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Conserved domains on  [gi|302595760|sp|C9REN7|]
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RecName: Full=Proteasome subunit beta; AltName: Full=20S proteasome beta subunit; AltName: Full=Proteasome core protein PsmB; Flags: Precursor

Protein Classification

archaeal proteasome endopeptidase complex subunit beta( domain architecture ID 10022721)

archaeal proteasome endopeptidase complex subunit beta is component of the proteasome core, a large protease complex with broad specificity involved in protein degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 6-192 4.21e-108

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: 308.37  E-value: 4.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   86 ATLLSNILHSSRMFPFLTQIIIGGYDLtDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDE-EGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 302595760  166 KALKSAMERDTYSGNGVSVAVITKEGV 192
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 6-192 4.21e-108

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: 308.37  E-value: 4.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   86 ATLLSNILHSSRMFPFLTQIIIGGYDLtDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDE-EGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 302595760  166 KALKSAMERDTYSGNGVSVAVITKEGV 192
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-196 5.06e-108

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: 308.41  E-value: 5.06e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLALK 166
Cdd:cd03764   81 TLLSNILNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 302595760 167 ALKSAMERDTYSGNGVSVAVITKEGVKLLS 196
Cdd:cd03764  159 AIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-199 1.70e-97

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 283.19  E-value: 1.70e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   3 TMKGTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISP 82
Cdd:COG0638   32 VKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  83 RACATLLSNILHSS---RMFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEE 159
Cdd:COG0638  112 EGLAKLLSDLLQGYtqyGVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDE 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 302595760 160 GLKLALKALKSAMERDTYSGNGVSVAVITKEGVKLLSDEE 199
Cdd:COG0638  190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-187 1.39e-71

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: 215.89  E-value: 1.39e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    5 KGTTTVGLICDDAVILATDKRASMGNLIADK-EAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPR 83
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   84 AC---ATLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:pfam00227  83 LAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 302595760  161 LKLALKALKSAMERDTYSGNGVSVAVI 187
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-204 1.15e-39

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 136.12  E-value: 1.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAqaivRALIAEARL----YKMRTGKNI 80
Cdd:PRK03996  35 RGTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLIDRARVeaqiNRLTYGEPI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  81 SPRACATLLSNILHSSRMF----PFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMS 156
Cdd:PRK03996 110 GVETLTKKICDHKQQYTQHggvrPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKA-TAIGAGRDTVMEFLEKNYKEDLS 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 302595760 157 IEEGLKLALKALKSAMErDTYSGNGVSVAVITKEG--VKLLSDEEITKLL 204
Cdd:PRK03996 188 LEEAIELALKALAKANE-GKLDPENVEIAYIDVETkkFRKLSVEEIEKYL 236
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 6-192 4.21e-108

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: 308.37  E-value: 4.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   86 ATLLSNILHSSRMFPFLTQIIIGGYDLtDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDE-EGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 302595760  166 KALKSAMERDTYSGNGVSVAVITKEGV 192
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-196 5.06e-108

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: 308.41  E-value: 5.06e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLALK 166
Cdd:cd03764   81 TLLSNILNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 302595760 167 ALKSAMERDTYSGNGVSVAVITKEGVKLLS 196
Cdd:cd03764  159 AIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-199 1.70e-97

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 283.19  E-value: 1.70e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   3 TMKGTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISP 82
Cdd:COG0638   32 VKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  83 RACATLLSNILHSS---RMFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEE 159
Cdd:COG0638  112 EGLAKLLSDLLQGYtqyGVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDE 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 302595760 160 GLKLALKALKSAMERDTYSGNGVSVAVITKEGVKLLSDEE 199
Cdd:COG0638  190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-193 4.87e-80

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: 237.34  E-value: 4.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEkTFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLALK 166
Cdd:cd01912   81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEA-PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKK 159

                        170       180
                 ....*....|....*....|....*..
gi 302595760 167 ALKSAMERDTYSGNGVSVAVITKEGVK 193
Cdd:cd01912  160 AIDSAIERDLSSGGGVDVAVITKDGVE 186
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-187 1.39e-71

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: 215.89  E-value: 1.39e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    5 KGTTTVGLICDDAVILATDKRASMGNLIADK-EAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPR 83
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   84 AC---ATLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:pfam00227  83 LAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 302595760  161 LKLALKALKSAMERDTYSGNGVSVAVI 187
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 7-187 1.01e-69

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: 211.20  E-value: 1.01e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSR--MFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLA 164
Cdd:cd01906   81 KLLANLLYEYTqsLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYK-ATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                        170       180
                 ....*....|....*....|...
gi 302595760 165 LKALKSAMERDTYSGNGVSVAVI 187
Cdd:cd01906  160 LKALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 7-170 3.86e-46

