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Conserved domains on  [gi|1938937547|pdb|6HEA|m]
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Chain m, Proteasome subunit beta

Protein Classification

archaeal proteasome endopeptidase complex subunit beta( domain architecture ID 10132942)

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
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 3.40e-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: 308.03  E-value: 3.40e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*....
6HEA_m      161 IYSAMKRDSASGDGIDVVKITEDEFYQYS 189
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKELE 188
 
Name Accession Description Interval E-value
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 3.40e-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: 308.03  E-value: 3.40e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*....
6HEA_m      161 IYSAMKRDSASGDGIDVVKITEDEFYQYS 189
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKELE 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-185 4.93e-105

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: 299.89  E-value: 4.93e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m          1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEkDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:TIGR03634  82 TLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIED-DYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....*
6HEA_m        161 IYSAMKRDSASGDGIDVVKITEDEF 185
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDGV 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-192 1.43e-92

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 269.71  E-value: 1.43e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSY---RYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELA 157
Cdd:COG0638 116 KLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                       170       180       190
                ....*....|....*....|....*....|....*
6HEA_m      158 VRAIYSAMKRDSASGDGIDVVKITEDEFYQYSPEE 192
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-180 5.88e-67

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: 203.57  E-value: 5.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m          1 TTTVGLVCKDGVVMATEKRATMGNFIASK-AAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         77 RAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGK-SIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVE 155
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
6HEA_m        156 LAVRAIYSAMKRDSASGDGIDVVKI 180
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-202 3.51e-35

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 123.79  E-value: 3.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         1 TTTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        81 TLTSNLLNSYRYF----PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVEL 156
Cdd:PRK03996 116 KKICDHKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDP-SGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIEL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
6HEA_m       157 AVRAIYSAMK-RDSASGDGIDVVKITEDEFYQYSPEEVEQILAKFRK 202
Cdd:PRK03996 195 ALKALAKANEgKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKLLK 241
 
Name Accession Description Interval E-value
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 3.40e-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: 308.03  E-value: 3.40e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*....
6HEA_m      161 IYSAMKRDSASGDGIDVVKITEDEFYQYS 189
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKELE 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-185 4.93e-105

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: 299.89  E-value: 4.93e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m          1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEkDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:TIGR03634  82 TLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIED-DYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....*
6HEA_m        161 IYSAMKRDSASGDGIDVVKITEDEF 185
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDGV 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-192 1.43e-92

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 269.71  E-value: 1.43e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSY---RYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELA 157
Cdd:COG0638 116 KLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                       170       180       190
                ....*....|....*....|....*....|....*
6HEA_m      158 VRAIYSAMKRDSASGDGIDVVKITEDEFYQYSPEE 192
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-183 9.39e-77

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: 228.10  E-value: 9.39e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGK-SIYSIDPIGGAIEEkDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVR 159
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGpFLYYVDPLGSLIEA-PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKK 159

                       170       180
                ....*....|....*....|....
6HEA_m      160 AIYSAMKRDSASGDGIDVVKITED 183
Cdd:cd01912 160 AIDSAIERDLSSGGGVDVAVITKD 183
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-180 5.88e-67

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: 203.57  E-value: 5.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m          1 TTTVGLVCKDGVVMATEKRATMGNFIASK-AAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         77 RAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGK-SIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVE 155
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
6HEA_m        156 LAVRAIYSAMKRDSASGDGIDVVKI 180
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 1-180 7.03e-64

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: 195.41  E-value: 7.03e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRY--FPYLVQLLIGGIDSEGK-SIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELA 157
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGpQLYSVDPSGSYIEYK-ATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
6HEA_m      158 VRAIYSAMKRDSASGDGIDVVKI 180
Cdd:cd01906 160 LKALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-163 1.35e-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: 151.01  E-value: 1.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRY-FPYLVQLLIGGIDSEGKSIYSIDPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVR 159
Cdd:cd01901  81 KELAKLLQVYTQgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
6HEA_m      160 AIYS 163
Cdd:cd01901 161 ALKS 164
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-183 1.93e-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: 146.24  E-value: 1.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIeEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRL-KGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|...
6HEA_m      161 IYSAMKRDSASGDGIDVVKITED 183
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVRED 182
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-184 7.21e-41

