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Conserved domains on  [gi|118376326|ref|XP_001021345|]
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proteasome subunit beta type protein [Tetrahymena thermophila SB210]

Protein Classification

proteasome subunit beta type-3( domain architecture ID 10132915)

proteasome subunit beta type-3 is a non-catalytic component of the 20S proteasome which degrades ubiquitin-tagged proteins in both the cytosol and nucleus

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-205 3.34e-114

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: 323.81  E-value: 3.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   7 YNGGSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVN 86
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  87 TFVNLISATLYEKRWGPYFVSPIVAGLEYDEvkgvIPITATYDSIGCTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDE 166
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDG----KPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 118376326 167 LEDIVAQSLSAGCDRDILSGWGGVVYTLTKDNLSVKVLK 205
Cdd:cd03759  157 LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-205 3.34e-114

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: 323.81  E-value: 3.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   7 YNGGSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVN 86
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  87 TFVNLISATLYEKRWGPYFVSPIVAGLEYDEvkgvIPITATYDSIGCTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDE 166
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDG----KPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 118376326 167 LEDIVAQSLSAGCDRDILSGWGGVVYTLTKDNLSVKVLK 205
Cdd:cd03759  157 LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-194 3.02e-43

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: 143.48  E-value: 3.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326    7 YNGGSMLAMKGEQCVAIGADRRLGAQFQTVATN-FQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKV 85
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   86 ---NTFVNLISATLYEKRWGPYFVSPIVAGleYDEVKGviPITATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGL 162
Cdd:pfam00227  82 elaARIADLLQAYTQYSGRRPFGVSLLIAG--YDEDGG--PHLYQIDPSG-SYIEYKATAIGSGSQYAYGVLEKLYRPDL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 118376326  163 KPDELEDIVAQSLSAGCDRDILSGWGGVVYTL 194
Cdd:pfam00227 157 TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 13-197 2.61e-23

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 92.90  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  13 LAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFVNLI 92
Cdd:COG0638   39 VGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  93 SATLYE---KRWGPYFVSPIVAGleYDEVKGVIpitATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDELED 169
Cdd:COG0638  119 SDLLQGytqYGVRPFGVALLIGG--VDDGGPRL---FSTDPSG-GLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                        170       180
                 ....*....|....*....|....*...
gi 118376326 170 IVAQSLSAGCDRDILSGWGGVVYTLTKD 197
Cdd:COG0638  193 LALRALYSAAERDSASGDGIDVAVITED 220
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-205 3.34e-114

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: 323.81  E-value: 3.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   7 YNGGSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVN 86
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  87 TFVNLISATLYEKRWGPYFVSPIVAGLEYDEvkgvIPITATYDSIGCTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDE 166
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDG----KPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 118376326 167 LEDIVAQSLSAGCDRDILSGWGGVVYTLTKDNLSVKVLK 205
Cdd:cd03759  157 LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-197 5.42e-64

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: 196.13  E-value: 5.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  10 GSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFV 89
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  90 NLISATLYEKRWGPYFVSPIVAGleYDEVKGviPITATYDSIGCTsIEGEFQVGGTGADGLIGSCESFWRKGLKPDELED 169
Cdd:cd01912   81 NLLSNILYSYRGFPYYVSLIVGG--VDKGGG--PFLYYVDPLGSL-IEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVE 155

                        170       180
                 ....*....|....*....|....*...
gi 118376326 170 IVAQSLSAGCDRDILSGWGGVVYTLTKD 197
Cdd:cd01912  156 LVKKAIDSAIERDLSSGGGVDVAVITKD 183
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 10-194 4.47e-46

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: 150.34  E-value: 4.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  10 GSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFV 89
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  90 NLISATLYEKRW--GPYFVSPIVAGleYDEVKGviPITATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDEL 167
Cdd:cd01906   81 KLLANLLYEYTQslRPLGVSLLVAG--VDEEGG--PQLYSVDPSG-SYIEYKATAIGSGSQYALGILEKLYKPDMTLEEA 155

                        170       180
                 ....*....|....*....|....*..
gi 118376326 168 EDIVAQSLSAGCDRDILSGWGGVVYTL 194
Cdd:cd01906  156 IELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-194 3.02e-43

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: 143.48  E-value: 3.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326    7 YNGGSMLAMKGEQCVAIGADRRLGAQFQTVATN-FQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKV 85
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   86 ---NTFVNLISATLYEKRWGPYFVSPIVAGleYDEVKGviPITATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGL 162
Cdd:pfam00227  82 elaARIADLLQAYTQYSGRRPFGVSLLIAG--YDEDGG--PHLYQIDPSG-SYIEYKATAIGSGSQYAYGVLEKLYRPDL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 118376326  163 KPDELEDIVAQSLSAGCDRDILSGWGGVVYTL 194
Cdd:pfam00227 157 TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-208 4.75e-32

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: 115.43  E-value: 4.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   3 DPFSYNGGSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKD 82
Cdd:cd03757    2 SPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  83 MKVNTFVNLISATLYEKRWGPYFVSPIVAGLEyDEVKGVIpitATYDSIGCTSIEGeFQVGGTGA-------DGLIGS-- 153
Cdd:cd03757   82 MSTEAIAQLLSTILYSRRFFPYYVFNILAGID-EEGKGVV---YSYDPVGSYERET-YSAGGSASsliqpllDNQVGRkn 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118376326 154 CESFWRKGLKPDELEDIVAQSLSAGCDRDILSGWGGVVYTLTKDNLSVKVLKTKQ 208
Cdd:cd03757  157 QNNVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRK 211
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 10-177 2.20e-30

