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Conserved domains on  [gi|300536583|emb|CBU84756|]
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unnamed protein product [Caenorhabditis elegans]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132891)

proteasome subunit alpha belonging to the peptidase T1A family, is a component of the proteasome complex that is involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-4 and fungal proteasome subunit alpha type-3

Gene Ontology:  GO:0051603|GO:0005839

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
3-213 1.37e-150

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: 418.29  E-value: 1.37e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   3 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITAD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  83 ANILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300536583 163 CIGSNHQAAVTLLKQEYK-SPNLEEAKQLAIKVLWKTLDV-KLASEKVEMAVL 213
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKdDMTLEEALALAVKVLSKTMDStKLTSEKLEFATL 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
3-213 1.37e-150

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: 418.29  E-value: 1.37e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   3 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITAD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  83 ANILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300536583 163 CIGSNHQAAVTLLKQEYK-SPNLEEAKQLAIKVLWKTLDV-KLASEKVEMAVL 213
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKdDMTLEEALALAVKVLSKTMDStKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
1-234 8.02e-105

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 304.08  E-value: 8.02e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   1 MARRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGIT 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  81 ADANILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300536583 161 ATCIGSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKL-ASEKVEMAVLTRR--DGKTVLEELTTKEVDALI 234
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDlTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILSHGetDGEPIQKMLSEKEIAELL 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
5-219 1.70e-75

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 228.30  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583    5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLD-DSVmtEKVYRLSDNISCTVAGITADA 83
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEpSSI--EKIFKIDDHIGAATSGLVADA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATC 163
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300536583  164 IGSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKLASEKVEMAVLTRRDGK 219
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDlSLDEAIELALKALYSAVEDKLTPENVEVAYITVEDKK 216
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
28-213 3.89e-62

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: 193.17  E-value: 3.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   28 ISHAGTCLGILSSEGIVVAAERKNV--HKLLDDSvMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEM 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKD-TVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  106 PVEqLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKSP-NL 184
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDlTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 300536583  185 EEAKQLAIKVLWKTLD-VKLASEKVEMAVL 213
Cdd:pfam00227 159 EEAVELAVKALKEAIDrDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
5-229 3.40e-58

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 184.58  E-value: 3.40e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADAN 84
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGkRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATCI 164
Cdd:COG0638   89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAI 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300536583 165 GSNHQAAVTLLKQEYKsPNL--EEAKQLAIKVLWKTLDVKLAS-EKVEMAVLTrRDGktvLEELTTKE 229
Cdd:COG0638  167 GSGSPFARGVLEKEYR-EDLslDEAVELALRALYSAAERDSASgDGIDVAVIT-EDG---FRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
5-27 2.52e-11

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: 56.74  E-value: 2.52e-11
                           10        20
                   ....*....|....*....|...
gi 300536583     5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
3-213 1.37e-150

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: 418.29  E-value: 1.37e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   3 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITAD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  83 ANILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300536583 163 CIGSNHQAAVTLLKQEYK-SPNLEEAKQLAIKVLWKTLDV-KLASEKVEMAVL 213
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKdDMTLEEALALAVKVLSKTMDStKLTSEKLEFATL 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-213 6.44e-115

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: 327.86  E-value: 6.44e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMtEKVYRLSDNISCTVAGITADAN 84
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCI 164
Cdd:cd01911   80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300536583 165 GSNHQAAVTLLKQEYKS-PNLEEAKQLAIKVLWKTLDVKLASEKVEMAVL 213
Cdd:cd01911  160 GKGSQEAKTFLEKRYKKdLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
1-234 8.02e-105

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 304.08  E-value: 8.02e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   1 MARRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGIT 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  81 ADANILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300536583 161 ATCIGSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKL-ASEKVEMAVLTRR--DGKTVLEELTTKEVDALI 234
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDlTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILSHGetDGEPIQKMLSEKEIAELL 238
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-234 2.93e-78