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: 136.94  E-value: 7.21e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLnsYRYFPYL-VQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVR 159
Cdd:cd03763  81 TMLKQHL--FRYQGHIgAALVLGGVDYTGPHLYSIYP-HGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCE 157

                       170       180
                ....*....|....*....|....*
6HEA_m      160 AIYSAMKRDSASGDGIDVVKITEDE 184
Cdd:cd03763 158 AIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-183 5.10e-40

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: 5.10e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYFpYLVQLLIGGID-SEGKSIYSIdPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVR 159
Cdd:cd03762  81 SLFKNLCYNYKEM-LSAGIIVAGWDeQNGGQVYSI-PLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158

                       170       180
                ....*....|....*....|....
6HEA_m      160 AIYSAMKRDSASGDGIDVVKITED 183
Cdd:cd03762 159 ALSLAMSRDGSSGGVIRLVIITKD 182
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-202 3.51e-35

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 123.79  E-value: 3.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         1 TTTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        81 TLTSNLLNSYRYF----PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVEL 156
Cdd:PRK03996 116 KKICDHKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDP-SGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIEL 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
6HEA_m       157 AVRAIYSAMK-RDSASGDGIDVVKITEDEFYQYSPEEVEQILAKFRK 202
Cdd:PRK03996 195 ALKALAKANEgKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKLLK 241
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-184 1.06e-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: 118.88  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        4 VGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIATLT 83
Cdd:cd03759   7 VAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSLI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       84 SNLLNSYRYFPYLVQLLIGGIDSEGKS-IYSIDPIGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRAIY 162
Cdd:cd03759  87 SSLLYEKRFGPYFVEPVVAGLDPDGKPfICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETISQALL 166

                       170       180
                ....*....|....*....|..
6HEA_m      163 SAMKRDSASGDGIDVVKITEDE 184
Cdd:cd03759 167 SAVDRDALSGWGAVVYIITKDK 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-200 3.31e-33

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 118.94  E-value: 3.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        81 TLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPIGGAIeEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAVRA 160
Cdd:PTZ00488 120 KILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRL-HGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
6HEA_m       161 IYSAMKRDSASGDGIDVVKITEDEFYQYSPEEVEQILAKF 200
Cdd:PTZ00488 199 IYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-183 5.74e-33

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: 117.36  E-value: 5.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        2 TTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIAT 81
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       82 LTSNLLNSYRYFPYLVQLLIGGIDSEGK-SIYSIDPIgGAIEEKDIVATGSGSLTAYGVL---EDRFTP------EIGVD 151
Cdd:cd03757  90 LLSTILYSRRFFPYYVFNILAGIDEEGKgVVYSYDPV-GSYERETYSAGGSASSLIQPLLdnqVGRKNQnnvertPLSLE 168

                       170       180       190
                ....*....|....*....|....*....|..
6HEA_m      152 EAVELAVRAIYSAMKRDSASGDGIDVVKITED 183
Cdd:cd03757 169 EAVSLVKDAFTSAAERDIYTGDSLEIVIITKD 200
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-182 9.11e-29

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: 106.65  E-value: 9.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03756  29 TTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYF----PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVEL 156
Cdd:cd03756 108 KKICDLKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDP-SGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIEL 186

                       170       180
                ....*....|....*....|....*.
6HEA_m      157 AVRAIYSAMKrDSASGDGIDVVKITE 182
Cdd:cd03756 187 ALKALYAALE-ENETPENVEIAYVTV 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-168 1.59e-25

