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Conserved domains on  [gi|17380182|sp|O64464|]
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RecName: Full=Proteasome subunit beta type-1; AltName: Full=20S proteasome alpha subunit F; AltName: Full=20S proteasome subunit beta-6

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-221 2.37e-131

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: 368.12  E-value: 2.37e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   7 WVYENNGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKR 86
Cdd:cd03757   2 SPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  87 MSCPAMAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPSPLLlp 166
Cdd:cd03757  82 MSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN-- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17380182 167 arDAVTPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYIDLRKD 221
Cdd:cd03757 160 --VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-221 2.37e-131

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: 368.12  E-value: 2.37e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   7 WVYENNGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKR 86
Cdd:cd03757   2 SPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  87 MSCPAMAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPSPLLlp 166
Cdd:cd03757  82 MSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN-- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17380182 167 arDAVTPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYIDLRKD 221
Cdd:cd03757 160 --VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 11-206 8.97e-39

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: 132.31  E-value: 8.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182    11 NNGGTCVAIAGADYCVVAADTRLSVGYNILTRD-HSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMS- 88
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182    89 --CPAMAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSpsplllp 166
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP------- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 17380182   167 ardavtPLSETEAVDLVKDVFASATERDIYTGDKLEIVVI 206
Cdd:pfam00227 155 ------DLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 13-217 3.42e-25

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 98.29  E-value: 3.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  13 GGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAM 92
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  93 AQLLSNTLY---YKRFFPYYAFNVLGGLDSEGkGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKspsplllpaRD 169
Cdd:COG0638 115 AKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYR---------ED 184

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17380182 170 avtpLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYID 217
Cdd:COG0638 185 ----LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 12-213 2.98e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 55.38  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   12 NGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPA 91
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   92 MAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGcVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKspsplllpardav 171
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK------------- 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17380182  172 TPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKR 213
Cdd:PTZ00488 184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKK 225
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-221 2.37e-131

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: 368.12  E-value: 2.37e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   7 WVYENNGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKR 86
Cdd:cd03757   2 SPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  87 MSCPAMAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPSPLLlp 166
Cdd:cd03757  82 MSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN-- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17380182 167 arDAVTPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYIDLRKD 221
Cdd:cd03757 160 --VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 14-214 7.43e-70

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: 211.53  E-value: 7.43e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  14 GTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMA 93
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  94 QLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSpsplllpardavtP 173
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKP-------------D 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17380182 174 LSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKRE 214
Cdd:cd01912 148 MTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 14-206 7.97e-50

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: 160.35  E-value: 7.97e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  14 GTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMA 93
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  94 QLLSNTLYYKRF--FPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSpsplllpardav 171
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP------------ 148

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17380182 172 tPLSETEAVDLVKDVFASATERDIYTGDKLEIVVI 206
Cdd:cd01906 149 -DMTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 11-206 8.97e-39

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: 132.31  E-value: 8.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182    11 NNGGTCVAIAGADYCVVAADTRLSVGYNILTRD-HSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMS- 88
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182    89 --CPAMAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSpsplllp 166
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP------- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 17380182   167 ardavtPLSETEAVDLVKDVFASATERDIYTGDKLEIVVI 206
Cdd:pfam00227 155 ------DLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 15-214 1.37e-38

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: 131.99  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  15 TCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMAQ 94
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  95 LLSNTLYYKRFFPYYAFNVLGGLDSEGKGcVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKspsplllpaRDavtpL 174
Cdd:cd03764  82 LLSNILNSSKYFPYIVQLLIGGVDEEGPH-LYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYK---------ED----M 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17380182 175 SETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKRE 214
Cdd:cd03764 148 TVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-211 5.66e-28

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: 104.63  E-value: 5.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  12 NGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPA 91
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  92 MAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTG-YSAQGTGSALIMPVLDNqLKSPSplllparda 170
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYGMCES-LWRPD--------- 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17380182 171 vtpLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGT 211
Cdd:cd03759 152 ---MEPDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 14-189 3.76e-27

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: 101.70  E-value: 3.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  14 GTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMA 93
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  94 QLLSNTLY-YKRFFPYYAFNVLGGLDsEGKGCVFTYDAVGSY-ERTGYSAQGTGSALIMPVLDNQLKSpsplllpardav 171
Cdd:cd01901  81 KELAKLLQvYTQGRPFGVNLIVAGVD-EGGGNLYYIDPSGPViENPGAVATGSRSQRAKSLLEKLYKP------------ 147

                       170
                ....*....|....*...
gi 17380182 172 tPLSETEAVDLVKDVFAS 189
Cdd:cd01901 148 -DMTLEEAVELALKALKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 13-217 3.42e-25

