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Conserved domains on  [gi|398366343|ref|NP_011779|]
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steryl deacetylase [Saccharomyces cerevisiae S288C]

Protein Classification

alpha/beta hydrolase; tannase/feruloyl esterase family alpha/beta hydrolase( domain architecture ID 10563476)

uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds| tannase/feruloyl esterase family alpha/beta hydrolase similar to Aspergillus oryzae tannase and Aspergillus niger feruloyl esterase B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 50-421 0e+00

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: 586.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343   50 LKFAALLFTVVPVFIILDSMKIIFQRKRRFCLDHVNRSFLRQSSWILDERICQYVLNPLFV----CLYPSTFSSPTyvKC 125
Cdd:pfam10340   1 LSFLYKLITVLPIKLVYRSIGITNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDslssTLYKFTGSSPT--RY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  126 NIPIEDQKSPENNIFQDHQLNAPKIVSTKFYQYVMPEGFDPTTDPVLVFYHGGGYALKLTPTSFSFLNNMRNAFPKMAIL 205
Cdd:pfam10340  79 NLPSEDLLPNYGEIFTHKYLNQDMIDSTKFWLRKVPETFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMAIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  206 VPDYTVTATDDQSKKYPLQILQNVAIFDYVVKTMGCKNVVIMGDSAGGNAVLNIVLYLRKCHREIYPKKVIAISPWANAT 285
Cdd:pfam10340 159 VSDYTVTANCPQSYTYPLQVLQCLAVYDYLTLTKGCKNVTLMGDSAGGNLVLNILLYLHKCNKVVLPKKAIAISPWLNLT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  286 FFHEGEKEYMQGTQEWDGLCLKSHSMFGRMFVGN-NPNVDFTSDPFVNIEKNFETKMWQDILKKCSVMITYGSDELLSFQ 364
Cdd:pfam10340 239 DRNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvEPEESLFTDPFVNIEMNFDIETWSKILEKCKLLITYGDDEILSDQ 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366343  365 NKILAKKMSDASEGcNHFTAKNVLVEHQGYHTGPILNYSRNMDRWTNIPSIARILEF 421
Cdd:pfam10340 319 IKSFIDKISELKAY-NHFTPNNVLIDKQGIHIGPILPYMTNLDKWSKKFSVKSILTF 374
 
Name Accession Description Interval E-value
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 50-421 0e+00

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: 586.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343   50 LKFAALLFTVVPVFIILDSMKIIFQRKRRFCLDHVNRSFLRQSSWILDERICQYVLNPLFV----CLYPSTFSSPTyvKC 125
Cdd:pfam10340   1 LSFLYKLITVLPIKLVYRSIGITNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDslssTLYKFTGSSPT--RY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  126 NIPIEDQKSPENNIFQDHQLNAPKIVSTKFYQYVMPEGFDPTTDPVLVFYHGGGYALKLTPTSFSFLNNMRNAFPKMAIL 205
Cdd:pfam10340  79 NLPSEDLLPNYGEIFTHKYLNQDMIDSTKFWLRKVPETFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMAIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  206 VPDYTVTATDDQSKKYPLQILQNVAIFDYVVKTMGCKNVVIMGDSAGGNAVLNIVLYLRKCHREIYPKKVIAISPWANAT 285
Cdd:pfam10340 159 VSDYTVTANCPQSYTYPLQVLQCLAVYDYLTLTKGCKNVTLMGDSAGGNLVLNILLYLHKCNKVVLPKKAIAISPWLNLT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  286 FFHEGEKEYMQGTQEWDGLCLKSHSMFGRMFVGN-NPNVDFTSDPFVNIEKNFETKMWQDILKKCSVMITYGSDELLSFQ 364
Cdd:pfam10340 239 DRNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvEPEESLFTDPFVNIEMNFDIETWSKILEKCKLLITYGDDEILSDQ 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366343  365 NKILAKKMSDASEGcNHFTAKNVLVEHQGYHTGPILNYSRNMDRWTNIPSIARILEF 421
Cdd:pfam10340 319 IKSFIDKISELKAY-NHFTPNNVLIDKQGIHIGPILPYMTNLDKWSKKFSVKSILTF 374
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
161-286 4.42e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 56.03  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 161 PEGfDPTTDPVLVFYHGGGYALkLTPTSFSFLNNMRNAFPKMAILVPDYTVtATDDqskKYPLQILQNVAIFDYVV---K 237
Cdd:COG0657    6 PAG-AKGPLPVVVYFHGGGWVS-GSKDTHDPLARRLAARAGAAVVSVDYRL-APEH---PFPAALEDAYAALRWLRanaA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366343 238 TMGC--KNVVIMGDSAGGNAVLNIVLYLRKcHREIYPKKVIAISPWANATF 286
Cdd:COG0657   80 ELGIdpDRIAVAGDSAGGHLAAALALRARD-RGGPRPAAQVLIYPVLDLTA 129
PRK10162 PRK10162
acetyl esterase;
165-336 2.00e-03

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 40.09  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 165 DPTTDPVLVFYHGGGYALKLTPTSFSFlnnMR--NAFPKMAILVPDYTVTAtddqSKKYPLQILQNVAIFDYV---VKTM 239
Cdd:PRK10162  77 QPDSQATLFYLHGGGFILGNLDTHDRI---MRllASYSGCTVIGIDYTLSP----EARFPQAIEEIVAVCCYFhqhAEDY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 240 GC--KNVVIMGDSAGGNAVLNIVLYLRKchREIYPKKVIAISPWANATFFHEGEKEYMQGTqEWDGLCLKSHSMFGRMFV 317
Cdd:PRK10162 150 GInmSRIGFAGDSAGAMLALASALWLRD--KQIDCGKVAGVLLWYGLYGLRDSVSRRLLGG-VWDGLTQQDLQMYEEAYL 226

                        170
                 ....*....|....*....
gi 398366343 318 gnnPNVDFTSDPFVNIEKN 336
Cdd:PRK10162 227 ---SNDADRESPYYCLFNN 242
 
Name Accession Description Interval E-value
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 50-421 0e+00

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: 586.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343   50 LKFAALLFTVVPVFIILDSMKIIFQRKRRFCLDHVNRSFLRQSSWILDERICQYVLNPLFV----CLYPSTFSSPTyvKC 125
Cdd:pfam10340   1 LSFLYKLITVLPIKLVYRSIGITNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDslssTLYKFTGSSPT--RY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  126 NIPIEDQKSPENNIFQDHQLNAPKIVSTKFYQYVMPEGFDPTTDPVLVFYHGGGYALKLTPTSFSFLNNMRNAFPKMAIL 205
Cdd:pfam10340  79 NLPSEDLLPNYGEIFTHKYLNQDMIDSTKFWLRKVPETFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMAIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  206 VPDYTVTATDDQSKKYPLQILQNVAIFDYVVKTMGCKNVVIMGDSAGGNAVLNIVLYLRKCHREIYPKKVIAISPWANAT 285
Cdd:pfam10340 159 VSDYTVTANCPQSYTYPLQVLQCLAVYDYLTLTKGCKNVTLMGDSAGGNLVLNILLYLHKCNKVVLPKKAIAISPWLNLT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  286 FFHEGEKEYMQGTQEWDGLCLKSHSMFGRMFVGN-NPNVDFTSDPFVNIEKNFETKMWQDILKKCSVMITYGSDELLSFQ 364
Cdd:pfam10340 239 DRNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvEPEESLFTDPFVNIEMNFDIETWSKILEKCKLLITYGDDEILSDQ 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366343  365 NKILAKKMSDASEGcNHFTAKNVLVEHQGYHTGPILNYSRNMDRWTNIPSIARILEF 421
Cdd:pfam10340 319 IKSFIDKISELKAY-NHFTPNNVLIDKQGIHIGPILPYMTNLDKWSKKFSVKSILTF 374
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
161-286 4.42e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 56.03  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 161 PEGfDPTTDPVLVFYHGGGYALkLTPTSFSFLNNMRNAFPKMAILVPDYTVtATDDqskKYPLQILQNVAIFDYVV---K 237
Cdd:COG0657    6 PAG-AKGPLPVVVYFHGGGWVS-GSKDTHDPLARRLAARAGAAVVSVDYRL-APEH---PFPAALEDAYAALRWLRanaA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366343 238 TMGC--KNVVIMGDSAGGNAVLNIVLYLRKcHREIYPKKVIAISPWANATF 286
Cdd:COG0657   80 ELGIdpDRIAVAGDSAGGHLAAALALRARD-RGGPRPAAQVLIYPVLDLTA 129
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 172-332 2.32e-08

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: 54.14  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  172 LVFYHGGGYALKLTPTSFSFLNNMRNAFPkMAILVPDYTVtATDDqskKYPLQILQNVAIFDYVVKT---MGCK--NVVI 246
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAG-AVVVSVDYRL-APEH---PFPAAYDDAYAALRWLAEQaaeLGADpsRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343  247 MGDSAGGNAVLNIVLYLRKcHREIYPKKVIAISPWANATFfhegEKEYMQGTQEWDGLCLKSHSM--FGRMFVgnnPNVD 324
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARD-EGLPKPAGQVLIYPGTDLRT----ESPSYLAREFADGPLLTRAAMdwFWRLYL---PGAD 147


                  ....*...
gi 398366343  325 FTsDPFVN 332
Cdd:pfam07859 148 RD-DPLAS 154
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
158-296 7.60e-04

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 40.77  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 158 YVMPEgfDPTTDPVLVFYHGGGYAlkltpTSFSFLNNMRnAFPKM--AILVPDYTvtATDDQSKKYPLQILQNV-AIFDY 234
Cdd:COG1506   14 LYLPA--DGKKYPVVVYVHGGPGS-----RDDSFLPLAQ-ALASRgyAVLAPDYR--GYGESAGDWGGDEVDDVlAAIDY 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366343 235 VVKT--MGCKNVVIMGDSAGGNAVLNIVLYlrkcHREIYpKKVIAISPWANATFFHEGEKEYMQ 296
Cdd:COG1506   84 LAARpyVDPDRIGIYGHSYGGYMALLAAAR----HPDRF-KAAVALAGVSDLRSYYGTTREYTE 142
PRK10162 PRK10162
acetyl esterase;
165-336 2.00e-03

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 40.09  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 165 DPTTDPVLVFYHGGGYALKLTPTSFSFlnnMR--NAFPKMAILVPDYTVTAtddqSKKYPLQILQNVAIFDYV---VKTM 239
Cdd:PRK10162  77 QPDSQATLFYLHGGGFILGNLDTHDRI---MRllASYSGCTVIGIDYTLSP----EARFPQAIEEIVAVCCYFhqhAEDY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366343 240 GC--KNVVIMGDSAGGNAVLNIVLYLRKchREIYPKKVIAISPWANATFFHEGEKEYMQGTqEWDGLCLKSHSMFGRMFV 317
Cdd:PRK10162 150 GInmSRIGFAGDSAGAMLALASALWLRD--KQIDCGKVAGVLLWYGLYGLRDSVSRRLLGG-VWDGLTQQDLQMYEEAYL 226

                        170
                 ....*....|....*....
gi 398366343 318 gnnPNVDFTSDPFVNIEKN 336
Cdd:PRK10162 227 ---SNDADRESPYYCLFNN 242
 
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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