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Conserved domains on  [gi|613388912|gb|EZZ92795|]
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hypothetical protein W395_01481 [Staphylococcus aureus VET0057R]

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, ...
102-300 1.10e-28

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: 109.61  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  102 VLYAHGGAWFQDPLKIHFEFIDELAETLNAKVIMPVYPKIPHQDYQATYVLFEKLYHDLLNQV----ADSKQIVVMGDSA 177
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAaelgADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  178 GGQIALSFAQLLKEKHIVQPGHIVLISPVLDATMQHPEIPAYLKKD-PMVGVDGSVFLAEQWAGDTPLDNYKVSPI-NGD 255
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLfASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 613388912  256 LDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDFI--PGyyQFH 300
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIeyPG--MPH 205
 
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.
102-300 1.10e-28

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: 109.61  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  102 VLYAHGGAWFQDPLKIHFEFIDELAETLNAKVIMPVYPKIPHQDYQATYVLFEKLYHDLLNQV----ADSKQIVVMGDSA 177
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAaelgADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  178 GGQIALSFAQLLKEKHIVQPGHIVLISPVLDATMQHPEIPAYLKKD-PMVGVDGSVFLAEQWAGDTPLDNYKVSPI-NGD 255
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLfASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 613388912  256 LDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDFI--PGyyQFH 300
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIeyPG--MPH 205
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
93-317 9.29e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 107.27  E-value: 9.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  93 DKQDKHQRVVLYAHGGAWFQDPLKIHFEFIDELAETLNAKVIMPVYPKIPHQDYQATYVLFEKLYHDLLNQVA----DSK 168
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAelgiDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912 169 QIVVMGDSAGGQIALSFAQLLKEKHIVQPGHIVLISPVLDATmqhpeipaylkkdpmvgvdgsvflaeqwagdtpldnyk 248
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT-------------------------------------- 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613388912 249 VSPINGDLDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDFI--PGyyQFHIYPVFP-IPERRRFLYQV 317
Cdd:COG0657  129 ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHvyPG--GGHGFGLLAgLPEARAALAEI 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.
102-300 1.10e-28

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: 109.61  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  102 VLYAHGGAWFQDPLKIHFEFIDELAETLNAKVIMPVYPKIPHQDYQATYVLFEKLYHDLLNQV----ADSKQIVVMGDSA 177
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAaelgADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  178 GGQIALSFAQLLKEKHIVQPGHIVLISPVLDATMQHPEIPAYLKKD-PMVGVDGSVFLAEQWAGDTPLDNYKVSPI-NGD 255
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSYLAREFADgPLLTRAAMDWFWRLYLPGADRDDPLASPLfASD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 613388912  256 LDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDFI--PGyyQFH 300
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIeyPG--MPH 205
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
93-317 9.29e-28

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 107.27  E-value: 9.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  93 DKQDKHQRVVLYAHGGAWFQDPLKIHFEFIDELAETLNAKVIMPVYPKIPHQDYQATYVLFEKLYHDLLNQVA----DSK 168
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAelgiDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912 169 QIVVMGDSAGGQIALSFAQLLKEKHIVQPGHIVLISPVLDATmqhpeipaylkkdpmvgvdgsvflaeqwagdtpldnyk 248
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT-------------------------------------- 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613388912 249 VSPINGDLDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDFI--PGyyQFHIYPVFP-IPERRRFLYQV 317
Cdd:COG0657  129 ASPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHvyPG--GGHGFGLLAgLPEARAALAEI 198
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
72-230 7.02e-08

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: 53.30  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912   72 YQFKMPVkvdkhfgstvyTVNDKQDKhqrVVLYAHGGAWFQDPLKIHFEFIDELAETL-NAKVIMPVYPKIPHQDYQATY 150
Cdd:pfam10340 109 WLRKVPE-----------TFDPKVDP---ILLYYHGGGFALKLIPVTLVFLNNLGKYFpDMAILVSDYTVTANCPQSYTY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912  151 ---VLFEKLYHDLLNQVADSKQIVVMGDSAGGQIALSFA-QLLKEKHIVQPGHIVLISPVLDATMQHPEIPAYLKKDPmv 226
Cdd:pfam10340 175 plqVLQCLAVYDYLTLTKGCKNVTLMGDSAGGNLVLNILlYLHKCNKVVLPKKAIAISPWLNLTDRNEKEKEYMKAND-- 252

                  ....
gi 613388912  227 GVDG 230
Cdd:pfam10340 253 KLDG 256
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
102-292 6.34e-05

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 44.07  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912 102 VLYA-HGG-----AWFQDpLKIHfEFIDELAETLNAK---VIMP--------VYPKIPHQDYqATYVLfeklyHDLLNQV 164
Cdd:COG2382  114 VLYLlDGGggdeqDWFDQ-GRLP-TILDNLIAAGKIPpmiVVMPdggdggdrGTEGPGNDAF-ERFLA-----EELIPFV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388912 165 -------ADSKQIVVMGDSAGGQIALSFAqllkekhivqpghivlispvldatMQHPEIPAYlkkdpmVGVdgsvFLAEQ 237
Cdd:COG2382  186 eknyrvsADPEHRAIAGLSMGGLAALYAA------------------------LRHPDLFGY------VGS----FSGSF 231
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 613388912 238 WAGDTPLDNYKVSPI--NGDLDGLGRITLTVGTKEVLYPDALNLSQLLSAKGIEHDF 292
Cdd:COG2382  232 WWPPGDADRGGWAELlaAGAPKKPLRFYLDVGTEDDLLEANRALAAALKAKGYDVEY 288
 
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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