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Conserved domains on  [gi|786582|gb|AAB33092|]
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proteasome subunit MB1, partial [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 ...
12-199 1.98e-137

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: 382.36  E-value: 1.98e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 171
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                       170       180
                ....*....|....*....|....*...
gi 786582   172 YQATYRDAYSGGAVNLYHVREDGWIRVS 199
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 ...
12-199 1.98e-137

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: 382.36  E-value: 1.98e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 171
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                       170       180
                ....*....|....*....|....*...
gi 786582   172 YQATYRDAYSGGAVNLYHVREDGWIRVS 199
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
6-215 3.73e-130

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 366.24  E-value: 3.73e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      6 IEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERI 85
Cdd:PTZ00488  34 IEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     86 SVAAASKLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYD 165
Cdd:PTZ00488 114 SVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 786582    166 LARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 215
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
8-190 5.39e-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: 178.53  E-value: 5.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582       8 MLHGTTTLAFKFRHGVIVAADSRATAGAYI-ASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERIS 86
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      87 V----AAASKLLANMVYQYKGMgLSMGSMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVE 161
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 786582     162 QAYDLARRAIYQATYRDAYSGGAVNLYHV 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
11-194 4.47e-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: 165.85  E-value: 4.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      11 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAA 90
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      91 SKLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 170
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 786582     171 IYQATYRDAYSGGAVNLYHVREDG 194
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
2-201 2.25e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 165.70  E-value: 2.25e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     2 EEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRN 81
Cdd:COG0638  26 EYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    82 KERISVAAASKLLANMVYQYKGMG---LSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDL 158
Cdd:COG0638 106 GEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDL 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 786582   159 EVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 201
Cdd:COG0638 186 SLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
12-199 1.98e-137

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: 382.36  E-value: 1.98e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 171
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                       170       180
                ....*....|....*....|....*...
gi 786582   172 YQATYRDAYSGGAVNLYHVREDGWIRVS 199
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
6-215 3.73e-130

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 366.24  E-value: 3.73e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      6 IEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERI 85
Cdd:PTZ00488  34 IEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     86 SVAAASKLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYD 165
Cdd:PTZ00488 114 SVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 786582    166 LARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 215
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
12-198 7.94e-84

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: 246.59  E-value: 7.94e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMGLSMGSMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 170
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160
                       170       180
                ....*....|....*....|....*...
gi 786582   171 IYQATYRDAYSGGAVNLYHVREDGWIRV 198
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
12-190 6.81e-62

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: 190.78  E-value: 6.81e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYK--GMGLSMGSMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLAR 168
Cdd:cd01906  81 KLLANLLYEYTqsLRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160
                       170       180
                ....*....|....*....|..
gi 786582   169 RAIYQATYRDAYSGGAVNLYHV 190
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
8-190 5.39e-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: 178.53  E-value: 5.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582       8 MLHGTTTLAFKFRHGVIVAADSRATAGAYI-ASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERIS 86
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      87 V----AAASKLLANMVYQYKGMgLSMGSMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVE 161
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 786582     162 QAYDLARRAIYQATYRDAYSGGAVNLYHV 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
11-194 4.47e-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: 165.85  E-value: 4.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      11 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAA 90
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582      91 SKLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 170
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 786582     171 IYQATYRDAYSGGAVNLYHVREDG 194
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
2-201 2.25e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 165.70  E-value: 2.25e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     2 EEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRN 81
Cdd:COG0638  26 EYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    82 KERISVAAASKLLANMVYQYKGMG---LSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDL 158
Cdd:COG0638 106 GEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDL 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 786582   159 EVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 201
Cdd:COG0638 186 SLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
12-199 1.30e-49

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: 159.73  E-value: 1.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMGLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 171
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160
                       170       180
                ....*....|....*....|....*...
gi 786582   172 YQATYRDAYSGGAVNLYHVREDGWIRVS 199
Cdd:cd03764 161 KSAIERDSASGDGIDVVVITKDGYKELE 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
12-172 8.75e-43

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: 8.75e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMG-LSMGSMICGWDKRGPGLYYVDSEGNRISGATF-SVGSGSVYAYGVMDRGYSYDLEVEQAYDLARR 169
Cdd:cd01901  81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160

