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Conserved domains on  [gi|757818969|pdb|3J9I|P]
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Chain P, Proteasome subunit alpha

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-208 8.38e-129

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: 361.65  E-value: 8.38e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd03756   4 RAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARVLI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGK 160
Cdd:cd03756  84 DRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGR 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3J9I_P      161 DAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITV 208
Cdd:cd03756 164 QAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
 
Name Accession Description Interval E-value
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-208 8.38e-129

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: 361.65  E-value: 8.38e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd03756   4 RAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARVLI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGK 160
Cdd:cd03756  84 DRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGR 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3J9I_P      161 DAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITV 208
Cdd:cd03756 164 QAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-224 1.13e-127

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 359.92  E-value: 1.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P         1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:PRK03996  12 RAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARVLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGK 160
Cdd:PRK03996  92 DRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGR 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
3J9I_P       161 DAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITVGNK-YRIYDQEEVKKFL 224
Cdd:PRK03996 172 DTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKkFRKLSVEEIEKYL 236
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-219 4.49e-94

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 274.71  E-value: 4.49e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVR-SRLIEQNSIEKIQLIDDYVAAVTSGLVADARVL 79
Cdd:COG0638  11 RAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVADAREL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       80 VDFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGgVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSG 159
Cdd:COG0638  91 VRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSG 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3J9I_P      160 KDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEEL-KAPEIASITvGNKYRIYDQEE 219
Cdd:COG0638 170 SPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASgDGIDVAVIT-EDGFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 22-194 8.57e-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: 201.26  E-value: 8.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P         22 VKKGSTALGMKFANGVLLISDKKV--RSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVN 99
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        100 IEnLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIG-PRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEK 178
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170
                  ....*....|....*.
3J9I_P        179 EAVTLGIKALKSSLEE 194
Cdd:pfam00227 160 EAVELAVKALKEAIDR 175
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 1-21 4.29e-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: 50.19  E-value: 4.29e-09
                           10        20
                   ....*....|....*....|.
3J9I_P           1 RAITVFSPDGRLFQVEYAREA 21
Cdd:smart00948   3 RSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-208 8.38e-129

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: 361.65  E-value: 8.38e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd03756   4 RAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARVLI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGK 160
Cdd:cd03756  84 DRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGR 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3J9I_P      161 DAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITV 208
Cdd:cd03756 164 QAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-224 1.13e-127

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 359.92  E-value: 1.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P         1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:PRK03996  12 RAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARVLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGK 160
Cdd:PRK03996  92 DRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGR 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
3J9I_P       161 DAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITVGNK-YRIYDQEEVKKFL 224
Cdd:PRK03996 172 DTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKkFRKLSVEEIEKYL 236
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-206 1.08e-106

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 305.91  E-value: 1.08e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd01911   3 RSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARVLV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQ-IGPRLFDCDPAGTINEYKATAIGSG 159
Cdd:cd01911  83 NRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEeGGPQLYQTDPSGTYFGYKATAIGKG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
3J9I_P      160 KDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASI 206
Cdd:cd01911 163 SQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-219 4.49e-94

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 274.71  E-value: 4.49e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVR-SRLIEQNSIEKIQLIDDYVAAVTSGLVADARVL 79
Cdd:COG0638  11 RAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVADAREL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       80 VDFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGgVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSG 159
Cdd:COG0638  91 VRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSG 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3J9I_P      160 KDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEEL-KAPEIASITvGNKYRIYDQEE 219
Cdd:COG0638 170 SPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASgDGIDVAVIT-EDGFRELSEEE 229
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-195 6.32e-73

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: 220.31  E-value: 6.32e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd03755   3 RAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIG-PRLFDCDPAGTINEYKATAIGSG 159
Cdd:cd03755  83 NRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRN 162

                       170       180       190
                ....*....|....*....|....*....|....*.
3J9I_P      160 KDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEG 195
Cdd:cd03755 163 SKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSG 198
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-224 2.33e-70

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: 214.49  E-value: 2.33e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        3 ITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDF 82
Cdd:cd03750   5 LTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       83 ARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDA 162
Cdd:cd03750  85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSN 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3J9I_P      163 VVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITVGNKYRIYDQEEVKKFL 224
Cdd:cd03750 165 AKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-206 1.66e-66

