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Conserved domains on  [gi|195539356|ref|NP_001124197|]
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proteasome subunit beta type-5 isoform 2 [Homo sapiens]

Protein Classification

proteasome subunit beta( domain architecture ID 10132926)

proteasome subunit beta is a subunit of the eukaryotic 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to the catalytic subunit beta type-5 (PSMB5) which has chymotrypsin-like activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-144 1.47e-101

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: 289.14  E-value: 1.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:cd03761   45 MAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGD 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVS 144
Cdd:cd03761  125 LFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 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 ...
 1-144 1.47e-101

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: 289.14  E-value: 1.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:cd03761   45 MAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGD 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVS 144
Cdd:cd03761  125 LFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-160 1.14e-97

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 281.88  E-value: 1.14e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:PTZ00488  84 MAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 160
Cdd:PTZ00488 164 MFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-135 2.07e-36

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: 123.83  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356    1 MAGGAADCSFWERLLARQCRIYELRNKERISV----AAASKLLANMVYQYKGMgLSMGTMICGWDKRG-PGLYYVDSEGN 75
Cdd:pfam00227  50 FAGLAADARTLVDRARAEAQLYRLRYGRPIPVelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGS 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   76 RISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHV 135
Cdd:pfam00227 129 YIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 2-139 2.54e-33

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: 116.15  E-value: 2.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356    2 AGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGAT 81
Cdd:TIGR03634  47 AGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDY 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 195539356   82 FSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 139
Cdd:TIGR03634 127 TATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRAIKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-146 7.73e-32

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 7.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMG---LSMGTMICGWDKRGPGLYYVDSEGNRI 77
Cdd:COG0638   80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195539356  78 SGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 146
Cdd:COG0638  160 EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-144 1.47e-101

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: 289.14  E-value: 1.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:cd03761   45 MAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGD 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVS 144
Cdd:cd03761  125 LFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-160 1.14e-97

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 281.88  E-value: 1.14e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:PTZ00488  84 MAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 160
Cdd:PTZ00488 164 MFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-143 1.75e-59

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: 182.64  E-value: 1.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDK-RGPGLYYVDSEGNRISG 79
Cdd:cd01912   45 TAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANLLSNILYSYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEA 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195539356  80 ATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRV 143
Cdd:cd01912  125 PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 1-135 2.18e-42

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: 139.17  E-value: 2.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYK--GMGLSMGTMICGWDK-RGPGLYYVDSEGNRI 77
Cdd:cd01906   45 FAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKLLANLLYEYTqsLRPLGVSLLVAGVDEeGGPQLYSVDPSGSYI 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 195539356  78 SGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHV 135
Cdd:cd01906  125 EYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-135 2.07e-36

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: 123.83  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356    1 MAGGAADCSFWERLLARQCRIYELRNKERISV----AAASKLLANMVYQYKGMgLSMGTMICGWDKRG-PGLYYVDSEGN 75
Cdd:pfam00227  50 FAGLAADARTLVDRARAEAQLYRLRYGRPIPVelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGS 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   76 RISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHV 135
Cdd:pfam00227 129 YIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 2-139 2.54e-33

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: 116.15  E-value: 2.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356    2 AGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGAT 81
Cdd:TIGR03634  47 AGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDY 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 195539356   82 FSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 139
Cdd:TIGR03634 127 TATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRAIKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-146 7.73e-32

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 7.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMG---LSMGTMICGWDKRGPGLYYVDSEGNRI 77
Cdd:COG0638   80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195539356  78 SGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 146
Cdd:COG0638  160 EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-144 4.44e-31

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: 110.42  E-value: 4.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGA 80
Cdd:cd03764   45 IAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDK 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195539356  81 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVS 144
Cdd:cd03764  125 YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-117 7.70e-28

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: 101.32  E-value: 7.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMG-LSMGTMICGWDKRGPGLYYVDSEGNRISG 79
Cdd:cd01901   45 LAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIEN 124

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 195539356  80 ATF-SVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIY 117
Cdd:cd01901  125 PGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELALKALK 163
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-139 2.34e-19

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: 79.93  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   2 AGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMgLSMGTMICGWDKRGPGLYYVDSEGNRISGAT 81
Cdd:cd03763   46 AGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPF 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 195539356  82 FSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 139
Cdd:cd03763  125 VTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-142 4.25e-17

