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Conserved domains on  [gi|17380183|sp|O65084|]
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RecName: Full=Proteasome subunit beta type-3; AltName: Full=20S proteasome alpha subunit C; AltName: Full=20S proteasome subunit beta-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 ...
 6-200 7.29e-134

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: 373.12  E-value: 7.29e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   6 YNGSALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPE 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  86 TFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKELAKDFVVAGTAAESLYGACESMYKPDMEPEELFET 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17380183 166 ISQALLSSIDRDCLSGWGGHVYVVSPNQVIERTLK 200
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 ...
 6-200 7.29e-134

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: 373.12  E-value: 7.29e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   6 YNGSALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPE 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  86 TFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKELAKDFVVAGTAAESLYGACESMYKPDMEPEELFET 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17380183 166 ISQALLSSIDRDCLSGWGGHVYVVSPNQVIERTLK 200
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-189 1.89e-54

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: 171.60  E-value: 1.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183     6 YNGSALVAMVGKNCFAIASDRRLGVQLQTIATD-FQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183    85 E---TFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEE 161
Cdd:pfam00227  82 ElaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSY-IEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 17380183   162 LFETISQALLSSIDRDCLSGWGGHVYVV 189
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-198 1.88e-21

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 87.89  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   8 GSALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETF 87
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  88 ASLVSALLYE---KRFGPYFCQPVIAGLgEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEELFE 164
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGV-DDGGPRLFSTDPSGGL-YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|....
gi 17380183 165 TISQALLSSIDRDCLSGWGGHVYVVSPNQVIERT 198
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-187 1.32e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 41.51  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183    4 FEYNGSALVAMVGKNCFA--IASdrrlgvqlQTIatdfQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERN 81
Cdd:PTZ00488  45 FKYGGGIIIAVDSKATAGpyIAS--------QSV----KKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   82 MRPETFASLVSALLYEKR-----FGPYFCqpviaglGEDDK-PFICTMDSIGAKELAKDFVVaGTAAESLYGACESMYKP 155
Cdd:PTZ00488 113 ISVAAASKILANIVWNYKgmglsMGTMIC-------GWDKKgPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17380183  156 DMEPEELFETISQALLSSIDRDCLSGWGGHVY 187
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINLY 216
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-200 7.29e-134

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: 373.12  E-value: 7.29e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   6 YNGSALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPE 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  86 TFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKELAKDFVVAGTAAESLYGACESMYKPDMEPEELFET 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17380183 166 ISQALLSSIDRDCLSGWGGHVYVVSPNQVIERTLK 200
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 11-198 3.59e-71

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: 214.23  E-value: 3.59e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  11 LVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFASL 90
Cdd:cd01912   3 IVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  91 VSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKELAkDFVVAGTAAESLYGACESMYKPDMEPEELFETISQAL 170
Cdd:cd01912  83 LSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEA-PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKAI 161

                       170       180
                ....*....|....*....|....*...
gi 17380183 171 LSSIDRDCLSGWGGHVYVVSPNQVIERT 198
Cdd:cd01912 162 DSAIERDLSSGGGVDVAVITKDGVEELR 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-189 1.89e-54

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: 171.60  E-value: 1.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183     6 YNGSALVAMVGKNCFAIASDRRLGVQLQTIATD-FQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183    85 E---TFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEE 161
Cdd:pfam00227  82 ElaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSY-IEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 17380183   162 LFETISQALLSSIDRDCLSGWGGHVYVV 189
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 9-189 1.16e-52

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: 166.90  E-value: 1.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   9 SALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFA 88
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  89 SLVSALLYEKRF--GPYFCQPVIAGLGEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEELFETI 166
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSY-IEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 17380183 167 SQALLSSIDRDCLSGWGGHVYVV 189
Cdd:cd01906 160 LKALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 9-172 3.43e-35

