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Conserved domains on  [gi|488377848|ref|WP_002447233|]
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alpha/beta hydrolase [Staphylococcus epidermidis]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

alpha/beta hydrolase 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

Graphical summary

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List of domain hits

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.
78-278 5.64e-49

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: 162.00  E-value: 5.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848   78 ILYLHGGYNTLQPSPFHWRLLDKLTLNTLHEVVLPIYPKSPDYHYLETFKAIRDVYNQLVE---EVGAD--NIVMMGDGS 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaELGADpsRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848  153 GGGLALSFVQSLINDNQEVPRKLFLLSPLLDATLTNPNITQTLEENDILVSRFGVHQLMKSWANDLPLSDARISPLYG-T 231
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 488377848  232 LKGLPPIYMYGGGREILSPDMHVFTHALEECGNDVEFKEYPKMVHDF 278
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 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.
78-278 5.64e-49

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: 162.00  E-value: 5.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848   78 ILYLHGGYNTLQPSPFHWRLLDKLTLNTLHEVVLPIYPKSPDYHYLETFKAIRDVYNQLVE---EVGAD--NIVMMGDGS 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaELGADpsRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848  153 GGGLALSFVQSLINDNQEVPRKLFLLSPLLDATLTNPNITQTLEENDILVSRFGVHQLMKSWANDLPLSDARISPLYG-T 231
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 488377848  232 LKGLPPIYMYGGGREILSPDMHVFTHALEECGNDVEFKEYPKMVHDF 278
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
63-293 7.29e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 114.97  E-value: 7.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848  63 MQVFRFNFRHEKNQKILYLHGGYNTLQPSPFHWRLLDKLTLNTLHEVVLPIYPKSPDYHYLETFKAIRDVYNQLVEE--- 139
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848 140 --VGADNIVMMGDGSGGGLALSFVQSLINDNQEVPRKLFLLSPLLDATLtnpnitqtleendilvsrfgvhqlmkswand 217
Cdd:COG0657   81 lgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA------------------------------- 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377848 218 lplsdariSPLYGTLKGLPPIYMYGGGREILSPDMHVFTHALEECGNDVEFKEYPKMVHDFPIYP-IRQSHKVLKHI 293
Cdd:COG0657  130 --------SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEI 198
 
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.
78-278 5.64e-49

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: 162.00  E-value: 5.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848   78 ILYLHGGYNTLQPSPFHWRLLDKLTLNTLHEVVLPIYPKSPDYHYLETFKAIRDVYNQLVE---EVGAD--NIVMMGDGS 152
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaELGADpsRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848  153 GGGLALSFVQSLINDNQEVPRKLFLLSPLLDATLTNPNITQTLEENDILVSRFGVHQLMKSWANDLPLSDARISPLYG-T 231
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 488377848  232 LKGLPPIYMYGGGREILSPDMHVFTHALEECGNDVEFKEYPKMVHDF 278
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
63-293 7.29e-31

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 114.97  E-value: 7.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848  63 MQVFRFNFRHEKNQKILYLHGGYNTLQPSPFHWRLLDKLTLNTLHEVVLPIYPKSPDYHYLETFKAIRDVYNQLVEE--- 139
Cdd:COG0657    1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANaae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848 140 --VGADNIVMMGDGSGGGLALSFVQSLINDNQEVPRKLFLLSPLLDATLtnpnitqtleendilvsrfgvhqlmkswand 217
Cdd:COG0657   81 lgIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA------------------------------- 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377848 218 lplsdariSPLYGTLKGLPPIYMYGGGREILSPDMHVFTHALEECGNDVEFKEYPKMVHDFPIYP-IRQSHKVLKHI 293
Cdd:COG0657  130 --------SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEI 198
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
78-188 5.23e-07

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: 50.60  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377848   78 ILYLHGGYNTLQPSPfhWRLLdklTLNTLHE------VVLPIYP----KSPDYHYLETFKAIRDVYNQLVEEVGADNIVM 147
Cdd:pfam10340 125 LLYYHGGGFALKLIP--VTLV---FLNNLGKyfpdmaILVSDYTvtanCPQSYTYPLQVLQCLAVYDYLTLTKGCKNVTL 199
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488377848  148 MGDGSGGGLALSFVQSLINDNQEV-PRKLFLLSPLLDATLTN 188
Cdd:pfam10340 200 MGDSAGGNLVLNILLYLHKCNKVVlPKKAIAISPWLNLTDRN 241
 
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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