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Conserved domains on  [gi|62955575|ref|NP_001017801|]
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proteasome subunit beta type-4 [Danio rerio]

Protein Classification

proteasome subunit beta( domain architecture ID 10132923)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-198 2.80e-133

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: 372.29  E-value: 2.80e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLGDGHSYTPK 82
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  83 AIHSWLTRVMYNRRSKMNPLWNTVVIGGFYN-GESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIENKEEITKEEA 161
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 62955575 162 RELIERCLKVLYYRDARSYNRHEIAIVTADGVEIIGP 198
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-198 2.80e-133

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: 372.29  E-value: 2.80e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLGDGHSYTPK 82
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  83 AIHSWLTRVMYNRRSKMNPLWNTVVIGGFYN-GESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIENKEEITKEEA 161
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 62955575 162 RELIERCLKVLYYRDARSYNRHEIAIVTADGVEIIGP 198
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-188 8.27e-39

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 132.31  E-value: 8.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575     1 MVTGTSVLGVKFKGGVIIAADMLGSYGSLARFRN-ISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLgDGHSY 79
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLR-YGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575    80 TPK--AIHSWLTRVMYNRRSKMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREviENKEEIT 157
Cdd:pfam00227  80 PVElaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 62955575   158 KEEARELIERCLKVLYYRDARSYNRHEIAIV 188
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-196 4.08e-14

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 68.63  E-value: 4.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQ----YLKQIIEQ--MVIDEELlgdg 76
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARelvrLARVEAQLyeLRYGEPI---- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  77 hsyTPKAIHSWLTRVMY-NRRSKMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPTVATGFGAYLAqplmREVIEN--K 153
Cdd:COG0638 110 ---SVEGLAKLLSDLLQgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFA----RGVLEKeyR 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 62955575 154 EEITKEEARELIERCLKVLYYRDARSYNRHEIAIVTADGVEII 196
Cdd:COG0638 183 EDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-179 4.49e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.83  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575    4 GTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVnNSTILGA-SGDYADYQYLKQIIEQMVIDEELLgDGHSYTPK 82
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEI-NPTLLGTmAGGAADCSFWERELAMQCRLYELR-NGELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   83 AIHSWLTRVMYNRRSkMNPLWNTVVIGGFYNGESfLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIenKEEITKEEAR 162
Cdd:PTZ00488 117 AASKILANIVWNYKG-MGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGF--KWDLNDEEAQ 192

                        170
                 ....*....|....*..
gi 62955575  163 ELIERCLKVLYYRDARS 179
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYS 209
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-198 2.80e-133

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: 372.29  E-value: 2.80e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLGDGHSYTPK 82
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  83 AIHSWLTRVMYNRRSKMNPLWNTVVIGGFYN-GESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIENKEEITKEEA 161
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 62955575 162 RELIERCLKVLYYRDARSYNRHEIAIVTADGVEIIGP 198
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-196 2.17e-66

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: 202.67  E-value: 2.17e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLgDGHSYTPKAI 84
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELR-NGRELSVKAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  85 HSWLTRVMYNRRSkmNPLWNTVVIGGF-YNGESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIenKEEITKEEARE 163
Cdd:cd01912  80 ANLLSNILYSYRG--FPYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY--KPDMTLEEAVE 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 62955575 164 LIERCLKVLYYRDARSYNRHEIAIVTADGVEII 196
Cdd:cd01912 156 LVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 5-188 4.35e-50

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 160.74  E-value: 4.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLgDGHSYTPKAI 84
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLR-YGEPIPVEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  85 HSWLTRVMYNRRSKMNPLWNTVVIGGF-YNGESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIenKEEITKEEARE 163
Cdd:cd01906  80 AKLLANLLYEYTQSLRPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY--KPDMTLEEAIE 157

                       170       180
                ....*....|....*....|....*
gi 62955575 164 LIERCLKVLYYRDARSYNRHEIAIV 188
Cdd:cd01906 158 LALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-188 8.27e-39

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 132.31  E-value: 8.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575     1 MVTGTSVLGVKFKGGVIIAADMLGSYGSLARFRN-ISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLgDGHSY 79
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLR-YGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575    80 TPK--AIHSWLTRVMYNRRSKMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREviENKEEIT 157
Cdd:pfam00227  80 PVElaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 62955575   158 KEEARELIERCLKVLYYRDARSYNRHEIAIV 188
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-170 1.41e-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: 110.18  E-value: 1.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVIDEELLgDGHSYTPKAI 84
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLR-YGEPISVVAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  85 HSWLTRVMYNRRSkMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPT-VATGFGAYLAQPLMREVIenKEEITKEEARE 163
Cdd:cd01901  80 AKELAKLLQVYTQ-GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGaVATGSRSQRAKSLLEKLY--KPDMTLEEAVE 156


                ....*..
gi 62955575 164 LIERCLK 170
Cdd:cd01901 157 LALKALK 163
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-196 4.08e-14

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 68.63  E-value: 4.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQ----YLKQIIEQ--MVIDEELlgdg 76
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARelvrLARVEAQLyeLRYGEPI---- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  77 hsyTPKAIHSWLTRVMY-NRRSKMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPTVATGFGAYLAqplmREVIEN--K 153
Cdd:COG0638 110 ---SVEGLAKLLSDLLQgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFA----RGVLEKeyR 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 62955575 154 EEITKEEARELIERCLKVLYYRDARSYNRHEIAIVTADGVEII 196
Cdd:COG0638 183 EDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-196 1.35e-13

