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Conserved domains on  [gi|20130281|ref|NP_611776|]
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proteasome beta5 subunit-related 1 [Drosophila melanogaster]

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 ...
 72-259 5.12e-125

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: 355.01  E-value: 5.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAI 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 20130281 232 YHATSKDAYSGGIVRLYHIHSEGWRNIC 259
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 ...
 72-259 5.12e-125

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: 355.01  E-value: 5.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAI 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 20130281 232 YHATSKDAYSGGIVRLYHIHSEGWRNIC 259
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-272 7.23e-105

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 306.53  E-value: 7.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   39 NPYELMAPP-FERPAENlpkilshcgIRMDFDHGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLA 117
Cdd:PTZ00488  15 HPGDFLAEYtFDHGDAN---------KAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  118 GGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAARIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVF 197
Cdd:PTZ00488  86 GGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMF 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130281  198 SVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAIYHATSKDAYSGGIVRLYHIHSEGWRNICNTDCSDLHDSYCA 272
Cdd:PTZ00488 166 SCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAA 240
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-250 3.60e-57

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 182.77  E-value: 3.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281    69 DHGTTTLGFKYRGGVILCADSRATSGQYIGS-QTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTV 147
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSkDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   148 DTAARIICNIS--TEYKGMG-LVMGMMLAGFDDEG-PKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEA 223
Cdd:pfam00227  82 ELAARIADLLQayTQYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 20130281   224 YDLARRAIYHATSKDAYSGGIVRLYHI 250
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 70-256 6.52e-48

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 160.31  E-value: 6.52e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  70 HGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAK----ECRLHQLRYRKRM 145
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADA----RELVRlarvEAQLYELRYGEPI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 146 TVDTAARIICNI---STEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQE 222
Cdd:COG0638 110 SVEGLAKLLSDLlqgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....
gi 20130281 223 AYDLARRAIYHATSKDAYSGGIVRLYHIHSEGWR 256
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 71-254 9.93e-47

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: 155.83  E-value: 9.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281    71 GTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTA 150
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   151 ARIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRA 230
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 20130281   231 IYHATSKDAYSGGIVRLYHIHSEG 254
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 ...
 72-259 5.12e-125

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: 355.01  E-value: 5.12e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAI 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 20130281 232 YHATSKDAYSGGIVRLYHIHSEGWRNIC 259
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-272 7.23e-105

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 306.53  E-value: 7.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   39 NPYELMAPP-FERPAENlpkilshcgIRMDFDHGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLA 117
Cdd:PTZ00488  15 HPGDFLAEYtFDHGDAN---------KAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  118 GGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAARIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVF 197
Cdd:PTZ00488  86 GGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMF 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130281  198 SVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAIYHATSKDAYSGGIVRLYHIHSEGWRNICNTDCSDLHDSYCA 272
Cdd:PTZ00488 166 SCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAA 240
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 72-259 3.95e-74

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: 226.17  E-value: 3.95e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMGLVMGMMLAGFD-DEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRA 230
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*....
gi 20130281 231 IYHATSKDAYSGGIVRLYHIHSEGWRNIC 259
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 72-250 2.05e-58

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: 185.78  E-value: 2.05e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYK--GMGLVMGMMLAGFD-DEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLAR 228
Cdd:cd01906  81 KLLANLLYEYTqsLRPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 20130281 229 RAIYHATSKDAYSGGIVRLYHI 250
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-250 3.60e-57

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 182.77  E-value: 3.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281    69 DHGTTTLGFKYRGGVILCADSRATSGQYIGS-QTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTV 147
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSkDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   148 DTAARIICNIS--TEYKGMG-LVMGMMLAGFDDEG-PKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEA 223
Cdd:pfam00227  82 ELAARIADLLQayTQYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 20130281   224 YDLARRAIYHATSKDAYSGGIVRLYHI 250
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 70-256 6.52e-48

