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Conserved domains on  [gi|489958961|ref|WP_003862268|]
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MULTISPECIES: alpha/beta fold hydrolase [Enterobacter]

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, ...
12-239 6.49e-27

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: 103.54  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLLGGTLCNARLWQPLIERLniSA---VLCITLTGA-ESAPQAS-----------RRLLKVLP-PRFLLAGFSLGAIV 75
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPAL--AAgyrVIAPDLRGHgRSDKPAGgytlddladdlAALLDALGlERVVLVGHSMGGMV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  76 ALQMAADAPERVNGLTLISvnplpvapdtlasrreavhtaqarGLADWLVSSLWQSYVAPSRLSDRILqeticrmaqecg 155
Cdd:COG0596  103 ALELAARHPERVAGLVLVD------------------------EVLAALAEPLRRPGLAPEALAALLR------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 156 ietfagqtemAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGNANVTRHTVEAGGHFIPLETPDEIAPLLRQ 235
Cdd:COG0596  147 ----------ALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216

                 ....
gi 489958961 236 WITE 239
Cdd:COG0596  217 FLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
12-239 6.49e-27

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: 103.54  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLLGGTLCNARLWQPLIERLniSA---VLCITLTGA-ESAPQAS-----------RRLLKVLP-PRFLLAGFSLGAIV 75
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPAL--AAgyrVIAPDLRGHgRSDKPAGgytlddladdlAALLDALGlERVVLVGHSMGGMV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  76 ALQMAADAPERVNGLTLISvnplpvapdtlasrreavhtaqarGLADWLVSSLWQSYVAPSRLSDRILqeticrmaqecg 155
Cdd:COG0596  103 ALELAARHPERVAGLVLVD------------------------EVLAALAEPLRRPGLAPEALAALLR------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 156 ietfagqtemAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGNANVTRHTVEAGGHFIPLETPDEIAPLLRQ 235
Cdd:COG0596  147 ----------ALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216

                 ....
gi 489958961 236 WITE 239
Cdd:COG0596  217 FLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
68-224 7.07e-12

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: 63.29  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   68 GFSLGAIVALQMAADAPERVNGLTLISVNPLPVAPDTLASRREAVHTAQARGLADWLV----SSLWQSYVAPSRLSDR-- 141
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFApnplGRLVAKLLALLLLRLRll 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  142 -ILQETICRMAQE-----CGIETFAGQTEMAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGNANVTRHTVE 215
Cdd:pfam00561 155 kALPLLNKRFPSGdyalaKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                  ....*....
gi 489958961  216 AGGHFIPLE 224
Cdd:pfam00561 235 DAGHFAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
12-237 8.28e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 58.03  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLL---GGTLCNarlWQPLIERLNISA-VLCITLTG-AESAPQASR-----------RLLKVLP-PRFLLAGFSLGAI 74
Cdd:PRK14875 133 PVVLIhgfGGDLNN---WLFNHAALAAGRpVIALDLPGhGASSKAVGAgsldelaaavlAFLDALGiERAHLVGHSMGGA 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  75 VALQMAADAPERVNGLTLISvnPLPVAPDTLASRREAVHTAQARG-LADWLVsslwQSYVAPSRLSDRILqETICRMAQE 153
Cdd:PRK14875 210 VALRLAARAPQRVASLTLIA--PAGLGPEINGDYIDGFVAAESRReLKPVLE----LLFADPALVTRQMV-EDLLKYKRL 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 154 CG----IETFAGQT-EMAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGnanVTRHTVEAGGHFIPLETPDE 228
Cdd:PRK14875 283 DGvddaLRALADALfAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPDG---VAVHVLPGAGHMPQMEAAAD 359

                 ....*....
gi 489958961 229 IAPLLRQWI 237
Cdd:PRK14875 360 VNRLLAEFL 368
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
63-237 1.50e-06

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 48.15  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   63 RFLLAGFSLGAIVALQMAADAPERVNGLTLisVNPLPVAPDTLAS-----------RREAVHTAQARGlaDW-------L 124
Cdd:TIGR01250  98 KFYLLGHSWGGMLAQEYALKYGQHLKGLII--SSMLDSAPEYVKElnrlrkelppeVRAAIKRCEASG--DYdnpeyqeA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  125 VSSLWQSYVAPSRLSDRILQETICRMAQECgIETFAGQTEMAI----HRQDNRTAFNALACPTLLLNGAQDViCTPHHHQ 200
Cdd:TIGR01250 174 VEVFYHHLLCRLRKWPEALKHLKSGGNTNV-YNIMQGPNEFTItgnlKDWDITDKLSEIKVPTLLTVGEFDT-MTPEAAR 251
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489958961  201 LLAAGNANVTRHTVEAGGHFIPLETPDEIAPLLRQWI 237
Cdd:TIGR01250 252 EMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
12-239 6.49e-27

