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Conserved domains on  [gi|1101274132|pdb|5L5R|Q]
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Chain Q, Proteasome subunit alpha type-4

Protein Classification

proteasome subunit alpha( domain architecture ID 10132902)

proteasome subunit alpha 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-7, -8 and fungal proteasome subunit alpha type-4

Gene Ontology:  GO:0051603|GO:0005839
PubMed:  7682410|7697118|1317508|8882582

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 5.55e-136

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: 381.33  E-value: 5.55e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPR-TVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDP-DGTPRLYQTDPSGTYSAWKANA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
5L5R_Q      164 IGRNSKTVREFLEKNYDRKEppaTVEECVKLTVRSLLEVVQTGAKNIEITVV 215
Cdd:cd03755 159 IGRNSKTVREFLEKNYKEEM---TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 5.55e-136

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: 381.33  E-value: 5.55e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPR-TVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDP-DGTPRLYQTDPSGTYSAWKANA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
5L5R_Q      164 IGRNSKTVREFLEKNYDRKEppaTVEECVKLTVRSLLEVVQTGAKNIEITVV 215
Cdd:cd03755 159 IGRNSKTVREFLEKNYKEEM---TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-236 3.74e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.02  E-value: 3.74e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         1 MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNA 80
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPS-SIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        81 DSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWS 160
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYLEYK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5L5R_Q       161 AQTIGRNSKTVREFLEKNYDrkePPATVEECVKLTVRSLLEVVQ--TGAKNIEITVVKPDSDIV-ALSSEEINQYVTQI 236
Cdd:PRK03996 164 ATAIGAGRDTVMEFLEKNYK---EDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVETKKFrKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-219 3.02e-83

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: 248.33  E-value: 3.02e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q          2 SGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLqdtrITPS---KVSKIDSHVVLSFSGL 78
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKL----VEPSsieKIFKIDDHIGAATSGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         79 NADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSS 158
Cdd:TIGR03633  77 VADARVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
5L5R_Q        159 WSAQTIGRNSKTVREFLEKNYDRKeppATVEECVKLTVRSLLEVVQ--TGAKNIEITVVKPDS 219
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYRED---LSLDEAIELALKALYSAVEdkLTPENVEVAYITVED 214
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-218 3.58e-68

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 210.00  E-value: 3.58e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        1 MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTL-KLQDTRiTPSKVSKIDSHVVLSFSGLN 79
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASK-SIEKIFKIDDHIGVAIAGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       80 ADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSgGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSW 159
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEE 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5L5R_Q      160 SAQTIGRNSKTVREFLEKNYDrkePPATVEECVKLTVRSLLEVVQ----TGaKNIEITVVKPD 218
Cdd:COG0638 162 KAVAIGSGSPFARGVLEKEYR---EDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITED 220
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-215 2.05e-63

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: 196.63  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         27 VKRGTCAVGVKGKNCVVLGCERRSTL--KLQDTRiTPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPV 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKD-TVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        105 TVEyLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDpRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYdrkEP 184
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYD-EDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY---RP 154

                         170       180       190
                  ....*....|....*....|....*....|....
5L5R_Q        185 PATVEECVKLTVRSLLEVVQ---TGAKNIEITVV 215
Cdd:pfam00227 155 DLTLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 5.58e-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: 55.97  E-value: 5.58e-11
                           10        20
                   ....*....|....*....|...
5L5R_Q           4 YDRALSIFSPDGHIFQVEYALEA 26
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 5.55e-136

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: 381.33  E-value: 5.55e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPR-TVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDP-DGTPRLYQTDPSGTYSAWKANA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
5L5R_Q      164 IGRNSKTVREFLEKNYDRKEppaTVEECVKLTVRSLLEVVQTGAKNIEITVV 215
Cdd:cd03755 159 IGRNSKTVREFLEKNYKEEM---TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 1.49e-106

