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MULTISPECIES: archaeal proteasome endopeptidase complex subunit beta [Methanoculleus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 11-196 1.12e-99

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: 286.80  E-value: 1.12e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....*.
gi 1055286705 171 AVRSAMRRDSASGEDIMLVVITKDKY 196
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKDGV 185
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 11-196 1.12e-99

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: 286.80  E-value: 1.12e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....*.
gi 1055286705 171 AVRSAMRRDSASGEDIMLVVITKDKY 196
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-198 2.16e-99

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: 286.07  E-value: 2.16e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALRA 171
Cdd:cd03764    81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSII-EDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                         170       180
                  ....*....|....*....|....*..
gi 1055286705 172 VRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:cd03764   160 IKSAIERDSASGDGIDVVVITKDGYKE 186
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 7-198 9.92e-93

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 270.86  E-value: 9.92e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMKGTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:COG0638    31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAASTLLSNYLNQN---RYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDE 163
Cdd:COG0638   111 VEGLAKLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1055286705 164 ARDLALRAVRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:COG0638   190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-191 8.56e-67

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 203.57  E-value: 8.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   8 IMKGTTTVGLIFDNGVVLATEMRATMGNMIASKR-AKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAA---STLLSNYLNQNRYYPYYVQLLVGGFDNEG-PSIYSVDaMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKED 162
Cdd:pfam00227  81 VELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQID-PSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 1055286705 163 EARDLALRAVRSAMRRDSASGEDIMLVVI 191
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-196 2.49e-42

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 143.21  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMKGTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:PTZ00488   35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAASTLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARD 166
Cdd:PTZ00488  115 VAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDN-DGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193

                         170       180       190
                  ....*....|....*....|....*....|
gi 1055286705 167 LALRAVRSAMRRDSASGEDIMLVVITKDKY 196
Cdd:PTZ00488  194 LGRRAIYHATFRDAYSGGAINLYHMQKDGW 223
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 11-196 1.12e-99

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: 286.80  E-value: 1.12e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....*.
gi 1055286705 171 AVRSAMRRDSASGEDIMLVVITKDKY 196
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-198 2.16e-99

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: 286.07  E-value: 2.16e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALRA 171
Cdd:cd03764    81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSII-EDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                         170       180
                  ....*....|....*....|....*..
gi 1055286705 172 VRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:cd03764   160 IKSAIERDSASGDGIDVVVITKDGYKE 186
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 7-198 9.92e-93

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 270.86  E-value: 9.92e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMKGTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:COG0638    31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAASTLLSNYLNQN---RYYPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDE 163
Cdd:COG0638   111 VEGLAKLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1055286705 164 ARDLALRAVRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:COG0638   190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-199 1.40e-76

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


Pssm-ID: 238893  Cd Length: 189  Bit Score: 228.48  E-value: 1.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYYPYYVQLLVGGFDN-EGPSIYSVDaMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:cd01912    81 NLLSNILYSYRGFPYYVSLIVGGVDKgGGPFLYYVD-PLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1055286705 171 AVRSAMRRDSASGEDIMLVVITKDKYEEH 199
Cdd:cd01912   160 AIDSAIERDLSSGGGVDVAVITKDGVEEL 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-191 8.56e-67

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 203.57  E-value: 8.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   8 IMKGTTTVGLIFDNGVVLATEMRATMGNMIASKR-AKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAA---STLLSNYLNQNRYYPYYVQLLVGGFDNEG-PSIYSVDaMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKED 162
Cdd:pfam00227  81 VELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQID-PSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 1055286705 163 EARDLALRAVRSAMRRDSASGEDIMLVVI 191
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 12-191 4.96e-64

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 196.18  E-value: 4.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYY--PYYVQLLVGGFDNE-GPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLA 168
Cdd:cd01906    81 KLLANLLYEYTQSlrPLGVSLLVAGVDEEgGPQLYSVDPSGSYI-EYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                         170       180
                  ....*....|....*....|...
gi 1055286705 169 LRAVRSAMRRDSASGEDIMLVVI 191
Cdd:cd01906   160 LKALKSALERDLYSGGNIEVAVI 182
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-199 1.51e-51

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: 164.73  E-value: 1.51e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGGATKeEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALRA 171
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLK-GDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                         170       180
                  ....*....|....*....|....*...
gi 1055286705 172 VRSAMRRDSASGEDIMLVVITKDKYEEH 199
Cdd:cd03761   160 IYHATHRDAYSGGNVNLYHVREDGWRKI 187
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 12-174 1.15e-46