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: 103.54  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLLGGTLCNARLWQPLIERLniSA---VLCITLTGA-ESAPQAS-----------RRLLKVLP-PRFLLAGFSLGAIV 75
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPAL--AAgyrVIAPDLRGHgRSDKPAGgytlddladdlAALLDALGlERVVLVGHSMGGMV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  76 ALQMAADAPERVNGLTLISvnplpvapdtlasrreavhtaqarGLADWLVSSLWQSYVAPSRLSDRILqeticrmaqecg 155
Cdd:COG0596  103 ALELAARHPERVAGLVLVD------------------------EVLAALAEPLRRPGLAPEALAALLR------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 156 ietfagqtemAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGNANVTRHTVEAGGHFIPLETPDEIAPLLRQ 235
Cdd:COG0596  147 ----------ALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216

                 ....
gi 489958961 236 WITE 239
Cdd:COG0596  217 FLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
68-224 7.07e-12

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: 63.29  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   68 GFSLGAIVALQMAADAPERVNGLTLISVNPLPVAPDTLASRREAVHTAQARGLADWLV----SSLWQSYVAPSRLSDR-- 141
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFApnplGRLVAKLLALLLLRLRll 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  142 -ILQETICRMAQE-----CGIETFAGQTEMAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGNANVTRHTVE 215
Cdd:pfam00561 155 kALPLLNKRFPSGdyalaKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                  ....*....
gi 489958961  216 AGGHFIPLE 224
Cdd:pfam00561 235 DAGHFAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
12-237 8.28e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 58.03  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLL---GGTLCNarlWQPLIERLNISA-VLCITLTG-AESAPQASR-----------RLLKVLP-PRFLLAGFSLGAI 74
Cdd:PRK14875 133 PVVLIhgfGGDLNN---WLFNHAALAAGRpVIALDLPGhGASSKAVGAgsldelaaavlAFLDALGiERAHLVGHSMGGA 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  75 VALQMAADAPERVNGLTLISvnPLPVAPDTLASRREAVHTAQARG-LADWLVsslwQSYVAPSRLSDRILqETICRMAQE 153
Cdd:PRK14875 210 VALRLAARAPQRVASLTLIA--PAGLGPEINGDYIDGFVAAESRReLKPVLE----LLFADPALVTRQMV-EDLLKYKRL 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 154 CG----IETFAGQT-EMAIHRQDNRTAFNALACPTLLLNGAQDVICTPHHHQLLAAGnanVTRHTVEAGGHFIPLETPDE 228
Cdd:PRK14875 283 DGvddaLRALADALfAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPDG---VAVHVLPGAGHMPQMEAAAD 359

                 ....*....
gi 489958961 229 IAPLLRQWI 237
Cdd:PRK14875 360 VNRLLAEFL 368
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-239 1.66e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 53.47  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  12 PLVLLGGTLCNARLWQPLIERLNIS--AVLCITLTG-----------------AESAPQASRRLLKVLPPRFLLAGFSLG 72
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAAAgyAVLAFDLRGhgrsdgprghvdsfddyVDDLRAALDALRARPGLPVVLLGHSMG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  73 AIVALQMAADAPERVNGLTLIsvnplpvAPDTLASRREAVHtaqARGLADWLVSSLWQsyvapsrlsdrilqeticrmaq 152
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLL-------APAYRADPLLGPS---ARWLRALRLAEALA---------------------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 153 ecgietfagqtemaihrqdnrtafnALACPTLLLNGAQDVICTPHHHQLLAAG-NANVTRHTVEAGGHFIPLETP-DEIA 230
Cdd:COG2267  158 -------------------------RIDVPVLVLHGGADRVVPPEAARRLAARlSPDVELVLLPGARHELLNEPArEEVL 212

                 ....*....
gi 489958961 231 PLLRQWITE 239
Cdd:COG2267  213 AAILAWLER 221
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
63-237 1.50e-06

