NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17508497|ref|NP_491261|]
View 

Proteasome subunit beta type-2 [Caenorhabditis elegans]

Protein Classification

proteasome subunit beta( domain architecture ID 10132911)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-199 7.82e-91

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: 264.06  E-value: 7.82e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   4 MHFLVGISTENYVILAADKaTFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSC 83
Cdd:cd03758   1 METLIGIKGKDFVILAADT-SAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  84 AHHFVRRSIAEGLRSQDHYTVDVLIGGYdDKEDKAFLGSVDYLANgLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGL 163
Cdd:cd03758  80 AANFTRRELAESLRSRTPYQVNLLLAGY-DKVEGPSLYYIDYLGT-LVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17508497 164 ALMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLDD 199
Cdd:cd03758 158 ELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-199 7.82e-91

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: 264.06  E-value: 7.82e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   4 MHFLVGISTENYVILAADKaTFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSC 83
Cdd:cd03758   1 METLIGIKGKDFVILAADT-SAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  84 AHHFVRRSIAEGLRSQDHYTVDVLIGGYdDKEDKAFLGSVDYLANgLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGL 163
Cdd:cd03758  80 AANFTRRELAESLRSRTPYQVNLLLAGY-DKVEGPSLYYIDYLGT-LVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17508497 164 ALMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLDD 199
Cdd:cd03758 158 ELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-189 6.24e-36

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: 124.22  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497     8 VGISTENYVILAADKATFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHHF 87
Cdd:pfam00227   8 VGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497    88 VRRSIAEGLRS-QDHYTVDVLIGGYDDKeDKAFLGSVDYLANGLGqQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALM 166
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIE-YKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 17508497   167 NKCIGEAKRRFVANIPGYKVVII 189
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-199 7.21e-13

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 64.78  E-value: 7.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADK-ATfaYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSP-SCAH 85
Cdd:COG0638  39 VGIKTKDGVVLAADRrAT--MGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVeGLAK 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  86 H---FVRRSIAEGLRSqdhYTVDVLIGGYDDKEDKAF----LGSV---DYLANGLGQQpylfrgfcgrFCYAIMDREYKK 155
Cdd:COG0638 117 LlsdLLQGYTQYGVRP---FGVALLIGGVDDGGPRLFstdpSGGLyeeKAVAIGSGSP----------FARGVLEKEYRE 183

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17508497 156 DMTEAEGLALMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLDD 199
Cdd:COG0638 184 DLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSE 227
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-199 7.82e-91

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: 264.06  E-value: 7.82e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   4 MHFLVGISTENYVILAADKaTFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSC 83
Cdd:cd03758   1 METLIGIKGKDFVILAADT-SAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  84 AHHFVRRSIAEGLRSQDHYTVDVLIGGYdDKEDKAFLGSVDYLANgLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGL 163
Cdd:cd03758  80 AANFTRRELAESLRSRTPYQVNLLLAGY-DKVEGPSLYYIDYLGT-LVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17508497 164 ALMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLDD 199
Cdd:cd03758 158 ELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-197 1.50e-51

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: 164.15  E-value: 1.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   7 LVGISTENYVILAADKATfAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHH 86
Cdd:cd01912   3 IVGIKGKDGVVLAADTRA-SAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  87 FVRRSIAEGLRsqDHYTVDVLIGGYDdKEDKAFLGSVDYLANgLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALM 166
Cdd:cd01912  82 LLSNILYSYRG--FPYYVSLIVGGVD-KGGGPFLYYVDPLGS-LIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELV 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 17508497 167 NKCIGEAKRRFVANIPGYKVVIIDKKGYRKL 197
Cdd:cd01912 158 KKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 8-189 6.24e-36

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: 124.22  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497     8 VGISTENYVILAADKATFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHHF 87
Cdd:pfam00227   8 VGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497    88 VRRSIAEGLRS-QDHYTVDVLIGGYDDKeDKAFLGSVDYLANGLGqQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALM 166
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIE-YKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 17508497   167 NKCIGEAKRRFVANIPGYKVVII 189
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 8-189 7.91e-35

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: 121.45  E-value: 7.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADKATfAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHHF 87
Cdd:cd01906   4 VGIKGKDGVVLAADKRV-TSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  88 VRRSIAEGLRSQDHYTVDVLIGGYdDKEDKAFLGSVDYLANgLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALMN 167
Cdd:cd01906  83 LANLLYEYTQSLRPLGVSLLVAGV-DEEGGPQLYSVDPSGS-YIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 17508497 168 KCIGEAKRRFVANIPGYKVVII 189
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 8-170 1.23e-22

