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Conserved domains on  [gi|556505242|ref|WP_023351247|]
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MULTISPECIES: alpha/beta hydrolase [Staphylococcus]

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 1.60e-45

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: 152.75  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242   78 ILYLHGGYNTLQPSPFHWRLLDKLALNTLHEVVLPIYPKAPEYH----LEDTYNAIKEVYdELVAEVGVD--HIVIMGDG 151
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLA-EQAAELGADpsRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242  152 SGGGLAMRFVQSLIEENEPVPSKLFLISPLLDATLSNKMITEDLEDEDILVSRFGVNELMKVWSNGLPLTDKRVSPLYGE 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 556505242  232 -LRGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDF 278
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.
78-278 1.60e-45

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: 152.75  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242   78 ILYLHGGYNTLQPSPFHWRLLDKLALNTLHEVVLPIYPKAPEYH----LEDTYNAIKEVYdELVAEVGVD--HIVIMGDG 151
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLA-EQAAELGADpsRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242  152 SGGGLAMRFVQSLIEENEPVPSKLFLISPLLDATLSNKMITEDLEDEDILVSRFGVNELMKVWSNGLPLTDKRVSPLYGE 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 556505242  232 -LRGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDF 278
Cdd:pfam07859 160 dLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
78-299 5.22e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 125.76  E-value: 5.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242  78 ILYLHGGYNTLQPSPFHWRLLDKLALNTLHEVVLPIYPKAPEYH----LEDTYNAIKEVYDElVAEVGVD--HIVIMGDG 151
Cdd:COG0657   16 VVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPfpaaLEDAYAALRWLRAN-AAELGIDpdRIAVAGDS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242 152 SGGGLAMRFVQSLIEENEPVPSKLFLISPLLDATlsnkmitedlededilvsrfgvnelmkvwsnglpltdkrVSPLYGE 231
Cdd:COG0657   95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------------ASPLRAD 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556505242 232 LRGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDFPLYP-IRQSHKVIKQITKAIRK 299
Cdd:COG0657  136 LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEIAAFLRR 204
PRK10162 PRK10162
acetyl esterase;
224-281 6.39e-03

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 37.78  E-value: 6.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556505242 224 RVSPLYGEL-----RGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDFPLY 281
Cdd:PRK10162 232 RESPYYCLFnndltRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHY 294
 
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 1.60e-45

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: 152.75  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242   78 ILYLHGGYNTLQPSPFHWRLLDKLALNTLHEVVLPIYPKAPEYH----LEDTYNAIKEVYdELVAEVGVD--HIVIMGDG 151
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPfpaaYDDAYAALRWLA-EQAAELGADpsRIAVAGDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242  152 SGGGLAMRFVQSLIEENEPVPSKLFLISPLLDATLSNKMITEDLEDEDILVSRFGVNELMKVWSNGLPLTDKRVSPLYGE 231
Cdd:pfam07859  80 AGGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 556505242  232 -LRGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDF 278
Cdd:pfam07859 160 dLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
78-299 5.22e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 125.76  E-value: 5.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242  78 ILYLHGGYNTLQPSPFHWRLLDKLALNTLHEVVLPIYPKAPEYH----LEDTYNAIKEVYDElVAEVGVD--HIVIMGDG 151
Cdd:COG0657   16 VVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPfpaaLEDAYAALRWLRAN-AAELGIDpdRIAVAGDS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242 152 SGGGLAMRFVQSLIEENEPVPSKLFLISPLLDATlsnkmitedlededilvsrfgvnelmkvwsnglpltdkrVSPLYGE 231
Cdd:COG0657   95 AGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT---------------------------------------ASPLRAD 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556505242 232 LRGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDFPLYP-IRQSHKVIKQITKAIRK 299
Cdd:COG0657  136 LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAgLPEARAALAEIAAFLRR 204
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
70-188 3.94e-06

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: 47.91  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556505242   70 FRHESNNKILYLHGGYNTLQPSP----FHW---RLLDKLALNTLHEVVLPIYPKAPEYHLEDTYNAIkeVYDELVAEVGV 142
Cdd:pfam10340 117 FDPKVDPILLYYHGGGFALKLIPvtlvFLNnlgKYFPDMAILVSDYTVTANCPQSYTYPLQVLQCLA--VYDYLTLTKGC 194
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 556505242  143 DHIVIMGDGSGGGLAMRFVQSLIEENEPV-PSKLFLISPLLDATLSN 188
Cdd:pfam10340 195 KNVTLMGDSAGGNLVLNILLYLHKCNKVVlPKKAIAISPWLNLTDRN 241
PRK10162 PRK10162
acetyl esterase;
224-281 6.39e-03

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 37.78  E-value: 6.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556505242 224 RVSPLYGEL-----RGLPPVYMYGGGKEIQNPDMKELARLLEDYGQYVEFNEYPKMVHDFPLY 281
Cdd:PRK10162 232 RESPYYCLFnndltRDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHY 294
 
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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