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Conserved domains on  [gi|1938963749|gb|QPK40859|]
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proteasome subunit beta 8, partial [Bos taurus]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-124 1.85e-81

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


The actual alignment was detected with superfamily member cd03761:

Pssm-ID: 469781  Cd Length: 188  Bit Score: 237.53  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:cd03761    65 LYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYR 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:cd03761   145 YDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-124 1.85e-81

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 237.53  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:cd03761    65 LYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYR 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:cd03761   145 YDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-135 3.04e-76

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 226.41  E-value: 3.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:PTZ00488  104 LYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLMHQY 135
Cdd:PTZ00488  184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-119 1.49e-31

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 110.76  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:TIGR03634  66 LYELRRGRPMSVKALATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYR 145

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDG 119
Cdd:TIGR03634 146 EDMSVEEAKKLAVRAIKSAIERDVASGNGIDVAVITKDG 184
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-115 3.44e-29

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 104.57  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNM--MCQYRGMG-LSMGSMICGWDKKG-PGLYYVDENGTRLSGNMFSTGSGNSHAYGVMD 76
Cdd:pfam00227  70 LYRLRYGRPIPVELAARIADLLqaYTQYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE 149

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938963749  77 SGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHM 115
Cdd:pfam00227 150 KLYRPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-124 4.08e-28

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 102.92  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:COG0638   100 LYELRYGEPISVEGLAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVL 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1938963749  76 DSGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:COG0638   178 EKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-124 1.85e-81

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 237.53  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:cd03761    65 LYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYR 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:cd03761   145 YDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-135 3.04e-76

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 226.41  E-value: 3.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:PTZ00488  104 LYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLMHQY 135
Cdd:PTZ00488  184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-124 3.03e-47

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 150.67  E-value: 3.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKK-GPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGY 79
Cdd:cd01912    65 LYELRNGRELSVKAAANLLSNILYSYRGFPYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1938963749  80 RPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:cd01912   145 KPDMTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 1-115 2.32e-32

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 112.59  E-value: 2.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYR--GMGLSMGSMICGWDKK-GPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDS 77
Cdd:cd01906    65 LYRLRYGEPIPVEALAKLLANLLYEYTqsLRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEK 144

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1938963749  78 GYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHM 115
Cdd:cd01906   145 LYKPDMTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-119 1.49e-31

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 110.76  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:TIGR03634  66 LYELRRGRPMSVKALATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYR 145

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDG 119
Cdd:TIGR03634 146 EDMSVEEAKKLAVRAIKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-124 7.14e-30

Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme for non-lysosomal protein degradation in both the cytosol and the nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are both members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239733  Cd Length: 188  Bit Score: 106.57  E-value: 7.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:cd03764    65 LYELRRGRPMSIKALATLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYK 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:cd03764   145 EDMTVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-115 3.44e-29

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 104.57  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNM--MCQYRGMG-LSMGSMICGWDKKG-PGLYYVDENGTRLSGNMFSTGSGNSHAYGVMD 76
Cdd:pfam00227  70 LYRLRYGRPIPVELAARIADLLqaYTQYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE 149

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938963749  77 SGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHM 115
Cdd:pfam00227 150 KLYRPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-124 4.08e-28

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 102.92  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:COG0638   100 LYELRYGEPISVEGLAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVL 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1938963749  76 DSGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVE 124
Cdd:COG0638   178 EKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-119 6.19e-19

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 78.42  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   2 YYLR-----NGERISVSAASKLLSNMMCQYRGMgLSMGSMICGWDK-KGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:cd03762    61 YYLDmhsieLGEPPLVKTAASLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYV 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1938963749  76 DSGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDG 119
Cdd:cd03762   140 DANYKPGMTLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDG 183
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-96 6.84e-19

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 77.44  E-value: 6.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMG-LSMGSMICGWDKKGPGLYYVDENGTRLSG-NMFSTGSGNSHAYGVMDSG 78
Cdd:cd01901    65 LYRLRYGEPISVVALAKELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKL 144