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: 121.73  E-value: 3.43e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   9 SALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFA 88
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  89 SLVSALLYEKRFG-PYFCQPVIAGLgEDDKPFICTMDSIGAKELAKDFVVAGTAAESLYGACESMYKPDMEPEELFETIS 167
Cdd:cd01901  81 KELAKLLQVYTQGrPFGVNLIVAGV-DEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....*
gi 17380183 168 QALLS 172
Cdd:cd01901 160 KALKS 164
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-204 2.89e-29

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: 108.12  E-value: 2.89e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   4 FEYNGSALVAMVGKNCFAIASDRRLgVQLQTIATDFQ-RIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNM 82
Cdd:cd03757   4 YTDNGGTVLAIAGNDFAVIAGDTRL-SEGYSILSRDSpKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  83 RPETFASLVSALLYEKRFGPYFCQPVIAGLGEDDKPFICTMDSIGAKELAKdFVVAGTAAESLYGACES------MYKPD 156
Cdd:cd03757  83 STEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERET-YSAGGSASSLIQPLLDNqvgrknQNNVE 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17380183 157 MEP---EELFETISQALLSSIDRDCLSGWGGHVYVVSPNQVIERTLKGRMD 204
Cdd:cd03757 162 RTPlslEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 23-197 5.33e-28

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: 103.87  E-value: 5.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  23 ASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFASLVSALLYEKRFGP 102
Cdd:cd03764  15 AADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSKYFP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183 103 YFCQPVIAGLgEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEELFETISQALLSSIDRDCLSGW 182
Cdd:cd03764  95 YIVQLLIGGV-DEEGPHLYSLDPLGSI-IEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAIKSAIERDSASGD 172

                       170
                ....*....|....*
gi 17380183 183 GGHVYVVSPNQVIER 197
Cdd:cd03764 173 GIDVVVITKDGYKEL 187
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-198 1.88e-21

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 87.89  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   8 GSALVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETF 87
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  88 ASLVSALLYE---KRFGPYFCQPVIAGLgEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMYKPDMEPEELFE 164
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGV-DDGGPRLFSTDPSGGL-YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|....
gi 17380183 165 TISQALLSSIDRDCLSGWGGHVYVVSPNQVIERT 198
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-166 3.63e-10

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


Pssm-ID: 239727  Cd Length: 193  Bit Score: 56.82  E-value: 3.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  11 LVAMVGKNCFAIASDRRLGVQLQTIATDFQRIFKIHDKLYVGLSGLATDVQ--TLY-QRFAfrhKLYQLREERNMRPETF 87
Cdd:cd03758   4 LIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLqfAEYiQKNI---QLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  88 ASLVSALLYE--KRFGPYFCQPVIAGLGEDDKPFICTMDSIGAkeLAK-DFVVAGTAAESLYGACESMYKPDMEPEELFE 164
Cdd:cd03758  81 ANFTRRELAEslRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGT--LVKvPYAAHGYGAYFCLSILDRYYKPDMTVEEALE 158


                ..
gi 17380183 165 TI 166
Cdd:cd03758 159 LM 160
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-181 3.55e-09

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: 54.15  E-value: 3.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  36 ATDfqRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFASLVSALLYEKRFGPYfCQPVIAGLGED 115
Cdd:cd03762  30 VTD--KLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLFKNLCYNYKEMLS-AGIIVAGWDEQ 106

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17380183 116 DKPFICTMdSIGAKELAKDFVVAGTAAESLYGACESMYKPDMEPEELFETISQALLSSIDRDCLSG 181
Cdd:cd03762 107 NGGQVYSI-PLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNALSLAMSRDGSSG 171
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-181 1.52e-07

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: 49.49  E-value: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   8 GSALVAMVGKNCFAIASDRRL--GVQLQTiaTDFQRIFKIHDKLYVGLSGLATDVQTLyQRFAFRHKLYQLREE--RNMR 83
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGsyGSLARF--KNVERIFKVGDNTLLGASGDYADFQYL-KRLLDQLVIDDECLDdgHSLS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  84 PETFASLVSALLYEKR--FGPYFCQPVIAGLGEDDKPFICTMDSIGAKeLAKDFVVAGTAAESLYGACESMY--KPDMEP 159
Cdd:cd03760  79 PKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTA-YEDPHVATGFGAYLALPLLREAWekKPDLTE 157