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 160.31  E-value: 6.52e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  70 HGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAK----ECRLHQLRYRKRM 145
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADA----RELVRlarvEAQLYELRYGEPI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 146 TVDTAARIICNI---STEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQE 222
Cdd:COG0638 110 SVEGLAKLLSDLlqgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....
gi 20130281 223 AYDLARRAIYHATSKDAYSGGIVRLYHIHSEGWR 256
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 71-254 9.93e-47

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: 155.83  E-value: 9.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281    71 GTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTA 150
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   151 ARIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRA 230
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 20130281   231 IYHATSKDAYSGGIVRLYHIHSEG 254
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-257 4.03e-45

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: 151.64  E-value: 4.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMGLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARRAI 231
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                       170       180
                ....*....|....*....|....*.
gi 20130281 232 YHATSKDAYSGGIVRLYHIHSEGWRN 257
Cdd:cd03764 161 KSAIERDSASGDGIDVVVITKDGYKE 186
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 72-233 5.81e-41

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: 140.22  E-value: 5.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAA 151
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 152 RIICNISTEYKGMG-LVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVF-SVGSGSPYALGVLDTGYRYDLSDQEAYDLARR 229
Cdd:cd01901  81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
gi 20130281 230 AIYH 233
Cdd:cd01901 161 ALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-254 4.93e-33

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: 120.41  E-value: 4.93e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADcvywDRVLAKECR----LHQLRYRKRMTV 147
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAAD----TQAIADYVRyyldMHSIELGEPPLV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 148 DTAARIICNISTEYKGMgLVMGMMLAGFDD-EGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDL 226
Cdd:cd03762  77 KTAASLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKF 155

                       170       180
                ....*....|....*....|....*...
gi 20130281 227 ARRAIYHATSKDAYSGGIVRLYHIHSEG 254
Cdd:cd03762 156 VKNALSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-258 1.19e-26

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: 103.43  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  72 TTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELND--YMLGtlAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDT 149
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPniYCCG--AGTAADTEAVTNMISSNLELHRLNTGRKPRVVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 150 AARIICNISTEYKGMgLVMGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAYDLARR 229
Cdd:cd03763  79 ALTMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCE 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 20130281 230 AIYHATSKDAYSGGIVRLYHIHSEG---WRNI 258
Cdd:cd03763 158 AIEAGIFNDLGSGSNVDLCVITKDGveyLRNY 189
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 70-266 6.22e-21

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: 89.00  E-value: 6.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281    70 HGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAAdcvywdrvLAKE-CRLHQLR---YRKR- 144
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG--------LAIElVRLFQVElehYEKIe 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   145 ---MTVDT-----AARIICNISTEYKGMGLVmgMMLAGFD--DEGPKLIYVDSEGMRSHGQVF-SVGSGSPYALGVLDTG 213
Cdd:TIGR03690  73 gvpLTLDGkanrlAAMVRGNLPAAMQGLAVV--PLLAGYDldAGAGRIFSYDVTGGRYEERGYhAVGSGSVFAKGALKKL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   214 YRYDLSDQEAYDLARRAIYHATSKDAYSGG--IVR-----LYHIHSEGWRNICNTDCSDL 266
Cdd:TIGR03690 151 YSPDLDEDDALRVAVEALYDAADDDSATGGpdLVRgiyptVVVITADGARRVPESELEEL 210
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-237 5.41e-20

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: 86.23  E-value: 5.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSgQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAKECRL----HQLRYRKRMT 146
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKRITS-KLVEPESIEKIYKIDDHVGAATSGLVADA----RVLIDRARVeaqiHRLTYGEPID 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 147 VDTAARIICNISTEYKGMGLV----MGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQE 222
Cdd:cd03756 103 VEVLVKKICDLKQQYTQHGGVrpfgVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEE 182

                       170
                ....*....|....*
gi 20130281 223 AYDLARRAIYHATSK 237
Cdd:cd03756 183 AIELALKALYAALEE 197
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
71-235 9.08e-19