                          90
                  ....*....|....*...
gi 1938963749  79 YRPDLSIEEAYDLGRRAI 96
Cdd:cd01901   145 YKPDMTLEEAVELALKAL 162
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-119 1.11e-13

proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239732  Cd Length: 189  Bit Score: 64.53  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMgLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYR 80
Cdd:cd03763    65 LHRLNTGRKPRVVTALTMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYK 143

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1938963749  81 PDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDG 119
Cdd:cd03763   144 PDMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-127 1.17e-10

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 56.88  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPG-LYYVDENGTRLSGNMFSTGSGNSHAYGVMDS-- 77
Cdd:cd03757    73 MYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERETYSAGGSASSLIQPLLDNqv 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938963749  78 -------GYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGwVKVESTD 127
Cdd:cd03757   153 grknqnnVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG-IEEETFP 208
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-96 1.28e-10

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 56.44  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQY--RGMGLSMGSMICGWDKK-GPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDS 77
Cdd:cd03758    66 LYKMRNGYELSPKAAANFTRRELAESlrSRTPYQVNLLLAGYDKVeGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR 145

                          90
                  ....*....|....*....
gi 1938963749  78 GYRPDLSIEEAYDLGRRAI 96
Cdd:cd03758   146 YYKPDMTVEEALELMKKCI 164
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
2-100 1.65e-08

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 50.99  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   2 YYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:PRK03996  101 NRLTYGEPIGVETLTKKICDHKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFL 178

                          90       100
                  ....*....|....*....|....*
gi 1938963749  76 DSGYRPDLSIEEAYDLGRRAIVHAT 100
Cdd:PRK03996  179 EKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-88 5.93e-08

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 49.63  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   2 YYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:cd03750    92 YYLVYGEPIPVSQLVREIASVMQEYtqsggvRPFGVSL--LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFL 169

                          90
                  ....*....|...
gi 1938963749  76 DSGYRPDLSIEEA 88
Cdd:cd03750   170 EKRYNEDLELEDA 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-100 2.24e-07

proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 47.71  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   2 YYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVM 75
Cdd:cd03756    93 HRLTYGEPIDVEVLVKKICDLKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFL 170

                          90       100
                  ....*....|....*....|....*
gi 1938963749  76 DSGYRPDLSIEEAYDLGRRAIVHAT 100
Cdd:cd03756   171 EKEYKEDMSLEEAIELALKALYAAL 195
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-91 2.55e-07

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 47.72  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   8 ERISVSAASKLLSNMMCQYRGMGLSMGSM---------ICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSG 78
Cdd:cd03753    98 EPMTVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEK 177

                          90
                  ....*....|...
gi 1938963749  79 YRPDLSIEEAYDL 91
Cdd:cd03753   178 YHKDMTLEEAEKL 190
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-96 9.83e-07

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 45.90  E-value: 9.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   2 YYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKK-GPGLYYVDENGTRLSGNMFSTGSGNSHAYGV 74
Cdd:cd01911    92 YRYTYGEPIPVEVLVKRIADLAQVYtqyggvRPFGVSL--LIAGYDEEgGPQLYQTDPSGTYFGYKATAIGKGSQEAKTF 169

                          90       100
                  ....*....|....*....|..
gi 1938963749  75 MDSGYRPDLSIEEAYDLGRRAI 96
Cdd:cd01911   170 LEKRYKKDLTLEEAIKLALKAL 191
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-107 8.77e-06

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 43.39  E-value: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938963749   1 LYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKG-PGLYYVDENG-TRLSGNMFSTGSGNSHAYGVMDSG 78
Cdd:cd03759    68 LYRLREEREIKPKTFSSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGcPSIPSDFVVSGTASEQLYGMCESL 147

                          90       100
                  ....*....|....*....|....*....
gi 1938963749  79 YRPDLSIEEAYDLGRRAIVHATHRDSYSG 107
Cdd:cd03759   148 WRPDMEPDELFETISQALLSAVDRDALSG 176
 
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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