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Conserved domains on  [gi|15220151|ref|NP_175158|]
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20S proteasome alpha subunit F2 [Arabidopsis thaliana]

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 ...
 6-215 1.86e-141

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: 396.28  E-value: 1.86e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  86 RYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220151 166 QAAKTYLERKFESFQESSKEDLIKDAIMAIRETLQGET-LKSSLCTVSVLG 215
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 ...
 6-215 1.86e-141

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: 396.28  E-value: 1.86e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  86 RYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220151 166 QAAKTYLERKFESFQESSKEDLIKDAIMAIRETLQGET-LKSSLCTVSVLG 215
Cdd:cd03749 161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-237 1.53e-68

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 212.39  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151    1 MFRNQ---YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL---SSHQrKIFKVDDHIGVAI 74
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIE-KIFKIDDHIGAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   75 AGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYF 154
Cdd:PRK03996  81 AGLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  155 EYQAFAIGSRSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRETLQGETLKSSLCtVSVLGVDEP-FHFLDQESIQKVID 233
Cdd:PRK03996 161 EYKATAIGAGRDTVMEFLEKNYK--EDLSLEEAIELALKALAKANEGKLDPENVE-IAYIDVETKkFRKLSVEEIEKYLE 237


                 ....
gi 15220151  234 TFEK 237
Cdd:PRK03996 238 KLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-214 2.25e-66

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: 204.72  E-value: 2.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151    29 VKQGSAAIGLRSRSHVVLAC---VNKAQSELSSHQ-RKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAAdkrATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   105 VgRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGA-HLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESfqESS 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15220151   184 KEDLIKDAIMAIRETLQGETLKSSLCTVSVL 214
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-197 3.59e-49

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 162.24  E-value: 3.59e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   1 MFRNQ---YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKA-QSELSSHQ--RKIFKVDDHIGVAI 74
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAtMGNLIASKsiEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  75 AGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWkRPYGVGLLVGGLDESGAHLYYNCPSGNYF 154
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15220151 155 EYQAFAIGSRSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRE 197
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYR--EDLSLDEAVELALRALYS 200
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 3.34e-10

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 54.04  E-value: 3.34e-10
                           10        20
                   ....*....|....*....|...
gi 15220151      6 YDTDVTTWSPTGRLFQVEYAMEA 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 ...
 6-215 1.86e-141

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: 396.28  E-value: 1.86e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLS 85
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  86 RYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRS 165
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220151 166 QAAKTYLERKFESFQESSKEDLIKDAIMAIRETLQGET-LKSSLCTVSVLG 215
Cdd:cd03749 161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-214 5.34e-103

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: 298.59  E-value: 5.34e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLldPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDES-GAHLYYNCPSGNYFEYQAFAIG 162
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15220151 163 SRSQAAKTYLERKFESFqeSSKEDLIKDAIMAIRETLQgETLKSSLCTVSVL 214
Cdd:cd01911 161 KGSQEAKTFLEKRYKKD--LTLEEAIKLALKALKEVLE-EDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-237 1.53e-68

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 212.39  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151    1 MFRNQ---YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL---SSHQrKIFKVDDHIGVAI 74
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIE-KIFKIDDHIGAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   75 AGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYF 154
Cdd:PRK03996  81 AGLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  155 EYQAFAIGSRSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRETLQGETLKSSLCtVSVLGVDEP-FHFLDQESIQKVID 233
Cdd:PRK03996 161 EYKATAIGAGRDTVMEFLEKNYK--EDLSLEEAIELALKALAKANEGKLDPENVE-IAYIDVETKkFRKLSVEEIEKYLE 237


                 ....
gi 15220151  234 TFEK 237
Cdd:PRK03996 238 KLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-214 2.25e-66

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: 204.72  E-value: 2.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151    29 VKQGSAAIGLRSRSHVVLAC---VNKAQSELSSHQ-RKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAAdkrATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   105 VgRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGA-HLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESfqESS 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15220151   184 KEDLIKDAIMAIRETLQGETLKSSLCTVSVL 214
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-203 2.33e-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: 190.23  E-value: 2.33e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLvePESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGS 163
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15220151 164 RSQAAKTYLERKFESfqESSKEDLIKDAIMAIRETLQGET 203
Cdd:cd03756 162 GRQAVTEFLEKEYKE--DMSLEEAIELALKALYAALEENE 199
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-200 1.94e-56

