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Conserved domains on  [gi|71998965|ref|NP_496177|]
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Proteasome subunit alpha type-3 [Caenorhabditis elegans]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132889)

proteasome subunit alpha is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 3.52e-121

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 343.88  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   5 GTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPD 84
Cdd:cd03751   1 GTGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  85 GFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTL-GISRPFGAGAFFMSWNKQtGGRLFLVEPSGLNYEYKAW 163
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLySSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998965 164 AVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:cd03751 160 AIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKAFELELSWV 212
 
Name Accession Description Interval E-value
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 3.52e-121

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 343.88  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   5 GTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPD 84
Cdd:cd03751   1 GTGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  85 GFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTL-GISRPFGAGAFFMSWNKQtGGRLFLVEPSGLNYEYKAW 163
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLySSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998965 164 AVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:cd03751 160 AIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKAFELELSWV 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-216 1.58e-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: 153.11  E-value: 1.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965    31 VDNAGTMIAIRGKNGVVVVADKLIS--SKLYTDNANPRMFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMP 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   109 IQnIANSVAEYIHIHTLGIS-RPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVGKHRQAAKAEIEKLKIEELDVN 187
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGrRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 71998965   188 QLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-232 3.38e-44

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 148.83  E-value: 3.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965    6 TGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDG 85
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   86 FALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHT-LGISRPFGAgAFFMSWNKQTGGRLFLVEPSGLNYEYKAWA 164
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTqHGGVRPFGV-ALLIAGVDDGGPRLFETDPSGAYLEYKATA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71998965  165 VGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNvQIEMGWVGEQTnGKYEEVPSEVV 232
Cdd:PRK03996 167 IGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPE-NVEIAYIDVET-KKFRKLSVEEI 232
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-230 1.14e-30

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 1.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   5 GTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPR-MFNVNDNVGVAVAGNYP 83
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEkIFKIDDHIGVAIAGLVA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  84 DGFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTLGISRPFGAGAFFMSWNKQtGGRLFLVEPSGLNYEYKAW 163
Cdd:COG0638  86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGVRPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAV 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71998965 164 AVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWVgeqTNGKYEEVPSE 230
Cdd:COG0638 165 AIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVI---TEDGFRELSEE 228
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 2.75e-10

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 54.04  E-value: 2.75e-10
                           10        20
                   ....*....|....*....|...
gi 71998965      8 YDLAASTFSPDGRIFQVEYAQKA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 3.52e-121

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 343.88  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   5 GTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPD 84
Cdd:cd03751   1 GTGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  85 GFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTL-GISRPFGAGAFFMSWNKQtGGRLFLVEPSGLNYEYKAW 163
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLySSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998965 164 AVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:cd03751 160 AIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKAFELELSWV 212
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-216 6.13e-89

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: 261.99  E-value: 6.13e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGFA 87
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  88 LKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTL-GISRPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVG 166
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQyGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71998965 167 KHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKdKNVQIEMGWV 216
Cdd:cd01911 161 KGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-216 1.58e-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: 153.11  E-value: 1.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965    31 VDNAGTMIAIRGKNGVVVVADKLIS--SKLYTDNANPRMFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMP 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   109 IQnIANSVAEYIHIHTLGIS-RPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVGKHRQAAKAEIEKLKIEELDVN 187
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGrRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 71998965   188 QLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-216 1.17e-44

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: 148.03  E-value: 1.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  35 GTMIAIRGKNGVVVVADKLISSKLYTDNAN-PRMFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMPIQNIA 113
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTvEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965 114 NSVAEYIHIHTlGISRPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVGKHRQAAKAEIEKLKIEELDVNQLVKEA 193
Cdd:cd01906  81 KLLANLLYEYT-QSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 71998965 194 ARIIMVVRDENKDKNVQIEMGWV 216
Cdd:cd01906 160 LKALKSALERDLYSGGNIEVAVI 182
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-232 3.38e-44

