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Conserved domains on  [gi|30424826|ref|NP_780413|]
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proteasome subunit beta type-11 [Mus musculus]

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 ...
 50-237 4.55e-104

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: 301.47  E-value: 4.55e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAV 209
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 30424826 210 AHATHRDAYSGGSVDLFHVRESGWEYVS 237
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 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 ...
 50-237 4.55e-104

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: 301.47  E-value: 4.55e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAV 209
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 30424826 210 AHATHRDAYSGGSVDLFHVRESGWEYVS 237
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 35-245 2.77e-76

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 233.34  E-value: 2.77e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   35 PQTFLQIHGPR---LAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRE 111
Cdd:PTZ00488  22 EYTFDHGDANKaieFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  112 LRLRELREGQLPSVAGTAKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRG 191
Cdd:PTZ00488 102 CRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAG 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30424826  192 YHYDMTIQEAYTLARCAVAHATHRDAYSGGSVDLFHVRESGWEYVSRSDACVLY 245
Cdd:PTZ00488 182 FKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLH 235
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 48-228 3.62e-40

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: 138.47  E-value: 3.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826    48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPAS-RKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVA 126
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   127 GTAKL--LAAMMSCYRGL-DLCVATALCGWDHSG-PALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAY 202
Cdd:pfam00227  83 LAARIadLLQAYTQYSGRrPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 30424826   203 TLARCAVAHATHRDAYSGGSVDLFHV 228
Cdd:pfam00227 163 ELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 49-232 6.37e-36

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: 127.33  E-value: 6.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826    49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   129 AKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCA 208
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 30424826   209 VAHATHRDAYSGGSVDLFHVRESG 232
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 48-240 1.77e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 117.17  E-value: 1.77e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAG 127
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 128 TAKLLAAMMSCYRGL---DLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTL 204
Cdd:COG0638 114 LAKLLSDLLQGYTQYgvrPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30424826 205 ARCAVAHATHRDAYSGGSVDLFHVRESGWEYVSRSD 240
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-237 4.55e-104

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: 301.47  E-value: 4.55e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAV 209
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 30424826 210 AHATHRDAYSGGSVDLFHVRESGWEYVS 237
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 35-245 2.77e-76

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 233.34  E-value: 2.77e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   35 PQTFLQIHGPR---LAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRE 111
Cdd:PTZ00488  22 EYTFDHGDANKaieFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  112 LRLRELREGQLPSVAGTAKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRG 191
Cdd:PTZ00488 102 CRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAG 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30424826  192 YHYDMTIQEAYTLARCAVAHATHRDAYSGGSVDLFHVRESGWEYVSRSDACVLY 245
Cdd:PTZ00488 182 FKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLH 235
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 50-236 3.36e-66

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: 205.37  E-value: 3.36e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGLDLCVATALCGWD-HSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCA 208
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
gi 30424826 209 VAHATHRDAYSGGSVDLFHVRESGWEYV 236
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 50-228 2.27e-47

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: 156.89  E-value: 2.27e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGL--DLCVATALCGWD-HSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLAR 206
Cdd:cd01906  81 KLLANLLYEYTQSlrPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 30424826 207 CAVAHATHRDAYSGGSVDLFHV 228
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 48-228 3.62e-40

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: 138.47  E-value: 3.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826    48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPAS-RKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVA 126
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   127 GTAKL--LAAMMSCYRGL-DLCVATALCGWDHSG-PALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAY 202
Cdd:pfam00227  83 LAARIadLLQAYTQYSGRrPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 30424826   203 TLARCAVAHATHRDAYSGGSVDLFHV 228
Cdd:pfam00227 163 ELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 49-232 6.37e-36

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: 127.33  E-value: 6.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826    49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826   129 AKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCA 208
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 30424826   209 VAHATHRDAYSGGSVDLFHVRESG 232
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-234 1.16e-33