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: 97.90  E-value: 1.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGnFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd01911  28 STAVGIKGKDGVVLAVEKKVTSK-LLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSYRYF----PYLVQLLIGGIDSE-GKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVE 155
Cdd:cd01911 107 KRIADLAQVYTQYggvrPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYK-ATAIGKGSQEAKTFLEKRYKKDLTLEEAIK 185

                       170
                ....*....|...
6HEA_m      156 LAVRAIYSAMKRD 168
Cdd:cd01911 186 LALKALKEVLEED 198
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-183 3.40e-20

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: 83.77  E-value: 3.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIK---IEANLYEIRRERKPtvR 77
Cdd:cd03760   3 TSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDqlvIDDECLDDGHSLSP--K 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       78 AIATLTSNLLNSYR--YFPYLVQLLIGGIDSEGKS-IYSIDPIGGAIEEkDIVATGSGSLTAYGVLED--RFTPEIGVDE 152
Cdd:cd03760  81 EIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPfLGYVDLLGTAYED-PHVATGFGAYLALPLLREawEKKPDLTEEE 159

                       170       180       190
                ....*....|....*....|....*....|....*
6HEA_m      153 AVELavraIYSAMK----RDSASGDGIDVVKITED 183
Cdd:cd03760 160 ARAL----IEECMKvlyyRDARSINKYQIAVVTKE 190
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-183 3.72e-18

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: 78.40  E-value: 3.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        2 TTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIAT 81
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       82 LTSNLLNSY--RYFPYLVQLLIGGIDS-EGKSIYSIDPIGGAIEEkDIVATGSGSLTAYGVLEDRFTPEIGVDEAVELAV 158
Cdd:cd03758  83 FTRRELAESlrSRTPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKV-PYAAHGYGAYFCLSILDRYYKPDMTVEEALELMK 161

                       170       180
                ....*....|....*....|....*
6HEA_m      159 RAIYSAMKRDSASGDGIDVVKITED 183
Cdd:cd03758 162 KCIKELKKRFIINLPNFTVKVVDKD 186
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-180 5.48e-18

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: 78.15  E-value: 5.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03753  28 STAIGIKTKEGVVLAVEKRIT-SPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNL-LNSYRYF--------PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVD 151
Cdd:cd03753 107 QAVSDLaLQFGEGDdgkkamsrPFGVALLIAGVDENGPQLFHTDP-SGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLE 185

                       170       180
                ....*....|....*....|....*....
6HEA_m      152 EAVELAVRAIYSAMKrDSASGDGIDVVKI 180
Cdd:cd03753 186 EAEKLALSILKQVME-EKLNSTNVELATV 213
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-198 6.34e-18

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: 78.52  E-value: 6.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYE-IRRERKPT---V 76
Cdd:cd03750  28 APSVGIKAANGVVLATEKKVP-SPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYlVYGEPIPVsqlV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       77 RAIATLTSNLLNSYRYFPYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDEAVEL 156
Cdd:cd03750 107 REIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDP-SGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDAIHT 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
6HEA_m      157 AVRAIysamkRDSASG----DGIDVVKITED-EFYQYSPEEVEQILA 198
Cdd:cd03750 186 AILTL-----KEGFEGqmteKNIEIGICGETkGFRLLTPAEIKDYLA 227
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 3-202 3.55e-17

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 76.81  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m         3 TVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIATL 82
Cdd:PTZ00246  34 TVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        83 TSNLLNSYRYF----PYLVQLLIGGIDS-EGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVELA 157
Cdd:PTZ00246 114 ICDLKQSYTQFgglrPFGVSFLFAGYDEnLGYQLYHTDPSGNYSGWK-ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLA 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
6HEA_m       158 VRAIYSAMKRDSASGDGIDVV----KITEDEFYQ--YSPEEVEQILAKFRK 202
Cdd:PTZ00246 193 AKVLTKSMDSTSPKADKIEVGilshGETDGEPIQkmLSEKEIAELLKKVTQ 243
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-161 1.14e-16

