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Conserved domains on  [gi|513829172|ref|WP_016513467|]
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MULTISPECIES: alpha/beta hydrolase [Bacillus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 12000796)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
89-333 1.41e-21

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: 92.18  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172   89 FSWMDEYARKGYDTWAMDFRGFGRSSRPKEMSDPSvqnrpvihlndaTKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAG 168
Cdd:pfam00561  17 RKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYR------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  169 NYAISHSQDINKLIL-----YGYMHGFTLPM--MTQP--FENPLQPNQFNPEAPAYQMvdfdkgMHHWHMMMGNKKIVTN 239
Cdd:pfam00561  85 AYAAKYPDRVKALVLlgaldPPHELDEADRFilALFPgfFDGFVADFAPNPLGRLVAK------LLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  240 EAMDAVKQVFIDsdpmskknnQTIRRPVGPLEDLFYIWKNQPLYDVSKITTPLLVIYGEDDIFADRNMMSKLTS-TKQKK 318
Cdd:pfam00561 159 LLNKRFPSGDYA---------LAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQlFPNAR 229
                         250
                  ....*....|....*
gi 513829172  319 EVVIPDATHWAVYEK 333
Cdd:pfam00561 230 LVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
89-333 1.41e-21

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: 92.18  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172   89 FSWMDEYARKGYDTWAMDFRGFGRSSRPKEMSDPSvqnrpvihlndaTKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAG 168
Cdd:pfam00561  17 RKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYR------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  169 NYAISHSQDINKLIL-----YGYMHGFTLPM--MTQP--FENPLQPNQFNPEAPAYQMvdfdkgMHHWHMMMGNKKIVTN 239
Cdd:pfam00561  85 AYAAKYPDRVKALVLlgaldPPHELDEADRFilALFPgfFDGFVADFAPNPLGRLVAK------LLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  240 EAMDAVKQVFIDsdpmskknnQTIRRPVGPLEDLFYIWKNQPLYDVSKITTPLLVIYGEDDIFADRNMMSKLTS-TKQKK 318
Cdd:pfam00561 159 LLNKRFPSGDYA---------LAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQlFPNAR 229
                         250
                  ....*....|....*
gi 513829172  319 EVVIPDATHWAVYEK 333
Cdd:pfam00561 230 LVVIPDAGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
89-348 2.69e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  89 FSWMDEYARKGYDTWAMDFRGFGRSSRPKEMSDpsvqnrpviHLNDATKDLETIVNWIKKKRNvKKIHIVGWSYGGVVAG 168
Cdd:COG2267   45 AELAEALAAAGYAVLAFDLRGHGRSDGPRGHVD---------SFDDYVDDLRAALDALRARPG-LPVVLLGHSMGGLIAL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 169 NYAISHSQDINKLILYgymhgftlpmmtqpfenplqpnqfnpeAPAYQmvdfdkgmhhwhmmmgnkkivtneamdavkqv 248
Cdd:COG2267  115 LYAARYPDRVAGLVLL---------------------------APAYR-------------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 249 fidSDPMskknnqtIRRPVGPLEDLFyIWKnqplyDVSKITTPLLVIYGEDDIFADRNMMSKLTS--TKQKKEVVIPDAT 326
Cdd:COG2267  136 ---ADPL-------LGPSARWLRALR-LAE-----ALARIDVPVLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGAR 199
                        250       260
                 ....*....|....*....|..
gi 513829172 327 HWAVYEKNRNTLFEQTLNFIEA 348
Cdd:COG2267  200 HELLNEPAREEVLAAILAWLER 221
PRK10749 PRK10749
lysophospholipase L2; Provisional
99-194 1.08e-04

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 43.45  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  99 GYDTWAMDFRGFGRSSRpkEMSDPsvQNRPVIHLNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAGNYAISHSQDI 178
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGR--LLDDP--HRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLFLQRHPGVF 156
                         90
                 ....*....|....*.
gi 513829172 179 NKLILYGYMHGFTLPM 194
Cdd:PRK10749 157 DAIALCAPMFGIVLPL 172
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
89-333 1.41e-21

