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Conserved domains on  [gi|4506179|ref|NP_002777|]
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proteasome subunit alpha type-1 isoform 2 [Homo sapiens]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132875)

proteasome subunit alpha is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to Homo sapiens proteasome subunit alpha type-1 and Schizosaccharomyces pombe proteasome subunit alpha type-6

CATH:  3.60.20.10
Gene Ontology:  GO:0051603|GO:0005839
PubMed:  7682410|1317508|8882582|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 3.12e-154

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: 427.86  E-value: 3.12e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLC 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   86 NFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506179  166 QSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVG 216
Cdd:cd03749 161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQELTIKNVSIAIVG 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 ...
 6-216 3.12e-154

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: 427.86  E-value: 3.12e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLC 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   86 NFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506179  166 QSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVG 216
Cdd:cd03749 161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQELTIKNVSIAIVG 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-238 2.88e-65

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 203.53  E-value: 2.88e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     1 MFRNQ---YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIA 75
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiePSSIEKIFKIDDHIGAASA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    76 GLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFD 155
Cdd:PRK03996  82 GLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   156 CRAMSIGARSQSARTYLERHMSEfmECNLNELVKHGLRALRETlpAEQDLTTKNVSIGIVG-KDLEFTIYDDDDVSPFLE 234
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKA--NEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLE 237


                 ....
gi 4506179   235 GLEE 238
Cdd:PRK03996 238 KLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-215 2.07e-61

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: 191.63  E-value: 2.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     29 VKQGSATVGLKSKTHAVLVALKRA--QSELAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrGSKLLSKDtvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    105 VsRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMG-PHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEfmECN 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 4506179    184 LNELVKHGLRALRETLpAEQDLTTKNVSIGIV 215
Cdd:pfam00227 158 LEEAVELAVKALKEAI-DRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-228 1.19e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 155.30  E-value: 1.19e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    1 MFRNQ---YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRA-QSELAAHQ--KKILHVDNHIGISI 74
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAtMGNLIASKsiEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   75 AGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQrYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYF 154
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506179  155 DCRAMSIGARSQSARTYLERHMSEFMecNLNELVKHGLRALRETlpAEQD-LTTKNVSIGIVGKDlEFTIYDDDD 228
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSA--AERDsASGDGIDVAVITED-GFRELSEEE 229
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 32-218 1.08e-15

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 73.01  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     32 GSATVGLKSKTHAVLVALKRAQSE-LAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRL 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGnFVASKnaKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    109 VSLIGSKTqiptqrYGRR--PYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMecNLNE 186
Cdd:TIGR03634  81 ATLLSNIL------NSNRffPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDM--SVEE 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 4506179    187 LVKHGLRALRETlpAEQDLTTKN-VSIGIVGKD 218
Cdd:TIGR03634 153 AKKLAVRAIKSA--IERDVASGNgIDVAVITKD 183
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 2.43e-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: 51.34  E-value: 2.43e-09
                           10        20
                   ....*....|....*....|...
gi 4506179       6 YDNDVTVWSPQGRIHQIEYAMEA 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 ...
 6-216 3.12e-154

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: 427.86  E-value: 3.12e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLC 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   86 NFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506179  166 QSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVG 216
Cdd:cd03749 161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQELTIKNVSIAIVG 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 3.19e-105

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: 303.60  E-value: 3.19e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLldPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYD-DMGPHIFQTCPSANYFDCRAMSIG 162
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDeEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4506179  163 ARSQSARTYLERHMSEFMECnlNELVKHGLRALRETLpaEQDLTTKNVSIGIV 215
Cdd:cd01911 161 KGSQEAKTFLEKRYKKDLTL--EEAIKLALKALKEVL--EEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-238 2.88e-65

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 203.53  E-value: 2.88e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     1 MFRNQ---YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIA 75
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiePSSIEKIFKIDDHIGAASA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    76 GLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFD 155
Cdd:PRK03996  82 GLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   156 CRAMSIGARSQSARTYLERHMSEfmECNLNELVKHGLRALRETlpAEQDLTTKNVSIGIVG-KDLEFTIYDDDDVSPFLE 234
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKA--NEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLE 237


                 ....
gi 4506179   235 GLEE 238
Cdd:PRK03996 238 KLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-215 2.07e-61

