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Conserved domains on  [gi|753535231|pdb|4QW4|W]
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Chain W, Proteasome subunit beta type-3

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 ...
 8-201 2.05e-115

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: 326.51  E-value: 2.05e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        8 NGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGdRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       87 FTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFET 166
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
4QW4_W      167 ISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLK 201
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 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 ...
 8-201 2.05e-115

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: 326.51  E-value: 2.05e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        8 NGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGdRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       87 FTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFET 166
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
4QW4_W      167 ISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLK 201
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-190 2.46e-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: 158.88  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W          8 NGGIVVAMTGKDCVAIACDLRLGSQSLGVSNK-FEKIFH-YGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPE 85
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKiDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W         86 ---TFTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKdFIVSGTASDQLFGMCESLYEPNLEPED 162
Cdd:pfam00227  83 laaRIADLLQAYTQYSGRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
4QW4_W        163 LFETISQALLNAADRDALSGWGAVVYII 190
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-197 7.21e-20

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 83.66  E-value: 7.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        9 GGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIF--HyGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFkiD-DHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       87 FTQLVSSSLYE---RRFGPYFVGPVVAGINSKSGKPF---IAGfdliGCIDEakDFIVSGTASDQLFGMCESLYEPNLEP 160
Cdd:COG0638 114 LAKLLSDLLQGytqYGVRPFGVALLIGGVDDGGPRLFstdPSG----GLYEE--KAVAIGSGSPFARGVLEKEYREDLSL 187

                       170       180       190
                ....*....|....*....|....*....|....*..
4QW4_W      161 EDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVK 197
Cdd:COG0638 188 DEAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 21-197 5.48e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 39.59  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        21 VAIACDLRLGSQSLGVSNKFEKIFHYGHVFLG-ITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERR 99
Cdd:PTZ00488  51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGtMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       100 FGPYFVGPVVAGINSKSGKPFIAGFDliGCIDEAKDFIVsGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDA 179
Cdd:PTZ00488 131 GMGLSMGTMICGWDKKGPGLFYVDND--GTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDA 207

                        170
                 ....*....|....*...
4QW4_W       180 LSGWGAVVYIIKKDEVVK 197
Cdd:PTZ00488 208 YSGGAINLYHMQKDGWKK 225
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-201 2.05e-115

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: 326.51  E-value: 2.05e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        8 NGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGdRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       87 FTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFET 166
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
4QW4_W      167 ISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLK 201
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-198 7.17e-63

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: 193.04  E-value: 7.17e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQL 90
Cdd:cd01912   3 IVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISdNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       91 VSSSLYERRFGPYFVGPVVAGINsKSGKPFIAGFDLIGCIDEAkDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQA 170
Cdd:cd01912  83 LSNILYSYRGFPYYVSLIVGGVD-KGGGPFLYYVDPLGSLIEA-PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
4QW4_W      171 LLNAADRDALSGWGAVVYIIKKDEVVKR 198
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-190 2.46e-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: 158.88  E-value: 2.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W          8 NGGIVVAMTGKDCVAIACDLRLGSQSLGVSNK-FEKIFH-YGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPE 85
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKiDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W         86 ---TFTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKdFIVSGTASDQLFGMCESLYEPNLEPED 162
Cdd:pfam00227  83 laaRIADLLQAYTQYSGRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
4QW4_W        163 LFETISQALLNAADRDALSGWGAVVYII 190
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 12-190 3.61e-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: 3.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQL 90
Cdd:cd01906   3 IVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDdHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       91 VSSSLYERRF--GPYFVGPVVAGINsKSGKPFIAGFDLIGCIDEAKdFIVSGTASDQLFGMCESLYEPNLEPEDLFETIS 168
Cdd:cd01906  83 LANLLYEYTQslRPLGVSLLVAGVD-EEGGPQLYSVDPSGSYIEYK-ATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
4QW4_W      169 QALLNAADRDALSGWGAVVYII 190
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 12-172 2.99e-32

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: 114.41  E-value: 2.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFH-YGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQL 90
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKnEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       91 VSSSLYERRFG-PYFVGPVVAGINSksGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQ 169
Cdd:cd01901  83 LAKLLQVYTQGrPFGVNLIVAGVDE--GGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ...
4QW4_W      170 ALL 172
Cdd:cd01901 161 ALK 163
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-205 9.18e-30

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: 109.27  E-value: 9.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        3 DPSSINGGIVVAMTGKDCVAIACDLRLgSQSLGVSNKFE-KIFHYGH-VFLGITGLATDVTTLNEMFRYKTNLYKLKEER 80
Cdd:cd03757   2 SPYTDNGGTVLAIAGNDFAVIAGDTRL-SEGYSILSRDSpKIFKLTDkCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       81 AIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAKdFIVSGTAS--------DQLFGMCES 152
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEE-GKGVVYSYDPVGSYERET-YSAGGSASsliqplldNQVGRKNQN 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
4QW4_W      153 LYEPN-LEPEDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD 205
Cdd:cd03757 159 NVERTpLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-197 7.21e-20

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 83.66  E-value: 7.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        9 GGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIF--HyGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFkiD-DHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       87 FTQLVSSSLYE---RRFGPYFVGPVVAGINSKSGKPF---IAGfdliGCIDEakDFIVSGTASDQLFGMCESLYEPNLEP 160
Cdd:COG0638 114 LAKLLSDLLQGytqYGVRPFGVALLIGGVDDGGPRLFstdPSG----GLYEE--KAVAIGSGSPFARGVLEKEYREDLSL 187