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 235.88  E-value: 2.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVmTEKVYRLSDNISCTVAGITADAN 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATCI 164
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300536583 165 GSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKLASEKVEMAVLTRRDGKtvLEELTTKEVDALI 234
Cdd:PRK03996 168 GAGRDTVMEFLEKNYKEDlSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKK--FRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
5-219 1.70e-75

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 228.30  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583    5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLD-DSVmtEKVYRLSDNISCTVAGITADA 83
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEpSSI--EKIFKIDDHIGAATSGLVADA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATC 163
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300536583  164 IGSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKLASEKVEMAVLTRRDGK 219
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDlSLDEAIELALKALYSAVEDKLTPENVEVAYITVEDKK 216
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-214 3.80e-74

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: 224.52  E-value: 3.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLD-DSVmtEKVYRLSDNISCTVAGITADA 83
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEpESI--EKIYKIDDHVGAATSGLVADA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATC 163
Cdd:cd03756   80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300536583 164 IGSNHQAAVTLLKQEYKSP-NLEEAKQLAIKVLWKTLDVKLASEKVEMAVLT 214
Cdd:cd03756  159 IGSGRQAVTEFLEKEYKEDmSLEEAIELALKALYAALEENETPENVEIAYVT 210
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
10-223 4.83e-63

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: 196.77  E-value: 4.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  10 TIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKnVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINH 89
Cdd:cd03750    6 TTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKK-VPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  90 LRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKhYGYQLYQSDPSGNYTGWKATCIGSNHQ 169
Cdd:cd03750   85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKATAIGKNYS 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300536583 170 AAVTLLKQEY-KSPNLEEAKQLAIKVLWKTLDVKLASEKVEMAVLTRRDGKTVLE 223
Cdd:cd03750  164 NAKTFLEKRYnEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLT 218
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
28-213 3.89e-62

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: 193.17  E-value: 3.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   28 ISHAGTCLGILSSEGIVVAAERKNV--HKLLDDSvMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEM 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKD-TVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  106 PVEqLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKSP-NL 184
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDlTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 300536583  185 EEAKQLAIKVLWKTLD-VKLASEKVEMAVL 213
Cdd:pfam00227 159 EEAVELAVKALKEAIDrDALSGGNIEVAVI 188
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-213 6.20e-62

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: 193.35  E-value: 6.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVmTEKVYRLSDNISCTVAGITADAN 84
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRT-VRKICMLDDHVCLAFAGLTADAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCI 164
Cdd:cd03755   80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300536583 165 GSNHQAAVTLLKQEYK-SPNLEEAKQLAIKVLWKTldVKLASEKVEMAVL 213
Cdd:cd03755  160 GRNSKTVREFLEKNYKeEMTRDDTIKLAIKALLEV--VQSGSKNIELAVM 207
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
32-213 3.52e-60

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: 187.70  E-value: 3.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  32 GTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPVEQLV 111
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 112 QNLCNEKQRYTQigGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKS-PNLEEAKQL 190
Cdd:cd01906   81 KLLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPdMTLEEAIEL 158
                        170       180
                 ....*....|....*....|....
gi 300536583 191 AIKVLWKTLDVKLAS-EKVEMAVL 213
Cdd:cd01906  159 ALKALKSALERDLYSgGNIEVAVI 182
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-213 2.88e-59

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: 186.77  E-value: 2.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLD-DSVmtEKVYRLSDNISCTVAGITADA 83
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEpSSV--EKIMEIDDHIGCAMSGLIADA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGK-----RPFGVSLLYIGWDKHyGYQLYQSDPSGNYTG 158
Cdd:cd03753   79 RTLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 300536583 159 WKATCIGSNHQAAVTLLKQEY-KSPNLEEAKQLAIKVLWKTLDVKLASEKVEMAVL 213
Cdd:cd03753  158 CDAKAIGSGSEGAQSSLQEKYhKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-212 6.96e-59

