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Conserved domains on  [gi|320144546|gb|EFW36310|]
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phospholipase/carboxylesterase [Staphylococcus aureus subsp. aureus MRSA177]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10785415)

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
PubMed:  19508187|12369917|37582413

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
8-195 1.26e-51

Predicted esterase [General function prediction only];


:

Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 164.70  E-value: 1.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   8 GQNGAPTLILLHGTGGDEFDLLPLGEALN-ENYHLLSIRGQVSE-NGMNRYFK-RLGEGVYDEEDLAFRGQELLTFIKEA 84
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAlPGAAVLAPRAPVPEgPGGRAWFDlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  85 AERYDFDIEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLYPVEVT---STKDLSDVSVLLSMGKHDPIVPLAASEQ 161
Cdd:COG0400   81 EARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEAlpaPEAALAGTPVFLAHGTQDPVIPVERARE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 320144546 162 VINLFNTRGAQVEEVWVK-GHEITETGLTAGQQIL 195
Cdd:COG0400  161 AAEALEAAGADVTYREYPgGHEISPEELADARAWL 195
 
Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
8-195 1.26e-51

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 164.70  E-value: 1.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   8 GQNGAPTLILLHGTGGDEFDLLPLGEALN-ENYHLLSIRGQVSE-NGMNRYFK-RLGEGVYDEEDLAFRGQELLTFIKEA 84
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAlPGAAVLAPRAPVPEgPGGRAWFDlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  85 AERYDFDIEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLYPVEVT---STKDLSDVSVLLSMGKHDPIVPLAASEQ 161
Cdd:COG0400   81 EARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEAlpaPEAALAGTPVFLAHGTQDPVIPVERARE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 320144546 162 VINLFNTRGAQVEEVWVK-GHEITETGLTAGQQIL 195
Cdd:COG0400  161 AAEALEAAGADVTYREYPgGHEISPEELADARAWL 195
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 12-188 3.17e-05

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 43.13  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   12 APTLILLHGTG--GDEFDLLPLGEALNENYHLLSIRGQVSENGMNryFKRLGEGVYDEEDLAFRGQELLTFIKEAAERY- 88
Cdd:pfam02230  14 QATVIFLHGLGdsGHGWADAAKTEAPLPNIKFIFPHGPEIPVTLN--GGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIe 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   89 ---DFDIEKA------VLVGFSNGSNIAINLMLRSEAPFKKAL----LYAPLYPVEVTSTKDLSDVSVLLSMGKHDPIVP 155
Cdd:pfam02230  92 eliDAEQKKGipssriIIGGFSQGAMLALYSALTLPLPLGGIVafsgFLPLPTKFPSHPNLVTKKTPIFLIHGEEDPVVP 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 320144546  156 LAASEQVINLFNTRGAQVEEVWVKG--HEITETGL 188
Cdd:pfam02230 172 LALGKLAKEYLKTSLNKVELKIYEGlaHSICGREM 206
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 3-113 2.65e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   3 HIFREGQNGAPTLILLHGTGGDEFDLLPLGEALNENYHLLSI----RGQVSengmnryfKRLGEGVYDEedLAfrgQELL 78
Cdd:PRK14875 122 RYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALdlpgHGASS--------KAVGAGSLDE--LA---AAVL 188

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 320144546  79 TFIKeaaeryDFDIEKAVLVGFSNGSNIAINLMLR 113
Cdd:PRK14875 189 AFLD------ALGIERAHLVGHSMGGAVALRLAAR 217
 
Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
8-195 1.26e-51

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 164.70  E-value: 1.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   8 GQNGAPTLILLHGTGGDEFDLLPLGEALN-ENYHLLSIRGQVSE-NGMNRYFK-RLGEGVYDEEDLAFRGQELLTFIKEA 84
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAlPGAAVLAPRAPVPEgPGGRAWFDlSFLEGREDEEGLAAAAEALAAFIDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  85 AERYDFDIEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLYPVEVT---STKDLSDVSVLLSMGKHDPIVPLAASEQ 161
Cdd:COG0400   81 EARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEAlpaPEAALAGTPVFLAHGTQDPVIPVERARE 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 320144546 162 VINLFNTRGAQVEEVWVK-GHEITETGLTAGQQIL 195
Cdd:COG0400  161 AAEALEAAGADVTYREYPgGHEISPEELADARAWL 195
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-183 2.52e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.79  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   3 HIFREGQNGAPTLILLHGTGGDEFDLLPLGEALNEN-YHLLSI--RGQvsenGMNRyfkRLGEGVYDEEDLAfrgQELLT 79
Cdd:COG2267   19 RRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFdlRGH----GRSD---GPRGHVDSFDDYV---DDLRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  80 FIKEAAERYDfdiEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLY---PV---------EVTSTKDLSDVS--VLL 145
Cdd:COG2267   89 ALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYradPLlgpsarwlrALRLAEALARIDvpVLV 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 320144546 146 SMGKHDPIVPLAASEQvinLFNTRGAQVEEVWVKG--HEI 183
Cdd:COG2267  166 LHGGADRVVPPEAARR---LAARLSPDVELVLLPGarHEL 202
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-181 2.80e-09

