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Conserved domains on  [gi|79315846|ref|NP_001030905|]
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N-terminal nucleophile aminohydrolases (Ntn hydrolases) superfamily protein [Arabidopsis thaliana]

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
8-223 4.49e-132

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: 370.05  E-value: 4.49e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   8 WSPYDNNGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNK 87
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  88 QMSCPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSPSPLLl 167
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79315846 168 pkqDSNTPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTELMDLRKD 223
Cdd:cd03757 160 ---VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
8-223 4.49e-132

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: 370.05  E-value: 4.49e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   8 WSPYDNNGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNK 87
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  88 QMSCPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSPSPLLl 167
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79315846 168 pkqDSNTPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTELMDLRKD 223
Cdd:cd03757 160 ---VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
13-208 3.78e-41

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: 138.47  E-value: 3.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846    13 NNGGTCVAIAGSDYCVIAADTRMSTGYSILSRD-YSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMS- 90
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846    91 --CPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllp 168
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP------- 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 79315846   169 kqdsntPLSEAEAVDLVKTVFASATERDIYTVNKLEIMIL 208
Cdd:pfam00227 155 ------DLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
15-214 2.46e-28

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 106.38  E-value: 2.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  15 GGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQAD----VKALQKVLKSRHLIYqhqhNKQMS 90
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADarelVRLARVEAQLYELRY----GEPIS 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  91 CPAMAQLLSNTLY---FKRFFPYYAFNVLGGLDEEGkGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLkspsplll 167
Cdd:COG0638 111 VEGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEY-------- 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 79315846 168 pKQDsntpLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:COG0638 182 -RED----LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
14-214 5.75e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 51.53  E-value: 5.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   14 NGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPA 93
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   94 MAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGcVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKspsplllpkqdsn 173
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK------------- 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 79315846  174 TPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:PTZ00488 184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWK 224
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
8-223 4.49e-132

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: 370.05  E-value: 4.49e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   8 WSPYDNNGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNK 87
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  88 QMSCPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSPSPLLl 167
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79315846 168 pkqDSNTPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTELMDLRKD 223
Cdd:cd03757 160 ---VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
16-216 1.83e-70

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: 213.07  E-value: 1.83e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  16 GTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMA 95
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  96 QLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqdsntP 175
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKP-------------D 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 79315846 176 LSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTE 216
Cdd:cd01912 148 MTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
16-208 7.30e-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: 165.75  E-value: 7.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  16 GTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMA 95
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  96 QLLSNTLYFKRF--FPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqdsn 173
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP------------ 148
                       170       180       190
                ....*....|....*....|....*....|....*
gi 79315846 174 tPLSEAEAVDLVKTVFASATERDIYTVNKLEIMIL 208
Cdd:cd01906 149 -DMTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
13-208 3.78e-41

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: 138.47  E-value: 3.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846    13 NNGGTCVAIAGSDYCVIAADTRMSTGYSILSRD-YSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMS- 90
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846    91 --CPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllp 168
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP------- 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 79315846   169 kqdsntPLSEAEAVDLVKTVFASATERDIYTVNKLEIMIL 208
Cdd:pfam00227 155 ------DLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
17-214 6.34e-35

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: 122.36  E-value: 6.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  17 TCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMAQ 96
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  97 LLSNTLYFKRFFPYYAFNVLGGLDEEGKGcVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKspsplllPKqdsntpL 176
Cdd:cd03764  82 LLSNILNSSKYFPYIVQLLIGGVDEEGPH-LYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYK-------ED------M 147
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 79315846 177 SEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:cd03764 148 TVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYK 185
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
16-191 1.74e-29

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: 107.87  E-value: 1.74e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  16 GTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMA 95
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  96 QLLSNTLY-FKRFFPYYAFNVLGGLDEEGkGCVFTYDAVGSY-ERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqdsn 173
Cdd:cd01901  81 KELAKLLQvYTQGRPFGVNLIVAGVDEGG-GNLYYIDPSGPViENPGAVATGSRSQRAKSLLEKLYKP------------ 147
                       170
                ....*....|....*...
gi 79315846 174 tPLSEAEAVDLVKTVFAS 191
Cdd:cd01901 148 -DMTLEEAVELALKALKS 164
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
14-218 4.33e-29

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: 107.71  E-value: 4.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  14 NGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPA 93
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  94 MAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVG-YGAQGSGSTLIMPFLDNqlkspspllLPKQDs 172
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYGMCES---------LWRPD- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 79315846 173 ntpLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTELM 218
Cdd:cd03759 152 ---MEPDELFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTL 194
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
15-214 2.46e-28

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 106.38  E-value: 2.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  15 GGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQAD----VKALQKVLKSRHLIYqhqhNKQMS 90
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADarelVRLARVEAQLYELRY----GEPIS 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  91 CPAMAQLLSNTLY---FKRFFPYYAFNVLGGLDEEGkGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLkspsplll 167
Cdd:COG0638 111 VEGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEY-------- 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 79315846 168 pKQDsntpLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:COG0638 182 -RED----LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
17-215 4.46e-17

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: 76.08  E-value: 4.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  17 TCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQAD-VKALQKVLKSRHLiYQHQHNKQMSCPAMA 95
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDrLQFAEYIQKNIQL-YKMRNGYELSPKAAA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  96 QLLSNTL--YFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqdsn 173
Cdd:cd03758  82 NFTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKP------------ 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 79315846 174 tPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKT 215
Cdd:cd03758 150 -DMTVEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRD 190
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
15-216 1.30e-15