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: 121.59  E-value: 1.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAV 209
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                       170       180
                ....*....|....*....|....*
gi 30424826 210 AHATHRDAYSGGSVDLFHVRESGWE 234
Cdd:cd03764 161 KSAIERDSASGDGIDVVVITKDGYK 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 48-240 1.77e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 117.17  E-value: 1.77e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAG 127
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 128 TAKLLAAMMSCYRGL---DLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTL 204
Cdd:COG0638 114 LAKLLSDLLQGYTQYgvrPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30424826 205 ARCAVAHATHRDAYSGGSVDLFHVRESGWEYVSRSD 240
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 50-211 3.40e-30

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: 111.72  E-value: 3.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGL-DLCVATALCGWDHSGPALFYVYSDGTCLQG-DIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARC 207
Cdd:cd01901  81 KELAKLLQVYTQGrPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
gi 30424826 208 AVAH 211
Cdd:cd01901 161 ALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-232 2.80e-28

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: 107.70  E-value: 2.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMmsCYRGLDLCVATALC-GWD-HSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARC 207
Cdd:cd03762  81 SLFKNL--CYNYKEMLSAGIIVaGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158

                       170       180
                ....*....|....*....|....*
gi 30424826 208 AVAHATHRDAYSGGSVDLFHVRESG 232
Cdd:cd03762 159 ALSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-235 4.68e-18

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: 80.32  E-value: 4.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 130 KLLAAMMSCYRGlDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAV 209
Cdd:cd03763  81 TMLKQHLFRYQG-HIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180
                ....*....|....*....|....*.
gi 30424826 210 AHATHRDAYSGGSVDLFHVRESGWEY 235
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDGVEY 185
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 49-205 2.62e-08

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: 53.11  E-value: 2.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  49 GTTTLAFRFRHGVIAAADTRSScgSYVACPAS-RKVIPVHQRLLGTTSGTSADCATWY---RVLRRELRLRELREGQLPS 124
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRIT--SPLMEPSSvEKIMEIDDHIGCAMSGLIADARTLIdhaRVEAQNHRFTYNEPMTVES 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 125 VA----------GTAKLLAAMMSCYRGLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHY 194
Cdd:cd03753 105 VTqavsdlalqfGEGDDGKKAMSRPFGVALLIA----GVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180

                       170
                ....*....|.
gi 30424826 195 DMTIQEAYTLA 205
Cdd:cd03753 181 DMTLEEAEKLA 191
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 49-240 1.47e-07

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: 51.11  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 129 AKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFS-VGSGSPYAYGVLD---------RGYHYDMTI 198
Cdd:cd03757  88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSaGGSASSLIQPLLDnqvgrknqnNVERTPLSL 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30424826 199 QEAYTLARCAVAHATHRDAYSGGSVDLFHVRESG--WEYVS-RSD 240
Cdd:cd03757 168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGieEETFPlRKD 212
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 51-204 6.72e-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: 48.74  E-value: 6.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  51 TTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATW----------YRVLRrelrlrelreG 120
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFaeyiqkniqlYKMRN----------G 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 121 QLPSVAGTA----KLLAAmmSCYRGLDLCVATALCGWD-HSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYD 195
Cdd:cd03758  73 YELSPKAAAnftrRELAE--SLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPD 150


                ....*....
gi 30424826 196 MTIQEAYTL 204
Cdd:cd03758 151 MTVEEALEL 159
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 49-225 8.78e-05

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: 42.70  E-value: 8.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826  49 GTTTLAFRFRHGVIAAADTRsscgsyvacPASRKVIP-----VHQ---RLLGTTSGTSADC----------ATWYRVLRr 110
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKR---------ITSKLVEPesiekIYKiddHVGAATSGLVADArvlidrarveAQIHRLTY- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424826 111 elrlrelreGQLPSVAGTAKLLAAMMSCYR--------GLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDIFSVGSGSP 182
Cdd:cd03756  98 ---------GEPIDVEVLVKKICDLKQQYTqhggvrpfGVALLIA----GVDDGGPRLFETDPSGAYNEYKATAIGSGRQ 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30424826 183 YAYGVLDRGYHYDMTIQEAYTLARCAVAHAThRDAYSGGSVDL 225
Cdd:cd03756 165 AVTEFLEKEYKEDMSLEEAIELALKALYAAL-EENETPENVEI 206
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 49-100 1.03e-03

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 39.48  E-value: 1.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 30424826  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSAD 100
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYAD 53
 
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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