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Conserved domains on  [gi|599657311|gb|EYF86109|]
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esterase [Staphylococcus aureus T16600]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
79-279 1.28e-33

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam07859:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 208  Bit Score: 122.32  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311   79 ILYIHGGFNALQPSPFHWRLLDKITLSTLYEVVLPIYPKTPEFH----IDDTFQAIQRVYDQlVSEVGH--QNVVVMGDG 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLAEQ-AAELGAdpSRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311  153 SGGALALSFVQSLLDNQQPLPNKLYLISPILDATLSNKDISDALIEQDAVLSQFGVNEIMKKWANGLPLTDKRISPI-NG 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLfAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 599657311  232 TIEGLPPVYMFGGGREMTHPDMKLFEQMMLQHHQYIEFYDYPKMVHDF 279
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
79-279 1.28e-33

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 122.32  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311   79 ILYIHGGFNALQPSPFHWRLLDKITLSTLYEVVLPIYPKTPEFH----IDDTFQAIQRVYDQlVSEVGH--QNVVVMGDG 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLAEQ-AAELGAdpSRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311  153 SGGALALSFVQSLLDNQQPLPNKLYLISPILDATLSNKDISDALIEQDAVLSQFGVNEIMKKWANGLPLTDKRISPI-NG 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLfAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 599657311  232 TIEGLPPVYMFGGGREMTHPDMKLFEQMMLQHHQYIEFYDYPKMVHDF 279
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
64-300 3.88e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 107.65  E-value: 3.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311  64 MQVFRFNFRHQIDKKILYIHGGFNALQPSPFHWRLLDKITLSTLYEVVLPIYPKTPEFH----IDDTFQAIQRVYDQlVS 139
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPfpaaLEDAYAALRWLRAN-AA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311 140 EVGH--QNVVVMGDGSGGALALSFVQSLLDNQQPLPNKLYLISPILDATLsnkdisdalieqdavlsqfgvneimkkwan 217
Cdd:COG0657   80 ELGIdpDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA------------------------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311 218 glpltdkriSPINGTIEGLPPVYMFGGGREMTHPDMKLFEQMMLQHHQYIEFYDYPKMVHDFPIYP-IRQSHKAIKQIAK 296
Cdd:COG0657  130 ---------SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEIAA 200

                 ....
gi 599657311 297 SIDE 300
Cdd:COG0657  201 FLRR 204
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
79-279 1.28e-33

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 122.32  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311   79 ILYIHGGFNALQPSPFHWRLLDKITLSTLYEVVLPIYPKTPEFH----IDDTFQAIQRVYDQlVSEVGH--QNVVVMGDG 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLAEQ-AAELGAdpSRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311  153 SGGALALSFVQSLLDNQQPLPNKLYLISPILDATLSNKDISDALIEQDAVLSQFGVNEIMKKWANGLPLTDKRISPI-NG 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLfAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 599657311  232 TIEGLPPVYMFGGGREMTHPDMKLFEQMMLQHHQYIEFYDYPKMVHDF 279
Cdd:pfam07859 160 DLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
64-300 3.88e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 107.65  E-value: 3.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311  64 MQVFRFNFRHQIDKKILYIHGGFNALQPSPFHWRLLDKITLSTLYEVVLPIYPKTPEFH----IDDTFQAIQRVYDQlVS 139
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPfpaaLEDAYAALRWLRAN-AA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311 140 EVGH--QNVVVMGDGSGGALALSFVQSLLDNQQPLPNKLYLISPILDATLsnkdisdalieqdavlsqfgvneimkkwan 217
Cdd:COG0657   80 ELGIdpDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA------------------------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311 218 glpltdkriSPINGTIEGLPPVYMFGGGREMTHPDMKLFEQMMLQHHQYIEFYDYPKMVHDFPIYP-IRQSHKAIKQIAK 296
Cdd:COG0657  130 ---------SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEIAA 200

                 ....
gi 599657311 297 SIDE 300
Cdd:COG0657  201 FLRR 204
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
71-189 3.01e-09

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 57.54  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599657311   71 FRHQIDKKILYIHGGFNALQPSPfhWRLldkITLSTLYE------VVLPIYPKTPEFHIDDTF--QAIQ--RVYDQLVSE 140
Cdd:pfam10340 117 FDPKVDPILLYYHGGGFALKLIP--VTL---VFLNNLGKyfpdmaILVSDYTVTANCPQSYTYplQVLQclAVYDYLTLT 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 599657311  141 VGHQNVVVMGDGSGGALALSFVQSLLD-NQQPLPNKLYLISPILDATLSN 189
Cdd:pfam10340 192 KGCKNVTLMGDSAGGNLVLNILLYLHKcNKVVLPKKAIAISPWLNLTDRN 241
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
241-302 9.01e-03

RecG-like helicase [Replication, recombination and repair];


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 37.72  E-value: 9.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599657311 241 MFGGGREMTHPDMKLFEQMMLQHHQYIEfydypkmvhdfPIYP----IRQS--HKAIKQIAKSIDEDV 302
Cdd:COG1200  119 RFRGGLQMVHPEYELLDEEEAELAGRLT-----------PVYPltegLSQKtlRKLIRQALDLLAPDL 175
 
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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