NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22538465|ref|NP_002786|]
View 

proteasome subunit beta type-3 [Homo sapiens]

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

 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_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-201 1.46e-135

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: 377.35  E-value: 1.46e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   6 YNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPY 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  86 TLMSMVANLLYEKRFGPYYTEPVIAGLDPKtFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFE 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22538465 166 TISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLK 201
Cdd:cd03759 160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 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 ...
 6-201 1.46e-135

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: 377.35  E-value: 1.46e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   6 YNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPY 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  86 TLMSMVANLLYEKRFGPYYTEPVIAGLDPKtFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFE 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22538465 166 TISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLK 201
Cdd:cd03759 160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-190 2.34e-46

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: 151.18  E-value: 2.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465     6 YNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTD-FQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465    85 ---YTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTfKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWEPNMDPD 161
Cdd:pfam00227  82 elaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDG-GPHLYQIDPSGS-YIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 22538465   162 HLFETISQAMLNAVDRDAVSGMGVIVHII 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-199 2.79e-26

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 100.60  E-value: 2.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   8 GGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTL 87
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  88 MSMVANLLYE---KRFGPYYTEPVIAGLDPKTFKPFicSLDLIGCPMvTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLF 164
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGGPRLF--STDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 22538465 165 ETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRT 199
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-193 4.82e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.83  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465    7 NGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYT 86
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   87 LMSMVANLLYEKRFGPYYTEPVIAGLDPKtfKPFICSLDLIGCPMVTDDFVVsGTCAEQMYGMCESLWEPNMDPDHLFET 166
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKK--GPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDL 194

                        170       180
                 ....*....|....*....|....*..
gi 22538465  167 ISQAMLNAVDRDAVSGMGVIVHIIEKD 193
Cdd:PTZ00488 195 GRRAIYHATFRDAYSGGAINLYHMQKD 221
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-201 1.46e-135

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: 377.35  E-value: 1.46e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   6 YNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPY 85
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  86 TLMSMVANLLYEKRFGPYYTEPVIAGLDPKtFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFE 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 22538465 166 TISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLK 201
Cdd:cd03759 160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-199 1.93e-75

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: 225.02  E-value: 1.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   9 GAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLM 88
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  89 SMVANLLYEKRFGPYYTEPVIAGLDPKTfKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETIS 168
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGG-GPFLYYVDPLGS-LIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                       170       180       190
                ....*....|....*....|....*....|.
gi 22538465 169 QAMLNAVDRDAVSGMGVIVHIIEKDKITTRT 199
Cdd:cd01912 159 KAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 9-190 1.45e-53

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: 169.21  E-value: 1.45e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   9 GAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLM 88
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  89 SMVANLLYEKRF--GPYYTEPVIAGLDPKTfKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFET 166
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEG-GPQLYSVDPSGS-YIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                       170       180
                ....*....|....*....|....
gi 22538465 167 ISQAMLNAVDRDAVSGMGVIVHII 190
Cdd:cd01906 159 ALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-190 2.34e-46

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: 151.18  E-value: 2.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465     6 YNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTD-FQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465    85 ---YTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTfKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWEPNMDPD 161
Cdd:pfam00227  82 elaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDG-GPHLYQIDPSGS-YIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 22538465   162 HLFETISQAMLNAVDRDAVSGMGVIVHII 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 11-172 5.76e-36

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: 123.66  E-value: 5.76e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  11 VMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSM 90
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  91 VANLLYEKRFG-PYYTEPVIAGLDPKtfKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQ 169
Cdd:cd01901  83 LAKLLQVYTQGrPFGVNLIVAGVDEG--GGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ...
gi 22538465 170 AML 172
Cdd:cd01901 161 ALK 163
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-205 5.44e-30

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


Pssm-ID: 239726  Cd Length: 212  Bit Score: 109.66  E-value: 5.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   7 NGGAVMAMKGKNCVAIAADRR----FGIQaqmvTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQI 82
Cdd:cd03757   7 NGGTVLAIAGNDFAVIAGDTRlsegYSIL----SRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  83 KPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTfKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWE-PNMDPD 161
Cdd:cd03757  83 STEAIAQLLSTILYSRRFFPYYVFNILAGIDEEG-KGVVYSYDPVGS-YERETYSAGGSASSLIQPLLDNQVGrKNQNNV 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 22538465 162 H--------LFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 205
Cdd:cd03757 161 ErtplsleeAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-193 2.82e-29

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: 107.34  E-value: 2.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  20 VAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKR 99
Cdd:cd03764  12 VVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465 100 FGPYYTEPVIAGLDPKtfKPFICSLDLIGcPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDA 179
Cdd:cd03764  92 YFPYIVQLLIGGVDEE--GPHLYSLDPLG-SIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAIKSAIERDS 168

                       170
                ....*....|....
gi 22538465 180 VSGMGVIVHIIEKD 193
Cdd:cd03764 169 ASGDGIDVVVITKD 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 8-199 2.79e-26

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 100.60  E-value: 2.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   8 GGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTL 87
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  88 MSMVANLLYE---KRFGPYYTEPVIAGLDPKTFKPFicSLDLIGCPMvTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLF 164
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGGPRLF--STDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*
gi 22538465 165 ETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRT 199
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-196 1.76e-18