                       170       180       190
                ....*....|....*....|....*....|....*..
4QW4_W      161 EDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVK 197
Cdd:COG0638 188 DEAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 10-194 1.74e-18

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: 79.22  E-value: 1.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       10 GIVVamtgKDCVAIACDLRLgsqSLG--VSNK-FEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPE 85
Cdd:cd03764   5 GIVC----KDGVVLAADKRA---SMGnfIASKnVKKIFQIDdKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       86 TFTQLVSSSLYERRFGPYFVGPVVAGINSKsgKPFIAGFDLIGCIDEaKDFIVSGTASDQLFGMCESLYEPNLEPEDLFE 165
Cdd:cd03764  78 ALATLLSNILNSSKYFPYIVQLLIGGVDEE--GPHLYSLDPLGSIIE-DKYTATGSGSPYAYGVLEDEYKEDMTVEEAKK 154

                       170       180
                ....*....|....*....|....*....
4QW4_W      166 TISQALLNAADRDALSGWGAVVYIIKKDE 194
Cdd:cd03764 155 LAIRAIKSAIERDSASGDGIDVVVITKDG 183
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 9-140 8.30e-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: 8.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        9 GGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATD----VTTLNEMFRyKTNLYKLKEEraIE 83
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGdNTLLGASGDYADfqylKRLLDQLVI-DDECLDDGHS--LS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
4QW4_W       84 PETFTQLVSSSLYERR--FGPYFVGPVVAGINSKsGKPFIAGFDLIGCIDEAkDFIVSG 140
Cdd:cd03760  79 PKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNE-GEPFLGYVDLLGTAYED-PHVATG 135
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-199 9.28e-07

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: 47.22  E-value: 9.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFH-YGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQL 90
Cdd:cd03762   3 IIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQlHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       91 VSSSLYERRFGPYfVGPVVAGINSKSGkPFIAGFDLIGCIDEaKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQA 170
Cdd:cd03762  83 FKNLCYNYKEMLS-AGIIVAGWDEQNG-GQVYSIPLGGMLIR-QPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNA 159

                       170       180       190
                ....*....|....*....|....*....|.
4QW4_W      171 LLNAADRDALSgwGAVVY--IIKKDEVVKRY 199
Cdd:cd03762 160 LSLAMSRDGSS--GGVIRlvIITKDGVERKF 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-196 1.49e-05

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: 43.72  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLgVSNK-FEKIfHY--GHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFT 88
Cdd:cd03763   3 IVGVVFKDGVVLGADTRATEGPI-VADKnCEKI-HYiaPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       89 QLVSSSLYerRFGPYfVGP--VVAGINSKSgkPFIAGFDLIGCIDEAKdFIVSGTASDQLFGMCESLYEPNLEPEDLFET 166
Cdd:cd03763  81 TMLKQHLF--RYQGH-IGAalVLGGVDYTG--PHLYSIYPHGSTDKLP-FVTMGSGSLAAMSVLEDRYKPDMTEEEAKKL 154

                       170       180       190
                ....*....|....*....|....*....|
4QW4_W      167 ISQALLNAADRDALSGWGAVVYIIKKDEVV 196
Cdd:cd03763 155 VCEAIEAGIFNDLGSGSNVDLCVITKDGVE 184
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-117 1.47e-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: 41.27  E-value: 1.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        8 NGGIVVAMTGKDCVAIACDLRLGSQsLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPET 86
Cdd:cd01911  26 NGSTAVGIKGKDGVVLAVEKKVTSK-LLDPSSVEKIFKIDdHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEV 104

                        90       100       110
                ....*....|....*....|....*....|....*..
4QW4_W       87 FTQLVSSSL------YERRfgPYFVGPVVAGINSKSG 117
Cdd:cd01911 105 LVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGG 139
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-200 5.03e-04

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: 39.49  E-value: 5.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       12 VVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYG-HVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQL 90
Cdd:cd03758   4 LIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSdHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAANF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       91 VSSSLYE--RRFGPYFVGPVVAGINSKSGkPFIAGFDLIGCIDEAkDFIVSGTASDQLFGMCESLYEPNLEPEDLFETIS 168
Cdd:cd03758  84 TRRELAEslRSRTPYQVNLLLAGYDKVEG-PSLYYIDYLGTLVKV-PYAAHGYGAYFCLSILDRYYKPDMTVEEALELMK 161

                       170       180       190
                ....*....|....*....|....*....|..
4QW4_W      169 QALLNAADRDALSGWGAVVYIIKKDEVVKRYL 200
Cdd:cd03758 162 KCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 21-197 5.48e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 39.59  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W        21 VAIACDLRLGSQSLGVSNKFEKIFHYGHVFLG-ITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERR 99
Cdd:PTZ00488  51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGtMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4QW4_W       100 FGPYFVGPVVAGINSKSGKPFIAGFDliGCIDEAKDFIVsGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDA 179
Cdd:PTZ00488 131 GMGLSMGTMICGWDKKGPGLFYVDND--GTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDA 207

                        170
                 ....*....|....*...
4QW4_W       180 LSGWGAVVYIIKKDEVVK 197
Cdd:PTZ00488 208 YSGGAINLYHMQKDGWKK 225
 
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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