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 48.15  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   63 RFLLAGFSLGAIVALQMAADAPERVNGLTLisVNPLPVAPDTLAS-----------RREAVHTAQARGlaDW-------L 124
Cdd:TIGR01250  98 KFYLLGHSWGGMLAQEYALKYGQHLKGLII--SSMLDSAPEYVKElnrlrkelppeVRAAIKRCEASG--DYdnpeyqeA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  125 VSSLWQSYVAPSRLSDRILQETICRMAQECgIETFAGQTEMAI----HRQDNRTAFNALACPTLLLNGAQDViCTPHHHQ 200
Cdd:TIGR01250 174 VEVFYHHLLCRLRKWPEALKHLKSGGNTNV-YNIMQGPNEFTItgnlKDWDITDKLSEIKVPTLLTVGEFDT-MTPEAAR 251
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489958961  201 LLAAGNANVTRHTVEAGGHFIPLETPDEIAPLLRQWI 237
Cdd:TIGR01250 252 EMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
66-242 6.53e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.09  E-value: 6.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  66 LAGFSLGAIVALQMAADAPErVNGltLISVNPlPVAPDTLASRreavhtaqARGLADWLVSSL--WQSYVAPSRLSDRIL 143
Cdd:COG1647   88 VIGLSMGGLLALLLAARYPD-VAG--LVLLSP-ALKIDDPSAP--------LLPLLKYLARSLrgIGSDIEDPEVAEYAY 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 144 QETICRMAQEcgIETFAGQTEMAIHRqdnrtafnaLACPTLLLNGAQDVICTPHHHQLLAA--GNANVTRHTVEAGGHFI 221
Cdd:COG1647  156 DRTPLRALAE--LQRLIREVRRDLPK---------ITAPTLIIQSRKDEVVPPESARYIYErlGSPDKELVWLEDSGHVI 224
                        170       180
                 ....*....|....*....|.
gi 489958961 222 PLetpDEIAPLLRQWITECIQ 242
Cdd:COG1647  225 TL---DKDREEVAEEILDFLE 242
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
7-94 1.15e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.28  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   7 DNTDLPLVLLGGTLCNARLWQPLIERLNIS--AVLCITLTG-----AESAPQASRRLLKVLP----PRFLLAGFSLGAIV 75
Cdd:COG1075    2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAgyPVYALNYPStngsiEDSAEQLAAFVDAVLAatgaEKVDLVGHSMGGLV 81
                         90       100
                 ....*....|....*....|.
gi 489958961  76 ALQMAA--DAPERVNGLTLIS 94
Cdd:COG1075   82 ARYYLKrlGGAAKVARVVTLG 102
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
13-191 1.97e-05

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 44.62  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  13 LVLLGGTLCNARLWQPLIERLNISAVLCITLT---------GAESAPQASRRLLKVLPPRFLLAGFSLGAIVALQMAADA 83
Cdd:PRK10349  16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLpgfgrsrgfGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTH 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  84 PERVNGLTLISVNPL--------PVAPDTLASRREAVHTAQARGLADWLvsSLWQSYVAPSRLSDRILQETIcrMAQEC- 154
Cdd:PRK10349  96 PERVQALVTVASSPCfsardewpGIKPDVLAGFQQQLSDDFQRTVERFL--ALQTMGTETARQDARALKKTV--LALPMp 171
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489958961 155 GIETFAGQTEMaIHRQDNRTAFNALACPTLLLNGAQD 191
Cdd:PRK10349 172 EVDVLNGGLEI-LKTVDLRQPLQNVSMPFLRLYGYLD 207
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
13-232 2.29e-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: 44.00  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   13 LVLL-GGTLCNARLWQPLIERLnisAVLCITLTG------AESAPQASRRLLKVL-----PPRFLLAGFSLGAIVALQMA 80
Cdd:pfam12697   1 VVLVhGAGLSAAPLAALLAAGV---AVLAPDLPGhgssspPPLDLADLADLAALLdelgaARPVVLVGHSLGGAVALAAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961   81 ADAPERVngltlISVNPLPVAPDTLASRREAVHTA-QARGLADWLVSSLWQSYVAPSRLSDRILQETICRMAQecgietf 159
Cdd:pfam12697  78 AAALVVG-----VLVAPLAAPPGLLAALLALLARLgAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA------- 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958961  160 agqtEMAIHRQDNRTAFNALACPTLLLNGAQDVIctPHHHQLLAAGNANVTRHTVEAGGHFiPLETPDEIAPL 232
Cdd:pfam12697 146 ----LLAALALLPLAAWRDLPVPVLVLAEEDRLV--PELAQRLLAALAGARLVVLPGAGHL-PLDDPEEVAEA 211
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
61-94 5.01e-04

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 40.15  E-value: 5.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489958961  61 PPRFLLAGFSLGAIVALQMAADAPErVNGLTLIS 94
Cdd:COG2945   95 PLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127
YpfH COG0400
Predicted esterase [General function prediction only];
61-241 5.48e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961  61 PPRFLLAGFSLGAIVALQMAADAPERVNGLTLISvnPLPVAPDTLASRREAvhtaqARGLadwlvsslwqsyvapsrlsd 140
Cdd:COG0400   88 PERIVLAGFSQGAAMALSLALRRPELLAGVVALS--GYLPGEEALPAPEAA-----LAGT-------------------- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958961 141 rilqeticrmaqecgietfagqtemaihrqdnrtafnalacPTLLLNGAQDVICTPHH----HQLLAAGNANVTRHTVEa 216
Cdd:COG0400  141 -----------------------------------------PVFLAHGTQDPVIPVERareaAEALEAAGADVTYREYP- 178
                        170       180
                 ....*....|....*....|....*
gi 489958961 217 GGHFIPletPDEIApLLRQWITECI 241
Cdd:COG0400  179 GGHEIS---PEELA-DARAWLAERL 199
 
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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