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: 79.19  E-value: 1.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  11 VMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSM 90
Cdd:cd03762   3 IIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  91 VANLLYEKRfGPYYTEPVIAGLDPKT-FKPFICSLdliGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQ 169
Cdd:cd03762  83 FKNLCYNYK-EMLSAGIIVAGWDEQNgGQVYSIPL---GGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158

                       170       180
                ....*....|....*....|....*...
gi 22538465 170 AMLNAVDRDAVSGmGVI-VHIIEKDKIT 196
Cdd:cd03762 159 ALSLAMSRDGSSG-GVIrLVIITKDGVE 185
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-193 2.47e-11

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: 60.28  E-value: 2.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   8 GGAVMAMKGKNCVAIAADRR--FGIQAQmvTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKfRLNLYE--LKEGRQIK 83
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLgsYGSLAR--FKNVERIFKVGDNTLLGASGDYADFQYLKRLLD-QLVIDDecLDDGHSLS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  84 PYTLMSMVANLLYEKR--FGPYYTEPVIAGLDPKTfKPFICSLDLIGCPMvTDDFVVSGTCAEQMYGMCESLWE--PNMD 159
Cdd:cd03760  79 PKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEG-EPFLGYVDLLGTAY-EDPHVATGFGAYLALPLLREAWEkkPDLT 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 22538465 160 PDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKD 193
Cdd:cd03760 157 EEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-200 4.54e-11

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: 59.52  E-value: 4.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  11 VMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSM 90
Cdd:cd03758   4 LIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAANF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  91 VANLLYE--KRFGPYYTEPVIAGLDPkTFKPFICSLDLIGCpMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETIS 168
Cdd:cd03758  84 TRRELAEslRSRTPYQVNLLLAGYDK-VEGPSLYYIDYLGT-LVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMK 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 22538465 169 QAMLNAVDRDAVSGMGVIVHIIEKDKITTRTL 200
Cdd:cd03758 162 KCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-194 7.66e-10

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: 56.05  E-value: 7.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  11 VMAMKGKNCVAIAADRRfgIQAQMVTTD--FQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLM 88
Cdd:cd03763   3 IVGVVFKDGVVLGADTR--ATEGPIVADknCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  89 SMVANLLYekRFGPYYTEP-VIAGLDPKtfKPFICSLDLIGC----PMVTDDfvvSGTCAEQmyGMCESLWEPNMDPDHL 163
Cdd:cd03763  81 TMLKQHLF--RYQGHIGAAlVLGGVDYT--GPHLYSIYPHGStdklPFVTMG---SGSLAAM--SVLEDRYKPDMTEEEA 151

                       170       180       190
                ....*....|....*....|....*....|.
gi 22538465 164 FETISQAMLNAVDRDAVSGMGVIVHIIEKDK 194
Cdd:cd03763 152 KKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-193 4.82e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.83  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465    7 NGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYT 86
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   87 LMSMVANLLYEKRFGPYYTEPVIAGLDPKtfKPFICSLDLIGCPMVTDDFVVsGTCAEQMYGMCESLWEPNMDPDHLFET 166
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKK--GPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDL 194

                        170       180
                 ....*....|....*....|....*..
gi 22538465  167 ISQAMLNAVDRDAVSGMGVIVHIIEKD 193
Cdd:PTZ00488 195 GRRAIYHATFRDAYSGGAINLYHMQKD 221
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-116 8.98e-05

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 41.66  E-value: 8.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   7 NGGAVMAMKGKNCVAIAADRRfgIQAQMVTTDFQ-KIFPMGDRLYIGLAGLATDVQTVAQRLK-----FRLNlYelkeGR 80
Cdd:cd01911  26 NGSTAVGIKGKDGVVLAVEKK--VTSKLLDPSSVeKIFKIDDHIGCAVAGLTADARVLVNRARveaqnYRYT-Y----GE 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22538465  81 QIKPYTLMSMVANLL------YEKRfgPYYTEPVIAGLDPKT 116
Cdd:cd01911  99 PIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEG 138
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-193 3.13e-04

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


Pssm-ID: 239730  Cd Length: 188  Bit Score: 39.92  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  12 MAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMV 91
Cdd:cd03761   4 LAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465  92 ANLLYEKRFGPYYTEPVIAGLDPktFKPFICSLDLIGCPMVTDDFVVsGTCAEQMYGMCESLWEPNMDPDHLFETISQAM 171
Cdd:cd03761  84 SNMLYQYKGMGLSMGTMICGWDK--TGPGLYYVDSDGTRLKGDLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|..
gi 22538465 172 LNAVDRDAVSGMGVIVHIIEKD 193
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVRED 182
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-114 3.27e-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: 37.34  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538465   8 GGAVMAMKGKNCVAIAADRRFGIQAQMVTTdFQKIFPMGDRLYIGLAGLATDVQTVAQRLK-----FRLNLYELKEGRQI 82
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVAKLQDPRT-VRKICMLDDHVCLAFAGLTADARVLINRARlecqsHRLTVEDPVTVEYI 105

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 22538465  83 KPYtlmsmVANLL--YEKRFG--PYYTEPVIAGLDP 114
Cdd:cd03755 106 TRY-----IAGLQqrYTQSGGvrPFGISTLIVGFDP 136
 
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