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 148.83  E-value: 3.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965    6 TGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDG 85
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   86 FALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHT-LGISRPFGAgAFFMSWNKQTGGRLFLVEPSGLNYEYKAWA 164
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTqHGGVRPFGV-ALLIAGVDDGGPRLFETDPSGAYLEYKATA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71998965  165 VGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNvQIEMGWVGEQTnGKYEEVPSEVV 232
Cdd:PRK03996 167 IGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPE-NVEIAYIDVET-KKFRKLSVEEI 232
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-211 2.53e-43

proteasome_alpha_archeal. 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: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 145.94  E-value: 2.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   7 GYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGF 86
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  87 ALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHT-LGISRPFGAGAFFMSWNKqTGGRLFLVEPSGLNYEYKAWAV 165
Cdd:cd03756  81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTqHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYNEYKATAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71998965 166 GKHRQAAKAEIEKLKIEELDVNQLVKEAARIIM-VVRDENKDKNVQI 211
Cdd:cd03756 160 GSGRQAVTEFLEKEYKEDMSLEEAIELALKALYaALEENETPENVEI 206
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-195 1.16e-39

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: 136.27  E-value: 1.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKL--YTDnanpRMFNVNDNVGVAVAGNYPDG 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELssYQK----KIFKVDDHIGIAIAGLTADA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  86 FALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTLGIS-RPFGAGaFFMSWNKQTGGRLFLVEPSGLNYEYKAWA 164
Cdd:cd03749  77 RVLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGrRPYGVG-LLIAGYDESGPHLFQTCPSGNYFEYKATS 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 71998965 165 VGKHRQAAKAEIEK--LKIEELDVNQLVKEAAR 195
Cdd:cd03749 156 IGARSQSARTYLERhfEEFEDCSLEELIKHALR 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-216 2.82e-39

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: 135.55  E-value: 2.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLY-TDNANPRMFNVNDNVGVAVAGNYPDGF 86
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLdQSFSSEKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  87 ALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHT-LGISRPFGAGAFFMSWNKQTGGRLFLVEPSGlNYE-YKAWA 164
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTqYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSG-NYSgWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71998965 165 VGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWV 216
Cdd:cd03752 162 IGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-178 3.79e-36

proteasome_alpha_type_6. 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: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 127.35  E-value: 3.79e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   7 GYDLAASTFSPDGRIFQVEYAQKAVDNAG-TMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDG 85
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  86 FALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTLGIS-RPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWA 164
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYmRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170
                ....*....|....
gi 71998965 165 VGKHRQAAKAEIEK 178
Cdd:cd03754 161 AGVKEQEATNFLEK 174
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-211 2.12e-33

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: 120.16  E-value: 2.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGFA 87
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  88 LKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTL-GISRPFGAGAFFMSWNKQTGGRLFLVEPSGLNYEYKAWAVG 166
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQsGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 71998965 167 KHRQAAKAEIEKLKIEELDVNQLVKEAARIIM-VVrdENKDKNVQI 211
Cdd:cd03755 161 RNSKTVREFLEKNYKEEMTRDDTIKLAIKALLeVV--QSGSKNIEL 204
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-230 5.03e-32

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 117.65  E-value: 5.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965    8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTD-NANPRMFNVNDNVGVAVAGNYPDGF 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   87 ALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHT-LGISRPFGAGAFFMSWNKQTGGRLFLVEPSGlNYE-YKAWA 164
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTqFGGLRPFGVSFLFAGYDENLGYQLYHTDPSG-NYSgWKATA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71998965  165 VGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMG--WVGEQTNGKYEEVPSE 230
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGilSHGETDGEPIQKMLSE 231
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-211 9.80e-32

proteasome_alpha_type_5. 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: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 115.90  E-value: 9.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGFA 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  88 LKNYAYGEAMKWLKDYREPMPIQNIANSVAEyihihtLGI------------SRPFGAgAFFMSWNKQTGGRLFLVEPSG 155
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSD------LALqfgegddgkkamSRPFGV-ALLIAGVDENGPQLFHTDPSG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71998965 156 LNYEYKAWAVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKD-KNVQI 211
Cdd:cd03753 154 TFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNsTNVEL 210
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-178 2.81e-31

proteasome_alpha_type_2. 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: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 115.11  E-value: 2.81e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   8 YDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPRMFNVNDNVGVAVAGNYPDGFA 87
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  88 LKNYAYGEAMKWLKDYREPMPI----QNIANSVAEYIHihtLGISRPFGAGAFFMSWNKqTGGRLFLVEPSGLNYEYKAW 163
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVsqlvREIASVMQEYTQ---SGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKAT 156

