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Conserved domains on  [gi|73747875|ref|NP_683720|]
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proteasome subunit beta type-8 isoform E2 precursor [Homo sapiens]

Protein Classification

proteasome subunit beta( domain architecture ID 10132926)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-260 3.95e-134

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: 376.58  E-value: 3.95e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 232
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 73747875 233 AYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-260 3.95e-134

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: 376.58  E-value: 3.95e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 232
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 73747875 233 AYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-271 3.87e-125

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 356.22  E-value: 3.87e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   39 SPELALPRGMQPTEFFQSLGGD-GERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTM 117
Cdd:PTZ00488   5 PEHFEHPPGAHPGDFLAEYTFDhGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  118 SGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNM 197
Cdd:PTZ00488  85 AGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNM 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747875  198 FSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQY 271
Cdd:PTZ00488 165 FSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-251 1.04e-57

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: 182.77  E-value: 1.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875    69 MAHGTTTLAFKFQHGVIAAVDSRASAGSYISALR-VNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERIS 147
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   148 VS----AASKLLSNMmcQYRGMG-LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSP 221
Cdd:pfam00227  81 VElaarIADLLQAYT--QYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 73747875   222 EEAYDLGRRAIAYATHRDSYSGGVVNMYHM 251
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 72-255 1.46e-52

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: 169.31  E-value: 1.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875    72 GTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAA 151
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   152 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 231
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 73747875   232 IAYATHRDSYSGGVVNMYHMKEDG 255
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 71-260 1.22e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 155.69  E-value: 1.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  71 HGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSA 150
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 151 ASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAY 225
Cdd:COG0638 114 LAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73747875 226 DLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-260 3.95e-134

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: 376.58  E-value: 3.95e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 232
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 73747875 233 AYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-271 3.87e-125

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 356.22  E-value: 3.87e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   39 SPELALPRGMQPTEFFQSLGGD-GERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTM 117
Cdd:PTZ00488   5 PEHFEHPPGAHPGDFLAEYTFDhGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  118 SGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNM 197
Cdd:PTZ00488  85 AGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNM 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747875  198 FSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQY 271
Cdd:PTZ00488 165 FSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 73-260 5.56e-83

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: 246.97  E-value: 5.56e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 231
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*....
gi 73747875 232 IAYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 73-251 9.23e-61

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: 190.40  E-value: 9.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYR--GMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGR 229
Cdd:cd01906  81 KLLANLLYEYTqsLRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 73747875 230 RAIAYATHRDSYSGGVVNMYHM 251
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-251 1.04e-57

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: 182.77  E-value: 1.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875    69 MAHGTTTLAFKFQHGVIAAVDSRASAGSYISALR-VNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERIS 147
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   148 VS----AASKLLSNMmcQYRGMG-LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSP 221
Cdd:pfam00227  81 VElaarIADLLQAYT--QYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 73747875   222 EEAYDLGRRAIAYATHRDSYSGGVVNMYHM 251
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 72-255 1.46e-52

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: 169.31  E-value: 1.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875    72 GTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAA 151
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   152 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 231
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 73747875   232 IAYATHRDSYSGGVVNMYHMKEDG 255
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-260 3.40e-51

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: 165.89  E-value: 3.40e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 232
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                       170       180
                ....*....|....*....|....*...
gi 73747875 233 AYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:cd03764 161 KSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 71-260 1.22e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 155.69  E-value: 1.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  71 HGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSA 150
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 151 ASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAY 225
Cdd:COG0638 114 LAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73747875 226 DLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVE 260
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 73-232 5.94e-42

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: 141.76  E-value: 5.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMG-LSMGSMICGWDKKGPGLYYVDEHGTRLSG-NMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRR 230
Cdd:cd01901  81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ..
gi 73747875 231 AI 232
Cdd:cd01901 161 AL 162
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-255 2.20e-34

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: 122.72  E-value: 2.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMgLSMGSMICGWDK-KGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 231
Cdd:cd03762  81 SLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNA 159

