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Conserved domains on  [gi|332264007|ref|XP_003281040|]
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proteasome subunit beta type-1 isoform X1 [Nomascus leucogenys]

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 ...
 30-241 8.70e-147

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: 408.19  E-value: 8.70e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  30 FSPYVFNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 109
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 110 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 189
Cdd:cd03757   81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332264007 190 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 241
Cdd:cd03757  161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 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 ...
 30-241 8.70e-147

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: 408.19  E-value: 8.70e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  30 FSPYVFNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 109
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 110 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 189
Cdd:cd03757   81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332264007 190 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 241
Cdd:cd03757  161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 34-226 1.59e-49

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: 160.43  E-value: 1.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007   34 VFNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDS-PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMT 112
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  113 ---TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgFKNMqnv 189
Cdd:pfam00227  81 velAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL--- 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 332264007  190 ehvplSLDRAMRLVKDVFISAAERDVYTGDALRICIV 226
Cdd:pfam00227 157 -----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-235 1.11e-29

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 110.62  E-value: 1.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  37 GGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAI 116
Cdd:COG0638   35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 117 AAMLSTILYS---RRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP 193
Cdd:COG0638  115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEK----------EYRE 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332264007 194 -LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 235
Cdd:COG0638  184 dLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 24-230 1.53e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 56.54  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  24 GPLQLRFSpyvfNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMY 103
Cdd:PTZ00488  30 ANKAIEFA----HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 104 KHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGaVYSFDPVGSYQRDSFKAGGSASAMLQPLLDnqVGF 183
Cdd:PTZ00488 106 ELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLD--AGF 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332264007 184 KnmqnvehVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 230
Cdd:PTZ00488 183 K-------WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-241 8.70e-147

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: 408.19  E-value: 8.70e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  30 FSPYVFNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 109
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 110 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 189
Cdd:cd03757   81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332264007 190 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 241
Cdd:cd03757  161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-235 2.24e-75

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: 226.56  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  38 GTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 117
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 118 AMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLSLD 197
Cdd:cd01912   81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD---------MTLE 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332264007 198 RAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 235
Cdd:cd01912  152 EAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 38-226 2.06e-53

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: 170.37  E-value: 2.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  38 GTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 117
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 118 AMLSTILYSRRF--FPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLS 195
Cdd:cd01906   81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD---------MT 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 332264007 196 LDRAMRLVKDVFISAAERDVYTGDALRICIV 226
Cdd:cd01906  152 LEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 34-226 1.59e-49

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: 160.43  E-value: 1.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007   34 VFNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDS-PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMT 112
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  113 ---TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgFKNMqnv 189
Cdd:pfam00227  81 velAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL--- 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 332264007  190 ehvplSLDRAMRLVKDVFISAAERDVYTGDALRICIV 226
Cdd:pfam00227 157 -----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-234 9.23e-41

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: 138.15  E-value: 9.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  39 TVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 118
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 119 MLSTILYSRRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDnqVGFKNmqnvehvPLSLDR 198
Cdd:cd03764   82 LLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE--DEYKE-------DMTVEE 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 332264007 199 AMRLVKDVFISAAERDVYTGDALRICIVTKEGIREE 234
Cdd:cd03764  152 AKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-231 2.64e-32

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 116.57  E-value: 2.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  35 FNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTG 114
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 115 AIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVG--SYQRDsFKAGGSASAMLQPLLDNQVGfKNMqnvehv 192
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcpSIPSD-FVVSGTASEQLYGMCESLWR-PDM------ 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332264007 193 plSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGI 231
Cdd:cd03759  153 --EPDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 38-209 7.34e-31

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: 111.72  E-value: 7.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  38 GTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 117
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 118 AMLSTILYSRRF-FPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDS-FKAGGSASAMLQPLLDNQVGFKnmqnvehvpLS 195
Cdd:cd01901   81 KELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPD---------MT 150

                        170
                 ....*....|....
gi 332264007 196 LDRAMRLVKDVFIS 209
Cdd:cd01901  151 LEEAVELALKALKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-235 1.11e-29

