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Conserved domains on  [gi|446695936|ref|WP_000773282|]
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MULTISPECIES: esterase [Enterobacteriaceae]

Protein Classification

esterase( domain architecture ID 11484866)

esterase similar esterase YbfF, which belongs to alpha/beta hydrolase family and cleaves an ester bond utilizing a water molecule; may have broad substrate specificity for long-chain substrates as well as substrates of small molecular weight

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 535.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  81 DKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 446695936 241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 535.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  81 DKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 446695936 241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-253 6.25e-42

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: 142.45  E-value: 6.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  97 ALTALAPDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596  105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446695936 177 vlwdqyphivgWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLN 253
Cdd:COG0596  154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-241 6.83e-24

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: 96.42  E-value: 6.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   94 AVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 446695936  238 AEKP 241
Cdd:pfam00561 242 LEGP 245
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 39-252 9.77e-14

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 68.54  E-value: 9.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   39 LVNDHNIIQVDMRNHGLSPrdpVMNYPA----MAQDLVDTLDAQQIDKATFIGHSMGGKAVMALTALAPDRIDKLVAIDI 114
Cdd:TIGR02427  36 LTPDFRVLRYDKRGHGLSD---APEGPYsiedLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  115 ApvdyhvrrhdeifAAINAVSESDaqtrQQAAAIMRQHLNE--EGVIQfllKSFVDGeWRFNVPVLWDQYPHIV------ 186
Cdd:TIGR02427 113 A-------------AKIGTPESWN----ARIAAVRAEGLAAlaDAVLE---RWFTPG-FREAHPARLDLYRNMLvrqppd 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446695936  187 GW----EKIPAWDH---------PTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
Cdd:TIGR02427 172 GYagccAAIRDADFrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFL 250
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 535.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  81 DKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 446695936 241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-253 6.25e-42

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: 142.45  E-value: 6.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596   25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  97 ALTALAPDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596  105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446695936 177 vlwdqyphivgWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLN 253
Cdd:COG0596  154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-241 6.83e-24

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: 96.42  E-value: 6.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   94 AVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 446695936  238 AEKP 241
Cdd:pfam00561 242 LEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 18-252 3.35e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 76.91  E-value: 3.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  18 PIVLVHGLFGSLDN-LGVLArDLVNDHNIIQVDMRNHGLS-PRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAV 95
Cdd:PRK14875 133 PVVLIHGFGGDLNNwLFNHA-ALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  96 MALTALAPDRIDKLVAidIAP--------VDYhvrrhdeIFAAINAVSESDAQ-------------TRQQAAAIMRQhLN 154
Cdd:PRK14875 212 LRLAARAPQRVASLTL--IAPaglgpeinGDY-------IDGFVAAESRRELKpvlellfadpalvTRQMVEDLLKY-KR 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 155 EEGVIQFLLK----SFVDGEWRFNV-PVLwdqyphivgwekiPAWDHPTLFIPGGNSPYVSEQYRDDLLaqfPQARAHVI 229
Cdd:PRK14875 282 LDGVDDALRAladaLFAGGRQRVDLrDRL-------------ASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVHVL 345

                        250       260
                 ....*....|....*....|...
gi 446695936 230 AGAGHWVHAEKPDAVLRAIRRYL 252
Cdd:PRK14875 346 PGAGHMPQMEAAADVNRLLAEFL 368
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
18-254 5.89e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.57  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  18 PIVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP--VMNYPAMAQDL---VDTLDAQQIDKATFIGHSMG 91
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDGPRghVDSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  92 GKAVMALTALAPDRIDKLVAidIAPVDYHvrrhdeifaainavsesdaqtrqqaaaimrqhlneegviqfllksfvDGEW 171
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVL--LAPAYRA-----------------------------------------------DPLL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 172 RFNVPVLWDQYPhivgWEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQF-PQARAHVIAGAGHWVHAEKP-DAVLRAIR 249
Cdd:COG2267  141 GPSARWLRALRL----AEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNEPArEEVLAAIL 216


                 ....*
gi 446695936 250 RYLND 254
Cdd:COG2267  217 AWLER 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 39-252 9.77e-14

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 68.54  E-value: 9.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   39 LVNDHNIIQVDMRNHGLSPrdpVMNYPA----MAQDLVDTLDAQQIDKATFIGHSMGGKAVMALTALAPDRIDKLVAIDI 114
Cdd:TIGR02427  36 LTPDFRVLRYDKRGHGLSD---APEGPYsiedLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  115 ApvdyhvrrhdeifAAINAVSESDaqtrQQAAAIMRQHLNE--EGVIQfllKSFVDGeWRFNVPVLWDQYPHIV------ 186
Cdd:TIGR02427 113 A-------------AKIGTPESWN----ARIAAVRAEGLAAlaDAVLE---RWFTPG-FREAHPARLDLYRNMLvrqppd 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446695936  187 GW----EKIPAWDH---------PTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
Cdd:TIGR02427 172 GYagccAAIRDADFrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFL 250
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 19-247 2.18e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 67.11  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   19 IVLVHGLFGSLDNLGVLARDLVNDHNiiqVDMRNHGLSPRDPVmNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVMAL 98
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAAGVAVLA---PDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   99 TALAPdridkLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVPVL 178
Cdd:pfam12697  77 AAAAL-----VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446695936  179 WDQYPHivgWEKIPAWdhptLFIPGGNSPYVSEQYRdDLLAQFPQARAHVIAGAGHWVHaEKPDAVLRA 247
Cdd:pfam12697 152 LLPLAA---WRDLPVP----VLVLAEEDRLVPELAQ-RLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 18-134 2.25e-08

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 53.14  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPV---MNYPAMAQD---LVDTLD--------AQQIDKA 83
Cdd:pfam07819   6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGFHLDFFsvdFNEELSAFHgrtLLDQAEylndairyILSLYAS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446695936   84 TF--------IGHSMGGK---AVMALTALAPDRIDKLVAIDiAPVDYHVRRHD----EIFAAINAV 134
Cdd:pfam07819  86 GRpgptsvilIGHSMGGIvarAALTLPNYIPQSVNTIITLS-SPHAKPPLTFDgdilKFYERLNAF 150
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
19-253 4.81e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.33  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  19 IVLVHGLFGSLDN-LGVLARDLVND-HNIIQVDMRNHGLSPRDPvmnYPAMAQDLVDTLDA----QQIDKATF--IGHSM 90
Cdd:COG1506   26 VVYVHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAGDW---GGDEVDDVLAAIDYlaarPYVDPDRIgiYGHSY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  91 GGKAVMALTALAPDRIDklVAIDIAPVdyhvrrhdeifaainavseSDAQTRQQAAAIMRQHLNeegviqfllksfvdGE 170
Cdd:COG1506  103 GGYMALLAAARHPDRFK--AAVALAGV-------------------SDLRSYYGTTREYTERLM--------------GG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 171 WRFNVPVLWDQYPHivgwEKIPAWDHPTLFIPGGNSPYV----SEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
Cdd:COG1506  148 PWEDPEAYAARSPL----AYADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLE 223


                 ....*..
gi 446695936 247 AIRRYLN 253
Cdd:COG1506  224 RILDFLD 230
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 18-112 1.30e-07

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 48.67  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  18 PIVLVHGLFGSLDNLGVLARDLvndhniiqvdmRNHGLSPRdpVMNYPAMAQDLVDTLD--AQQID---------KATFI 86
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRL-----------RAAGYPVY--ALNYPSTNGSIEDSAEqlAAFVDavlaatgaeKVDLV 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 446695936  87 GHSMGGkaVMALTALA----PDRIDKLVAI 112
Cdd:COG1075   74 GHSMGG--LVARYYLKrlggAAKVARVVTL 101
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 19-240 8.44e-07

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: 48.75  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   19 IVLVHGLFGSLDNLGVLARDLVndHNIIQV---DMRNHGLSP--RDPVMNYPAMAQDL---VDTLDAQQIDKATFI-GHS 89
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALA--AQGFAVyayDHRGHGRSDgkRGHVPSFDDYVDDLdtfVDKIREEHPGLPLFLlGHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   90 MGGKAVMALTALAPDRIDKLV----AIDIAPvdYHVRRHDEIFAAI----------NAVSESDAQTR-QQAAAIMRQH-L 153
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLIlsapALKIKP--YLAPPILKLLAKLlgklfprlrvPNNLLPDSLSRdPEVVAAYAADpL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  154 NEEGVIQFLLKSFVD-GEWrfnvpvLWDQYPHIvgweKIpawdhPTLFIPGGNSPYVSEQYRDDLLAQFP--QARAHVIA 230
Cdd:pfam12146 163 VHGGISARTLYELLDaGER------LLRRAAAI----TV-----PLLLLHGGADRVVDPAGSREFYERAGstDKTLKLYP 227

                         250
                  ....*....|
gi 446695936  231 GAGHWVHAEK 240
Cdd:pfam12146 228 GLYHELLNEP 237
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 4-123 1.75e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 48.20  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   4 NIRAQTAQNQhnNSPIVLVHGLFGSLD----NLGVLARDlvndHNIIQVDMRNHGLS--------PRDPVMNYPAMAQDL 71
Cdd:PLN02824  19 NIRYQRAGTS--GPALVLVHGFGGNADhwrkNTPVLAKS----HRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446695936  72 VDTLDAQQIDKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRR 123
Cdd:PLN02824  93 NDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRGLHIKK 144
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
19-253 2.00e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 44.55  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDPV-MNYPAMAQDLVDTLD--AQQIDKATFIGHSMGGKA 94
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEilKAGYDKVIVIGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  95 VMALTALAPDrIDKLVAIDiAPVDY--------HVRRHdeIFAAINAVSESDAQTRQQAAAIMRQHLNeeGVIQFLLksf 166
Cdd:COG1647   98 ALLLAARYPD-VAGLVLLS-PALKIddpsapllPLLKY--LARSLRGIGSDIEDPEVAEYAYDRTPLR--ALAELQR--- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 167 vdgewrfnvpvLWDQYPhivgwEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARAHVIA--GAGHWVHAEK-PDA 243
Cdd:COG1647  169 -----------LIREVR-----RDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWleDSGHVITLDKdREE 232

                        250
                 ....*....|
gi 446695936 244 VLRAIRRYLN 253
Cdd:COG1647  233 VAEEILDFLE 242
COG4814 COG4814
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
1-112 2.36e-05

Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];


Pssm-ID: 443842  Cd Length: 286  Bit Score: 44.55  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLV----------------------------NDHN-IIQVDMR 51
Cdd:COG4814   28 TKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNekygvghkvltvtvskdgkitysgkirkNAKNpIIQVGFE 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446695936  52 NHglspRDPVMNYPAMAQDLVDTLDAQ-QIDKATFIGHSMGGKAVMA-LTALAPDR----IDKLVAI 112
Cdd:COG4814  108 DN----RDSIKKQAKWLKKVLKYLKKKyGFKKFNAVGHSMGGLALTYyLEKYGNDKslpkLNKLVTI 170
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 19-252 4.59e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 43.36  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP-VMNYPAM--AQDLVDTL------DAQQIdkaTFIGH 88
Cdd:COG1073   40 VVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESEGEPrEEGSPERrdARAAVDYLrtlpgvDPERI---GLLGI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  89 SMGGkaVMALTALAPDRIDKLVAIDIAPVDYhvrrhdeifaainavsesDAQTRQQAAAIMRQHLneeGVIQFL----LK 164
Cdd:COG1073  117 SLGG--GYALNAAATDPRVKAVILDSPFTSL------------------EDLAAQRAKEARGAYL---PGVPYLpnvrLA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936 165 SFVDGEWRfnvPVlwdqyphivgwEKIPAWDHPTLFIPGGNSPYVSEQYRDDLLAQFPQARA-HVIAGAGH----WVHAE 239
Cdd:COG1073  174 SLLNDEFD---PL-----------AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvdlyDRPEE 239

                        250
                 ....*....|....
gi 446695936 240 KPDAVLRA-IRRYL 252
Cdd:COG1073  240 EYFDKLAEfFKKNL 253
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 19-104 1.27e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 39.05  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446695936  19 IVLVHGLFGSLDN-LGVLarDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM- 96
Cdd:PRK11126   5 LVFLHGLLGSGQDwQPVG--EALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMy 82


                 ....*....
gi 446695936  97 -ALTALAPD 104
Cdd:PRK11126  83 yACQGLAGG 91
 
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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