                ...
gi 786582   170 AIY 172
Cdd:cd01901 161 ALK 163
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
12-194 1.56e-29

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: 108.44  E-value: 1.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMgLSMGSMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 171
Cdd:cd03763  81 TMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159
                       170       180
                ....*....|....*....|...
gi 786582   172 YQATYRDAYSGGAVNLYHVREDG 194
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
12-197 8.16e-29

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: 106.54  E-value: 8.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    12 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAS 91
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    92 KLLANMVYQYKGMgLSMGSMICGWDK-RGPGLYYVdSEGNRISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLARR 169
Cdd:cd03762  81 SLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSI-PLGGMLIRQPFAIgGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
                       170       180
                ....*....|....*....|....*...
gi 786582   170 AIYQATYRDAYSGGAVNLYHVREDGWIR 197
Cdd:cd03762 159 ALSLAMSRDGSSGGVIRLVIITKDGVER 186
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
13-171 1.03e-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: 72.23  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    13 TTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAAsk 92
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    93 llANMV------YQYKGMGLSMGSMICGWDKR-GPGLYYVDSEGNrISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAY 164
Cdd:cd03758  81 --ANFTrrelaeSLRSRTPYQVNLLLAGYDKVeGPSLYYIDYLGT-LVKVPYAAhGYGAYFCLSILDRYYKPDMTVEEAL 157

                ....*..
gi 786582   165 DLARRAI 171
Cdd:cd03758 158 ELMKKCI 164
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
11-194 2.77e-14

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: 68.82  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAA 90
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    91 SKLLANMVYQYKGMGLSMGSMICGWDKRGPG-LYYVDSEGNRISGATFSVGSGSVYAYGVMD---------RGYSYDLEV 160
Cdd:cd03757  88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPLSL 167
                       170       180       190
                ....*....|....*....|....*....|....
gi 786582   161 EQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 194
Cdd:cd03757 168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
10-174 1.02e-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: 67.08  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    10 HGTTTLAFKFRHGVIVAADSRATAgAYIASQTVKKVIEINPYLLGTMAGGAGDCsfweRLLARQCRI----YELRNKERI 85
Cdd:cd01911  26 NGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRARVeaqnYRYTYGEPI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    86 SVAAASKLLANM--VY-QYKGM---GLSMgsMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDL 158
Cdd:cd01911 101 PVEVLVKRIADLaqVYtQYGGVrpfGVSL--LIAGYDEeGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDL 178
                       170
                ....*....|....*.
gi 786582   159 EVEQAYDLARRAIYQA 174
Cdd:cd01911 179 TLEEAIKLALKALKEV 194
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
11-187 7.13e-13

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: 64.66  E-value: 7.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATaGAYIASQTVKKVIEINPYLLGTMAGGAGDCsfweRLLARQCRIYELRNK----ERIS 86
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADA----RVLIDRARVEAQIHRltygEPID 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    87 VAAASKLLANMVYQY------KGMGLSMgsMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV 160
Cdd:cd03756 103 VEVLVKKICDLKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSL 180
                       170       180
                ....*....|....*....|....*..
gi 786582   161 EQAYDLARRAIYqATYRDAYSGGAVNL 187
Cdd:cd03756 181 EEAIELALKALY-AALEENETPENVEI 206
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
11-175 1.47e-11

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 61.77  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     11 GTTTLAFKFRHGVIVAADSRATaGAYIASQTVKKVIEINPYLLGTMAGGAGDCsfweRLL---AR-QCRIYELRNKERIS 86
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLidrARvEAQINRLTYGEPIG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     87 VAAASKLLANM--VY-QYKGM---GLSMgsMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV 160
Cdd:PRK03996 111 VETLTKKICDHkqQYtQHGGVrpfGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSL 188
                        170
                 ....*....|....*
gi 786582    161 EQAYDLARRAIYQAT 175
Cdd:PRK03996 189 EEAIELALKALAKAN 203
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
11-167 8.88e-11

