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Conserved domains on  [gi|1101273882|pdb|5L5D|S]
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Chain S, Proteasome subunit alpha type-6

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 6-217 4.20e-110

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.


The actual alignment was detected with superfamily member cd03749:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 211  Bit Score: 315.00  E-value: 4.20e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       86 NYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
5L5D_S      166 QGAKTYLERTLDTFikIDGNPDELIKAGVEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749 161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
 
Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-217 4.20e-110

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: 315.00  E-value: 4.20e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       86 NYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
5L5D_S      166 QGAKTYLERTLDTFikIDGNPDELIKAGVEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749 161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-234 1.32e-53

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 172.33  E-value: 1.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S         6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDEHMGLSLAGLAPDAR 82
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIEK-IFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        83 VLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIG 162
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5L5D_S       163 ARSQGAKTYLERTLDTfikiDGNPDELIKAGVEAISQSLrDESLTVDNLSIAIVGKDTP-FTIYDGEAVAKYI 234
Cdd:PRK03996 169 AGRDTVMEFLEKNYKE----DLSLEEAIELALKALAKAN-EGKLDPENVEIAYIDVETKkFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-216 4.53e-49

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: 159.27  E-value: 4.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S         29 IKQGSVTVGLRSNTHAVLVALKRN---ADELSSYQ-KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrgSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        105 VERAGHlLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGA-HLLEFQPSGNVTELYGTAIGARSQGAKTYLERtldtFIKID 183
Cdd:pfam00227  81 VELAAR-IADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK----LYRPD 155

                         170       180       190
                  ....*....|....*....|....*....|...
5L5D_S        184 GNPDELIKAGVEAISQSLRDESLTVDNLSIAIV 216
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-220 1.27e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.14  E-value: 1.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNAdeLSSYQ-----KKIIKCDEHMGLSLAGLAPD 80
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAT--MGNLIasksiEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       81 ARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQsYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTA 160
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVA 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      161 IGARSQGAKTYLERTLDTfikiDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDT 220
Cdd:COG0638 166 IGSGSPFARGVLEKEYRE----DLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDG 221
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 7.51e-09

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: 49.80  E-value: 7.51e-09
                           10        20
                   ....*....|....*....|...
5L5D_S           6 YDGDTVTFSPTGRLFQVEYALEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-217 4.20e-110

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: 315.00  E-value: 4.20e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       86 NYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
5L5D_S      166 QGAKTYLERTLDTFikIDGNPDELIKAGVEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749 161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 2.95e-81

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: 241.58  E-value: 2.95e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDEHMGLSLAGLAPDARV 83
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLldPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       84 LSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKS-GAHLLEFQPSGNVTELYGTAIG 162
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
5L5D_S      163 ARSQGAKTYLERTLDTFIkidgNPDELIKAGVEAISQSLrDESLTVDNLSIAIV 216
Cdd:cd01911 161 KGSQEAKTFLEKRYKKDL----TLEEAIKLALKALKEVL-EEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-234 1.32e-53

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 172.33  E-value: 1.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S         6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDEHMGLSLAGLAPDAR 82
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIEK-IFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        83 VLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIG 162
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5L5D_S       163 ARSQGAKTYLERTLDTfikiDGNPDELIKAGVEAISQSLrDESLTVDNLSIAIVGKDTP-FTIYDGEAVAKYI 234
Cdd:PRK03996 169 AGRDTVMEFLEKNYKE----DLSLEEAIELALKALAKAN-EGKLDPENVEIAYIDVETKkFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-216 4.53e-49

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: 159.27  E-value: 4.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S         29 IKQGSVTVGLRSNTHAVLVALKRN---ADELSSYQ-KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrgSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        105 VERAGHlLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGA-HLLEFQPSGNVTELYGTAIGARSQGAKTYLERtldtFIKID 183
Cdd:pfam00227  81 VELAAR-IADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK----LYRPD 155

                         170       180       190
                  ....*....|....*....|....*....|...
5L5D_S        184 GNPDELIKAGVEAISQSLRDESLTVDNLSIAIV 216
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 8.41e-49

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: 159.42  E-value: 8.41e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDEHMGLSLAGLAPDAR 82
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLvepESIEK-IYKIDDHVGAATSGLVADAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       83 VLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIG 162
Cdd:cd03756  81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
5L5D_S      163 ARSQGAKTYLERTLdtfiKIDGNPDELIKAGVEAISQSLRDEsLTVDNLSIAIV 216
Cdd:cd03756 161 SGRQAVTEFLEKEY----KEDMSLEEAIELALKALYAALEEN-ETPENVEIAYV 209
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 8.40e-46