                       170       180
                ....*....|....*....|....
gi 73747875 232 IAYATHRDSYSGGVVNMYHMKEDG 255
Cdd:cd03762 160 LSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-255 6.44e-25

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: 98.04  E-value: 6.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  73 TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAAS 152
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 153 KLLSNMMCQYRGMgLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 232
Cdd:cd03763  81 TMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180
                ....*....|....*....|...
gi 73747875 233 AYATHRDSYSGGVVNMYHMKEDG 255
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-263 3.02e-17

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: 78.07  E-value: 3.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  72 GTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAA 151
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 152 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPG-LYYVDEHGTRLSGNMFSTGSGNTYAYGVMDS---------GYRPNLSP 221
Cdd:cd03757  88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvgrknqnnVERTPLSL 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 73747875 222 EEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGwVKVESTD 263
Cdd:cd03757 168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG-IEEETFP 208
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 74-233 7.81e-15

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: 71.08  E-value: 7.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  74 TTLAFKFQHGVIAAVDSraSAGSYISALR--VNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAA 151
Cdd:cd03758   3 TLIGIKGKDFVILAADT--SAARSILVLKddEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 152 SKLLSNMMCQY--RGMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLG 228
Cdd:cd03758  81 ANFTRRELAESlrSRTPYQVNLLLAGYDKVeGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160


                ....*
gi 73747875 229 RRAIA 233
Cdd:cd03758 161 KKCIK 165
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 63-227 2.14e-14

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: 70.44  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  63 RNVQIEMA-----HGTTTLAFKFQHGVIAAVDSRASAgSYISALRVNKVIEINPYLLGTMSGCAADCqyweRLLAK---- 133
Cdd:cd03753  13 RLFQVEYAieaikLGSTAIGIKTKEGVVLAVEKRITS-PLMEPSSVEKIMEIDDHIGCAMSGLIADA----RTLIDharv 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 134 ECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSM---------ICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGN 204
Cdd:cd03753  88 EAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGS 167

                       170       180
                ....*....|....*....|...
gi 73747875 205 TYAYGVMDSGYRPNLSPEEAYDL 227
Cdd:cd03753 168 EGAQSSLQEKYHKDMTLEEAEKL 190
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-260 3.58e-14

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: 69.14  E-value: 3.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  72 GTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRL-YYLRNGERISVSA 150
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDdECLDDGHSLSPKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 151 ASKLLSNMMCQYRGMG--LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYR--PNLSPEEAY 225
Cdd:cd03760  82 IHSYLTRVLYNRRSKMnpLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkPDLTEEEAR 161

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73747875 226 DLGRRAIAYATHRDSYSGGVVNMYHMKEDGwVKVE 260
Cdd:cd03760 162 ALIEECMKVLYYRDARSINKYQIAVVTKEG-VEIE 195
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 60-237 1.51e-13

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: 67.85  E-value: 1.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  60 DGeRNVQIEMA-----HGTTTLAFKFQHGVIAAVDSRASAgSYISALRVNKVIEINPYLLGTMSGCAADCqyweRLLAKE 134
Cdd:cd01911  11 EG-RLFQVEYAleavkNGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 135 CRL----YYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKK-GPGLYYVDEhgtrlSGNMF----- 198
Cdd:cd01911  85 ARVeaqnYRYTYGEPIPVEVLVKRIADLAQVYtqyggvRPFGVSL--LIAGYDEEgGPQLYQTDP-----SGTYFgykat 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 73747875 199 STGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIaYATH 237
Cdd:cd01911 158 AIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKAL-KEVL 195
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 60-246 3.63e-12

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: 63.89  E-value: 3.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  60 DGeRNVQIEMA-----HGTTTLAFKFQHGVIAAVDSRAsAGSYISALRVNKVIEINPYLLGTMSGCAADCQY---WERLL 131
Cdd:cd03756  12 DG-RLYQVEYAreavkRGTTALGIKCKEGVVLAVDKRI-TSKLVEPESIEKIYKIDDHVGAATSGLVADARVlidRARVE 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 132 AKECRLYYlrnGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNT 205
Cdd:cd03756  90 AQIHRLTY---GEPIDVEVLVKKICDLKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQ 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 73747875 206 YAYGVMDSGYRPNLSPEEAYDLGRRAIaYATHRDSYSGGVV 246
Cdd:cd03756 165 AVTEFLEKEYKEDMSLEEAIELALKAL-YAALEENETPENV 204
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-243 6.83e-12

