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Conserved domains on  [gi|491918477|ref|WP_005671459|]
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alpha/beta fold hydrolase [Massilia timonae]

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, ...
 59-275 8.16e-22

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: 90.83  E-value: 8.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  59 IVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNSQETGTARDGATIVEELRQTLRHKGLAPpYILVGHSLGGLYMQ 138
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLER-VVLVGHSMGGMVAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477 139 LFAKRYPQEVSGLVLVDPLLPGVVKKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQVLSLAPIDDkpivmlinkpsg 218
Cdd:COG0596  105 ELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD------------ 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491918477 219 sTAVGVDFGafnkdqktRELVSgLYPKAKKIVV-DSDHQVQRQNPADVVNAIRNILAK 275
Cdd:COG0596  173 -PIVPPALA--------RRLAE-LLPNAELVVLpGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-275 8.16e-22

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: 90.83  E-value: 8.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  59 IVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNSQETGTARDGATIVEELRQTLRHKGLAPpYILVGHSLGGLYMQ 138
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLER-VVLVGHSMGGMVAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477 139 LFAKRYPQEVSGLVLVDPLLPGVVKKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQVLSLAPIDDkpivmlinkpsg 218
Cdd:COG0596  105 ELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD------------ 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491918477 219 sTAVGVDFGafnkdqktRELVSgLYPKAKKIVV-DSDHQVQRQNPADVVNAIRNILAK 275
Cdd:COG0596  173 -PIVPPALA--------RRLAE-LLPNAELVVLpGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-226 9.25e-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: 72.15  E-value: 9.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477   59 IVFENGLRATVDGWDKVIDSLVPD-ASIFAYNRPGYGNSQETGTARDGAT--IVEELRQTLRHKGLAPPYiLVGHSLGGL 135
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTddLAEDLEYILEALGLEKVN-LVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  136 YMQLFAKRYPQEVSGLVLVDPLLPGVV----------KKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQVLSLAPID 205
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHEldeadrfilaLFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180
                  ....*....|....*....|.
gi 491918477  206 DKPIVMLINKPSGSTAVGVDF 226
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLF 182
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 59-134 1.21e-07

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 51.38  E-value: 1.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491918477  59 IVFENGLRATVDGWDKVIDSLvPDASIFAYNRPGYGNSQETGTArDGATIVEELRQTLRHKGLAPpYILVGHSLGG 134
Cdd:PRK11126   5 LVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAISVD-GFADVSRLLSQTLQSYNILP-YWLVGYSLGG 77
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 109-191 3.77e-04

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: 41.21  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  109 VEELRQTLrhkGLAPPYILvGHSLGGLYMQLFAKRYPQEVSGLVLVDPLLpgvvkkseEFPVWTRGAKRL--FFSSTVNK 186
Cdd:TIGR01250  87 LEEVREKL---GLDKFYLL-GHSWGGMLAQEYALKYGQHLKGLIISSMLD--------SAPEYVKELNRLrkELPPEVRA 154


                  ....*
gi 491918477  187 EIDAI 191
Cdd:TIGR01250 155 AIKRC 159
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-275 8.16e-22

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: 90.83  E-value: 8.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  59 IVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNSQETGTARDGATIVEELRQTLRHKGLAPpYILVGHSLGGLYMQ 138
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLER-VVLVGHSMGGMVAL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477 139 LFAKRYPQEVSGLVLVDPLLPGVVKKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQVLSLAPIDDkpivmlinkpsg 218
Cdd:COG0596  105 ELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKD------------ 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491918477 219 sTAVGVDFGafnkdqktRELVSgLYPKAKKIVV-DSDHQVQRQNPADVVNAIRNILAK 275
Cdd:COG0596  173 -PIVPPALA--------RRLAE-LLPNAELVVLpGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-226 9.25e-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: 72.15  E-value: 9.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477   59 IVFENGLRATVDGWDKVIDSLVPD-ASIFAYNRPGYGNSQETGTARDGAT--IVEELRQTLRHKGLAPPYiLVGHSLGGL 135
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTddLAEDLEYILEALGLEKVN-LVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  136 YMQLFAKRYPQEVSGLVLVDPLLPGVV----------KKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQVLSLAPID 205
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHEldeadrfilaLFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180
                  ....*....|....*....|.
gi 491918477  206 DKPIVMLINKPSGSTAVGVDF 226
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLF 182
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
59-156 8.13e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 8.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  59 IVFENGLRATVDGWDKVIDSLV-PDASIFAYNRPGYGNSQ-ETGTARDGATIVEELRQTLRHKGLAP--PYILVGHSLGG 134
Cdd:COG2267   31 VVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDgPRGHVDSFDDYVDDLRAALDALRARPglPVVLLGHSMGG 110

                         90       100
                 ....*....|....*....|..
gi 491918477 135 LYMQLFAKRYPQEVSGLVLVDP 156
Cdd:COG2267  111 LIALLYAARYPDRVAGLVLLAP 132
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 84-197 8.29e-09

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: 54.91  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477   84 SIFAYNRPGYGNSQ-ETGTARDGATIVEELRQ-----TLRHKGLapPYILVGHSLGGLYMQLFAKRYPQEVSGLVLVDPL 157
Cdd:pfam12146  33 AVYAYDHRGHGRSDgKRGHVPSFDDYVDDLDTfvdkiREEHPGL--PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPA 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 491918477  158 L---PGVVKKSEEFPVWTRGakRLFFSSTVNKEIDAIHQTSEQ 197
Cdd:pfam12146 111 LkikPYLAPPILKLLAKLLG--KLFPRLRVPNNLLPDSLSRDP 151
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 59-178 3.11e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 52.86  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477   59 IVFENGLRATVDgwdKVIDSLVPDASIFAYNRPGYGNSqetGTARDGATIVEELRQTLRHKGLAPPYILVGHSLGGLYMQ 138
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGHGSS---SPPPLDLADLADLAALLDELGAARPVVLVGHSLGGAVAL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 491918477  139 LFAKRYPqeVSGlVLVDPLLPGVVKKSEEFPVWTRGAKRL 178
Cdd:pfam12697  75 AAAAAAL--VVG-VLVAPLAAPPGLLAALLALLARLGAAL 111
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 59-134 1.21e-07