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: 151.73  E-value: 8.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQK---KIIKCDEHMGLSLAGLAPDAR 82
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFsseKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       83 VLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQsYGG-RPYGVGLLIIGYDKS-GAHLLEFQPSGNVTELYGTA 160
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQ-YGGlRPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
5L5D_S      161 IGARSQGAKTYLERTldtfIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIV 216
Cdd:cd03752 162 IGNNNQAAQSLLKQD----YKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-220 1.27e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.14  E-value: 1.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNAdeLSSYQ-----KKIIKCDEHMGLSLAGLAPD 80
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAT--MGNLIasksiEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       81 ARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQsYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTA 160
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVA 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      161 IGARSQGAKTYLERTLDTfikiDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDT 220
Cdd:COG0638 166 IGSGSPFARGVLEKEYRE----DLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDG 221
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 2.05e-43

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: 145.56  E-value: 2.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDEHMGLSLAGLAPDARV 83
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLmePSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       84 LSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKA-----QKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYG 158
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgeGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
5L5D_S      159 TAIGARSQGAKTYLErtlDTFIKiDGNPDELIKAGVEAISQSLrDESLTVDNLSIAIV 216
Cdd:cd03753 161 KAIGSGSEGAQSSLQ---EKYHK-DMTLEEAEKLALSILKQVM-EEKLNSTNVELATV 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-216 8.38e-41

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: 137.63  E-value: 8.38e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       35 TVGLRSNTHAVLVALKRNA---DELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHL 111
Cdd:cd01906   3 IVGIKGKDGVVLAADKRVTsglLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      112 LCDKAQKNTQSYggRPYGVGLLIIGYDK-SGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERtldtFIKIDGNPDELI 190
Cdd:cd01906  83 LANLLYEYTQSL--RPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEK----LYKPDMTLEEAI 156

                       170       180
                ....*....|....*....|....*.
5L5D_S      191 KAGVEAISQSLRDESLTVDNLSIAIV 216
Cdd:cd01906 157 ELALKALKSALERDLYSGGNIEVAVI 182
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-234 1.58e-39

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: 135.91  E-value: 1.58e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       12 TFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSY--QKKIIKCDEHMGLSLAGLAPDARVLSNYLR 89
Cdd:cd03750   7 TFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDEssVHKVEQITPHIGMVYSGMGPDFRVLVKKAR 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       90 QQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAK 169
Cdd:cd03750  87 KIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAK 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
5L5D_S      170 TYLERTLDTFIKIDGNpdelIKAGVEAISQSLrDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI 234
Cdd:cd03750 167 TFLEKRYNEDLELEDA----IHTAILTLKEGF-EGQMTEKNIEIGICGETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 1.22e-38

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: 132.87  E-value: 1.22e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDEHMGLSLAGLAPDARV 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLqdPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       84 LSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSG-AHLLEFQPSGNVTELYGTAIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
5L5D_S      163 ARSQGAKTYLERTLdtfiKIDGNPDELIKAGVEAISQSLRDESltvDNLSIAIV 216
Cdd:cd03755 161 RNSKTVREFLEKNY----KEEMTRDDTIKLAIKALLEVVQSGS---KNIELAVM 207
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 6-234 4.88e-37

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 130.36  E-value: 4.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S         6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQK---KIIKCDEHMGLSLAGLAPDAR 82
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKineKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        83 VLSNYLR---QQCNYSslvFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYD-KSGAHLLEFQPSGNVTELYG 158
Cdd:PTZ00246  85 ILINQCRlyaQRYRYT---YGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDeNLGYQLYHTDPSGNYSGWKA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5L5D_S       159 TAIGARSQGAKTYLERTLdtfiKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPftiyDGEAVAKYI 234
Cdd:PTZ00246 162 TAIGQNNQTAQSILKQEW----KEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGET----DGEPIQKML 229
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-224 2.28e-32

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: 117.00  E-value: 2.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDEHMGLSLAGLAPDARV 83
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLyePGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       84 LSNYLRQQC-----NYSSLVFNRKLAVERAGHLlcdkaQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYG 158
Cdd:cd03751  84 LVSRAREEAenyrdNYGTPIPVKVLADRVAMYM-----HAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5L5D_S      159 TAIGARSQGAKTYLErtldtfiKIDGN---PDELIKAGVEAIsQSLRDESltvdnlsiaivgKDTPFTI 224
Cdd:cd03751 159 CAIGKGKQAAKTELE-------KLKFSeltCREAVKEAAKII-YIVHDEI------------KDKAFEL 207
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-216 6.31e-32

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: 115.79  E-value: 6.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       13 FSPTGRLFQVEYALEAIKQGSVT-VGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLR 89
Cdd:cd03754   9 FSPEGRLYQVEYAFKAVKNAGLTsVAVRGKDCAVVVTQKKVPDKLidPSTVTHLFRITDEIGCVMTGMIADSRSQVQRAR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       90 QQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYD-KSGAHLLEFQPSGNVTELYGTAIGARSQGA 168
Cdd:cd03754  89 YEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDeELGPQLYKCDPAGYFAGYKATAAGVKEQEA 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
5L5D_S      169 KTYLERTLDTFIKIDGNPDELIKAGVEAISQSLrDESLTVDNLSIAIV 216
Cdd:cd03754 169 TNFLEKKLKKKPDLIESYEETVELAISCLQTVL-STDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-198 4.77e-28