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: 185.90  E-value: 6.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILSSEGIVVAAERKNVHKLLDDSVMTEkVYRLSDNISCTVAGITADA 83
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTH-LFRITDEIGCVMTGMIADS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATC 163
Cdd:cd03754   81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300536583 164 IGSNHQAAVTLL-----KQEYKSPNLEEAKQLAIKVLWKTLDVKLASEKVEMAV 212
Cdd:cd03754  161 AGVKEQEATNFLekklkKKPDLIESYEETVELAISCLQTVLSTDFKATEIEVGV 214
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
5-229 3.40e-58

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 184.58  E-value: 3.40e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADAN 84
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGkRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATCI 164
Cdd:COG0638   89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAI 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300536583 165 GSNHQAAVTLLKQEYKsPNL--EEAKQLAIKVLWKTLDVKLAS-EKVEMAVLTrRDGktvLEELTTKE 229
Cdd:COG0638  167 GSGSPFARGVLEKEYR-EDLslDEAVELALRALYSAAERDSASgDGIDVAVIT-EDG---FRELSEEE 229
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-213 1.95e-57

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: 181.72  E-value: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAERKNVHKLlddSVMTEKVYRLSDNISCTVAGITADAN 84
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  85 ILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATCI 164
Cdd:cd03749   78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300536583 165 GSNHQAAVTLLKQ---EYKSPNLEEAKQLAIKVLWKTL--DVKLASEKVEMAVL 213
Cdd:cd03749  157 GARSQSARTYLERhfeEFEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIV 210
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-211 2.85e-48

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: 158.60  E-value: 2.85e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583   5 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILSSEGIVVAAErKNVH-KLLDDSVmTEKVYRLSDNISCTVAGITADA 83
Cdd:cd03751    4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVE-KLVTsKLYEPGS-NKRIFNVDRHIGIAVAGLLADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  84 NILINHLRWWAASYRNSYGEEMPVEQLVQNLCNEKQRYTQIGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATC 163
Cdd:cd03751   82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGCA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300536583 164 IGSNHQAAVTLL-KQEYKSPNLEEAKQLAIKVLWKTLD-VKLASEKVEMA 211
Cdd:cd03751  161 IGKGKQAAKTELeKLKFSELTCREAVKEAAKIIYIVHDeIKDKAFELELS 210
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
32-195 2.60e-40

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: 136.37  E-value: 2.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  32 GTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPVEQLV 111
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 112 QNLCNEKQRYTQiggKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGW-KATCIGSNHQAAVTLLKQEYKS-PNLEEAKQ 189
Cdd:cd01901   81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPdMTLEEAVE 156

                 ....*.
gi 300536583 190 LAIKVL 195
Cdd:cd01901  157 LALKAL 162
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
33-223 4.86e-21

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: 86.92  E-value: 4.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  33 TCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPVE---Q 109
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKalaT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 110 LVQNLCNEkqrytqiGGKRPFGVSLLYIGWDKHyGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKsPNL--EEA 187
Cdd:cd03764   82 LLSNILNS-------SKYFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYK-EDMtvEEA 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 300536583 188 KQLAIKVLWKTLDVKLAS-EKVEMAVLTrRDGKTVLE 223
Cdd:cd03764  153 KKLAIRAIKSAIERDSASgDGIDVVVIT-KDGYKELE 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
32-218 2.40e-19

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: 82.49  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  32 GTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPVE--- 108
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKaaa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 109 QLVQNLCNEKQRYtqiggkrPFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKsPNL--EE 186
Cdd:cd01912   81 NLLSNILYSYRGF-------PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYK-PDMtlEE 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 300536583 187 AKQLAIKVlwktldvklasekveMAVLTRRDG 218
Cdd:cd01912  153 AVELVKKA---------------IDSAIERDL 169
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
5-27 2.52e-11