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: 306.68  E-value: 1.49e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPS-SVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDE-EGGPQLYQTDPSGTYFGYKATA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
5L5R_Q      164 IGRNSKTVREFLEKNYDRKEppaTVEECVKLTVRSLLEVVQTG--AKNIEITVV 215
Cdd:cd01911 159 IGKGSQEAKTFLEKRYKKDL---TLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-236 3.74e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.02  E-value: 3.74e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         1 MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNA 80
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPS-SIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        81 DSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWS 160
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYLEYK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5L5R_Q       161 AQTIGRNSKTVREFLEKNYDrkePPATVEECVKLTVRSLLEVVQ--TGAKNIEITVVKPDSDIV-ALSSEEINQYVTQI 236
Cdd:PRK03996 164 ATAIGAGRDTVMEFLEKNYK---EDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVETKKFrKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-219 3.02e-83

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: 248.33  E-value: 3.02e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q          2 SGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLqdtrITPS---KVSKIDSHVVLSFSGL 78
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKL----VEPSsieKIFKIDDHIGAATSGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         79 NADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSS 158
Cdd:TIGR03633  77 VADARVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
5L5R_Q        159 WSAQTIGRNSKTVREFLEKNYDRKeppATVEECVKLTVRSLLEVVQ--TGAKNIEITVVKPDS 219
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYRED---LSLDEAIELALKALYSAVEdkLTPENVEVAYITVED 214
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-216 8.75e-82

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: 244.16  E-value: 8.75e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        3 GYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADS 82
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       83 RILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWSAQ 162
Cdd:cd03756  80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYNEYKAT 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
5L5R_Q      163 TIGRNSKTVREFLEKNYDRKeppATVEECVKLTVRSLLEVVQ--TGAKNIEITVVK 216
Cdd:cd03756 158 AIGSGRQAVTEFLEKEYKED---MSLEEAIELALKALYAALEenETPENVEIAYVT 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-218 3.58e-68

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 210.00  E-value: 3.58e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        1 MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTL-KLQDTRiTPSKVSKIDSHVVLSFSGLN 79
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASK-SIEKIFKIDDHIGVAIAGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       80 ADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSgGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSW 159
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEE 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5L5R_Q      160 SAQTIGRNSKTVREFLEKNYDrkePPATVEECVKLTVRSLLEVVQ----TGaKNIEITVVKPD 218
Cdd:COG0638 162 KAVAIGSGSPFARGVLEKEYR---EDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITED 220
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-232 8.35e-65

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: 201.40  E-value: 8.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRiTPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDES-SVHKVEQITPHIGMVYSGMGPDFR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03750  80 VLVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD--EGGPYLYQVDPSGSYFTWKATA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      164 IGRNSKTVREFLEKNY-DRKEPPATVEECVkLTVRSLLEVVQTgAKNIEITVVKPDSDIVALSSEEINQY 232
Cdd:cd03750 158 IGKNYSNAKTFLEKRYnEDLELEDAIHTAI-LTLKEGFEGQMT-EKNIEIGICGETKGFRLLTPAEIKDY 225
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-215 2.05e-63

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: 196.63  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         27 VKRGTCAVGVKGKNCVVLGCERRSTL--KLQDTRiTPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPV 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKD-TVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        105 TVEyLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDpRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYdrkEP 184
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYD-EDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY---RP 154

                         170       180       190
                  ....*....|....*....|....*....|....
5L5R_Q        185 PATVEECVKLTVRSLLEVVQ---TGAKNIEITVV 215
Cdd:pfam00227 155 DLTLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-218 1.74e-62

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: 194.87  E-value: 1.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDpRDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWD-KHYGFQLYQSDPSGNYSGWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
5L5R_Q      164 IGRNSKTVREFLEKNYdrkEPPATVEECVKLTVRSLlevvqtgAKNIEITVVKPD 218
Cdd:cd03752 162 IGNNNQAAQSLLKQDY---KDDMTLEEALALAVKVL-------SKTMDSTKLTSE 206
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 8.94e-58

