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Conserved domains on  [gi|19113642|ref|NP_596850|]
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sterol deacetylase Say1 [Schizosaccharomyces pombe]

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) ...
 4-374 2.60e-148

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: 424.25  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642     4 LSLLYRILT-LPIILVgttilYFTIG-TNFPHDELRHNLLSTLFCSSMLHLSKGLTVKDVRIFFHDSIGSTLLKN----- 76
Cdd:pfam10340   1 LSFLYKLITvLPIKLV-----YRSIGiTNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDSLSSTLYKFtgssp 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642    77 -RKKLNSENELPNYGEKFTHKYDNQDMPDS--VWLAKVnGMT---KSDPIILHLHGGMMALPYDKVILVGLSNLYKLFST 150
Cdd:pfam10340  76 tRYNLPSEDLLPNYGEIFTHKYLNQDMIDStkFWLRKV-PETfdpKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   151 TmnrppSILLVDYSLVS---QGYTYPKQVRECLNVYQVLI-SKGFRNITVLGESAGGTLILSFLYQiseLSKLNKVVWPK 226
Cdd:pfam10340 155 M-----AILVSDYTVTAncpQSYTYPLQVLQCLAVYDYLTlTKGCKNVTLMGDSAGGNLVLNILLY---LHKCNKVVLPK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   227 GVALISPWLDLT--NAKKIGSYRANDGLDVICYETLNRFGKAYVNN---EESLFTSSVVNINMNCDISIWSKIppIQDGK 301
Cdd:pfam10340 227 KAIAISPWLNLTdrNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvepEESLFTDPFVNIEMNFDIETWSKI--LEKCK 304

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113642   302 VLVLFGENEVFRDEILSWTSKIGLLKAY----PNRVLMDKQGIHIGlfleespSIGPGMTNLDIWKKKFSVNSLYTF 374
Cdd:pfam10340 305 LLITYGDDEILSDQIKSFIDKISELKAYnhftPNNVLIDKQGIHIG-------PILPYMTNLDKWSKKFSVKSILTF 374
 
Name Accession Description Interval E-value
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 4-374 2.60e-148

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: 424.25  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642     4 LSLLYRILT-LPIILVgttilYFTIG-TNFPHDELRHNLLSTLFCSSMLHLSKGLTVKDVRIFFHDSIGSTLLKN----- 76
Cdd:pfam10340   1 LSFLYKLITvLPIKLV-----YRSIGiTNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDSLSSTLYKFtgssp 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642    77 -RKKLNSENELPNYGEKFTHKYDNQDMPDS--VWLAKVnGMT---KSDPIILHLHGGMMALPYDKVILVGLSNLYKLFST 150
Cdd:pfam10340  76 tRYNLPSEDLLPNYGEIFTHKYLNQDMIDStkFWLRKV-PETfdpKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   151 TmnrppSILLVDYSLVS---QGYTYPKQVRECLNVYQVLI-SKGFRNITVLGESAGGTLILSFLYQiseLSKLNKVVWPK 226
Cdd:pfam10340 155 M-----AILVSDYTVTAncpQSYTYPLQVLQCLAVYDYLTlTKGCKNVTLMGDSAGGNLVLNILLY---LHKCNKVVLPK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   227 GVALISPWLDLT--NAKKIGSYRANDGLDVICYETLNRFGKAYVNN---EESLFTSSVVNINMNCDISIWSKIppIQDGK 301
Cdd:pfam10340 227 KAIAISPWLNLTdrNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvepEESLFTDPFVNIEMNFDIETWSKI--LEKCK 304

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113642   302 VLVLFGENEVFRDEILSWTSKIGLLKAY----PNRVLMDKQGIHIGlfleespSIGPGMTNLDIWKKKFSVNSLYTF 374
Cdd:pfam10340 305 LLITYGDDEILSDQIKSFIDKISELKAYnhftPNNVLIDKQGIHIG-------PILPYMTNLDKWSKKFSVKSILTF 374
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
115-238 1.71e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.41  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642 115 TKSDPIILHLHGG-MMALPYDKVilvglSNLYKLFSTTMNRPpsILLVDYSLVSQgYTYPKQVRECLNVYQVLISKGFR- 192
Cdd:COG0657  10 KGPLPVVVYFHGGgWVSGSKDTH-----DPLARRLAARAGAA--VVSVDYRLAPE-HPFPAALEDAYAALRWLRANAAEl 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19113642 193 -----NITVLGESAGGTLILSFLYqiseLSKLNKVVWPKGVALISPWLDLT 238
Cdd:COG0657  82 gidpdRIAVAGDSAGGHLAAALAL----RARDRGGPRPAAQVLIYPVLDLT 128
 