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: 180.25  E-value: 1.94e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLqdPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESG-AHLYYNCPSGNYFEYQAFAIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15220151 163 SRSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRETLQ 200
Cdd:cd03755 161 RNSKTVREFLEKNYK--EEMTRDDTIKLAIKALLEVVQ 196
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-228 1.11e-55

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: 179.05  E-value: 1.11e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLidESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGS 163
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220151 164 RSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRETLQGETLKSSLcTVSVLGVDEPFHFLDQESI 228
Cdd:cd03750 161 NYSNAKTFLEKRYN--EDLELEDAIHTAILTLKEGFEGQMTEKNI-EIGICGETKGFRLLTPAEI 222
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-200 3.85e-54

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: 174.45  E-value: 3.85e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLmePSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKA-----QVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQA 158
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgeGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15220151 159 FAIGSRSQAAKTylerkfeSFQESSKEDL-IKDAIMAIRETLQ 200
Cdd:cd03753 161 KAIGSGSEGAQS-------SLQEKYHKDMtLEEAEKLALSILK 196
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-197 7.14e-53

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: 171.31  E-value: 7.14e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGRV 83
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLyePGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  84 LSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGS 163
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGK 163

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15220151 164 RSQAAKTYLERKfeSFQESSKEDLIKDA---IMAIRE 197
Cdd:cd03751 164 GKQAAKTELEKL--KFSELTCREAVKEAakiIYIVHD 198
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 33-214 3.86e-52

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: 168.44  E-value: 3.86e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  33 SAAIGLRSRSHVVLACVNKAQSEL---SSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLV 109
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLlvaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 110 VHLADKAQVCTQRswKRPYGVGLLVGGLDE-SGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESfqESSKEDLI 188
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP--DMTLEEAI 156

                       170       180
                ....*....|....*....|....*.
gi 15220151 189 KDAIMAIRETLQGETLKSSLCTVSVL 214
Cdd:cd01906 157 ELALKALKSALERDLYSGGNIEVAVI 182
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-214 4.45e-50

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: 164.06  E-value: 4.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQR---KIFKVDDHIGVAIAGLTADGR 82
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFsseKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  83 VLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDES-GAHLYYNCPSGNYFEYQAFAI 161
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAI 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220151 162 GSRSQAAKTYLERKFesfqessKEDL-IKDAI-MAIR---ETLQGETLKSSLCTVSVL 214
Cdd:cd03752 163 GNNNQAAQSLLKQDY-------KDDMtLEEALaLAVKvlsKTMDSTKLTSEKLEFATL 213
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-197 3.59e-49

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 162.24  E-value: 3.59e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   1 MFRNQ---YDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKA-QSELSSHQ--RKIFKVDDHIGVAI 74
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAtMGNLIASKsiEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  75 AGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWkRPYGVGLLVGGLDESGAHLYYNCPSGNYF 154
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15220151 155 EYQAFAIGSRSQAAKTYLERKFEsfQESSKEDLIKDAIMAIRE 197
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYR--EDLSLDEAVELALRALYS 200
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-232 2.67e-43

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 148.08  E-value: 2.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151    5 QYDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQR---KIFKVDDHIGVAIAGLTADG 81
Cdd:PTZ00246   4 RYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKineKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   82 RVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDES-GAHLYYNCPSGNYFEYQAFA 160
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220151  161 IGSRSQAAKTYLERKFesfqessKEDLIKD-----AIMAIRETLQGETLKSSLCTVSVLGVDEPfhflDQESIQKVI 232
Cdd:PTZ00246 164 IGQNNQTAQSILKQEW-------KEDLTLEqglllAAKVLTKSMDSTSPKADKIEVGILSHGET----DGEPIQKML 229
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-210 3.31e-41

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: 141.22  E-value: 3.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151   6 YDTDVTTWSPTGRLFQVEYAMEAVKQGS-AAIGLRSRSHVVLACVNKAQSEL--SSHQRKIFKVDDHIGVAIAGLTADGR 82
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLidPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  83 VLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGV-GLLVGGLDESGAHLYYNCPSGNYFEYQAFAI 161
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVsMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15220151 162 GSRSQAAKTYLERKFESFqESSKEDLIKDAIMAIretlqgETLKSSLCT 210
Cdd:cd03754 162 GVKEQEATNFLEKKLKKK-PDLIESYEETVELAI------SCLQTVLST 203
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 33-197 2.09e-39