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 104.40  E-value: 4.77e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       35 TVGLRSNTHAVLVALKRNADEL---SSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHL 111
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLpvaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      112 LCDKAQKNTQsygGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTE-LYGTAIGARSQGAKTYLERTldtfIKIDGNPDELI 190
Cdd:cd01901  83 LAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIEnPGAVATGSRSQRAKSLLEKL----YKPDMTLEEAV 155


                ....*...
5L5D_S      191 KAGVEAIS 198
Cdd:cd01901 156 ELALKALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-219 6.40e-17

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: 75.75  E-value: 6.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       35 TVGLRSNTHAVLVALKRNADE---LSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHL 111
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGnfiASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      112 LCDKaqknTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKIdgnpDELIK 191
Cdd:cd03764  83 LSNI----LNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTV----EEAKK 154

                       170       180
                ....*....|....*....|....*...
5L5D_S      192 AGVEAISQSLRDESLTVDNLSIAIVGKD 219
Cdd:cd03764 155 LAIRAIKSAIERDSASGDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-219 1.03e-12

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: 64.39  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       35 TVGLRSNTHAVLVALKR---NADELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHL 111
Cdd:cd01912   3 IVGIKGKDGVVLAADTRasaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      112 LcdkaqKNTQ-SYGGRPYGVGLLIIGYDK-SGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERtldtFIKIDGNPDEL 189
Cdd:cd01912  83 L-----SNILySYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDR----GYKPDMTLEEA 153

                       170       180       190
                ....*....|....*....|....*....|
5L5D_S      190 IKAGVEAISQSLRDESLTVDNLSIAIVGKD 219
Cdd:cd01912 154 VELVKKAIDSAIERDLSSGGGVDVAVITKD 183
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 6-28 3.20e-09

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: 50.81  E-value: 3.20e-09
                          10        20
                  ....*....|....*....|...
5L5D_S          6 YDGDTVTFSPTGRLFQVEYALEA 28
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 7.51e-09

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: 49.80  E-value: 7.51e-09
                           10        20
                   ....*....|....*....|...
5L5D_S           6 YDGDTVTFSPTGRLFQVEYALEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-197 6.39e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 45.75  E-value: 6.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S        29 IKQGSVTVGLRSNThAVLVALKRNADE----LSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:PTZ00488  36 FAHGTTTLAFKYGG-GIIIAVDSKATAgpyiASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       105 VERAGHLLCDKaqknTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGnvTELYGTAIGARSqgAKTYLERTLDTFIKIDG 184
Cdd:PTZ00488 115 VAAASKILANI----VWNYKGMGLSMGTMICGWDKKGPGLFYVDNDG--TRLHGNMFSCGS--GSTYAYGVLDAGFKWDL 186

                        170
                 ....*....|...
5L5D_S       185 NPDELIKAGVEAI 197
Cdd:PTZ00488 187 NDEEAQDLGRRAI 199
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-198 4.45e-04

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: 39.87  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       61 KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKntqsYGGRpYGVGLLIIGYDKS 140
Cdd:cd03763  32 EKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTMLKQHLFR----YQGH-IGAALVLGGVDYT 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
5L5D_S      141 GAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLdtfiKIDGNPDELIKAGVEAIS 198
Cdd:cd03763 107 GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRY----KPDMTEEEAKKLVCEAIE 160
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-203 1.59e-03

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


Pssm-ID: 239730  Cd Length: 188  Bit Score: 38.38  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       61 KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKaqknTQSYGGRPYGVGLLIIGYDKS 140
Cdd:cd03761  32 KKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNM----LYQYKGMGLSMGTMICGWDKT 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5L5D_S      141 GAHLLEFQPSGnvTELYGTAIGARSqgAKTYLERTLDTFIKIDGNPDELIKAGVEAISQ-SLRD 203
Cdd:cd03761 108 GPGLYYVDSDG--TRLKGDLFSVGS--GSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHaTHRD 167
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 57-202 8.74e-03

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


Pssm-ID: 239728  Cd Length: 195  Bit Score: 36.07  E-value: 8.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S       57 SSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLcdkaqkNTQSYGGR--PYGVGLLI 134
Cdd:cd03759  31 STDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSLI------SSLLYEKRfgPYFVEPVV 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5L5D_S      135 IGYDKSGAHLL-------------EFQPSGNVTE-LYGTAigarsqgaktylertlDTFIKIDGNPDELIkagvEAISQS 200
Cdd:cd03759 105 AGLDPDGKPFIctmdligcpsipsDFVVSGTASEqLYGMC----------------ESLWRPDMEPDELF----ETISQA 164


                ..
5L5D_S      201 LR 202
Cdd:cd03759 165 LL 166
 
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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