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 151.39  E-value: 1.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYY-PYYVQLLVGGFDNEGPSIYSVDAMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:cd01901    81 KELAKLLQVYTQGrPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                  ....
gi 1055286705 171 AVRS 174
Cdd:cd01901   161 ALKS 164
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-196 2.49e-42

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 143.21  E-value: 2.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMKGTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMS 86
Cdd:PTZ00488   35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  87 VGAASTLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARD 166
Cdd:PTZ00488  115 VAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDN-DGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQD 193

                         170       180       190
                  ....*....|....*....|....*....|
gi 1055286705 167 LALRAVRSAMRRDSASGEDIMLVVITKDKY 196
Cdd:PTZ00488  194 LGRRAIYHATFRDAYSGGAINLYHMQKDGW 223
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-199 2.27e-41

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


Pssm-ID: 239732  Cd Length: 189  Bit Score: 138.87  E-value: 2.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLnqnryYPY--YVQ--LLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDL 167
Cdd:cd03763    81 TMLKQHL-----FRYqgHIGaaLVLGGVDYTGPHLYSIYP-HGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKL 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1055286705 168 ALRAVRSAMRRDSASGEDIMLVVITKDKYEEH 199
Cdd:cd03763   155 VCEAIEAGIFNDLGSGSNVDLCVITKDGVEYL 186
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-200 3.41e-37

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: 128.11  E-value: 3.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  12 TTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAS 91
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  92 TLLSNYLNQNRYYpYYVQLLVGGFD-NEGPSIYSVdAMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLALR 170
Cdd:cd03762    81 SLFKNLCYNYKEM-LSAGIIVAGWDeQNGGQVYSI-PLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1055286705 171 AVRSAMRRDSASGEDIMLVVITKDKYEEHI 200
Cdd:cd03762   159 ALSLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-198 9.85e-33

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 117.36  E-value: 9.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:cd03757     8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNRYYPYYVQLLVGGFDNEG-PSIYSVDAMgGATKEEEIVATGSGSPFAYGVLEDQ---------YHADMK 160
Cdd:cd03757    88 AQLLSTILYSRRFFPYYVFNILAGIDEEGkGVVYSYDPV-GSYERETYSAGGSASSLIQPLLDNQvgrknqnnvERTPLS 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1055286705 161 EDEARDLALRAVRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:cd03757   167 LEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEE 204
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-195 1.26e-32

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: 116.57  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:cd03759     3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNRYYPYYVQLLVGGFDNEG-PSIYSVDAMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEARDLAL 169
Cdd:cd03759    83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162

                         170       180
                  ....*....|....*....|....*.
gi 1055286705 170 RAVRSAMRRDSASGEDIMLVVITKDK 195
Cdd:cd03759   163 QALLSAVDRDALSGWGAVVYIITKDK 188
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 11-202 8.68e-30

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


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 109.80  E-value: 8.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDGK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNYLNQNryYPYYVQ------LLVG-GFDNEGPSIYSVDAMGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDE 163
Cdd:TIGR03690  82 ANRLAAMVRGN--LPAAMQglavvpLLAGyDLDAGAGRIFSYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1055286705 164 ARDLALRAVRSAMRRDSAS-GEDI------MLVVITKDKYEEHIES 202
Cdd:TIGR03690 160 ALRVAVEALYDAADDDSATgGPDLvrgiypTVVVITADGARRVPES 205
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-176 3.47e-25

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 97.51  E-value: 3.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  10 KGTTTVGLIFDNGVVLATEMRATMGnMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGA 89
Cdd:cd01911    26 NGSTAVGIKGKDGVVLAVEKKVTSK-LLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  90 ASTLLSNYLNQNRYY----PYYVQLLVGGFDNE-GPSIYSVDAMGG-----ATkeeeivATGSGSPFAYGVLEDQYHADM 159
Cdd:cd01911   105 LVKRIADLAQVYTQYggvrPFGVSLLIAGYDEEgGPQLYQTDPSGTyfgykAT------AIGKGSQEAKTFLEKRYKKDL 178

                         170
                  ....*....|....*..
gi 1055286705 160 KEDEARDLALRAVRSAM 176
Cdd:cd01911   179 TLEEAIKLALKALKEVL 195
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
10-194 4.01e-25