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: 89.38  E-value: 1.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADKAtFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHHF 87
Cdd:cd01901   4 VAIKGKGGVVLAADKR-LSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  88 VRRSIAEgLRSQDHYTVDVLIGGYDdkEDKAFLGSVDYLANGLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALMN 167
Cdd:cd01901  83 LAKLLQV-YTQGRPFGVNLIVAGVD--EGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ...
gi 17508497 168 KCI 170
Cdd:cd01901 160 KAL 162
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-198 3.06e-20

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: 83.84  E-value: 3.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADK-ATfaYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPscahH 86
Cdd:cd03764   4 VGIVCKDGVVLAADKrAS--MGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSI----K 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  87 FVRRSIAEGLRSQDH--YTVDVLIGGYDDKEDKAFlgSVDYLAnGLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLA 164
Cdd:cd03764  78 ALATLLSNILNSSKYfpYIVQLLIGGVDEEGPHLY--SLDPLG-SIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKK 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 17508497 165 LMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLD 198
Cdd:cd03764 155 LAIRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-199 7.21e-13

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 64.78  E-value: 7.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADK-ATfaYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSP-SCAH 85
Cdd:COG0638  39 VGIKTKDGVVLAADRrAT--MGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVeGLAK 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  86 H---FVRRSIAEGLRSqdhYTVDVLIGGYDDKEDKAF----LGSV---DYLANGLGQQpylfrgfcgrFCYAIMDREYKK 155
Cdd:COG0638 117 LlsdLLQGYTQYGVRP---FGVALLIGGVDDGGPRLFstdpSGGLyeeKAVAIGSGSP----------FARGVLEKEYRE 183

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17508497 156 DMTEAEGLALMNKCIGEAKRRFVANIPGYKVVIIDKKGYRKLDD 199
Cdd:COG0638 184 DLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSE 227
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-193 1.26e-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: 52.57  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAADKATfAYGAILADSENDKEYRLGKKlTMMCIGeeGDVAQFgDWTKRNL-------QLYSvrNGYEVS 80
Cdd:cd03760   6 IAIKYKDGVIIAADTLG-SYGSLARFKNVERIFKVGDN-TLLGAS--GDYADF-QYLKRLLdqlviddECLD--DGHSLS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  81 PSCAHHFV------RRSiaeglrSQDHYTVDVLIGGYDDkEDKAFLGSVDYLANGLgQQPYLFRGFCGRFCYAIMDREYK 154
Cdd:cd03760  79 PKEIHSYLtrvlynRRS------KMNPLWNTLVVGGVDN-EGEPFLGYVDLLGTAY-EDPHVATGFGAYLALPLLREAWE 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17508497 155 K--DMTEAEGLALMNKCIGEAKRRFVANIPGYKVVIIDKKG 193
Cdd:cd03760 151 KkpDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEG 191
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-170 1.12e-06

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: 46.81  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   8 VGISTENYVILAAD-KATfaYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHH 86
Cdd:cd03763   4 VGVVFKDGVVLGADtRAT--EGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  87 FVRRSIaegLRSQDHYTVDVLIGGYDDKedKAFL------GSVDYLanglgqqPYLFRGfCGRFC-YAIMDREYKKDMTE 159
Cdd:cd03763  82 MLKQHL---FRYQGHIGAALVLGGVDYT--GPHLysiyphGSTDKL-------PFVTMG-SGSLAaMSVLEDRYKPDMTE 148

                       170
                ....*....|.
gi 17508497 160 AEGLALMNKCI 170
Cdd:cd03763 149 EEAKKLVCEAI 159
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 16-176 3.23e-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: 45.68  E-value: 3.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  16 VILAADKATFAyGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHHFVRRSIaeg 95
Cdd:cd03762  12 VVLGADSRTST-GSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLFKNLC--- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  96 LRSQDHYTVDVLIGGYDDKEDkaflGSVDYLANG--LGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALMNKCIGEA 173
Cdd:cd03762  88 YNYKEMLSAGIIVAGWDEQNG----GQVYSIPLGgmLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNALSLA 163


                ...
gi 17508497 174 KRR 176
Cdd:cd03762 164 MSR 166
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-197 2.83e-03

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: 37.22  E-value: 2.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497   7 LVGISTENYVILAADKaTFAYGAILADSENDKEYRLGKKLTMMCIGEEGDVAQFGDWTKRNLQLYSVRNGYEVSPSCAHH 86
Cdd:cd03759   6 VVAMAGKDCVAIASDL-RLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508497  87 FVRRSIAEglRSQDHYTVDVLIGGYDDKeDKAFLGSVDYLANGLGQQPYLFRGFCGRFCYAIMDREYKKDMTEAEGLALM 166
Cdd:cd03759  85 LISSLLYE--KRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETI 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 17508497 167 NKCIGEAKRRFVANIPGYKVVII--DKKGYRKL 197
Cdd:cd03759 162 SQALLSAVDRDALSGWGAVVYIItkDKVTTRTL 194
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH