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Conserved domains on  [gi|189053214|dbj|BAG34836|]
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unnamed protein product [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 ...
60-247 1.47e-139

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: 389.68  E-value: 1.47e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 219
Cdd:cd03761   81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                        170       180
                 ....*....|....*....|....*...
gi 189053214 220 YQATYRDAYSGGAVNLYHVREDGWIRVS 247
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 ...
60-247 1.47e-139

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: 389.68  E-value: 1.47e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 219
Cdd:cd03761   81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                        170       180
                 ....*....|....*....|....*...
gi 189053214 220 YQATYRDAYSGGAVNLYHVREDGWIRVS 247
Cdd:cd03761  161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
54-263 4.42e-132

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 373.17  E-value: 4.42e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  54 IEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERI 133
Cdd:PTZ00488  34 IEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 134 SVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYD 213
Cdd:PTZ00488 114 SVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189053214 214 LARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 263
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
56-238 1.80e-58

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: 184.31  E-value: 1.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214   56 MLHGTTTLAFKFRHGVIVAADSRATAGAYI-ASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERIS 134
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  135 V----AAASKLLANMVYQYKGMgLSMGTMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVE 209
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 189053214  210 QAYDLARRAIYQATYRDAYSGGAVNLYHV 238
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
29-249 5.37e-52

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 169.17  E-value: 5.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  29 DLGPGSLSDGLSLAAPGWGVP--EEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAG 106
Cdd:COG0638    3 PSQQSSYDRAITIFSPDGRLYqvEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 107 GAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMG---LSMGTMICGWDKRGPGLYYVDSEGNRISGA 183
Cdd:COG0638   83 LVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189053214 184 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 249
Cdd:COG0638  163 AVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
59-242 9.03e-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: 167.00  E-value: 9.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214   59 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAA 138
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  139 SKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 218
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 189053214  219 IYQATYRDAYSGGAVNLYHVREDG 242
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
60-247 1.47e-139

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: 389.68  E-value: 1.47e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 219
Cdd:cd03761   81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                        170       180
                 ....*....|....*....|....*...
gi 189053214 220 YQATYRDAYSGGAVNLYHVREDGWIRVS 247
Cdd:cd03761  161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
54-263 4.42e-132

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 373.17  E-value: 4.42e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  54 IEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERI 133
Cdd:PTZ00488  34 IEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 134 SVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYD 213
Cdd:PTZ00488 114 SVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 189053214 214 LARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 263
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKE 243
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
60-246 3.47e-85

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: 251.98  E-value: 3.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMGLSMGTMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 218
Cdd:cd01912   81 NLLSNILYSYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160
                        170       180
                 ....*....|....*....|....*...
gi 189053214 219 IYQATYRDAYSGGAVNLYHVREDGWIRV 246
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
60-238 3.07e-63

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: 196.18  E-value: 3.07e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYK--GMGLSMGTMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLAR 216
Cdd:cd01906   81 KLLANLLYEYTqsLRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160
                        170       180
                 ....*....|....*....|..
gi 189053214 217 RAIYQATYRDAYSGGAVNLYHV 238
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
56-238 1.80e-58

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: 184.31  E-value: 1.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214   56 MLHGTTTLAFKFRHGVIVAADSRATAGAYI-ASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERIS 134
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  135 V----AAASKLLANMVYQYKGMgLSMGTMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVE 209
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRP-FGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 189053214  210 QAYDLARRAIYQATYRDAYSGGAVNLYHV 238
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
29-249 5.37e-52

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 169.17  E-value: 5.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  29 DLGPGSLSDGLSLAAPGWGVP--EEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAG 106
Cdd:COG0638    3 PSQQSSYDRAITIFSPDGRLYqvEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 107 GAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMG---LSMGTMICGWDKRGPGLYYVDSEGNRISGA 183
Cdd:COG0638   83 LVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189053214 184 TFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSD 249
Cdd:COG0638  163 AVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
59-242 9.03e-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: 167.00  E-value: 9.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214   59 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAA 138
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  139 SKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRA 218
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 189053214  219 IYQATYRDAYSGGAVNLYHVREDG 242
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
60-247 2.00e-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: 161.27  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 219
Cdd:cd03764   81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160
                        170       180
                 ....*....|....*....|....*...
gi 189053214 220 YQATYRDAYSGGAVNLYHVREDGWIRVS 247
Cdd:cd03764  161 KSAIERDSASGDGIDVVVITKDGYKELE 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
60-220 4.09e-44