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: 204.11  E-value: 1.66e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLV 80
Cdd:cd03753   3 RGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       81 DFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGV-----RPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATA 155
Cdd:cd03753  83 DHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDAKA 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
3J9I_P      156 IGSGKDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASI 206
Cdd:cd03753 163 IGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 22-194 8.57e-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: 201.26  E-value: 8.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P         22 VKKGSTALGMKFANGVLLISDKKV--RSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVN 99
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        100 IEnLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIG-PRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEK 178
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170
                  ....*....|....*.
3J9I_P        179 EAVTLGIKALKSSLEE 194
Cdd:pfam00227 160 EAVELAVKALKEAIDR 175
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-193 4.16e-65

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: 200.65  E-value: 4.16e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        4 TVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQ-NSIEKIQLIDDYVAAVTSGLVADARVLVDF 82
Cdd:cd03752   8 TIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQsFSSEKIYKIDDHIACAVAGITSDANILINY 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       83 ARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQI-GPRLFDCDPAGTINEYKATAIGSGKD 161
Cdd:cd03752  88 ARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQ 167

                       170       180       190
                ....*....|....*....|....*....|..
3J9I_P      162 AVVSFLEREYKENLPEKEAVTLGIKALKSSLE 193
Cdd:cd03752 168 AAQSLLKQDYKDDMTLEEALALAVKVLSKTMD 199
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-203 2.88e-58

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: 183.20  E-value: 2.88e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        1 RAITVFSPDGRLFQVEYAREAVKKGS-TALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVL 79
Cdd:cd03754   4 RHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       80 VDFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQ-IGPRLFDCDPAGTINEYKATAIGS 158
Cdd:cd03754  84 VQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEeLGPQLYKCDPAGYFAGYKATAAGV 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
3J9I_P      159 GKDAVVSFLEREYKEN----LPEKEAVTLGIKALKSSLeeGEELKAPEI 203
Cdd:cd03754 164 KEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVL--STDFKATEI 210
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-209 1.37e-56

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: 178.64  E-value: 1.37e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        3 ITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNsiEKIQLIDDYVAAVTSGLVADARVLVDF 82
Cdd:cd03749   5 VTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIAGLTADARVLSRY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       83 ARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDA 162
Cdd:cd03749  83 MRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
3J9I_P      163 VVSFLEREYK--ENLPEKEAVTLGIKALKSSLEEGEELKapeIASITVG 209
Cdd:cd03749 163 ARTYLERHFEefEDCSLEELIKHALRALRETLPGEQELT---IKNVSIA 208
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 26-194 7.65e-55

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: 173.45  E-value: 7.65e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       26 STALGMKFANGVLLISDKKVRSRLIEQN-SIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLV 104
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASsTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      105 KRVADQMQQYTQYggVRPYGVSLIFAGIDQI-GPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTL 183
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                       170
                ....*....|.
3J9I_P      184 GIKALKSSLEE 194
Cdd:cd01906 159 ALKALKSALER 169
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-181 5.13e-54

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: 172.08  E-value: 5.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        2 AITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVD 81
Cdd:cd03751   7 SASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRHLVS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       82 FARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKD 161
Cdd:cd03751  87 RAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQ 166

                       170       180
                ....*....|....*....|
3J9I_P      162 AVVSFLEREYKENLPEKEAV 181
Cdd:cd03751 167 AAKTELEKLKFSELTCREAV 186
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 4-193 1.92e-53

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 172.34  E-value: 1.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P         4 TVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQ-NSIEKIQLIDDYVAAVTSGLVADARVLVDF 82
Cdd:PTZ00246  10 TTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADANILINQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        83 ARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQ-IGPRLFDCDPAGTINEYKATAIGSGKD 161
Cdd:PTZ00246  90 CRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDEnLGYQLYHTDPSGNYSGWKATAIGQNNQ 169

                        170       180       190
                 ....*....|....*....|....*....|..
3J9I_P       162 AVVSFLEREYKENLPEKEAVTLGIKALKSSLE 193
Cdd:PTZ00246 170 TAQSILKQEWKEDLTLEQGLLLAAKVLTKSMD 201
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 26-190 2.41e-41

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: 138.30  E-value: 2.41e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       26 STALGMKFANGVLLISDKKVRSRLIEQNS-IEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLV 104
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSpVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      105 KRVADQMQQYTQyggVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEY-KATAIGSGKDAVVSFLEREYKENLPEKEAVTL 183
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVEL 157