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: 74.18  E-value: 4.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   2 AGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMgLSMGTMICGWDK-RGPGLYYVdSEGNRISGA 80
Cdd:cd03762   46 SGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSI-PLGGMLIRQ 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195539356  81 TFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIR 142
Cdd:cd03762  124 PFAIgGSGSTYIYGYVDANYKPGMTLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVER 186
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-139 1.07e-08

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: 51.88  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   2 AGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPG-LYYVDSEGNRISGA 80
Cdd:cd03757   54 SGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERET 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195539356  81 TFSVGSGSVYAYGVMD---------RGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 139
Cdd:cd03757  134 YSAGGSASSLIQPLLDnqvgrknqnNVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-119 8.53e-08

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: 49.36  E-value: 8.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCsfweRLLARQCRI----YELRNKERISVAAASKLLANM--VY-QYKGM---GLSMgtMICGWDK-RGPGLYY 69
Cdd:cd01911   71 VAGLTADA----RVLVNRARVeaqnYRYTYGEPIPVEVLVKRIADLaqVYtQYGGVrpfGVSL--LIAGYDEeGGPQLYQ 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195539356  70 VDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQA 119
Cdd:cd01911  145 TDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEV 194
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-116 2.26e-07

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: 47.97  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCSFWERLLARQCRIYELRNKERISVAAAskllANMV------YQYKGMGLSMGTMICGWDKR-GPGLYYVDSE 73
Cdd:cd03758   46 CSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA----ANFTrrelaeSLRSRTPYQVNLLLAGYDKVeGPSLYYIDYL 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 195539356  74 GNrISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 116
Cdd:cd03758  122 GT-LVKVPYAAhGYGAYFCLSILDRYYKPDMTVEEALELMKKCI 164
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
17-120 7.41e-07

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 47.14  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356  17 RQCRIYELRNKERISVAAASKLLANM--VY-QYKGM---GLSMgtMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVY 90
Cdd:PRK03996  96 VEAQINRLTYGEPIGVETLTKKICDHkqQYtQHGGVrpfGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDT 173

                         90       100       110
                 ....*....|....*....|....*....|
gi 195539356  91 AYGVMDRGYSYDLEVEQAYDLARRAIYQAT 120
Cdd:PRK03996 174 VMEFLEKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-108 2.79e-06

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: 45.39  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   2 AGGAADCsfweRLLARQCR----IYELRNKERISVAAASKLLANMVYQY--KG----MGLSMgtMICGWDKRGPGLYYVD 71
Cdd:cd03750   72 SGMGPDF----RVLVKKARkiaqQYYLVYGEPIPVSQLVREIASVMQEYtqSGgvrpFGVSL--LIAGWDEGGPYLYQVD 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195539356  72 SEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQA 108
Cdd:cd03750  146 PSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDA 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-132 3.73e-06

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: 45.01  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   2 AGGAADCsfweRLLARQCRIYELRNK----ERISVAAASKLLANMVYQYKGMG----LSMGTMICGWDKRGPGLYYVDSE 73
Cdd:cd03756   73 SGLVADA----RVLIDRARVEAQIHRltygEPIDVEVLVKKICDLKQQYTQHGgvrpFGVALLIAGVDDGGPRLFETDPS 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 195539356  74 GNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYqATYRDAYSGGAVNL 132
Cdd:cd03756  149 GAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALY-AALEENETPENVEI 206
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-112 3.00e-05

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: 42.32  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356   1 MAGGAADCsfweRLLARQCRIyELRN-----KERISVAAASKLLANMVYQYKGMGLSMGTM---------ICGWDKRGPG 66
Cdd:cd03753   71 MSGLIADA----RTLIDHARV-EAQNhrftyNEPMTVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQ 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 195539356  67 LYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLA 112
Cdd:cd03753  146 LFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLA 191
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-139 7.36e-04

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: 38.38  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195539356  21 IYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRG-PGLYYVDSEGNRISGATFSV-GSGSVYAYGVMDRG 98
Cdd:cd03759   68 LYRLREEREIKPKTFSSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPSDFVVsGTASEQLYGMCESL 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 195539356  99 YSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 139
Cdd:cd03759  148 WRPDMEPDELFETISQALLSAVDRDALSGWGAVVYIITKDK 188
 
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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