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: 182.92  E-value: 8.94e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQD-TRItpSKVSKIDSHVVLSFSGLNADS 82
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEpSSV--EKIMEIDDHIGCAMSGLIADA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       83 RILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGV-----RPFGVSTLIAGFDprDDEPKLYQTEPSGIYS 157
Cdd:cd03753  79 RTLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVD--ENGPQLFHTDPSGTFT 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      158 SWSAQTIGRNSKTVREFLEKNYDRKeppATVEECVKLTVRSLLEVVQT--GAKNIEITVV 215
Cdd:cd03753 157 RCDAKAIGSGSEGAQSSLQEKYHKD---MTLEEAEKLALSILKQVMEEklNSTNVELATV 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-215 1.66e-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: 182.11  E-value: 1.66e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRitpSKVSKIDSHVVLSFSGLNADSR 83
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ---KKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWSAQT 163
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD--ESGPHLFQTCPSGNYFEYKATS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
5L5R_Q      164 IGRNSKTVREFLEKNYDrKEPPATVEECVKLTVRSLLEVVQTG----AKNIEITVV 215
Cdd:cd03749 156 IGARSQSARTYLERHFE-EFEDCSLEELIKHALRALRETLPGEqeltIKNVSIAIV 210
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 31-215 2.44e-57

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: 180.77  E-value: 2.44e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLT 110
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      111 RYVAGVQQRYTQSggVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYdrkEPPATVEE 190
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDE-EGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY---KPDMTLEE 154

                       170       180
                ....*....|....*....|....*...
5L5R_Q      191 CVKLTVRSLLEVVQTGA---KNIEITVV 215
Cdd:cd01906 155 AIELALKALKSALERDLysgGNIEVAVI 182
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 4-235 3.44e-51

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 167.34  E-value: 3.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q         4 YDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSR 83
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        84 ILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEpKLYQTEPSGIYSSWSAQT 163
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGY-QLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5L5R_Q       164 IGRNSKTVREFLEKNYDRKeppATVEECVKLTVRSLLEVVQT---GAKNIEITVVKPDSDivalSSEEINQYVTQ 235
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKED---LTLEQGLLLAAKVLTKSMDStspKADKIEVGILSHGET----DGEPIQKMLSE 231
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-202 1.36e-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: 159.37  E-value: 1.36e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        2 SGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPsKVSKIDSHVVLSFSGLNAD 81
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNK-RIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       82 SRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWSA 161
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYD--SDGPQLYMIEPSGVSYGYFG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
5L5R_Q      162 QTIGRNSKTVREFLEKnydRKEPPATVEECVKLTVRSLLEV 202
Cdd:cd03751 159 CAIGKGKQAAKTELEK---LKFSELTCREAVKEAAKIIYIV 196
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 2.41e-46

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: 153.93  E-value: 2.41e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q        3 GYDRALSIFSPDGHIFQVEYALEAVKR-GTCAVGVKGKNCVVLGCERrstlKLQDTRITPSKVS---KIDSHVVLSFSGL 78
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNaGLTSVAVRGKDCAVVVTQK----KVPDKLIDPSTVThlfRITDEIGCVMTGM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       79 NADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPrDDEPKLYQTEPSGIYSS 158
Cdd:cd03754  77 IADSRSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDE-ELGPQLYKCDPAGYFAG 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      159 WSAQTIGRNSKTVREFLEKNYDRKE-PPATVEECVKLTVRSLLEVVQTG--AKNIEITVV 215
Cdd:cd03754 156 YKATAAGVKEQEATNFLEKKLKKKPdLIESYEETVELAISCLQTVLSTDfkATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 31-201 8.31e-38

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: 130.21  E-value: 8.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLT 110
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      111 RYVAGVQQRYTQsggVRPFGVSTLIAGFDprDDEPKLYQTEPSGIYSSWS-AQTIGRNSKTVREFLEKNYdrkEPPATVE 189
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVD--EGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLY---KPDMTLE 152

                       170
                ....*....|..
5L5R_Q      190 ECVKLTVRSLLE 201
Cdd:cd01901 153 EAVELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-218 9.95e-22