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: 74.71  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATMgNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIA 80
Cdd:cd03755  28 TTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYIT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       81 TLTSNLLNSY------RyfPYLVQLLIGGIDSEGKS-IYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEA 153
Cdd:cd03755 107 RYIAGLQQRYtqsggvR--PFGISTLIVGFDPDGTPrLYQTDPSGTYSAWK-ANAIGRNSKTVREFLEKNYKEEMTRDDT 183


                ....*...
6HEA_m      154 VELAVRAI 161
Cdd:cd03755 184 IKLAIKAL 191
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-163 1.14e-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: 71.93  E-value: 1.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        2 TTVGLVCKDGVVMATEKratmgnFIASK-----AAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTV 76
Cdd:cd03751  32 TAIGIRCKDGVVLAVEK------LVTSKlyepgSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       77 RAIATLTSNLLNSYRYF----PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFTPEIGVDE 152
Cdd:cd03751 106 KVLADRVAMYMHAYTLYssvrPFGCSVLLGGYDSDGPQLYMIEP-SGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCRE 184

                       170
                ....*....|.
6HEA_m      153 AVELAVRAIYS 163
Cdd:cd03751 185 AVKEAAKIIYI 195
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-169 2.60e-14

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: 68.47  E-value: 2.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        1 TTTVGLVCKDGVVMATEKRATmgnfiaSKAA---KKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVR 77
Cdd:cd03749  28 SATVGLKSKTHAVLVALKRAT------SELSsyqKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       78 AIATLTSNLL--NSYRYF--PYLVQLLIGGIDSEGKSIYSIDPiGGAIEEKDIVATGSGSLTAYGVLEDRFT--PEIGVD 151
Cdd:cd03749 102 RLVSKVAEKAqiNTQRYGrrPYGVGLLIAGYDESGPHLFQTCP-SGNYFEYKATSIGARSQSARTYLERHFEefEDCSLE 180

                       170
                ....*....|....*...
6HEA_m      152 EAVELAVRAIYSAMKRDS 169
Cdd:cd03749 181 ELIKHALRALRETLPGEQ 198
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-177 4.66e-14

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: 67.76  E-value: 4.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        2 TTVGLVCKDGVVMATEKRATMGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIAT 81
Cdd:cd03752  31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQLVQ 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       82 LTSNLLNSYRYF----PYLVQLLIGGIDS-EGKSIYSIDPIGGAIEEKdIVATGSGSLTAYGVLEDRFTPEIGVDEAVEL 156
Cdd:cd03752 111 RLCDIKQGYTQYgglrPFGVSFLYAGWDKhYGFQLYQSDPSGNYSGWK-ATAIGNNNQAAQSLLKQDYKDDMTLEEALAL 189

                       170       180
                ....*....|....*....|.
6HEA_m      157 AVRAIYSAMKRDSASGDGIDV 177
Cdd:cd03752 190 AVKVLSKTMDSTKLTSEKLEF 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-168 2.41e-06

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: 46.46  E-value: 2.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m        2 TTVGLVCKDGVVMATEKRATmGNFIASKAAKKIYQIADRMAMTTAGSVGDAQFLARIIKIEANLYEIRRERKPTVRAIAT 81
Cdd:cd03754  31 TSVAVRGKDCAVVVTQKKVP-DKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPVDVLAK 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6HEA_m       82 LTSNLLNSY--RYF--PYLVQLLIGGIDSE-GKSIYSIDPIGGAIEEKdivATGSG--SLTAYGVLEDRF----TPEIGV 150
Cdd:cd03754 110 RIADINQVYtqHAYmrPLGVSMILIGIDEElGPQLYKCDPAGYFAGYK---ATAAGvkEQEATNFLEKKLkkkpDLIESY 186

                       170
                ....*....|....*...
6HEA_m      151 DEAVELAVRAIYSAMKRD 168
Cdd:cd03754 187 EETVELAISCLQTVLSTD 204
 
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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