNYKAWCLGFA 158
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVLtrfvVKPLKEWFQRVVLGFL 227
PRK10673 PRK10673
esterase;
20-147 1.96e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 41.64  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   20 IVLGHGFGTDQSVWKHLVPHLVDDYRVVLYD--NMGAGTTNP--DYFDFDRysnlegysfDLIAILEDLKIESCIFVGHS 95
Cdd:PRK10673  19 IVLVHGLFGSLDNLGVLARDLVNDHDIIQVDmrNHGLSPRDPvmNYPAMAQ---------DLLDTLDALQIEKATFIGHS 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15235567   96 VSAMIGVLASLNRPDLFSKIVMISASPryvndVDYQggFEQEDlnQLFEAIR 147
Cdd:PRK10673  90 MGGKAVMALTALAPDRIDKLVAIDIAP-----VDYH--VRRHD--EIFAAIN 132
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 14-148 2.17e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 41.90  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   14 GSGEAtIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYD--NMGA-GTTNPDYFDFDRYSNLEgysfdliAILEDLKIESCI 90
Cdd:PRK03592  25 GEGDP-IVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDliGMGAsDKPDIDYTFADHARYLD-------AWFDALGLDDVV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235567   91 FVGHSVSAMIGVLASLNRPDLFSKIVMISASPRYVNDVDYQGGFEqedlnQLFEAIRS 148
Cdd:PRK03592  97 LVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVR-----ELFQALRS 149
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 19-119 2.66e-03

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 38.71  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567   19 TIVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTTN---PDY-FDFdrysNLEGYSFDLIAILEDLKIESCIFVGH 94
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpqPGYgFNY----TLDEYVSSLESLIDELKSDKVSLVVQ 204

                         90       100
                 ....*....|....*....|....*
gi 15235567   95 SVSAMIGVLASLNRPDLFSKIVMIS 119
Cdd:PLN03084 205 GYFSPPVVKYASAHPDKIKKLILLN 229
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 9-121 6.05e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 37.51  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235567    9 NVKVIGSGEAT-----IVLGHGFGTDQSVWKHLVPHLVDDYRVVLYDNMGAGTTN-PDYFDFdrysNLEGYSFDLIAILE 82
Cdd:PLN02679  75 NYLVKGSPEVTssgppVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDkPPGFSY----TMETWAELILDFLE 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15235567   83 DLKIESCIFVGHSVSAMIGVLASLN-RPDLFSKIVMISAS 121
Cdd:PLN02679 151 EVVQKPTVLIGNSVGSLACVIAASEsTRDLVRGLVLLNCA 190
 
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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