                ....*..
3J9I_P      184 GIKALKS 190
Cdd:cd01901 158 ALKALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-193 2.32e-33

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: 118.51  E-value: 2.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDKKVR-SRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLVK 105
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      106 RVADQMQQYtqygGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLGI 185
Cdd:cd03764  82 LLSNILNSS----KYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157


                ....*...
3J9I_P      186 KALKSSLE 193
Cdd:cd03764 158 RAIKSAIE 165
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-193 5.51e-25

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: 96.74  E-value: 5.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDKKV-RSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLVK 105
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRAsAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      106 RVADQMQQYTQYggvrPYGVSLIFAGIDQI-GPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLG 184
Cdd:cd01912  82 LLSNILYSYRGF----PYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELV 157


                ....*....
3J9I_P      185 IKALKSSLE 193
Cdd:cd01912 158 KKAIDSAIE 166
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-190 2.42e-13

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: 65.68  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDKKVRSRLIEQN-SIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLVK 105
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      106 RVADQMQQYTQYggvrpYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLGI 185
Cdd:cd03763  82 MLKQHLFRYQGH-----IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVC 156


                ....*
3J9I_P      186 KALKS 190
Cdd:cd03763 157 EAIEA 161
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-223 6.19e-12

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 62.22  E-value: 6.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDKK-VRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVN---IEN 102
Cdd:cd03758   3 TLIGIKGKDFVILAADTSaARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSpkaAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      103 LVKR-VADQMQQYTqyggvrPYGVSLIFAGIDQI-GPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEA 180
Cdd:cd03758  83 FTRReLAESLRSRT------PYQVNLLLAGYDKVeGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
3J9I_P      181 VTLGIKALKssleegeELKAPEIASITvGNKYRIYDQEEVKKF 223
Cdd:cd03758 157 LELMKKCIK-------ELKKRFIINLP-NFTVKVVDKDGIRDL 191
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-188 2.85e-09

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: 54.54  E-value: 2.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDKKVRSRLIEQN-SIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSlvniENLVK 105
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANrVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGE----PPLVK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P      106 RVADQMQQYTqYGGVRPYGVSLIFAGID-QIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLG 184
Cdd:cd03762  78 TAASLFKNLC-YNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFV 156


                ....
3J9I_P      185 IKAL 188
Cdd:cd03762 157 KNAL 160
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 1-21 3.79e-09

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 50.43  E-value: 3.79e-09
                          10        20
                  ....*....|....*....|.
3J9I_P          1 RAITVFSPDGRLFQVEYAREA 21
Cdd:pfam10584   3 RSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 1-21 4.29e-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: 50.19  E-value: 4.29e-09
                           10        20
                   ....*....|....*....|.
3J9I_P           1 RAITVFSPDGRLFQVEYAREA 21
Cdd:smart00948   3 RSLTTFSPDGRLFQVEYAMEA 23
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 25-188 1.11e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.84  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P        25 GSTALGMKFANGVLLISDKK-VRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENL 103
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKaTAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       104 VKRVADQMQQYtqyggvRPYGVSL--IFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAV 181
Cdd:PTZ00488 119 SKILANIVWNY------KGMGLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQ 192


                 ....*..
3J9I_P       182 TLGIKAL 188
Cdd:PTZ00488 193 DLGRRAI 199
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-187 1.37e-08

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


Pssm-ID: 239730  Cd Length: 188  Bit Score: 52.63  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       27 TALGMKFANGVLLISDkkvrSR-----LIEQNSIEKIQLIDDYVAAVTSGLVADA----RVLVDFARIsaqqEKVTYGSL 97
Cdd:cd03761   2 TTLAFIFQGGVIVAVD----SRatagsYIASQTVKKVIEINPYLLGTMAGGAADCqyweRVLGRECRL----YELRNKER 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J9I_P       98 VNIENLVKRVADQMQQYtqyggvRPYGVSL--IFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENL 175
Cdd:cd03761  74 ISVAAASKLLSNMLYQY------KGMGLSMgtMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDL 147

                       170
                ....*....|..
3J9I_P      176 PEKEAVTLGIKA 187
Cdd:cd03761 148 SVEEAYDLARRA 159
 
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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