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: 72.22  E-value: 1.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  15 GGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKsRHLIYQHQH--NKQMSCP 92
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLD-QLVIDDECLddGHSLSPK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  93 AMAQLLSNTLYFKR--FFPYYAFNVLGGLDEEGK---GCVftyDAVGSYERVGYGAQGSGSTLIMPFLDNQLKspsplll 167
Cdd:cd03760  81 EIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEpflGYV---DLLGTAYEDPHVATGFGAYLALPLLREAWE------- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 79315846 168 PKQDsntpLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIKTE 216
Cdd:cd03760 151 KKPD----LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIE 195
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
17-201 4.12e-12

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: 62.63  E-value: 4.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  17 TCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKsrhliYQ-HQHNKQMSCP--- 92
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVR-----YYlDMHSIELGEPplv 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  93 -AMAQLLSNTLYFKRFFpYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqd 171
Cdd:cd03762  77 kTAASLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKP---------- 145
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 79315846 172 sntPLSEAEAVDLVKTVFASATERD------IYTVN 201
Cdd:cd03762 146 ---GMTLEECIKFVKNALSLAMSRDgssggvIRLVI 178
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
13-208 1.76e-10

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: 58.22  E-value: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  13 NNGGTCVAIAGSDYCVIAADTRMStgySILSRDYS--KIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMS 90
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVEKKVT---SKLLDPSSveKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  91 CPAMAQLLSN-----TLY-FKRffPYYAFNVLGGLDEEGKGCVFTYDAVGSYerVGYGAQ--GSGSTLIMPFLDNQLKSp 162
Cdd:cd01911 102 VEVLVKRIADlaqvyTQYgGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTY--FGYKATaiGKGSQEAKTFLEKRYKK- 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 79315846 163 splllpkqdsntPLSEAEAVDLVKTVFASATERDIyTVNKLEIMIL 208
Cdd:cd01911 177 ------------DLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
17-214 1.02e-09

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: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  17 TCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMAQ 96
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  97 LLSNTLyfkrfFPYY----AFNVLGGLDEEGKGcVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSpsplllpkqds 172
Cdd:cd03763  82 MLKQHL-----FRYQghigAALVLGGVDYTGPH-LYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKP----------- 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 79315846 173 ntPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:cd03763 145 --DMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVE 184
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
14-214 5.75e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 51.53  E-value: 5.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   14 NGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPA 93
Cdd:PTZ00488  38 HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846   94 MAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGcVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKspsplllpkqdsn 173
Cdd:PTZ00488 118 ASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK------------- 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 79315846  174 TPLSEAEAVDLVKTVFASATERDIYTVNKLEIMILKADGIK 214
Cdd:PTZ00488 184 WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWK 224
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
28-212 1.38e-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: 46.85  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  28 VIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMAQLLSNTLYfkrf 107
Cdd:cd03761  13 IVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLY---- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846 108 fPYYAFNV-----LGGLDEEGKGcVFTYDAVGSyeRVGyG---AQGSGSTLIMPFLDnqlkspsplllpkQDSNTPLSEA 179
Cdd:cd03761  89 -QYKGMGLsmgtmICGWDKTGPG-LYYVDSDGT--RLK-GdlfSVGSGSTYAYGVLD-------------SGYRYDLSVE 150
                       170       180       190
                ....*....|....*....|....*....|...
gi 79315846 180 EAVDLVKTVFASATERDIYTVNKLEIMILKADG 212
Cdd:cd03761 151 EAYDLARRAIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
13-161 6.20e-06

proteasome_alpha_type_1. 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: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 45.36  E-value: 6.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  13 NNGGTCVAIAGSDYCVIAADTRMStgySILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCP 92
Cdd:cd03749  25 KQGSATVGLKSKTHAVLVALKRAT---SELSSYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVS 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  93 AMAQLLS-----NT-LYFKRffPYYAFNVLGGLDEEG--------KGCVFTYDAVgsyervgygAQGSGSTLIMPFLDNQ 158
Cdd:cd03749 102 RLVSKVAekaqiNTqRYGRR--PYGVGLLIAGYDESGphlfqtcpSGNYFEYKAT---------SIGARSQSARTYLERH 170

                ...
gi 79315846 159 LKS 161
Cdd:cd03749 171 FEE 173
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
13-208 3.66e-05

proteasome_alpha_type_4. 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: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 43.10  E-value: 3.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  13 NNGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCP 92
Cdd:cd03752  27 SHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVE 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  93 AMAQLLSNTlyfKRFFPYYA----FNV---LGGLDEEGKGCVFTYDAVGSYErvGYGAQGSGStlimpfldNQLKSPSPL 165
Cdd:cd03752 107 QLVQRLCDI---KQGYTQYGglrpFGVsflYAGWDKHYGFQLYQSDPSGNYS--GWKATAIGN--------NNQAAQSLL 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 79315846 166 llpKQDSNTPLSEAEAVDLVKTVFASATERDIYTVNKLEIMIL 208
Cdd:cd03752 174 ---KQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
15-160 4.95e-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: 36.96  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315846  15 GGTCVAIAGSDyCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKalqkVLKSRHLIYQHQHNKQMSCPAM 94
Cdd:cd03755  27 GTTAVGVRGKD-CVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR----VLINRARLECQSHRLTVEDPVT 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79315846  95 AQLLSNTL--YFKRFF------PYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLK 160
Cdd:cd03755 102 VEYITRYIagLQQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYK 175
 
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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