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


Pssm-ID: 239727  Cd Length: 193  Bit Score: 66.45  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   6 SVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYAD-YQYLKQIIEQMVIDEelLGDGHSYTPKAI 84
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDrLQFAEYIQKNIQLYK--MRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  85 HSWLTR-VMYNRRSKmNPLWNTVVIGGFYNGE-SFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREviENKEEITKEEAR 162
Cdd:cd03758  81 ANFTRReLAESLRSR-TPYQVNLLLAGYDKVEgPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR--YYKPDMTVEEAL 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 62955575 163 ELIERCLKVLYYRDARSYNRHEIAIVTADGVEII 196
Cdd:cd03758 158 ELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDL 191
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-195 1.38e-13

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: 66.51  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEqMVIDEELLGDGHSYTPKAI 84
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILK-AEARLYELRRGRPMSIKAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  85 HSWLTRVMYNrrSKMNPLWNTVVIGGFYNGESFLGYVDKLGVAYEAPTVATGFGAYLAQPLMREviENKEEITKEEAREL 164
Cdd:cd03764  80 ATLLSNILNS--SKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLED--EYKEDMTVEEAKKL 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 62955575 165 IERCLKVLYYRDARSYNRHEIAIVTADGVEI 195
Cdd:cd03764 156 AIRAIKSAIERDSASGDGIDVVVITKDGYKE 186
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-194 5.79e-13

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 64.97  E-value: 5.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   4 GTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQYLKQIIEQMVideELLGDGHSYTP-- 81
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARI---KMYKYSHNKEMst 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  82 KAIHSWLTRVMYNRRSkmNPLWNTVVIGGF-YNGESFLGYVDKLGvAYEAPT-VATGFGAYLAQPLMREVIENKEEITKE 159
Cdd:cd03757  85 EAIAQLLSTILYSRRF--FPYYVFNILAGIdEEGKGVVYSYDPVG-SYERETySAGGSASSLIQPLLDNQVGRKNQNNVE 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 62955575 160 EARELIERCLKVLyyRDARS--YNRH-------EIAIVTADGVE 194
Cdd:cd03757 162 RTPLSLEEAVSLV--KDAFTsaAERDiytgdslEIVIITKDGIE 203
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-193 7.92e-11

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: 58.79  E-value: 7.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   3 TGTSVLGVKFKGGVIIAADM-LGSYGSLARFrNISRLMKVNNSTILGASGDYADYQYLKQIIeQMVIDEELLGDGHSYTP 81
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLrLGVQQQTVST-DFQKVFRIGDRLYIGLAGLATDVQTLAQKL-RFRVNLYRLREEREIKP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  82 KAIHSWLTRVMYNRRskMNPLWNTVVIGGF-YNGESFLGYVDKLGvayeAPTVATGFG-AYLAQPLMREVIEN--KEEIT 157
Cdd:cd03759  80 KTFSSLISSLLYEKR--FGPYFVEPVVAGLdPDGKPFICTMDLIG----CPSIPSDFVvSGTASEQLYGMCESlwRPDME 153

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 62955575 158 KEEARELIERCLKVLYYRDARSYNRHEIAIVTADGV 193
Cdd:cd03759 154 PDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-179 4.49e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.83  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575    4 GTSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVnNSTILGA-SGDYADYQYLKQIIEQMVIDEELLgDGHSYTPK 82
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEI-NPTLLGTmAGGAADCSFWERELAMQCRLYELR-NGELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   83 AIHSWLTRVMYNRRSkMNPLWNTVVIGGFYNGESfLGYVDKLGVAYEAPTVATGFGAYLAQPLMREVIenKEEITKEEAR 162
Cdd:PTZ00488 117 AASKILANIVWNYKG-MGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGF--KWDLNDEEAQ 192

                        170
                 ....*....|....*..
gi 62955575  163 ELIERCLKVLYYRDARS 179
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYS 209
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-194 1.65e-06

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: 46.83  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVNNSTILGASGDYADYQ----YLKQIIEQMVIDEellgdGHSYT 80
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQaiadYVRYYLDMHSIEL-----GEPPL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955575  81 PKAIHSWLTRVMYNRRskmNPLWNTVVIGGFYNGESFLGYVDKLGVA-YEAPTVATGFGAYLAQPLMREviENKEEITKE 159
Cdd:cd03762  76 VKTAASLFKNLCYNYK---EMLSAGIIVAGWDEQNGGQVYSIPLGGMlIRQPFAIGGSGSTYIYGYVDA--NYKPGMTLE 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 62955575 160 EARELIERCLKVLYYRDARSYNRHEIAIVTADGVE 194
Cdd:cd03762 151 ECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVE 185
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-58 4.13e-03

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: 36.84  E-value: 4.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62955575   5 TSVLGVKFKGGVIIAADMLGSYGSLARFRNISRLMKVnNSTILGA-SGDYADYQY 58
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEI-NPYLLGTmAGGAADCQY 54
 
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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