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: 59.27  E-value: 8.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAGAYIASqTVKKVIEINPYLLGTMAGGAGDCsfweRLLARQCRIyELRN-----KERI 85
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADA----RTLIDHARV-EAQNhrftyNEPM 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    86 SVAAASKLLANMVYQYKGMGLSMGSM---------ICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSY 156
Cdd:cd03753 101 TVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180
                       170
                ....*....|.
gi 786582   157 DLEVEQAYDLA 167
Cdd:cd03753 181 DMTLEEAEKLA 191
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
11-163 9.58e-11

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: 59.26  E-value: 9.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAgAYIASQTVKKVIEINPYLLGTMAGGAGDCsfweRLLARQCR----IYELRNKERIS 86
Cdd:cd03750  27 GAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDF----RVLVKKARkiaqQYYLVYGEPIP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    87 VAAASKLLANMVYQY--KG----MGLSMgsMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV 160
Cdd:cd03750 102 VSQLVREIASVMQEYtqSGgvrpFGVSL--LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLEL 179

                ...
gi 786582   161 EQA 163
Cdd:cd03750 180 EDA 182
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
11-194 4.93e-10

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: 56.81  E-value: 4.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYllgTMAGGAGDCSFWE---RLLARQCRIYELR-NKERIS 86
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDN---TLLGASGDYADFQylkRLLDQLVIDDECLdDGHSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    87 VAAASKLLANMVYQY--KGMGLSMGSMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV--E 161
Cdd:cd03760  79 PKEIHSYLTRVLYNRrsKMNPLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLteE 158
                       170       180       190
                ....*....|....*....|....*....|...
gi 786582   162 QAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 194
Cdd:cd03760 159 EARALIEECMKVLYYRDARSINKYQIAVVTKEG 191
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
11-194 5.36e-10

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: 56.48  E-value: 5.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAAA 90
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    91 SKLLANMVYQYKGMGLSMGSMICGWDKRG-PGLYYVDSEGNRISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLAR 168
Cdd:cd03759  83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPSDFVVsGTASEQLYGMCESLWRPDMEPDELFETIS 162
                       170       180
                ....*....|....*....|....*.
gi 786582   169 RAIYQATYRDAYSGGAVNLYHVREDG 194
Cdd:cd03759 163 QALLSAVDRDALSGWGAVVYIITKDK 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
10-167 1.39e-04

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: 41.56  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    10 HGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSFWERLLARQCRIYELRNKERISVAA 89
Cdd:cd03752  28 HAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    90 ASKLLANM--VY-QYKGM---GLSMgsMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQ 162
Cdd:cd03752 108 LVQRLCDIkqGYtQYGGLrpfGVSF--LYAGWDKhYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEE 185

                ....*
gi 786582   163 AYDLA 167
Cdd:cd03752 186 ALALA 190
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
22-175 2.35e-04

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 40.99  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     22 GVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAGDCSfwerLLARQCRIYELRNK----ERISVAAASKLLANM 97
Cdd:PTZ00246  42 GVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADAN----ILINQCRLYAQRYRytygEPQPVEQLVVQICDL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582     98 ---VYQYKGM---GLSMgsMICGWDKR-GPGLYYVDSEGNrISG--ATfSVGSGSVYAYGVMDRGYSYDLEVEQAYDLAR 168
Cdd:PTZ00246 118 kqsYTQFGGLrpfGVSF--LFAGYDENlGYQLYHTDPSGN-YSGwkAT-AIGQNNQTAQSILKQEWKEDLTLEQGLLLAA 193

                 ....*..
gi 786582    169 RAIYQAT 175
Cdd:PTZ00246 194 KVLTKSM 200
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
11-143 6.31e-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: 36.50  E-value: 6.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 786582    11 GTTTLAFKFRHGVIVAADSRATAGAyiaSQTVKKVIEINPYLLGTMAGGAGDCsfweRLLARQCRIYELRNK-------- 82
Cdd:cd03749  27 GSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADA----RVLSRYMRQECLNYRfvydspip 99
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 786582    83 -ERISVAAASKLLANMVYQYK---GMGLsmgsMICGWDKRGPGLYYVDSEGNRISGATFSVGSGS 143
Cdd:cd03749 100 vSRLVSKVAEKAQINTQRYGRrpyGVGL----LIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
 
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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