                       170
                ....*....|....*
gi 71998965 164 AVGKHRQAAKAEIEK 178
Cdd:cd03750 157 AIGKNYSNAKTFLEK 171
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-230 1.14e-30

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 1.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965   5 GTGYDLAASTFSPDGRIFQVEYAQKAVDNAGTMIAIRGKNGVVVVADKLISSKLYTDNANPR-MFNVNDNVGVAVAGNYP 83
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEkIFKIDDHIGVAIAGLVA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  84 DGFALKNYAYGEAMKWLKDYREPMPIQNIANSVAEYIHIHTLGISRPFGAGAFFMSWNKQtGGRLFLVEPSGLNYEYKAW 163
Cdd:COG0638  86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGVRPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAV 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71998965 164 AVGKHRQAAKAEIEKLKIEELDVNQLVKEAARIIMVVRDENKDKNVQIEMGWVgeqTNGKYEEVPSE 230
Cdd:COG0638 165 AIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVI---TEDGFRELSEE 228
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-197 7.30e-28

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: 104.40  E-value: 7.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  35 GTMIAIRGKNGVVVVADKLISSKLYTDNAN-PRMFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMPIQNIA 113
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPvIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965 114 NSVAEYIHIHTLGisRPFGAGAFFMSWNKqTGGRLFLVEPSGLNYEY-KAWAVGKHRQAAKAEIEKLKIEELDVNQLVKE 192
Cdd:cd01901  81 KELAKLLQVYTQG--RPFGVNLIVAGVDE-GGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVEL 157


                ....*
gi 71998965 193 AARII 197
Cdd:cd01901 158 ALKAL 162
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 8-30 1.97e-11

Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 56.97  E-value: 1.97e-11
                          10        20
                  ....*....|....*....|...
gi 71998965     8 YDLAASTFSPDGRIFQVEYAQKA 30
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 2.75e-10

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 54.04  E-value: 2.75e-10
                           10        20
                   ....*....|....*....|...
gi 71998965      8 YDLAASTFSPDGRIFQVEYAQKA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-155 5.15e-10

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: 57.07  E-value: 5.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  35 GTMIAIRGKNGVVVVADKLISSKLYTDNAN-PRMFNVNDNVGVAVAGNYPDGFALKNYaygeAMKWLKDYR----EPMPI 109
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNfDKIFKISDNILLGTAGSAADTQALTRL----LKRNLRLYElrngRELSV 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71998965 110 QNIANSVAEYIHIHtlgisRPFGAGAFFM--SWNKQTGGRLFLVEPSG 155
Cdd:cd01912  77 KAAANLLSNILYSY-----RGFPYYVSLIvgGVDKGGGPFLYYVDPLG 119
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-197 6.75e-05

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: 42.62  E-value: 6.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965  36 TMIAIRGKNGVVVVADKLISSKLYTDNANPR-MFNVNDNVGVAVAGNYPDGFALKNYAYGEAMKWLKDYREPMPIQNIAN 114
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKkIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998965 115 SVAeyihiHTLGISRPFgagaFFMSWN-----KQTGGRLFLVEPSGLNYEYKAWAVGKHRQAAKAEIEKLKIEELDVNQL 189
Cdd:cd03764  82 LLS-----NILNSSKYF----PYIVQLliggvDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEA 152


                ....*...
gi 71998965 190 VKEAARII 197
Cdd:cd03764 153 KKLAIRAI 160
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-84 1.14e-03

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: 39.09  E-value: 1.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71998965  35 GTMIAIRGKNGVVVVADKLIS--SKLYTDNAnPRMFNVNDNVGVAVAGNYPD 84
Cdd:cd03760   3 TSVIAIKYKDGVIIAADTLGSygSLARFKNV-ERIFKVGDNTLLGASGDYAD 53
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-84 1.80e-03

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 38.38  E-value: 1.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998965  33 NAGTMIAIRGKNGVVVVADKLISSKLYTDNAN-PRMFNVNDNVGVAVAGNYPD 84
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDfQKVFRIGDRLYIGLAGLATD 54
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-89 9.97e-03

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: 36.08  E-value: 9.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71998965  31 VDNAGTMIAIRGKNGVVVVADKLISS--KLYTDNaNPRMFNVNDNVGVAVAGNYPDGFALK 89
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDTRLSEgySILSRD-SPKIFKLTDKCVLGSSGFQADILALT 64
 
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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