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: 150.62  E-value: 3.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSR-MFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:cd01901   81 KELAKLLQVYTqGRPFGVNLIVAGVD-EGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                 ....*
gi 302595760 166 KALKS 170
Cdd:cd01901  160 KALKS 164
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-196 5.55e-44

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: 145.85  E-value: 5.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMFPFLTQIIIGGYDLTdGPKLFSLDPLGGMNEEKTFtSTGSGSPIAYGVLEAEYDRDMSIEEGLKLALK 166
Cdd:cd03761   81 KLLSNMLYQYKGMGLSMGTMICGWDKT-GPGLYYVDSDGTRLKGDLF-SVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 302595760 167 ALKSAMERDTYSGNGVSVAVITKEGVKLLS 196
Cdd:cd03761  159 AIYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-204 1.15e-39

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 136.12  E-value: 1.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAqaivRALIAEARL----YKMRTGKNI 80
Cdd:PRK03996  35 RGTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLIDRARVeaqiNRLTYGEPI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  81 SPRACATLLSNILHSSRMF----PFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMS 156
Cdd:PRK03996 110 GVETLTKKICDHKQQYTQHggvrPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKA-TAIGAGRDTVMEFLEKNYKEDLS 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 302595760 157 IEEGLKLALKALKSAMErDTYSGNGVSVAVITKEG--VKLLSDEEITKLL 204
Cdd:PRK03996 188 LEEAIELALKALAKANE-GKLDPENVEIAYIDVETkkFRKLSVEEIEKYL 236
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-193 1.22e-39

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: 134.66  E-value: 1.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACA 86
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMFpFLTQIIIGGYDLTDGPKLFSLdPLGGMNEEKTFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLALK 166
Cdd:cd03762   81 SLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSI-PLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158

                        170       180
                 ....*....|....*....|....*..
gi 302595760 167 ALKSAMERDTYSGNGVSVAVITKEGVK 193
Cdd:cd03762  159 ALSLAMSRDGSSGGVIRLVIITKDGVE 185
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-195 3.06e-39

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: 133.48  E-value: 3.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   7 TTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKniSPRACA 86
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGR--KPRVVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 --TLLSNILhssrmFPFLTQI----IIGGYDLTdGPKLFSLDPLGGMNEEKtFTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:cd03763   79 alTMLKQHL-----FRYQGHIgaalVLGGVDYT-GPHLYSIYPHGSTDKLP-FVTMGSGSLAAMSVLEDRYKPDMTEEEA 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 302595760 161 LKLALKALKSAMERDTYSGNGVSVAVITKEGVKLL 195
Cdd:cd03763  152 KKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVEYL 186
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 6-203 3.92e-37

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 130.11  E-value: 3.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  86 ATLLSNILHSSRMFPFLTQIIIGGYDLTdGPKLFSLDPLGGMNEEKTFtSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:PTZ00488 119 SKILANIVWNYKGMGLSMGTMICGWDKK-GPGLFYVDNDGTRLHGNMF-SCGSGSTYAYGVLDAGFKWDLNDEEAQDLGR 196

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 302595760 166 KALKSAMERDTYSGNGVSVAVITKEGVKLLSDEEITKL 203
Cdd:PTZ00488 197 RAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDL 234
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-193 8.51e-37

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: 128.15  E-value: 8.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  86 ATLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEkTFTSTGSGSPIAYGVLEAEYDR---------DMS 156
Cdd:cd03757   88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERE-TYSAGGSASSLIQPLLDNQVGRknqnnvertPLS 166

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 302595760 157 IEEGLKLALKALKSAMERDTYSGNGVSVAVITKEGVK 193
Cdd:cd03757  167 LEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-187 3.11e-36

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: 126.40  E-value: 3.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASMGnLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRA 84
Cdd:cd01911   26 NGSTAVGIKGKDGVVLAVEKKVTSK-LLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  85 CATLLSNILH----SSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:cd01911  105 LVKRIADLAQvytqYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKA-TAIGKGSQEAKTFLEKRYKKDLTLEEA 183

                        170       180
                 ....*....|....*....|....*..
gi 302595760 161 LKLALKALKSAMERDTYSGNgVSVAVI 187
Cdd:cd01911  184 IKLALKALKEVLEEDKKAKN-IEIAVV 209
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-188 2.14e-35