Name Accession Description Interval E-value
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 4-374 2.60e-148

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: 424.25  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642     4 LSLLYRILT-LPIILVgttilYFTIG-TNFPHDELRHNLLSTLFCSSMLHLSKGLTVKDVRIFFHDSIGSTLLKN----- 76
Cdd:pfam10340   1 LSFLYKLITvLPIKLV-----YRSIGiTNFPKRRLRLDLLSRIFCRESLHLSDELICQYVLNPLFDSLSSTLYKFtgssp 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642    77 -RKKLNSENELPNYGEKFTHKYDNQDMPDS--VWLAKVnGMT---KSDPIILHLHGGMMALPYDKVILVGLSNLYKLFST 150
Cdd:pfam10340  76 tRYNLPSEDLLPNYGEIFTHKYLNQDMIDStkFWLRKV-PETfdpKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFPD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   151 TmnrppSILLVDYSLVS---QGYTYPKQVRECLNVYQVLI-SKGFRNITVLGESAGGTLILSFLYQiseLSKLNKVVWPK 226
Cdd:pfam10340 155 M-----AILVSDYTVTAncpQSYTYPLQVLQCLAVYDYLTlTKGCKNVTLMGDSAGGNLVLNILLY---LHKCNKVVLPK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   227 GVALISPWLDLT--NAKKIGSYRANDGLDVICYETLNRFGKAYVNN---EESLFTSSVVNINMNCDISIWSKIppIQDGK 301
Cdd:pfam10340 227 KAIAISPWLNLTdrNEKEKEYMKANDKLDGLCYKGLNMFGKLYVPNvepEESLFTDPFVNIEMNFDIETWSKI--LEKCK 304

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113642   302 VLVLFGENEVFRDEILSWTSKIGLLKAY----PNRVLMDKQGIHIGlfleespSIGPGMTNLDIWKKKFSVNSLYTF 374
Cdd:pfam10340 305 LLITYGDDEILSDQIKSFIDKISELKAYnhftPNNVLIDKQGIHIG-------PILPYMTNLDKWSKKFSVKSILTF 374
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 158-315 3.95e-09

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: 56.07  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   158 ILLVDYSLVSQgYTYPKQVRECLNVYQVLISKG------FRNITVLGESAGGTLILsflyQISELSKLNKVVWPKGVALI 231
Cdd:pfam07859  32 VVSVDYRLAPE-HPFPAAYDDAYAALRWLAEQAaelgadPSRIAVAGDSAGGNLAA----AVALRARDEGLPKPAGQVLI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642   232 SPWLDLTNAKKigSYRANDGLD--VICYETLNRFGKAYVNNEES-------LFTSSVvninmncdisiwSKIPPiqdgkV 302
Cdd:pfam07859 107 YPGTDLRTESP--SYLAREFADgpLLTRAAMDWFWRLYLPGADRddplaspLFASDL------------SGLPP-----A 167

                         170
                  ....*....|...
gi 19113642   303 LVLFGENEVFRDE 315
Cdd:pfam07859 168 LVVVAEFDPLRDE 180
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
115-238 1.71e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.41  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113642 115 TKSDPIILHLHGG-MMALPYDKVilvglSNLYKLFSTTMNRPpsILLVDYSLVSQgYTYPKQVRECLNVYQVLISKGFR- 192
Cdd:COG0657  10 KGPLPVVVYFHGGgWVSGSKDTH-----DPLARRLAARAGAA--VVSVDYRLAPE-HPFPAALEDAYAALRWLRANAAEl 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19113642 193 -----NITVLGESAGGTLILSFLYqiseLSKLNKVVWPKGVALISPWLDLT 238
Cdd:COG0657  82 gidpdRIAVAGDSAGGHLAAALAL----RARDRGGPRPAAQVLIYPVLDLT 128
 
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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