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: 63.03  E-value: 6.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  72 GTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAA 151
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 152 SKLLSNMMCQYRGMGLSMGSMICGWDKKG-PGLYYVDEHG-TRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGR 229
Cdd:cd03759  83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGcPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162

                       170
                ....*....|....
gi 73747875 230 RAIAYATHRDSYSG 243
Cdd:cd03759 163 QALLSAVDRDALSG 176
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 65-224 7.59e-12

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: 63.49  E-value: 7.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  65 VQIEMA-----HGTTTLAFKFQHGVIAAVDSRASAgSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYY 139
Cdd:cd03750  15 VQIEYAlaavsSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYY 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 140 LRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDS 213
Cdd:cd03750  94 LVYGEPIPVSQLVREIASVMQEYtqsggvRPFGVSL--LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEK 171

                       170
                ....*....|.
gi 73747875 214 GYRPNLSPEEA 224
Cdd:cd03750 172 RYNEDLELEDA 182
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
60-236 1.37e-10

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 59.85  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875   60 DGeRNVQIEMA-----HGTTTLAFKFQHGVIAAVDSRasagsYISALRVNKVIE----INPYLLGTMSGCAADCQY---W 127
Cdd:PRK03996  20 DG-RLYQVEYAreavkRGTTAVGVKTKDGVVLAVDKR-----ITSPLIEPSSIEkifkIDDHIGAASAGLVADARVlidR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  128 ERLLAKECRLYYlrnGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTG 201
Cdd:PRK03996  94 ARVEAQINRLTY---GEPIGVETLTKKICDHKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 73747875  202 SGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYAT 236
Cdd:PRK03996 169 AGRDTVMEFLEKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 66-232 3.29e-03

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: 38.04  E-value: 3.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  66 QIEMA-----HGTTTLAFKFQ-HGVIAAVDSRASA-GSYisalrVNKVIEINPYLLGTMSGCAADCQYWERLLAKEC--- 135
Cdd:cd03749  16 QVEYAmeavkQGSATVGLKSKtHAVLVALKRATSElSSY-----QKKIFKVDDHIGIAIAGLTADARVLSRYMRQEClny 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 136 RLYYLRNG--ERISVSAASKLLSNMmcQ---YRGMGLsmGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSG----NTY 206
Cdd:cd03749  91 RFVYDSPIpvSRLVSKVAEKAQINT--QrygRRPYGV--GLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARsqsaRTY 166

                       170       180
                ....*....|....*....|....*.
gi 73747875 207 AYGVMDSgyRPNLSPEEAYDLGRRAI 232
Cdd:cd03749 167 LERHFEE--FEDCSLEELIKHALRAL 190
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 60-237 7.50e-03

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: 36.87  E-value: 7.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875  60 DGeRNVQIEMA-----HGTTTLAFKFQHGVIAAVDSRASAGSYISalRVNKVI-EINPYLLGTMSGCAADCQYWERLLAK 133
Cdd:cd03751  14 DG-RVFQVEYAnkaveNSGTAIGIRCKDGVVLAVEKLVTSKLYEP--GSNKRIfNVDRHIGIAVAGLLADGRHLVSRARE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747875 134 ECRLYYLRNGERISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYA 207
Cdd:cd03751  91 EAENYRDNYGTPIPVKVLADRVAMYMHAYtlyssvRPFGCSV--LLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAA 168

                       170       180       190
                ....*....|....*....|....*....|.
gi 73747875 208 YGVMDSGYRPNLSPEEA-YDLGRraIAYATH 237
Cdd:cd03751 169 KTELEKLKFSELTCREAvKEAAK--IIYIVH 197
 
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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