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: 191.63  E-value: 2.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     29 VKQGSATVGLKSKTHAVLVALKRA--QSELAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrGSKLLSKDtvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    105 VsRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMG-PHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEfmECN 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 4506179    184 LNELVKHGLRALRETLpAEQDLTTKNVSIGIV 215
Cdd:pfam00227 158 LEEAVELAVKALKEAI-DRDALSGGNIEVAVI 188
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 8.34e-60

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: 188.31  E-value: 8.34e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLvePESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGA 163
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGS 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4506179  164 RSQSARTYLERHMSEFMecNLNELVKHGLRALRETLpaEQDLTTKNVSIGIV 215
Cdd:cd03756 162 GRQAVTEFLEKEYKEDM--SLEEAIELALKALYAAL--EENETPENVEIAYV 209
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-233 2.81e-56

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: 179.83  E-value: 2.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELA--AHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIdeSSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGA 163
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179  164 RSQSARTYLERHMSEFMEcnLNELVKHGLRALRETlpAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFL 233
Cdd:cd03750 161 NYSNAKTFLEKRYNEDLE--LEDAIHTAILTLKEG--FEGQMTEKNIEIGICGETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 7.57e-51

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: 165.59  E-value: 7.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLmePSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIgSKTQIptqRYGR---------RPYGVGLLIAGYDDMGPHIFQTCPSANYF 154
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAV-SDLAL---QFGEgddgkkamsRPFGVALLIAGVDENGPQLFHTDPSGTFT 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506179  155 DCRAMSIGARSQSARTYLERHMSEFMEcnLNELVKHGLRALRETLpaEQDLTTKNVSIGIV 215
Cdd:cd03753 157 RCDAKAIGSGSEGAQSSLQEKYHKDMT--LEEAEKLALSILKQVM--EEKLNSTNVELATV 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 2.62e-50

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: 164.07  E-value: 2.62e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLqdPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYD-DMGPHIFQTCPSANYFDCRAMSIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDpDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4506179  163 ARSQSARTYLERHMSEFMecNLNELVKHGLRALRETLpaeqDLTTKNVSIGIV 215
Cdd:cd03755 161 RNSKTVREFLEKNYKEEM--TRDDTIKLAIKALLEVV----QSGSKNIELAVM 207
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 5.08e-48

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: 158.28  E-value: 5.08e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQK---KILHVDNHIGISIAGLTADAR 82
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFsseKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   83 LLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDD-MGPHIFQTCPSANYFDCRAMSI 161
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKhYGFQLYQSDPSGNYSGWKATAI 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4506179  162 GARSQSARTYLERHMSEfmECNLNELVKHGLRALRETLPAEQdLTTKNVSIGIV 215
Cdd:cd03752 163 GNNNQAAQSLLKQDYKD--DMTLEEALALAVKVLSKTMDSTK-LTSEKLEFATL 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 33-215 5.63e-47

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: 154.58  E-value: 5.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   33 SATVGLKSKTHAVLVALKRAQSELAAH---QKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLV 109
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVAsstVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179  110 SLIGSKTQIPTQRygRRPYGVGLLIAGYD-DMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMEcnLNELV 188
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMT--LEEAI 156

                       170       180
                ....*....|....*....|....*...
gi 4506179  189 KHGLRALRETLpaEQDLTT-KNVSIGIV 215
Cdd:cd01906 157 ELALKALKSAL--ERDLYSgGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-228 1.19e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 155.30  E-value: 1.19e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    1 MFRNQ---YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRA-QSELAAHQ--KKILHVDNHIGISI 74
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAtMGNLIASKsiEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   75 AGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQrYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYF 154
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506179  155 DCRAMSIGARSQSARTYLERHMSEFMecNLNELVKHGLRALRETlpAEQD-LTTKNVSIGIVGKDlEFTIYDDDD 228
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSA--AERDsASGDGIDVAVITED-GFRELSEEE 229
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-189 3.43e-44

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: 148.58  E-value: 3.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADARL 83
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLyePGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   84 LCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGA 163
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGK 163

                       170       180
                ....*....|....*....|....*.
gi 4506179  164 RSQSARTYLERHMSEFMECnlNELVK 189
Cdd:cd03751 164 GKQAAKTELEKLKFSELTC--REAVK 187
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-239 8.30e-40