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 83.73  E-value: 9.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   71 GTTTLGFKYRGGVILCADSRATSgQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVL---AK-ECRLHQLRYRKRMT 146
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLidrARvEAQINRLTYGEPIG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  147 VDTAARIICNISTEYKGMGLV----MGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQE 222
Cdd:PRK03996 111 VETLTKKICDHKQQYTQHGGVrpfgVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEE 190

                        170
                 ....*....|...
gi 20130281  223 AYDLARRAIYHAT 235
Cdd:PRK03996 191 AIELALKALAKAN 203
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 69-238 6.47e-18

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: 80.56  E-value: 6.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  69 DHGTTTLGFKYRGGVILCADSRATSgQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAKECRL----HQLRYRKR 144
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRARVeaqnYRYTYGEP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 145 MTVDTAARIICNIS---TEYKGM---GLvmGMMLAGFDDE-GPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYD 217
Cdd:cd01911 100 IPVEVLVKRIADLAqvyTQYGGVrpfGV--SLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKD 177

                       170       180
                ....*....|....*....|.
gi 20130281 218 LSDQEAYDLARRAIYHATSKD 238
Cdd:cd01911 178 LTLEEAIKLALKALKEVLEED 198
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-227 4.32e-15

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: 72.75  E-value: 4.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSGQYIGSqTMRKIVELNDYMLGTLAGGAADCvywdRVLAK----ECRLHQLRYRKRMT 146
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADA----RTLIDharvEAQNHRFTYNEPMT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 147 VDTAARIICNISTEY-------KGMGLVMG--MMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYD 217
Cdd:cd03753 102 VESVTQAVSDLALQFgegddgkKAMSRPFGvaLLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKD 181

                       170
                ....*....|
gi 20130281 218 LSDQEAYDLA 227
Cdd:cd03753 182 MTLEEAEKLA 191
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-231 6.11e-13

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: 66.45  E-value: 6.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  73 TTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTAAR 152
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 153 IICNISTEY--KGMGLVMGMMLAGFDD-EGPKLIYVDSEGmRSHGQVFSV-GSGSPYALGVLDTGYRYDLSDQEAYDLAR 228
Cdd:cd03758  83 FTRRELAESlrSRTPYQVNLLLAGYDKvEGPSLYYIDYLG-TLVKVPYAAhGYGAYFCLSILDRYYKPDMTVEEALELMK 161


                ...
gi 20130281 229 RAI 231
Cdd:cd03758 162 KCI 164
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 69-254 2.17e-12

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: 64.97  E-value: 2.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  69 DHGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVD 148
Cdd:cd03757   6 DNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 149 TAARIICNISTEYKGMGLVMGMMLAGFDDEGPKLIY----VDSEGMRSHGqvfSVGSGSPYALGVLD---------TGYR 215
Cdd:cd03757  86 AIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYsydpVGSYERETYS---AGGSASSLIQPLLDnqvgrknqnNVER 162

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20130281 216 YDLSDQEAYDLARRAIYHATSKDAYSGGIVRLYHIHSEG 254
Cdd:cd03757 163 TPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-231 8.49e-11

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: 60.45  E-value: 8.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSgQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAK----ECRLHQLRYRKRMT 146
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADA----RVLINrarlECQSHRLTVEDPVT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 147 VDTAARIICNISTEYKGMGLV----MGMMLAGFD-DEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQ 221
Cdd:cd03755 102 VEYITRYIAGLQQRYTQSGGVrpfgISTLIVGFDpDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRD 181

                       170
                ....*....|
gi 20130281 222 EAYDLARRAI 231
Cdd:cd03755 182 DTIKLAIKAL 191
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 70-227 6.78e-09

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: 55.05  E-value: 6.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  70 HGTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAKECRL----HQLRYRKRM 145
Cdd:cd03752  28 HAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDA----NILINYARLiaqrYLYSYQEPI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 146 TVDTAARIICNIS---TEYKGM---GLvmGMMLAGFDD-EGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDL 218
Cdd:cd03752 104 PVEQLVQRLCDIKqgyTQYGGLrpfGV--SFLYAGWDKhYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDM 181