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: 146.77  E-value: 4.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMG-LSMGTMICGWDKRGPGLYYVDSEGNRISGATF-SVGSGSVYAYGVMDRGYSYDLEVEQAYDLARR 217
Cdd:cd01901   81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160

                 ...
gi 189053214 218 AIY 220
Cdd:cd01901  161 ALK 163
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
60-242 2.41e-30

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: 111.91  E-value: 2.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMgLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAI 219
Cdd:cd03763   81 TMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159
                        170       180
                 ....*....|....*....|...
gi 189053214 220 YQATYRDAYSGGAVNLYHVREDG 242
Cdd:cd03763  160 EAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
60-245 2.46e-30

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: 111.93  E-value: 2.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  60 TTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAS 139
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 140 KLLANMVYQYKGMgLSMGTMICGWDK-RGPGLYYVdSEGNRISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLARR 217
Cdd:cd03762   81 SLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSI-PLGGMLIRQPFAIgGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
                        170       180
                 ....*....|....*....|....*...
gi 189053214 218 AIYQATYRDAYSGGAVNLYHVREDGWIR 245
Cdd:cd03762  159 ALSLAMSRDGSSGGVIRLVIITKDGVER 186
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
58-222 1.02e-14

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: 70.93  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  58 HGTTTLAFKFRHGVIVAADSRATAgAYIASQTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCRI----YELRNKERI 133
Cdd:cd01911   26 NGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRARVeaqnYRYTYGEPI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 134 SVAAASKLLANM--VY-QYKGM---GLSMgtMICGWDK-RGPGLYYVDSEGNrISG--ATfSVGSGSVYAYGVMDRGYSY 204
Cdd:cd01911  101 PVEVLVKRIADLaqVYtQYGGVrpfGVSL--LIAGYDEeGGPQLYQTDPSGT-YFGykAT-AIGKGSQEAKTFLEKRYKK 176
                        170
                 ....*....|....*...
gi 189053214 205 DLEVEQAYDLARRAIYQA 222
Cdd:cd01911  177 DLTLEEAIKLALKALKEV 194
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
59-242 1.05e-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: 70.75  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAA 138
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 139 SKLLANMVYQYKGMGLSMGTMICGWDKRGPG-LYYVDSEGNRISGATFSVGSGSVYAYGVMD---------RGYSYDLEV 208
Cdd:cd03757   88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPLSL 167
                        170       180       190
                 ....*....|....*....|....*....|....
gi 189053214 209 EQAYDLARRAIYQATYRDAYSGGAVNLYHVREDG 242
Cdd:cd03757  168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
61-219 1.69e-14

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: 69.92  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  61 TTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAAsk 140
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 141 llANMV------YQYKGMGLSMGTMICGWDKR-GPGLYYVDSEGNrISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAY 212
Cdd:cd03758   81 --ANFTrrelaeSLRSRTPYQVNLLLAGYDKVeGPSLYYIDYLGT-LVKVPYAAhGYGAYFCLSILDRYYKPDMTVEEAL 157

                 ....*..
gi 189053214 213 DLARRAI 219
Cdd:cd03758  158 ELMKKCI 164
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
59-235 2.84e-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: 66.97  E-value: 2.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATaGAYIASQTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCRIYELRNK----ERIS 134
Cdd:cd03756   28 GTTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADA----RVLIDRARVEAQIHRltygEPID 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 135 VAAASKLLANMVYQYKGMG----LSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQ 210
Cdd:cd03756  103 VEVLVKKICDLKQQYTQHGgvrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEE 182
                        170       180
                 ....*....|....*....|....*
gi 189053214 211 AYDLARRAIYqATYRDAYSGGAVNL 235
Cdd:cd03756  183 AIELALKALY-AALEENETPENVEI 206
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
59-223 6.17e-12

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 63.70  E-value: 6.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATaGAYIASQTVKKVIEINPYLLGTMAGGAADCsfweRLL---AR-QCRIYELRNKERIS 134
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLidrARvEAQINRLTYGEPIG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 135 VAAASKLLANM--VY-QYKGM---GLSMgtMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV 208
Cdd:PRK03996 111 VETLTKKICDHkqQYtQHGGVrpfGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSL 188
                        170
                 ....*....|....*
gi 189053214 209 EQAYDLARRAIYQAT 223
Cdd:PRK03996 189 EEAIELALKALAKAN 203
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
59-215 2.14e-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: 61.58  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAGAYIASqTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCRIyELRN-----KERI 133
Cdd:cd03753   27 GSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADA----RTLIDHARV-EAQNhrftyNEPM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 134 SVAAASKLLANMVYQYKGMGLSMGTM---------ICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSY 204
Cdd:cd03753  101 TVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180
                        170
                 ....*....|.
gi 189053214 205 DLEVEQAYDLA 215
Cdd:cd03753  181 DMTLEEAEKLA 191
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
59-242 5.37e-11