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: 124.37  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIV-RALIaEARLYKMRTGKNISPR 83
Cdd:cd03756   27 RGTTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADARVLIdRARV-EAQIHRLTYGEPIDVE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  84 ACATLLSNILHSSRMF----PFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMSIEE 159
Cdd:cd03756  105 VLVKKICDLKQQYTQHggvrPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKA-TAIGSGRQAVTEFLEKEYKEDMSLEE 182

                        170       180
                 ....*....|....*....|....*....
gi 302595760 160 GLKLALKALKSAMErDTYSGNGVSVAVIT 188
Cdd:cd03756  183 AIELALKALYAALE-ENETPENVEIAYVT 210
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-192 1.09e-33

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: 119.65  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:cd03759    3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  86 ATLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:cd03759   83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162

                        170       180
                 ....*....|....*....|....*..
gi 302595760 166 KALKSAMERDTYSGNGVSVAVITKEGV 192
Cdd:cd03759  163 QALLSAVDRDALSGWGAVVYIITKDKV 189
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 6-203 1.44e-32

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 117.50  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760    6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDGK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   86 ATLLSNILHSS---RMFPFLTQIIIGGYDLTDGP-KLFSLDPLGGMNEEKTFTSTGSGSPIAYGVLEAEYDRDMSIEEGL 161
Cdd:TIGR03690  82 ANRLAAMVRGNlpaAMQGLAVVPLLAGYDLDAGAgRIFSYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDDAL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 302595760  162 KLALKALKSAMERDTYSGN-----GV--SVAVITKEGVKLLSDEEITKL 203
Cdd:TIGR03690 162 RVAVEALYDAADDDSATGGpdlvrGIypTVVVITADGARRVPESELEEL 210
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-195 2.19e-30

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: 110.75  E-value: 2.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   8 TTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRACAT 87
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  88 LLSNILHSS--RMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEkTFTSTGSGSPIAYGVLEAEYDRDMSIEEGLKLAL 165
Cdd:cd03758   83 FTRRELAESlrSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKV-PYAAHGYGAYFCLSILDRYYKPDMTVEEALELMK 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 302595760 166 KALKSAMERDTYSGNGVSVAVITKEGVKLL 195
Cdd:cd03758  162 KCIKELKKRFIINLPNFTVKVVDKDGIRDL 191
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-194 5.40e-28

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: 104.96  E-value: 5.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRAL---IAEARLYKmrTGKNISP 82
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLdqlVIDDECLD--DGHSLSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  83 RACATLLSNILHS--SRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTFTsTGSGSPIAYGVL--EAEYDRDMSIE 158
Cdd:cd03760   80 KEIHSYLTRVLYNrrSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVA-TGFGAYLALPLLreAWEKKPDLTEE 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 302595760 159 EGLKLALKALKSAMERDTYSGNGVSVAVITKEGVKL 194
Cdd:cd03760  159 EARALIEECMKVLYYRDARSINKYQIAVVTKEGVEI 194
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 9-204 3.80e-27

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 104.16  E-value: 3.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   9 TVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQaivrALIAEARLYKMR----TGKNISPRA 84
Cdd:PTZ00246  34 TVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADAN----ILINQCRLYAQRyrytYGEPQPVEQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  85 CATLLSNILHSSRMF----PFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:PTZ00246 110 LVVQICDLKQSYTQFgglrPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKA-TAIGQNNQTAQSILKQEWKEDLTLEQG 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 302595760 161 LKLALKALKSAMERDTYSGNGVSVAVITKEG------VKLLSDEEITKLL 204
Cdd:PTZ00246 189 LLLAAKVLTKSMDSTSPKADKIEVGILSHGEtdgepiQKMLSEKEIAELL 238
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-187 4.37e-24

proteasome_alpha_type_7. 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: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 94.74  E-value: 4.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASMgNLIADKEAKKLYKIDDYIAMTIAGSVGDAqaivRALIAEARL----YKMRTGKNI 80
Cdd:cd03755   26 KGTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADA----RVLINRARLecqsHRLTVEDPV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  81 S----PRACATLLSNILHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMS 156
Cdd:cd03755  101 TveyiTRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKA-NAIGRNSKTVREFLEKNYKEEMT 179

                        170       180       190
                 ....*....|....*....|....*....|.
gi 302595760 157 IEEGLKLALKALKSAMERdtySGNGVSVAVI 187
Cdd:cd03755  180 RDDTIKLAIKALLEVVQS---GSKNIELAVM 207
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-187 6.84e-24