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: 56.74  E-value: 2.52e-11
                           10        20
                   ....*....|....*....|...
gi 300536583     5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
5-27 5.20e-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: 55.82  E-value: 5.20e-11
                          10        20
                  ....*....|....*....|...
gi 300536583    5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
33-193 3.72e-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: 54.90  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  33 TCLGILSSEGIVVAAE-RKNVHKLLDDSvMTEKVYRLSDNISCTVAGITADAniliNHLRWWAAS----YRNSYGEEMPV 107
Cdd:cd03763    2 TIVGVVFKDGVVLGADtRATEGPIVADK-NCEKIHYIAPNIYCCGAGTAADT----EAVTNMISSnlelHRLNTGRKPRV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 108 EQLVQNLCNEKQRYTqiGGKrpfGVSLLYIGWDKhYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKsPNL--E 185
Cdd:cd03763   77 VTALTMLKQHLFRYQ--GHI---GAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYK-PDMteE 149

                 ....*...
gi 300536583 186 EAKQLAIK 193
Cdd:cd03763  150 EAKKLVCE 157
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
28-190 1.19e-06

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: 48.02  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  28 ISHAGTCLGILSSEGIVVAA-----ERKNVHkllddSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYG 102
Cdd:cd03757    5 TDNGGTVLAIAGNDFAVIAGdtrlsEGYSIL-----SRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 103 EEMPVEQLVQNLCnekqryTQIGGKR--PFGVSLLYIGWDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQ--E 178
Cdd:cd03757   80 KEMSTEAIAQLLS------TILYSRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvG 153
                        170
                 ....*....|..
gi 300536583 179 YKSPNLEEAKQL 190
Cdd:cd03757  154 RKNQNNVERTPL 165
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
28-196 4.59e-05

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 43.44  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  28 ISHAGTCLGILSSEGIVVAAERKNVHKLLDDSVMTEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPV 107
Cdd:PTZ00488  36 FAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 108 EQLVQNLCNEKQRYtqiggkRPFGVSL--LYIGWDKHyGYQLYQSDPSGN-YTGWKATCiGSNHQAAVTLLKQEYK-SPN 183
Cdd:PTZ00488 116 AAASKILANIVWNY------KGMGLSMgtMICGWDKK-GPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKwDLN 187
                        170
                 ....*....|...
gi 300536583 184 LEEAKQLAIKVLW 196
Cdd:PTZ00488 188 DEEAQDLGRRAIY 200
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
33-193 2.10e-04

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: 41.03  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  33 TCLGILSSEGIVVAAERKNVH--KLLDDSVmtEKVYRLSDNISCTVAGITADAN-----ILIN-HLRwwaaSYRNSYgeE 104
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARsiLVLKDDE--DKIYKLSDHKLMACSGEAGDRLqfaeyIQKNiQLY----KMRNGY--E 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583 105 MPVEQLVQNLCNEKQRYTQIGGkrPFGVSLLYIGWDKHYGYQLYQSDpsgnYTGwkaTCIGSNHQA-------AVTLLKQ 177
Cdd:cd03758   75 LSPKAAANFTRRELAESLRSRT--PYQVNLLLAGYDKVEGPSLYYID----YLG---TLVKVPYAAhgygayfCLSILDR 145
                        170
                 ....*....|....*...
gi 300536583 178 EYKsPNL--EEAKQLAIK 193
Cdd:cd03758  146 YYK-PDMtvEEALELMKK 162
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
62-195 3.82e-04

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: 40.29  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300536583  62 TEKVYRLSDNISCTVAGITADANILINHLRWWAASYRNSYGEEMPVE---QLVQNLCNEKQRYTQIGgkrpfgvsLLYIG 138
Cdd:cd03762   31 TDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKtaaSLFKNLCYNYKEMLSAG--------IIVAG 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300536583 139 WDKHYGYQLYQSDPSGNYTGWKATCIGSNHQAAVTLLKQEYKsPN--LEEAKQLAIKVL 195
Cdd:cd03762  103 WDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYK-PGmtLEECIKFVKNAL 160
 
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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