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 138.45  E-value: 8.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     5 QYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSEL---AAHQKKILHVDNHIGISIAGLTADA 81
Cdd:PTZ00246   4 RYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLldpGKINEKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    82 RLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYD-DMGPHIFQTCPSANYFDCRAMS 160
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDeNLGYQLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   161 IGARSQSARTYLERHMSEFMecNLNElvkhGLRALRETLPAEQDLTTKNvsigivGKDLEFTI--YDDDDVSPFLEGLEE 238
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKEDL--TLEQ----GLLLAAKVLTKSMDSTSPK------ADKIEVGIlsHGETDGEPIQKMLSE 231


                 .
gi 4506179   239 R 239
Cdd:PTZ00246 232 K 232
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 1.96e-37

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: 131.20  E-value: 1.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    6 YDNDVTVWSPQGRIHQIEYAMEAVKQGSAT-VGLKSKTHAVLVALKRAQSEL--AAHQKKILHVDNHIGISIAGLTADAR 82
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGLTsVAVRGKDCAVVVTQKKVPDKLidPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   83 LLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDD-MGPHIFQTCPSANYFDCRAMSI 161
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEeLGPQLYKCDPAGYFAGYKATAA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506179  162 GARSQSARTYLERHM--SEFMECNLNELVKHGLRALRETLpaEQDLTTKNVSIGIV 215
Cdd:cd03754 162 GVKEQEATNFLEKKLkkKPDLIESYEETVELAISCLQTVL--STDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 33-197 6.33e-35

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: 122.89  E-value: 6.33e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   33 SATVGLKSKTHAVLVALKRAQSELAAH---QKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLV 109
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAgspVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179  110 SLIGSKTQIPTQrygRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCR-AMSIGARSQSARTYLERHMSEFMecNLNELV 188
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDM--TLEEAV 155


                ....*....
gi 4506179  189 KHGLRALRE 197
Cdd:cd01901 156 ELALKALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-218 1.30e-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: 75.37  E-value: 1.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   35 TVGLKSKTHAVLVALKRAQSE-LAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSL 111
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGnFIASKnvKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179  112 IGSktqIPTQrYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMecNLNELVKHG 191
Cdd:cd03764  83 LSN---ILNS-SKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDM--TVEEAKKLA 156

                       170       180
                ....*....|....*....|....*...
gi 4506179  192 LRALRETLpaEQDLTTKN-VSIGIVGKD 218
Cdd:cd03764 157 IRAIKSAI--ERDSASGDgIDVVVITKD 182
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 32-218 1.08e-15

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 73.01  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179     32 GSATVGLKSKTHAVLVALKRAQSE-LAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRL 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGnFVASKnaKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179    109 VSLIGSKTqiptqrYGRR--PYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMecNLNE 186
Cdd:TIGR03634  81 ATLLSNIL------NSNRffPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDM--SVEE 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 4506179    187 LVKHGLRALRETlpAEQDLTTKN-VSIGIVGKD 218
Cdd:TIGR03634 153 AKKLAVRAIKSA--IERDVASGNgIDVAVITKD 183
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-218 1.93e-13

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: 66.70  E-value: 1.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   35 TVGLKSKTHAVLVALKRA-QSELAAHQ--KKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSL 111
Cdd:cd01912   3 IVGIKGKDGVVLAADTRAsAGSLVASRnfDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179  112 IgSKTQiptQRYGRRPYGVGLLIAGYD-DMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMEcnLNELVKH 190
Cdd:cd01912  83 L-SNIL---YSYRGFPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMT--LEEAVEL 156

                       170       180
                ....*....|....*....|....*....
gi 4506179  191 GLRALRETLpaEQDLTT-KNVSIGIVGKD 218
Cdd:cd01912 157 VKKAIDSAI--ERDLSSgGGVDVAVITKD 183
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 6-28 2.69e-10

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: 53.89  E-value: 2.69e-10
                          10        20
                  ....*....|....*....|...
gi 4506179      6 YDNDVTVWSPQGRIHQIEYAMEA 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 2.43e-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: 51.34  E-value: 2.43e-09
                           10        20
                   ....*....|....*....|...
gi 4506179       6 YDNDVTVWSPQGRIHQIEYAMEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-181 2.87e-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: 40.64  E-value: 2.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506179   36 VGLKSKTHAVLVALKRA-QSELAA--HQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLI 112
Cdd:cd03763   4 VGVVFKDGVVLGADTRAtEGPIVAdkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTML 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506179  113 gSKTQIPTQRYgrrpYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFME 181
Cdd:cd03763  84 -KQHLFRYQGH----IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMT 147
 
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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