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: 94.71  E-value: 6.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:cd03753   27 GSTAIGIKTKEGVVLAVEKRIT-SPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  86 ATLLSNI-LHSSRMF--------PFLTQIIIGGYDlTDGPKLFSLDPLGgmneekTFT-----STGSGSPIAYGVLEAEY 151
Cdd:cd03753  106 TQAVSDLaLQFGEGDdgkkamsrPFGVALLIAGVD-ENGPQLFHTDPSG------TFTrcdakAIGSGSEGAQSSLQEKY 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 302595760 152 DRDMSIEEGLKLALKALKSAMErDTYSGNGVSVAVI 187
Cdd:cd03753  179 HKDMTLEEAEKLALSILKQVME-EKLNSTNVELATV 213
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-187 3.86e-22

proteasome_alpha_type_4. 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: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 90.10  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   8 TTVGLICDDAVILATDKRASMGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQaivrALIAEARLYKMRTGKNIS-PRACA 86
Cdd:cd03752   31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDAN----ILINYARLIAQRYLYSYQePIPVE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  87 TLLSNILHSSRMF-------PFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMSIEE 159
Cdd:cd03752  107 QLVQRLCDIKQGYtqygglrPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKA-TAIGNNNQAAQSLLKQDYKDDMTLEE 185

                        170       180
                 ....*....|....*....|....*...
gi 302595760 160 GLKLALKALKSAMERDTYSGNGVSVAVI 187
Cdd:cd03752  186 ALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-187 7.10e-21

proteasome_alpha_type_1. 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: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 86.58  E-value: 7.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   1 MDTMK-GTTTVGLICDDAVILATDKRASmgNLIADKEaKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKN 79
Cdd:cd03749   21 MEAVKqGSATVGLKSKTHAVLVALKRAT--SELSSYQ-KKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  80 ISPRACATLLS-----NILHSSRMfPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYD-- 152
Cdd:cd03749   98 IPVSRLVSKVAekaqiNTQRYGRR-PYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKA-TSIGARSQSARTYLERHFEef 174

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 302595760 153 RDMSIEEGLKLALKALKSAM--ERDTYSGNgVSVAVI 187
Cdd:cd03749  175 EDCSLEELIKHALRALRETLpgEQELTIKN-VSIAIV 210
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-200 7.20e-20

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: 84.30  E-value: 7.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   5 KGTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISP-- 82
Cdd:cd03750   26 SGAPSVGIKAANGVVLATEKKVP-SPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVsq 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  83 --RACATLLSNILHSSRMFPFLTQIIIGGYDlTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRDMSIEEG 160
Cdd:cd03750  105 lvREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTWKA-TAIGKNYSNAKTFLEKRYNEDLELEDA 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 302595760 161 LKLALKALKSAMERDTySGNGVSVAVITKEGV-KLLSDEEI 200
Cdd:cd03750  183 IHTAILTLKEGFEGQM-TEKNIEIGICGETKGfRLLTPAEI 222
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-187 1.87e-15

proteasome_alpha_type_6. 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: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 72.27  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   6 GTTTVGLICDDAVILATDKRASmGNLIADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISPRAC 85
Cdd:cd03754   29 GLTSVAVRGKDCAVVVTQKKVP-DKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPVDVL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  86 ATLLSNI----LHSSRMFPFLTQIIIGGYDLTDGPKLFSLDPLGGMNEEKTfTSTGSGSPIAYGVLEAEYDRD----MSI 157
Cdd:cd03754  108 AKRIADInqvyTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKA-TAAGVKEQEATNFLEKKLKKKpdliESY 186

                        170       180       190
                 ....*....|....*....|....*....|
gi 302595760 158 EEGLKLALKALKSAMERDtYSGNGVSVAVI 187
Cdd:cd03754  187 EETVELAISCLQTVLSTD-FKATEIEVGVV 215
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-166 9.22e-15

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 70.00  E-value: 9.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760   8 TTVGLICDDAVILATDKrasmgnLIADK-----EAKKLYKIDDYIAMTIAGSVGDAQAIVRALIAEARLYKMRTGKNISP 82
Cdd:cd03751   32 TAIGIRCKDGVVLAVEK------LVTSKlyepgSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302595760  83 RACATLLSNILH------SSRmfPFLTQIIIGGYDlTDGPKLFSLDPlGGMNEEKTFTSTGSGSPIAYGVLEAEYDRDMS 156
Cdd:cd03751  106 KVLADRVAMYMHaytlysSVR--PFGCSVLLGGYD-SDGPQLYMIEP-SGVSYGYFGCAIGKGKQAAKTELEKLKFSELT 181

                        170
                 ....*....|
gi 302595760 157 IEEGLKLALK 166
Cdd:cd03751  182 CREAVKEAAK 191
 
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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