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: 60.28  E-value: 5.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELR-NKERISVAA 137
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLdDGHSLSPKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 138 ASKLLANMVYQY--KGMGLSMGTMICGWDKRG-PGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV--EQAY 212
Cdd:cd03760   82 IHSYLTRVLYNRrsKMNPLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLteEEAR 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 189053214 213 DLARRAIYQATYRDAYSGGAVNLYHVREDG 242
Cdd:cd03760  162 ALIEECMKVLYYRDARSINKYQIAVVTKEG 191
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
59-211 7.09e-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: 60.41  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAgAYIASQTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCR----IYELRNKERIS 134
Cdd:cd03750   27 GAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDF----RVLVKKARkiaqQYYLVYGEPIP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 135 VAAASKLLANMVYQY--KG----MGLSMgtMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEV 208
Cdd:cd03750  102 VSQLVREIASVMQEYtqSGgvrpFGVSL--LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLEL 179

                 ...
gi 189053214 209 EQA 211
Cdd:cd03750  180 EDA 182
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
59-242 3.22e-09

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: 55.33  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAA 138
Cdd:cd03759    3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 139 SKLLANMVYQYKGMGLSMGTMICGWDKRG-PGLYYVDSEGNRISGATFSV-GSGSVYAYGVMDRGYSYDLEVEQAYDLAR 216
Cdd:cd03759   83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPSDFVVsGTASEQLYGMCESLWRPDMEPDELFETIS 162
                        170       180
                 ....*....|....*....|....*.
gi 189053214 217 RAIYQATYRDAYSGGAVNLYHVREDG 242
Cdd:cd03759  163 QALLSAVDRDALSGWGAVVYIITKDK 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
58-215 2.14e-05

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: 44.26  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  58 HGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAA 137
Cdd:cd03752   28 HAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 138 ASKLLANM--VY-QYKGM---GLSMgtMICGWDK-RGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQ 210
Cdd:cd03752  108 LVQRLCDIkqGYtQYGGLrpfGVSF--LYAGWDKhYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEE 185

                 ....*
gi 189053214 211 AYDLA 215
Cdd:cd03752  186 ALALA 190
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
70-223 3.40e-05

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 44.07  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  70 GVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSfwerLLARQCRIYELRNK----ERISVAAASKLLANM 145
Cdd:PTZ00246  42 GVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADAN----ILINQCRLYAQRYRytygEPQPVEQLVVQICDL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214 146 ---VYQYKGM---GLSMgtMICGWDKR-GPGLYYVDSEGNrISG--ATfSVGSGSVYAYGVMDRGYSYDLEVEQAYDLAR 216
Cdd:PTZ00246 118 kqsYTQFGGLrpfGVSF--LFAGYDENlGYQLYHTDPSGN-YSGwkAT-AIGQNNQTAQSILKQEWKEDLTLEQGLLLAA 193

                 ....*..
gi 189053214 217 RAIYQAT 223
Cdd:PTZ00246 194 KVLTKSM 200
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
59-191 2.79e-04

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: 41.12  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADSRATAGAyiaSQTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCRIYELRNK-------- 130
Cdd:cd03749   27 GSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADA----RVLSRYMRQECLNYRfvydspip 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189053214 131 -ERISVAAASKLLANM-VYQYKGMGLsmGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGS 191
Cdd:cd03749  100 vSRLVSKVAEKAQINTqRYGRRPYGV--GLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
59-177 3.09e-03

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 37.98  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189053214  59 GTTTLAFKFRHGVIVAADsRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCsfweRLLARQCRI----YELRNKERIS 134
Cdd:cd03754   29 GLTSVAVRGKDCAVVVTQ-KKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS----RSQVQRARYeaaeFKYKYGYEMP 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 189053214 135 VAAASKLLANM--VY-QYKGM---GLSMgtMICGWD-KRGPGLYYVDSEG 177
Cdd:cd03754  104 VDVLAKRIADInqVYtQHAYMrplGVSM--ILIGIDeELGPQLYKCDPAG 151
 
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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