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 97.98  E-value: 4.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  10 KGTTTVGLIFDNGVVLATEMRATmGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGA 89
Cdd:PRK03996   35 RGTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVET 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  90 ASTLLSNYLNQNRYY----PYYVQLLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEAR 165
Cdd:PRK03996  114 LTKKICDHKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDP-SGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAI 192

                         170       180
                  ....*....|....*....|....*....
gi 1055286705 166 DLALRAVRSAMrRDSASGEDIMLVVITKD 194
Cdd:PRK03996  193 ELALKALAKAN-EGKLDPENVEIAYIDVE 220
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-192 3.90e-24

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: 94.70  E-value: 3.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  10 KGTTTVGLIFDNGVVLATEMRATmGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGA 89
Cdd:cd03756    27 RGTTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  90 ASTLLSNYLNQNRYY----PYYVQLLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYHADMKEDEAR 165
Cdd:cd03756   106 LVKKICDLKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDP-SGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAI 184

                         170       180
                  ....*....|....*....|....*..
gi 1055286705 166 DLALRAVRSAMrRDSASGEDIMLVVIT 192
Cdd:cd03756   185 ELALKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-198 5.50e-24

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: 93.80  E-value: 5.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  13 TTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAAST 92
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  93 L----LSNYLNQNRyyPYYVQLLVGGFDN-EGPSIYSVDAMGGATKeEEIVATGSGSPFAYGVLEDQYHADMKEDEARDL 167
Cdd:cd03758    83 FtrreLAESLRSRT--PYQVNLLLAGYDKvEGPSLYYIDYLGTLVK-VPYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1055286705 168 ALRAVRSAMRRDSASGEDIMLVVITKDKYEE 198
Cdd:cd03758   160 MKKCIKELKKRFIINLPNFTVKVVDKDGIRD 190
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-194 9.43e-24

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: 93.40  E-value: 9.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQvECNLFEMRRGKTMSVGAA 90
Cdd:cd03760     2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLD-QLVIDDECLDDGHSLSPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 StlLSNYLNQ------NRYYPYYVQLLVGGFDNEG-PSIYSVDaMGGATKEEEIVATGSGSPFAYGVLEDQYHA--DMKE 161
Cdd:cd03760    81 E--IHSYLTRvlynrrSKMNPLWNTLVVGGVDNEGePFLGYVD-LLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTE 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1055286705 162 DEARDLALRAVRSAMRRDSASGEDIMLVVITKD 194
Cdd:cd03760   158 EEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-176 1.40e-20

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: 85.47  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMK-GTTTVGLIFDNGVVLATEMRATMGNMIASkRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTM 85
Cdd:cd03753    22 EAIKlGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  86 SVGAASTLLSNYLNQ-----------NRyyPYYVQLLVGGFDNEGPSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQ 154
Cdd:cd03753   101 TVESVTQAVSDLALQfgegddgkkamSR--PFGVALLIAGVDENGPQLFHTDPSGTFT-RCDAKAIGSGSEGAQSSLQEK 177

                         170       180
                  ....*....|....*....|..
gi 1055286705 155 YHADMKEDEARDLALRAVRSAM 176
Cdd:cd03753   178 YHKDMTLEEAEKLALSILKQVM 199
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-195 1.13e-16

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: 75.44  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  10 KGTTTVGLIFDNGVVLATEMRATmgNMIASKRA-KKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVG 88
Cdd:cd03750    26 SGAPSVGIKAANGVVLATEKKVP--SPLIDESSvHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  89 A----ASTLLSNYLNQNRYYPYYVQLLVGGFDNEGPSIYSVDAMGG-----ATkeeeivATGSGSPFAYGVLEDQYHADM 159
Cdd:cd03750   104 QlvreIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSyftwkAT------AIGKNYSNAKTFLEKRYNEDL 177

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1055286705 160 KEDEARDLALRAVRSAMRRDsASGEDIMLVVITKDK 195
Cdd:cd03750   178 ELEDAIHTAILTLKEGFEGQ-MTEKNIEIGICGETK 212
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-171 3.80e-15

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 70.86  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  10 KGTTTVGLIFDNGVVLATEMRATMgNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMrrgkTMSVGA 89
Cdd:cd03755    26 KGTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRL----TVEDPV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  90 ASTLLSNYLN--QNRYY------PYYVQLLVGGFDNEG-PSIYSVDAMGGATkEEEIVATGSGSPFAYGVLEDQYHADMK 160
Cdd:cd03755   101 TVEYITRYIAglQQRYTqsggvrPFGISTLIVGFDPDGtPRLYQTDPSGTYS-AWKANAIGRNSKTVREFLEKNYKEEMT 179