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 98.29  E-value: 3.42e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  13 GGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAM 92
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  93 AQLLSNTLY---YKRFFPYYAFNVLGGLDSEGkGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKspsplllpaRD 169
Cdd:COG0638 115 AKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYR---------ED 184

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17380182 170 avtpLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYID 217
Cdd:COG0638 185 ----LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 15-216 1.09e-15

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 72.23  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  15 TCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGD-------IKalhKNLAarelLYQHQHNKRM 87
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDrlqfaeyIQ---KNIQ----LYKMRNGYEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  88 SCPAMAQLLSNTL--YYKRFFPYYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSpsplll 165
Cdd:cd03758  76 SPKAAANFTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKP------ 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17380182 166 pardavtPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKREYI 216
Cdd:cd03758 150 -------DMTVEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-212 1.02e-13

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: 66.82  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  13 GGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELL-YQHQHNKRMSCPA 91
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDdECLDDGHSLSPKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  92 MAQLLSNTLYYKR--FFPYYAFNVLGGLDSEGK---GCVftyDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPSplllp 166
Cdd:cd03760  82 IHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEpflGYV---DLLGTAYEDPHVATGFGAYLALPLLREAWEKKP----- 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17380182 167 ardavtPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTK 212
Cdd:cd03760 154 ------DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 15-215 1.52e-11

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: 61.06  E-value: 1.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  15 TCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALhKNLAARELLYQHQHNKRMSCPAMA- 93
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAV-TNMISSNLELHRLNTGRKPRVVTAl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  94 QLLSNTLyykrfFPYY----AFNVLGGLDSEGKGcVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPsplllpard 169
Cdd:cd03763  81 TMLKQHL-----FRYQghigAALVLGGVDYTGPH-LYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPD--------- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17380182 170 avtpLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTK--REY 215
Cdd:cd03763 146 ----MTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVEylRNY 189
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 26-215 1.21e-09

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: 55.69  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  26 VVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMAQLLSNTLY-YKR 104
Cdd:cd03762  13 VLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLFKNLCYnYKE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182 105 FFpyYAFNVLGGLDSEGKGCVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKSPsplllpardavtpLSETEAVDLVK 184
Cdd:cd03762  93 ML--SAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPG-------------MTLEECIKFVK 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 17380182 185 DVFASATERDIYTGDKLEIVVINKAGTKREY 215
Cdd:cd03762 158 NALSLAMSRDGSSGGVIRLVIITKDGVERKF 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 12-213 2.98e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 55.38  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   12 NGGTCVAIAGADYCVVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPA 91
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182   92 MAQLLSNTLYYKRFFPYYAFNVLGGLDSEGKGcVFTYDAVGSYERTGYSAQGTGSALIMPVLDNQLKspsplllpardav 171
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK------------- 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17380182  172 TPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAGTKR 213
Cdd:PTZ00488 184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKK 225
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 26-210 1.75e-07

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: 49.55  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  26 VVAADTRLSVGYNILTRDHSKICELADKCALASSGFQGDIKALHKNLAARELLYQHQHNKRMSCPAMAQLLSNTLY-YK- 103
Cdd:cd03761  13 IVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYqYKg 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182 104 -------------RFFP--YYafnvlggLDSEG---KGCVFtydAVGSyertgysaqgtGSALIMPVLDNQLKspsplll 165
Cdd:cd03761  93 mglsmgtmicgwdKTGPglYY-------VDSDGtrlKGDLF---SVGS-----------GSTYAYGVLDSGYR------- 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17380182 166 pardavTPLSETEAVDLVKDVFASATERDIYTGDKLEIVVINKAG 210
Cdd:cd03761 145 ------YDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 11-206 3.39e-07

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: 48.98  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  11 NNGGTCVAIAGADYCVVAADTRLSvgyNILTRDHS--KICELADKCALASSGFQGDIKALHKnlAARE--LLYQHQHNKR 86
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVEKKVT---SKLLDPSSveKIFKIDDHIGCAVAGLTADARVLVN--RARVeaQNYRYTYGEP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380182  87 MSCPAMAQLLSN-----TLYY-KRffPYYAFNVLGGLDSEGKGCVFTYDAVGSYerTGYSAQ--GTGSALIMPVLDNQLK 158
Cdd:cd01911 100 IPVEVLVKRIADlaqvyTQYGgVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTY--FGYKATaiGKGSQEAKTFLEKRYK 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17380182 159 SpsplllpardavtPLSETEAVDLVKDVFASATERDIyTGDKLEIVVI 206
Cdd:cd01911 176 K-------------DLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
 
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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