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 110.62  E-value: 1.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  37 GGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAI 116
Cdd:COG0638   35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 117 AAMLSTILYS---RRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP 193
Cdd:COG0638  115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEK----------EYRE 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 332264007 194 -LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 235
Cdd:COG0638  184 dLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-236 4.20e-23

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: 92.26  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  39 TVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 118
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 119 MLSTIL--YSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP-LS 195
Cdd:cd03758   83 FTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR----------YYKPdMT 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 332264007 196 LDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETV 236
Cdd:cd03758  153 VEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 37-232 5.62e-23

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: 92.25  E-value: 5.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  37 GGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIE-ARLKMYKHSNNKAMTTGA 115
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDqLVIDDECLDDGHSLSPKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 116 IAAMLSTILYSRR--FFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgfKNMQNvehvp 193
Cdd:cd03760   82 IHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAW--EKKPD----- 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 332264007 194 LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIR 232
Cdd:cd03760  155 LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-234 6.06e-16

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: 73.41  E-value: 6.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  39 TVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 118
Cdd:cd03762    2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 119 MLSTILYSRRFFpYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQvgFK-NMqnvehvplSLD 197
Cdd:cd03762   82 LFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDAN--YKpGM--------TLE 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 332264007 198 RAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREE 234
Cdd:cd03762  151 ECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERK 187
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 24-230 1.53e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 56.54  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  24 GPLQLRFSpyvfNGGTVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMY 103
Cdd:PTZ00488  30 ANKAIEFA----HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 104 KHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGaVYSFDPVGSYQRDSFKAGGSASAMLQPLLDnqVGF 183
Cdd:PTZ00488 106 ELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLD--AGF 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 332264007 184 KnmqnvehVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 230
Cdd:PTZ00488 183 K-------WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-165 2.10e-09

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: 55.53  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  30 FSP--------YVF----NGGTVLAIAGEDFAIVASD----TRLSEGFSVHtrdspKCYKLTDKTVIGCSGFHGDCLTLT 93
Cdd:cd01911    8 FSPegrlfqveYALeavkNGSTAVGIKGKDGVVLAVEkkvtSKLLDPSSVE-----KIFKIDDHIGCAVAGLTADARVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  94 KIieARLKM--YKHSNNKAMTTGAIAAMLSTIL------YSRRffPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRdsFKA 165
Cdd:cd01911   83 NR--ARVEAqnYRYTYGEPIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTYFG--YKA 156
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-230 4.23e-08

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: 51.43  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  39 TVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKtvIGC--SGFHGDCLTLTKIIEARLKMykHSNNKAMTTGAI 116
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPN--IYCcgAGTAADTEAVTNMISSNLEL--HRLNTGRKPRVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 117 AAMlsTILySRRFFPY--YV--YNIIGGLDEEGKgAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQvgFKNmqnvehv 192
Cdd:cd03763   78 TAL--TML-KQHLFRYqgHIgaALVLGGVDYTGP-HLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDR--YKP------- 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332264007 193 PLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 230
Cdd:cd03763  145 DMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-232 1.07e-06

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: 47.62  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  39 TVLAIAGEDFAIVASDTRLSEGFSVHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 118
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007 119 MLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYsFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLSLDR 198
Cdd:cd03761   82 LLSNMLYQYKGMGLSMGTMICGWDKTGPGLYY-VDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYD---------LSVEE 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 332264007 199 AMRLVKDVFISAAERDVYTGDALRICIVTKEGIR 232
Cdd:cd03761  152 AYDLARRAIYHATHRDAYSGGNVNLYHVREDGWR 185
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-158 9.04e-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: 39.14  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  30 FSP--------YVF----NGG-TVLAIAGEDFAIVASDTRLSEGFsVHTRDSPKCYKLTDKtvIGC--SGFHGDCLTLtk 94
Cdd:cd03754    9 FSPegrlyqveYAFkavkNAGlTSVAVRGKDCAVVVTQKKVPDKL-IDPSTVTHLFRITDE--IGCvmTGMIADSRSQ-- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332264007  95 IIEARLKM--YKHSNNKAMTTGAIAAMLSTI--LYSRRFF--PYYVYNIIGGLDEEGKGAVYSFDPVGSY 158
Cdd:cd03754   84 VQRARYEAaeFKYKYGYEMPVDVLAKRIADInqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYF 153
 
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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