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: 54.62  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   3 HIFREGQNGaPTLILLHGTGGDEFDLLPLGEALNENYHLLSI--RGQvsenGmnryFKRLGEGVYDEEDLAfrgQELLTF 80
Cdd:COG0596   15 HYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPdlRGH----G----RSDKPAGGYTLDDLA---DDLAAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  81 IKEaaerydFDIEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLY-------------------PVEVTSTKDLSD- 140
Cdd:COG0596   83 LDA------LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLaalaeplrrpglapealaaLLRALARTDLREr 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 320144546 141 -----VSVLLSMGKHDPIVPLAASEQVINLFntRGAQVEEVWVKGH 181
Cdd:COG0596  157 laritVPTLVIWGEKDPIVPPALARRLAELL--PNAELVVLPGAGH 200
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 12-188 3.17e-05

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 43.13  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   12 APTLILLHGTG--GDEFDLLPLGEALNENYHLLSIRGQVSENGMNryFKRLGEGVYDEEDLAFRGQELLTFIKEAAERY- 88
Cdd:pfam02230  14 QATVIFLHGLGdsGHGWADAAKTEAPLPNIKFIFPHGPEIPVTLN--GGMRMPAWFDLVGLSPNAKEDEAGIKNSAETIe 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   89 ---DFDIEKA------VLVGFSNGSNIAINLMLRSEAPFKKAL----LYAPLYPVEVTSTKDLSDVSVLLSMGKHDPIVP 155
Cdd:pfam02230  92 eliDAEQKKGipssriIIGGFSQGAMLALYSALTLPLPLGGIVafsgFLPLPTKFPSHPNLVTKKTPIFLIHGEEDPVVP 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 320144546  156 LAASEQVINLFNTRGAQVEEVWVKG--HEITETGL 188
Cdd:pfam02230 172 LALGKLAKEYLKTSLNKVELKIYEGlaHSICGREM 206
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
13-182 4.48e-05

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 42.92  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  13 PTLILLHGTGGDE---FDLLPLGEALNE---------------NYHLLSIRGQvsENGMNRYFkrlgegvydEEDLAfrg 74
Cdd:COG2382  113 PVLYLLDGGGGDEqdwFDQGRLPTILDNliaagkippmivvmpDGGDGGDRGT--EGPGNDAF---------ERFLA--- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  75 QELLTFIKeaaERYDFDIEKA--VLVGFSNGSNIAINLMLRseAP--FKKALLYAPLYPVEVTSTKDLSDVSVL------ 144
Cdd:COG2382  179 EELIPFVE---KNYRVSADPEhrAIAGLSMGGLAALYAALR--HPdlFGYVGSFSGSFWWPPGDADRGGWAELLaagapk 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 320144546 145 ------LSMGKHDPIVPlaASEQVINLFNTRGAQVEEVWVKG-HE 182
Cdd:COG2382  254 kplrfyLDVGTEDDLLE--ANRALAAALKAKGYDVEYREFPGgHD 296
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
9-126 1.99e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 40.70  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   9 QNGAPTLILLHGTGGDEFDLLPLGEALNEN-YHLLSIrgqvsengmnryfkRL-GEGVYDEEDLAFRGQELLTFIKEA-- 84
Cdd:COG1647   12 EGGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAP--------------RLpGHGTSPEDLLKTTWEDWLEDVEEAye 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 320144546  85 --AERYDfdieKAVLVGFSNGSNIAINLMLRSEAPfKKALLYAP 126
Cdd:COG1647   78 ilKAGYD----KVIVIGLSMGGLLALLLAARYPDV-AGLVLLSP 116
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 3-113 2.65e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   3 HIFREGQNGAPTLILLHGTGGDEFDLLPLGEALNENYHLLSI----RGQVSengmnryfKRLGEGVYDEedLAfrgQELL 78
Cdd:PRK14875 122 RYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALdlpgHGASS--------KAVGAGSLDE--LA---AAVL 188

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 320144546  79 TFIKeaaeryDFDIEKAVLVGFSNGSNIAINLMLR 113
Cdd:PRK14875 189 AFLD------ALGIERAHLVGHSMGGAVALRLAAR 217
PRK11460 PRK11460
putative hydrolase; Provisional
 1-183 2.45e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 37.71  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   1 MEHIFREGQNGA----PTLILLHGTGGDEFDLLPLGEALNENY---HLLSIRG-QVSENGMNRYFKRLgEGVYDE---ED 69
Cdd:PRK11460   1 MKHDHFVVQSPDkpaqQLLLLFHGVGDNPVAMGEIGSWFAPAFpdaLVVSVGGpEPSGNGAGRQWFSV-QGITEDnrqAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546  70 LAFRGQELLTFIKEAAERYDFDIEKAVLVGFSNGSNIAINLmLRSEAPFKKALL-----YAPLypvevtSTKDLSDVSVL 144
Cdd:PRK11460  80 VAAIMPTFIETVRYWQQQSGVGASATALIGFSQGAIMALEA-VKAEPGLAGRVIafsgrYASL------PETAPTATTIH 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 320144546 145 LSMGKHDPIVPLAASEQVINLFNTRGAQ-----VEEVwvkGHEI 183
Cdd:PRK11460 153 LIHGGEDPVIDVAHAVAAQEALISLGGDvtldiVEDL---GHAI 193
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 13-138 2.94e-03

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: 37.48  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320144546   13 PTLILLHG--TGGDEFDllPLGEALNEN---YHLLSIRGQ-VSENGMNRYfkrlgegVYDEEDLAfrgqELLTFIKEAae 86
Cdd:pfam00561   1 PPVLLLHGlpGSSDLWR--KLAPALARDgfrVIALDLRGFgKSSRPKAQD-------DYRTDDLA----EDLEYILEA-- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320144546   87 rydFDIEKAVLVGFSNGSNIAINLMLRSEAPFKKALLYAPLYPVEVTSTKDL 138
Cdd:pfam00561  66 ---LGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADR 114
 
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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