                       170       180
                ....*....|....*....|..
gi 17380183 160 EELFETISQALLSSIDRDCLSG 181
Cdd:cd03760 158 EEARALIEECMKVLYYRDARSI 179
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-177 4.73e-06

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: 45.51  E-value: 4.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   5 EY------NGSALVAMVGKNCFAIASDRRLGVQLQTIATdFQRIFKIHDKLYVGLSGLATDVQTLYQR---FAFRHKL-Y 74
Cdd:cd01911  18 EYaleavkNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSS-VEKIFKIDDHIGCAVAGLTADARVLVNRarvEAQNYRYtY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  75 qlreERNMRPETFASLVSALL------YEKRfgPYFCQPVIAGLGEDDKPFICTMD-----------SIGAKELAkdfvv 137
Cdd:cd01911  97 ----GEPIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDpsgtyfgykatAIGKGSQE----- 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17380183 138 agtAAESLygacESMYKPDMEPEELFETISQALLSSIDRD 177
Cdd:cd01911 166 ---AKTFL----EKRYKKDLTLEEAIKLALKALKEVLEED 198
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-192 8.13e-06

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 44.54  E-value: 8.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  40 QRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETFASLVSALLYEKRFGPYFCQPVIAGLgedDK-- 117
Cdd:cd03761  32 KKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQYKGMGLSMGTMICGW---DKtg 108

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17380183 118 PFICTMDSIGAKELAKDFVVaGTAAESLYGACESMYKPDMEPEELFETISQALLSSIDRDCLSGWGGHVYVVSPN 192
Cdd:cd03761 109 PGLYYVDSDGTRLKGDLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-187 1.32e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 41.51  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183    4 FEYNGSALVAMVGKNCFA--IASdrrlgvqlQTIatdfQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERN 81
Cdd:PTZ00488  45 FKYGGGIIIAVDSKATAGpyIAS--------QSV----KKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   82 MRPETFASLVSALLYEKR-----FGPYFCqpviaglGEDDK-PFICTMDSIGAKELAKDFVVaGTAAESLYGACESMYKP 155
Cdd:PTZ00488 113 ISVAAASKILANIVWNYKgmglsMGTMIC-------GWDKKgPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17380183  156 DMEPEELFETISQALLSSIDRDCLSGWGGHVY 187
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINLY 216
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-194 3.10e-03

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: 37.18  E-value: 3.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  12 VAMVGKNCFAIASDRRlgvqlqtiAT--------DFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMR 83
Cdd:cd03763   4 VGVVFKDGVVLGADTR--------ATegpivadkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  84 PETFASLVSALLYekRFGPYFCQPVIAGlGEDDK-PFICTMDSIGAKELAKdFVVAGT---AAESLYgacESMYKPDMEP 159
Cdd:cd03763  76 VVTALTMLKQHLF--RYQGHIGAALVLG-GVDYTgPHLYSIYPHGSTDKLP-FVTMGSgslAAMSVL---EDRYKPDMTE 148

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17380183 160 EELFETISQALLSSIDRDCLSGWGGHVYVVSPNQV 194
Cdd:cd03763 149 EEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGV 183
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-175 4.57e-03

proteasome_alpha_type_7. 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: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 36.57  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183   8 GSALVAMVGKNCFAIASDRRLGVQLQTIATdFQRIFKIHDKLYVGLSGLATDVQTLYQRFAFRHKLYQLREERNMRPETF 87
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVAKLQDPRT-VRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYI 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380183  88 ASLVSALL--YEKRFG--PYFCQPVIAGLGEDDKPFICTMDSIGAKELAKDFVVaGTAAESLYGACESMYKPDMEPEELF 163
Cdd:cd03755 106 TRYIAGLQqrYTQSGGvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI-GRNSKTVREFLEKNYKEEMTRDDTI 184

                       170
                ....*....|..
gi 17380183 164 ETISQALLSSID 175
Cdd:cd03755 185 KLAIKALLEVVQ 196
 
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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