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 51.38  E-value: 1.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491918477  59 IVFENGLRATVDGWDKVIDSLvPDASIFAYNRPGYGNSQETGTArDGATIVEELRQTLRHKGLAPpYILVGHSLGG 134
Cdd:PRK11126   5 LVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAISVD-GFADVSRLLSQTLQSYNILP-YWLVGYSLGG 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 26-156 7.27e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.94  E-value: 7.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  26 GSVSSAPATASVDmiaGRQVESLTiKNPSANVSIVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNS---QETGTA 102
Cdd:PRK14875 105 EDAGPAPRKARIG---GRTVRYLR-LGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASskaVGAGSL 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491918477 103 RDGATIVEELrqtLRHKGLAPPyILVGHSLGGLYMQLFAKRYPQEVSGLVLVDP 156
Cdd:PRK14875 181 DELAAAVLAF---LDALGIERA-HLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 43-171 1.66e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 48.75  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  43 RQVESLTIKNPSANVSIVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNSQE-----TGTARDGATIVEELRQTLR 117
Cdd:PLN02894  92 RFINTVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdftcKSTEETEAWFIDSFEEWRK 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491918477 118 HKGLAPpYILVGHSLGGLYMQLFAKRYPQEVSGLVLVDPllPGVVKKSEEFPVW 171
Cdd:PLN02894 172 AKNLSN-FILLGHSFGGYVAAKYALKHPEHVQHLILVGP--AGFSSESDDKSEW 222
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 109-191 3.77e-04

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: 41.21  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  109 VEELRQTLrhkGLAPPYILvGHSLGGLYMQLFAKRYPQEVSGLVLVDPLLpgvvkkseEFPVWTRGAKRL--FFSSTVNK 186
Cdd:TIGR01250  87 LEEVREKL---GLDKFYLL-GHSWGGMLAQEYALKYGQHLKGLIISSMLD--------SAPEYVKELNRLrkELPPEVRA 154


                  ....*
gi 491918477  187 EIDAI 191
Cdd:TIGR01250 155 AIKRC 159
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 79-197 5.30e-04

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 41.23  E-value: 5.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  79 LVPDASIFAYNRPGYGNSQETGT-----ARDgatIVEELRQTLRHkGlapPYILVGHSLGGLYMQLFAKRYPQ---EVSG 150
Cdd:COG3319  624 LGPDRPVYGLQAPGLDGGEPPPAsveemAAR---YVEAIRAVQPE-G---PYHLLGWSFGGLVAYEMARQLEAqgeEVAL 696

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 491918477 151 LVLVDPLLPGVVKKSEEFPVWTRGAKRLFFSSTVNKEIDAIHQTSEQ 197
Cdd:COG3319  697 LVLLDSYAPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPE 743
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 78-155 1.05e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 39.68  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477   78 SLVPDASIFAYNRPGYGNSQETgtARDGATIVEELRQTLRHKGLAPPYILVGHSLGGLYMQLFAKRYPQ---EVSGLVLV 154
Cdd:pfam00975  22 RLPPPAEVLAVQYPGRGRGEPP--LNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVARRLERqgeAVRSLFLS 99


                  .
gi 491918477  155 D 155
Cdd:pfam00975 100 D 100
PLN02578 PLN02578
hydrolase
 57-156 1.53e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 39.44  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  57 VSIVFENGLRATVDGWDKVIDSLVPDASIFAYNRPGYGNSQETGTARDGATIVEELRQTLRHKgLAPPYILVGHSLGGLY 136
Cdd:PLN02578  87 LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEV-VKEPAVLVGNSLGGFT 165

                         90       100
                 ....*....|....*....|
gi 491918477 137 MQLFAKRYPQEVSGLVLVDP 156
Cdd:PLN02578 166 ALSTAVGYPELVAGVALLNS 185
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
91-162 2.55e-03

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 37.91  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  91 PGYGNS----------QETGTAR-------DGATI---VEELRQTLRHkgLAPPYILVGHSLGGLYMQLFAKRYPQEVSG 150
Cdd:COG3545    4 PGLGGSgpdhwqswweRELPTVRrveqpdwDRPDLddwLAALDAAVAA--ADGPVVLVAHSLGCLAVAHWAARLPRKVAG 81

                         90
                 ....*....|....*
gi 491918477 151 LVLV---DPLLPGVV 162
Cdd:COG3545   82 ALLVappDPERPGFL 96
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 59-156 4.74e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.96  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491918477  59 IVFENGLRATVDGWDKVIDSLV-PDASIFAYNRPGYGNSQETGtardGATIVEELRQTLRHKGlAPPYILVGHSLGGLYM 137
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRaAGYPVYALNYPSTNGSIEDS----AEQLAAFVDAVLAATG-AEKVDLVGHSMGGLVA 82

                         90       100
                 ....*....|....*....|.
gi 491918477 138 QLFAKRY--PQEVSGLVLVDP 156
Cdd:COG1075   83 RYYLKRLggAAKVARVVTLGT 103
 
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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