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: 92.18  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172   89 FSWMDEYARKGYDTWAMDFRGFGRSSRPKEMSDPSvqnrpvihlndaTKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAG 168
Cdd:pfam00561  17 RKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYR------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  169 NYAISHSQDINKLIL-----YGYMHGFTLPM--MTQP--FENPLQPNQFNPEAPAYQMvdfdkgMHHWHMMMGNKKIVTN 239
Cdd:pfam00561  85 AYAAKYPDRVKALVLlgaldPPHELDEADRFilALFPgfFDGFVADFAPNPLGRLVAK------LLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  240 EAMDAVKQVFIDsdpmskknnQTIRRPVGPLEDLFYIWKNQPLYDVSKITTPLLVIYGEDDIFADRNMMSKLTS-TKQKK 318
Cdd:pfam00561 159 LLNKRFPSGDYA---------LAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQlFPNAR 229
                         250
                  ....*....|....*
gi 513829172  319 EVVIPDATHWAVYEK 333
Cdd:pfam00561 230 LVVIPDAGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
89-348 2.69e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  89 FSWMDEYARKGYDTWAMDFRGFGRSSRPKEMSDpsvqnrpviHLNDATKDLETIVNWIKKKRNvKKIHIVGWSYGGVVAG 168
Cdd:COG2267   45 AELAEALAAAGYAVLAFDLRGHGRSDGPRGHVD---------SFDDYVDDLRAALDALRARPG-LPVVLLGHSMGGLIAL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 169 NYAISHSQDINKLILYgymhgftlpmmtqpfenplqpnqfnpeAPAYQmvdfdkgmhhwhmmmgnkkivtneamdavkqv 248
Cdd:COG2267  115 LYAARYPDRVAGLVLL---------------------------APAYR-------------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 249 fidSDPMskknnqtIRRPVGPLEDLFyIWKnqplyDVSKITTPLLVIYGEDDIFADRNMMSKLTS--TKQKKEVVIPDAT 326
Cdd:COG2267  136 ---ADPL-------LGPSARWLRALR-LAE-----ALARIDVPVLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGAR 199
                        250       260
                 ....*....|....*....|..
gi 513829172 327 HWAVYEKNRNTLFEQTLNFIEA 348
Cdd:COG2267  200 HELLNEPAREEVLAAILAWLER 221
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
91-347 2.22e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 80.06  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  91 WMDEYARKGYDTWAMDFRGFGRSSRpkEMSDPSVQnrpvihlndatkDLETIVNWIKKKRNV--KKIHIVGWSYGGVVAG 168
Cdd:COG1506   43 LAQALASRGYAVLAPDYRGYGESAG--DWGGDEVD------------DVLAAIDYLAARPYVdpDRIGIYGHSYGGYMAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 169 NYAISHSQDINKLILYGymhgftlpmmtqpfenplqpnqfnpeapayqmvdfdkGMHHWHMMMGNKKIVTNEAMDavkqv 248
Cdd:COG1506  109 LAAARHPDRFKAAVALA-------------------------------------GVSDLRSYYGTTREYTERLMG----- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 249 fidsdpmskknnqtirrpvGPLEDLFYIWKNQPLYDVSKITTPLLVIYGEDDIFAD----RNMMSKLTSTKQKKE-VVIP 323
Cdd:COG1506  147 -------------------GPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPpeqaERLYEALKKAGKPVElLVYP 207
                        250       260
                 ....*....|....*....|....
gi 513829172 324 DATHWAVYEKNRNtLFEQTLNFIE 347
Cdd:COG1506  208 GEGHGFSGAGAPD-YLERILDFLD 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
91-347 2.78e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 71.51  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  91 WMDEYARKGYDTWAMDFRGFGRSsrPKEMSDPSVQnrpvihlnDATKDLETIVNWIKKKrnVKKIHIVGWSYGGVVAGNY 170
Cdd:COG1647   34 LAEALAKAGYTVYAPRLPGHGTS--PEDLLKTTWE--------DWLEDVEEAYEILKAG--YDKVIVIGLSMGGLLALLL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 171 AISHSqDINKLILYgymhgftlpmmtqpfenplqpnqfnpeAPAYQMVDFDKGMHHWHMMMGN--KKIVTNEAMDAVKQV 248
Cdd:COG1647  102 AARYP-DVAGLVLL---------------------------SPALKIDDPSAPLLPLLKYLARslRGIGSDIEDPEVAEY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 249 FIDSDPMskknnqtirRPVGPLEDLFYIWKNqplyDVSKITTPLLVIYGEDDIFAD----RNMMSKLTStKQKKEVVIPD 324
Cdd:COG1647  154 AYDRTPL---------RALAELQRLIREVRR----DLPKITAPTLIIQSRKDEVVPpesaRYIYERLGS-PDKELVWLED 219
                        250       260
                 ....*....|....*....|...
gi 513829172 325 ATHWAVYEKNRNTLFEQTLNFIE 347
Cdd:COG1647  220 SGHVITLDKDREEVAEEILDFLE 242
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
90-348 5.00e-14