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: 135.22  E-value: 2.09e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  33 SAAIGLRSRSHVVLACVNKAQSEL---SSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLV 109
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLpvaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 110 VHLADKAQVCTQRswkRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQ-AFAIGSRSQAAKTYLERKFESfqESSKEDLI 188
Cdd:cd01901  81 KELAKLLQVYTQG---RPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKP--DMTLEEAV 155


                ....*....
gi 15220151 189 KDAIMAIRE 197
Cdd:cd01901 156 ELALKALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-196 5.63e-20

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: 85.00  E-value: 5.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  35 AIGLRSRSHVVLACVNKAQSE---LSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVH 111
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGnfiASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 112 LADkaqVCTQRSWkRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFEsfQESSKEDLIKDA 191
Cdd:cd03764  83 LSN---ILNSSKY-FPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYK--EDMTVEEAKKLA 156


                ....*
gi 15220151 192 IMAIR 196
Cdd:cd03764 157 IRAIK 161
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 36-198 7.14e-19

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


Pssm-ID: 238893  Cd Length: 189  Bit Score: 81.72  E-value: 7.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  36 IGLRSRSHVVLAC---VNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVgRLVVHL 112
Cdd:cd01912   4 VGIKGKDGVVLAAdtrASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV-KAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 113 AdkAQVCTQRSWKrPYGVGLLVGGLDE-SGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESfqESSKEDLIKDA 191
Cdd:cd01912  83 L--SNILYSYRGF-PYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKP--DMTLEEAVELV 157


                ....*..
gi 15220151 192 IMAIRET 198
Cdd:cd01912 158 KKAIDSA 164
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 6-28 4.92e-11

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 56.20  E-value: 4.92e-11
                          10        20
                  ....*....|....*....|...
gi 15220151     6 YDTDVTTWSPTGRLFQVEYAMEA 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 3.34e-10

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 54.04  E-value: 3.34e-10
                           10        20
                   ....*....|....*....|...
gi 15220151      6 YDTDVTTWSPTGRLFQVEYAMEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-194 3.34e-08

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: 52.20  E-value: 3.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  36 IGLRSRSHVVLACVNKAQSE---LSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYesplpvGRlvvhl 112
Cdd:cd03763   4 VGVVFKDGVVLGADTRATEGpivADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNT------GR----- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 113 adKAQVCTQRSWKR----PY----GVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKF-ESFQESS 183
Cdd:cd03763  73 --KPRVVTALTMLKqhlfRYqghiGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYkPDMTEEE 150

                       170
                ....*....|.
gi 15220151 184 KEDLIKDAIMA 194
Cdd:cd03763 151 AKKLVCEAIEA 161
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 60-192 6.54e-04

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 39.90  E-value: 6.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  60 QRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLvvhladkAQVCTQRSWKRPYGV--GLLVGGL 137
Cdd:cd03762  31 TDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTA-------ASLFKNLCYNYKEMLsaGIIVAGW 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220151 138 DESGAHLYYNCPSGNYFEYQAFAI-GSRSQAAKTYLERKFESfqESSKED---LIKDAI 192
Cdd:cd03762 104 DEQNGGQVYSIPLGGMLIRQPFAIgGSGSTYIYGYVDANYKP--GMTLEEcikFVKNAL 160
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 56-223 8.62e-04

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 39.55  E-value: 8.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151  56 LSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLvvhladkAQ-VCTQRSWKR--PYGVGL 132
Cdd:cd03757  35 LSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI-------AQlLSTILYSRRffPYYVFN 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220151 133 LVGGLDESG-AHLYYNCPSGNYFEYQAFAIGSRSQAA----------KTYLERKFESFQESSKEDLIKDAIM--AIRETL 199
Cdd:cd03757 108 ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIqplldnqvgrKNQNNVERTPLSLEEAVSLVKDAFTsaAERDIY 187

                       170       180
                ....*....|....*....|....
gi 15220151 200 QGETLKssLCTVSVLGVDEPFHFL 223
Cdd:cd03757 188 TGDSLE--IVIITKDGIEEETFPL 209
 
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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