                         170
                  ....*....|.
gi 1055286705 161 EDEARDLALRA 171
Cdd:cd03755   180 RDDTIKLAIKA 190
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-180 4.14e-14

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 68.09  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   7 EIMK-GTTTVGLIFDNGVVLATEMRATmgNMIASKRaKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTM 85
Cdd:cd03749    22 EAVKqGSATVGLKSKTHAVLVALKRAT--SELSSYQ-KKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  86 SVGAASTLLSNYLNQN-RYY---PYYVQLLVGGFDNEGPSIYSVDAmGGATKEEEIVATGSGSPFAYGVLEDQYH--ADM 159
Cdd:cd03749    99 PVSRLVSKVAEKAQINtQRYgrrPYGVGLLIAGYDESGPHLFQTCP-SGNYFEYKATSIGARSQSARTYLERHFEefEDC 177

                         170       180
                  ....*....|....*....|.
gi 1055286705 160 KEDEARDLALRAVRSAMRRDS 180
Cdd:cd03749   178 SLEELIKHALRALRETLPGEQ 198
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-164 1.40e-11

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 61.14  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  13 TTVGLIFDNGVVLATEmratmgNMIASK-----RAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSV 87
Cdd:cd03751    32 TAIGIRCKDGVVLAVE------KLVTSKlyepgSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  88 GAASTLLSNYLNQNRYY----PYYVQLLVGGFDNEGPSIYSVDAMGGATKEEEIvATGSGSPFAYGVLEDQYHADMKEDE 163
Cdd:cd03751   106 KVLADRVAMYMHAYTLYssvrPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGC-AIGKGKQAAKTELEKLKFSELTCRE 184


                  .
gi 1055286705 164 A 164
Cdd:cd03751   185 A 185
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-197 5.71e-09

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 54.47  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705   8 IMKGTTTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSV 87
Cdd:PTZ00246   28 INNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  88 gaaSTLLSNYLNQNRYY-------PYYVQLLVGGFD-NEGPSIYSVDAMGG-----ATkeeeivATGSGSPFAYGVLEDQ 154
Cdd:PTZ00246  108 ---EQLVVQICDLKQSYtqfgglrPFGVSFLFAGYDeNLGYQLYHTDPSGNysgwkAT------AIGQNNQTAQSILKQE 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1055286705 155 YHADMKEDEARDLALRAVRSAMRRDSASGEDIMLVVITKDKYE 197
Cdd:PTZ00246  179 WKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGETD 221
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-191 5.00e-08

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: 51.19  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  13 TTVGLIFDNGVVLATEMRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVgaaST 92
Cdd:cd03752    31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPV---EQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  93 LLSNYLNQNRYY-------PYYVQLLVGGFD-NEGPSIYSVDAMG--GATKEEEIvatGSGSPFAYGVLEDQYHADMKED 162
Cdd:cd03752   108 LVQRLCDIKQGYtqygglrPFGVSFLYAGWDkHYGFQLYQSDPSGnySGWKATAI---GNNNQAAQSLLKQDYKDDMTLE 184

                         170       180
                  ....*....|....*....|....*....
gi 1055286705 163 EARDLALRAVRSAMRRDSASGEDIMLVVI 191
Cdd:cd03752   185 EALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 11-179 1.09e-06

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


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 47.61  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  11 GTTTVGLIFDNGVVLATEmRATMGNMIASKRAKKIYQITPRIGMTTAGGVGDAQQLVRIMQVECNLFEMRRGKTMSVGAA 90
Cdd:cd03754    29 GLTSVAVRGKDCAVVVTQ-KKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPVDVL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055286705  91 STLLSNyLNQ---NRYY--PYYVQLLVGGFDNE-GPSIYSVDAMGGAT---------KEEEivatgsgspfAYGVLEDQY 155
Cdd:cd03754   108 AKRIAD-INQvytQHAYmrPLGVSMILIGIDEElGPQLYKCDPAGYFAgykataagvKEQE----------ATNFLEKKL 176

                         170       180
                  ....*....|....*....|....*...
gi 1055286705 156 ----HADMKEDEARDLALRAVRSAMRRD 179
Cdd:cd03754   177 kkkpDLIESYEETVELAISCLQTVLSTD 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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