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 71.10  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  90 SWMDEYARK----GYDTWAMDFRGFGRSS-RPKEMSDPsvqnrpvihlndATKDLETIVNWIKKKRNVKKIHIV--GWSY 162
Cdd:COG1073   51 EQRALYAQRlaelGFNVLAFDYRGYGESEgEPREEGSP------------ERRDARAAVDYLRTLPGVDPERIGllGISL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 163 GGVVAGNYAISHsQDINKLILygymhgftlpmmtqpfenplqpnqfnpEAPAYQMVDFDKgmHHWHMMMGnkkivtneam 242
Cdd:COG1073  119 GGGYALNAAATD-PRVKAVIL---------------------------DSPFTSLEDLAA--QRAKEARG---------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 243 davkqVFIDSDPMskknnqtirRPVGPLEDLFyiwkNQ---PLYDVSKITTPLLVIYGEDDIFADRNMMSKL--TSTKQK 317
Cdd:COG1073  159 -----AYLPGVPY---------LPNVRLASLL----NDefdPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLyeAAAEPK 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 513829172 318 KEVVIPDATHWAVYEKNRNTLFEQTLNFIEA 348
Cdd:COG1073  221 ELLIVPGAGHVDLYDRPEEEYFDKLAEFFKK 251
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
97-333 1.96e-12

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: 65.79  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  97 RKGYDTWAMDFRGFGRSSRPkemsdpsvqnRPVIHLNDATKDLETIVnwikKKRNVKKIHIVGWSYGGVVAGNYAISHSQ 176
Cdd:COG0596   47 AAGYRVIAPDLRGHGRSDKP----------AGGYTLDDLADDLAALL----DALGLERVVLVGHSMGGMVALELAARHPE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 177 DINKLILygymhgftlpmmtqpfenplqpnqfnpeapayqmvdfdkgmhhwhmmmgnkkivTNEAMDAVKQVFidsdpms 256
Cdd:COG0596  113 RVAGLVL------------------------------------------------------VDEVLAALAEPL------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 257 kknnqtiRRPVGPLEDLFYIWKNQPLYDVS----KITTPLLVIYGEDDIFADRNMMSKLTST-KQKKEVVIPDATHWAVY 331
Cdd:COG0596  132 -------RRPGLAPEALAALLRALARTDLRerlaRITVPTLVIWGEKDPIVPPALARRLAELlPNAELVVLPGAGHFPPL 204

                 ..
gi 513829172 332 EK 333
Cdd:COG0596  205 EQ 206
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
89-332 7.41e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 58.25  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172   89 FSWMDEYARKGYDTWAMDFRGFGRSSRPkemsdpsvqnrpvihlNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAG 168
Cdd:pfam12697  11 AAPLAALLAAGVAVLAPDLPGHGSSSPP----------------PLDLADLADLAALLDELGAARPVVLVGHSLGGAVAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  169 NYAishSQDINKLILYGymhgftlPMMTQPFENPLQPNQFNPEAPAYQMVDFDKGMhhwhmmmgnkkivtneamdAVKQV 248
Cdd:pfam12697  75 AAA---AAALVVGVLVA-------PLAAPPGLLAALLALLARLGAALAAPAWLAAE-------------------SLARG 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  249 FIDSDPMskknNQTIRRPVGPLEDLFYIWKNQPLYDVSKITTPLLVIYGEDDIFADRnMMSKLTSTKQKKEVVIPDATHW 328
Cdd:pfam12697 126 FLDDLPA----DAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPEL-AQRLLAALAGARLVVLPGAGHL 200