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: 109.79  E-value: 2.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  10 GSMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFV 89
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  90 NLISATLYEKRWG-PYFVSPIVAGleYDEVKGVIpitATYDSIGCTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDELE 168
Cdd:cd01901   81 KELAKLLQVYTQGrPFGVNLIVAG--VDEGGGNL---YYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAV 155


                 ....*....
gi 118376326 169 DIVAQSLSA 177
Cdd:cd01901  156 ELALKALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-197 2.33e-26

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: 100.02  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  21 VAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFVNLISATLYEKR 100
Cdd:cd03764   12 VVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326 101 WGPYFVSPIVAGleYDEVKGVIpitATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDELEDIVAQSLSAGCD 180
Cdd:cd03764   92 YFPYIVQLLIGG--VDEEGPHL---YSLDPLG-SIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAIKSAIE 165

                        170
                 ....*....|....*..
gi 118376326 181 RDILSGWGGVVYTLTKD 197
Cdd:cd03764  166 RDSASGDGIDVVVITKD 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 13-197 2.61e-23

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 92.90  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  13 LAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFVNLI 92
Cdd:COG0638   39 VGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  93 SATLYE---KRWGPYFVSPIVAGleYDEVKGVIpitATYDSIGcTSIEGEFQVGGTGADGLIGSCESFWRKGLKPDELED 169
Cdd:COG0638  119 SDLLQGytqYGVRPFGVALLIGG--VDDGGPRL---FSTDPSG-GLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                        170       180
                 ....*....|....*....|....*...
gi 118376326 170 IVAQSLSAGCDRDILSGWGGVVYTLTKD 197
Cdd:COG0638  193 LALRALYSAAERDSASGDGIDVAVITED 220
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-198 5.72e-17

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: 75.34  E-value: 5.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   7 YNGGsmlamkgeqcVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVN 86
Cdd:cd03762    8 YDGG----------VVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  87 TFVNLISATLYEKRWGPYfVSPIVAGleYDEVKG--VIPITatydsIGCTSIEGEFQVGGTGADGLIGSCESFWRKGLKP 164
Cdd:cd03762   78 TAASLFKNLCYNYKEMLS-AGIIVAG--WDEQNGgqVYSIP-----LGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTL 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 118376326 165 DELEDIVAQSLSAGCDRDILSgwGGVVYT--LTKDN 198
Cdd:cd03762  150 EECIKFVKNALSLAMSRDGSS--GGVIRLviITKDG 183
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-120 5.02e-10

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: 56.44  E-value: 5.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  11 SMLAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFVN 90
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 118376326  91 LISATLYE--KRWGPYFVSPIVAGleYDEVKG 120
Cdd:cd03758   83 FTRRELAEslRSRTPYQVNLLLAG--YDKVEG 112
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 15-197 5.11e-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: 51.04  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  15 MKGEQCVAIGADRRlgaqfqtvAT--------NFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVN 86
Cdd:cd03763    6 VVFKDGVVLGADTR--------ATegpivadkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  87 TFVNLISATLYekRWGPYF-VSPIVAGLEYdevKGviPITATYDSIGCTSiEGEFQVGGTGADGLIGSCESFWRKGLKPD 165
Cdd:cd03763   78 TALTMLKQHLF--RYQGHIgAALVLGGVDY---TG--PHLYSIYPHGSTD-KLPFVTMGSGSLAAMSVLEDRYKPDMTEE 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 118376326 166 ELEDIVAQSLSAGCDRDILSGwGGV-VYTLTKD 197
Cdd:cd03763  150 EAKKLVCEAIEAGIFNDLGSG-SNVdLCVITKD 181
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 9-114 9.14e-08

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: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   9 GGSMLAMKGEQCVAIGADRRLG----AQFQtvatNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKD-M 83
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLGSygslARFK----NVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHsL 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 118376326  84 KVNTFVNLISATLYEKR--WGPYFVSPIVAGLE 114
Cdd:cd03760   78 SPKEIHSYLTRVLYNRRskMNPLWNTLVVGGVD 110
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-120 1.00e-04

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: 41.66  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326   8 NGGSMLAMKGEQCVAIGADRRLGAQFQTVATNfQKVFRIQDNILLGLTGLATDVQTfhrLIQYK----VNlYRLRENKDM 83
Cdd:cd01911   26 NGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARV---LVNRArveaQN-YRYTYGEPI 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 118376326  84 KVNTFVNLIS--ATLYEKRWG--PYFVSPIVAGleYDEVKG 120
Cdd:cd01911  101 PVEVLVKRIAdlAQVYTQYGGvrPFGVSLLIAG--YDEEGG 139
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-198 2.33e-04

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: 40.31  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  13 LAMKGEQCVAIGADRRLGAQFQTVATNFQKVFRIQDNILLGLTGLATDVQTFHRLIQYKVNLYRLRENKDMKVNTFVNLI 92
Cdd:cd03761    4 LAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118376326  93 SATLYEKRWGPYFVSPIVAGleYDEvKGviPITATYDSIGcTSIEGE-FQVgGTGADGLIGSCESFWRKGLKPDELEDIV 171
Cdd:cd03761   84 SNMLYQYKGMGLSMGTMICG--WDK-TG--PGLYYVDSDG-TRLKGDlFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLA 156

                        170       180
                 ....*....|....*....|....*...
gi 118376326 172 AQSLSAGCDRDILSGwGGV-VYTLTKDN 198
Cdd:cd03761  157 RRAIYHATHRDAYSG-GNVnLYHVREDG 183
 
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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