                ....*....
gi 20130281 219 SDQEAYDLA 227
Cdd:cd03752 182 TLEEALALA 190
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-223 2.09e-08

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: 53.86  E-value: 2.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSgQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLA----KECRLHQLRYRKRMT 146
Cdd:cd03750  27 GAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDF----RVLVkkarKIAQQYYLVYGEPIP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 147 VDTAARIICNISTEYKGMGLV----MGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQE 222
Cdd:cd03750 102 VSQLVREIASVMQEYTQSGGVrpfgVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELED 181


                .
gi 20130281 223 A 223
Cdd:cd03750 182 A 182
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-203 1.93e-07

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: 50.75  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSGQyigSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAK----ECRLHQLRYRKRMT 146
Cdd:cd03749  27 GSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADA----RVLSRymrqECLNYRFVYDSPIP 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130281 147 VDTAARIICN---ISTEYKG---MGLvmGMMLAGFDDEGPKLIYVDSEGMRSHGQVFSVGSGS 203
Cdd:cd03749 100 VSRLVSKVAEkaqINTQRYGrrpYGV--GLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 71-245 2.53e-07

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: 50.26  E-value: 2.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAK-----ECRLHQLRYRKRM 145
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQlviddECLDDGHSLSPKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 146 TVDTAARIICNISTEYKgmGLVMGMMLAGFDDEG-PKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRY--DLSDQE 222
Cdd:cd03760  82 IHSYLTRVLYNRRSKMN--PLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEEE 159

                       170       180
                ....*....|....*....|....*...
gi 20130281 223 AYDLARRAI----YH-ATSKDAYSGGIV 245
Cdd:cd03760 160 ARALIEECMkvlyYRdARSINKYQIAVV 187
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 74-235 8.22e-07

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 49.47  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281   74 TLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAKECRLHQLRYR----KRMTVDT 149
Cdd:PTZ00246  34 TVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADA----NILINQCRLYAQRYRytygEPQPVEQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  150 AARIICNISTEYKGMGLV----MGMMLAGFD-DEGPKLIYVDSEGMRSHGQVFSVGSGSPYALGVLDTGYRYDLSDQEAY 224
Cdd:PTZ00246 110 LVVQICDLKQSYTQFGGLrpfgVSFLFAGYDeNLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGL 189

                        170
                 ....*....|.
gi 20130281  225 DLARRAIYHAT 235
Cdd:PTZ00246 190 LLAAKVLTKSM 200
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 71-242 1.60e-06

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: 48.01  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILCADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCVYWDRVLAKECRLHQLRYRKRMTVDTA 150
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281 151 ARIICNISTEYKGMGLVMGMMLAGFDDEG-PKLIYVDSEGMRSHGQVFSV-GSGSPYALGVLDTGYRYDLSDQEAYDLAR 228
Cdd:cd03759  83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPSDFVVsGTASEQLYGMCESLWRPDMEPDELFETIS 162

                       170
                ....*....|....
gi 20130281 229 RAIYHATSKDAYSG 242
Cdd:cd03759 163 QALLSAVDRDALSG 176
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-189 9.74e-04

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: 39.91  E-value: 9.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130281  71 GTTTLGFKYRGGVILcADSRATSGQYIGSQTMRKIVELNDYMLGTLAGGAADCvywdRVLAKECRLHQLRYRKR----MT 146
Cdd:cd03754  29 GLTSVAVRGKDCAVV-VTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS----RSQVQRARYEAAEFKYKygyeMP 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 20130281 147 VDTAARIICNIS---TEYKGMGLvMG--MMLAGFDDE-GPKLIYVDSEG 189
Cdd:cd03754 104 VDVLAKRIADINqvyTQHAYMRP-LGvsMILIGIDEElGPQLYKCDPAG 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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