                  ....
gi 513829172  329 AVYE 332
Cdd:pfam12697 201 PLDD 204
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
96-327 8.17e-10

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: 58.38  E-value: 8.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172   96 ARKGYDTWAMDFRGFGRSsrPKEMSDpsvqnrpVIHLNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAGNYAISHS 175
Cdd:pfam12146  28 AAQGFAVYAYDHRGHGRS--DGKRGH-------VPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  176 QDINKLILYGYMHGFTLPMMT--QPFENPLqpnqFNPEAPAYQMVDFDKGmhhwHMMMGNKKIVtnEAMDAvkqvfidsD 253
Cdd:pfam12146  99 DKVDGLILSAPALKIKPYLAPpiLKLLAKL----LGKLFPRLRVPNNLLP----DSLSRDPEVV--AAYAA--------D 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513829172  254 P-MSKKNnqTIRRPVGPLEDLFYIWKNQPlydvsKITTPLLVIYGEDDIFAD----RNMMSKLTSTkQKKEVVIPDATH 327
Cdd:pfam12146 161 PlVHGGI--SARTLYELLDAGERLLRRAA-----AITVPLLLLHGGADRVVDpagsREFYERAGST-DKTLKLYPGLYH 231
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
96-171 7.29e-05

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 43.98  E-value: 7.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513829172  96 ARKGYDTWAMDFRGFGrssrpKEMsdpsvqNR-PVIHLNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAGNYA 171
Cdd:COG0429   87 YARGWDVVRLNFRGCG-----GEP------NLlPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYL 152
PRK10749 PRK10749
lysophospholipase L2; Provisional
99-194 1.08e-04

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 43.45  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  99 GYDTWAMDFRGFGRSSRpkEMSDPsvQNRPVIHLNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAGNYAISHSQDI 178
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGR--LLDDP--HRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLFLQRHPGVF 156
                         90
                 ....*....|....*.
gi 513829172 179 NKLILYGYMHGFTLPM 194
Cdd:PRK10749 157 DAIALCAPMFGIVLPL 172
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
104-185 1.08e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 43.75  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172 104 AMDFRGFGRSSRPkemsDPSVQNRpvihlnDATKD--LETIVNWiKKKRNVKKIHIVGWSYGGVVAGNYAISHSQDINKL 181
Cdd:PLN02894 136 AIDQLGWGGSSRP----DFTCKST------EETEAwfIDSFEEW-RKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHL 204

                 ....
gi 513829172 182 ILYG 185
Cdd:PLN02894 205 ILVG 208
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
96-181 4.74e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.04  E-value: 4.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  96 ARKGYDTWAMDFRGFGRSSRpkemsdpsvqnrpvihlnDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVVAgNYAISHS 175
Cdd:COG1075   29 RAAGYPVYALNYPSTNGSIE------------------DSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA-RYYLKRL 89

                 ....*.
gi 513829172 176 QDINKL 181
Cdd:COG1075   90 GGAAKV 95
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
87-183 2.16e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 39.79  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  87 PKFSwmdEYARKGYDTWAMDFRGFGRSSRPKEmsdpsvqnrpviHLNDATKDLETIVNWIKKKRNVKKIHIVGWSYGGVV 166
Cdd:PLN03087 223 PNFS---DAAKSTYRLFAVDLLGFGRSPKPAD------------SLYTLREHLEMIERSVLERYKVKSFHIVAHSLGCIL 287
                         90
                 ....*....|....*..
gi 513829172 167 AGNYAISHSQDINKLIL 183
Cdd:PLN03087 288 ALALAVKHPGAVKSLTL 304
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
91-171 7.43e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 37.25  E-value: 7.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829172  91 WMDEYARKGYDTWAMDFRGFGRSSRPKEMSDPSVQNRPvihLNDATKDLETIVNWIKKKRNV--KKIHIVGWSYGGVVAG 168
Cdd:COG0412   48 VARRLAAAGYVVLAPDLYGRGGPGDDPDEARALMGALD---PELLAADLRAALDWLKAQPEVdaGRVGVVGFCFGGGLAL 124

                 ...
gi 513829172 169 NYA 171
Cdd:COG0412  125 LAA 127
 
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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