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: 89.04  E-value: 9.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLT 110
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      111 RYVAGVQQRYtQSGgvrPFGVSTLIAGFDPrDDEPKLYQTEPSG--IYSSWSAQTIGrnSKTVREFLEKNYdrkEPPATV 188
Cdd:cd01912  81 NLLSNILYSY-RGF---PYYVSLIVGGVDK-GGGPFLYYVDPLGslIEAPFVATGSG--SKYAYGILDRGY---KPDMTL 150

                       170       180       190
                ....*....|....*....|....*....|....
5L5R_Q      189 EECVKLTVRSLLEV----VQTGaKNIEITVVKPD 218
Cdd:cd01912 151 EEAVELVKKAIDSAierdLSSG-GGVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-199 4.45e-16

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: 73.83  E-value: 4.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLT 110
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      111 RYVAGVqqryTQSGGVRPFGVSTLIAGFDprDDEPKLYQTEPSG--IYSSWSAQtiGRNSKTVREFLEKNYDRKeppATV 188
Cdd:cd03764  81 TLLSNI----LNSSKYFPYIVQLLIGGVD--EEGPHLYSLDPLGsiIEDKYTAT--GSGSPYAYGVLEDEYKED---MTV 149

                       170
                ....*....|.
5L5R_Q      189 EECVKLTVRSL 199
Cdd:cd03764 150 EEAKKLAIRAI 160
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 5.58e-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: 55.97  E-value: 5.58e-11
                           10        20
                   ....*....|....*....|...
5L5R_Q           4 YDRALSIFSPDGHIFQVEYALEA 26
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 ...
 4-26 9.19e-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: 55.05  E-value: 9.19e-11
                          10        20
                  ....*....|....*....|...
5L5R_Q          4 YDRALSIFSPDGHIFQVEYALEA 26
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-145 2.45e-07

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: 49.55  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       30 GTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYL 109
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                        90       100       110
                ....*....|....*....|....*....|....*...
5L5R_Q      110 TRYVAGV--QQRYTqsggvrPFGVSTLIAGFDPrDDEP 145
Cdd:cd03759  83 SSLISSLlyEKRFG------PYFVEPVVAGLDP-DGKP 113
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-218 8.39e-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: 45.33  E-value: 8.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       30 GTCaVGVKGKN-CVVLGCERRSTLKLQDTRITPsKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEY 108
Cdd:cd03757   9 GTV-LAIAGNDfAVIAGDTRLSEGYSILSRDSP-KIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      109 LTRYVAGV--QQRYTqsggvrPFGVSTLIAGFDpRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLE-----KN-YD 180
Cdd:cd03757  87 IAQLLSTIlySRRFF------PYYVFNILAGID-EEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrKNqNN 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
5L5R_Q      181 RKEPPATVEECVKLTV---RSLLEV-VQTGaKNIEITVVKPD 218
Cdd:cd03757 160 VERTPLSLEEAVSLVKdafTSAAERdIYTG-DSLEIVIITKD 200
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-194 3.39e-05

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: 43.34  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERRSTlklQDTRI---TPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRL-TLEDPVTV 106
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRAT---EGPIVadkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLnTGRKPRVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      107 EYLTRyvagVQQ---RYtqSGGVrpfGVSTLIAGFDPRDdePKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYdrkE 183
Cdd:cd03763  78 TALTM----LKQhlfRY--QGHI---GAALVLGGVDYTG--PHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRY---K 143

                       170
                ....*....|.
5L5R_Q      184 PPATVEECVKL 194
Cdd:cd03763 144 PDMTEEEAKKL 154
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-199 1.99e-03

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: 37.97  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q       31 TCAVGVKGKNCVVLGCERR-STLKLQDTRITpSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYL 109
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRtSTGSYVANRVT-DKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5R_Q      110 TRYVAGVQQRYTQ--SGGVrpfgvstLIAGFDPRdDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYdrkEPPAT 187
Cdd:cd03762  80 ASLFKNLCYNYKEmlSAGI-------IVAGWDEQ-NGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANY---KPGMT 148

                       170
                ....*....|..
5L5R_Q      188 VEECVKLTVRSL 199
Cdd:cd03762 149 LEECIKFVKNAL 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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