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Conserved domains on  [gi|46254554|gb|AAS86250|]
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testes-specific alpha4-t1 proteasome subunit [Drosophila melanogaster]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132902)

proteasome subunit alpha is a component of the proteasome complex that is involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-7, -8 and fungal proteasome subunit alpha type-4

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.94e-126

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: 355.90  E-value: 4.94e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 46254554 165 RWANTVREFFEKAYSDHEvtTKCDAIKLAMRALLEVTQMSQMRLEVAVL 213
Cdd:cd03755 161 RNSKTVREFLEKNYKEEM--TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.94e-126

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: 355.90  E-value: 4.94e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 46254554 165 RWANTVREFFEKAYSDHEvtTKCDAIKLAMRALLEVTQMSQMRLEVAVL 213
Cdd:cd03755 161 RNSKTVREFLEKNYKEEM--TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-239 6.44e-81

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 242.82  E-value: 6.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDaDGSARLFHTEPSGIFHEYKATATG 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46254554  165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRALLEVTQMSQM--RLEVAV--LENGKPMKMLDsvviSEIVKIVQNEKE 239
Cdd:PRK03996 169 AGRDTVMEFLEKNYKE-DLSLE-EAIELALKALAKANEGKLDpeNVEIAYidVETKKFRKLSV----EEIEKYLEKLLK 241
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-221 5.64e-77

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 232.16  E-value: 5.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554     5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDaDGSARLFHTEPSGIFHEYKATATG 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATAIG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46254554   165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRALLEVTQ--MSQMRLEVAV--LENGKPMKM 221
Cdd:TIGR03633 162 AGRQAVTEFLEKEYRE-DLSLD-EAIELALKALYSAVEdkLTPENVEVAYitVEDKKFRKL 220
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-197 1.35e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 198.06  E-value: 1.35e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   1 MSSRYGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEK-SSVSEMQEDRTVRKISMLDRHVALAFAGLT 79
Cdd:COG0638   5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRrATMGNLIASKSIEKIFKIDDHIGVAIAGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  80 ADARILINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQcNGRRPFGISCLIGGIDADGsARLFHTEPSGIFHEYK 159
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEK 162

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 46254554 160 ATATGRWANTVREFFEKAYSDhEVTTKcDAIKLAMRAL 197
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYRE-DLSLD-EAVELALRAL 198
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-213 1.18e-61

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 191.63  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    28 VRKGSTAVGVRGANCVVLGVEK--SSVSEMQEDRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVT 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKraTRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   106 LEyITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATGRWANTVREFFEKAYsdHEVTT 185
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY--RPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 46254554   186 KCDAIKLAMRALLEVTQ---MSQMRLEVAVL 213
Cdd:pfam00227 158 LEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 1.89e-09

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 51.73  E-value: 1.89e-09
                           10        20
                   ....*....|....*....|...
gi 46254554      5 YGRALTIFSPDGHLLQVEYAQEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.94e-126

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: 355.90  E-value: 4.94e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 46254554 165 RWANTVREFFEKAYSDHEvtTKCDAIKLAMRALLEVTQMSQMRLEVAVL 213
Cdd:cd03755 161 RNSKTVREFLEKNYKEEM--TRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.41e-96

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: 280.10  E-value: 4.41e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 46254554 165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRALLEVTQ--MSQMRLEVAVL 213
Cdd:cd01911 161 KGSQEAKTFLEKRYKK-DLTLE-EAIKLALKALKEVLEedKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-239 6.44e-81

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 242.82  E-value: 6.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDaDGSARLFHTEPSGIFHEYKATATG 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46254554  165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRALLEVTQMSQM--RLEVAV--LENGKPMKMLDsvviSEIVKIVQNEKE 239
Cdd:PRK03996 169 AGRDTVMEFLEKNYKE-DLSLE-EAIELALKALAKANEGKLDpeNVEIAYidVETKKFRKLSV----EEIEKYLEKLLK 241
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-221 5.64e-77

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 232.16  E-value: 5.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554     5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDaDGSARLFHTEPSGIFHEYKATATG 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATAIG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46254554   165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRALLEVTQ--MSQMRLEVAV--LENGKPMKM 221
Cdd:TIGR03633 162 AGRQAVTEFLEKEYRE-DLSLD-EAIELALKALYSAVEdkLTPENVEVAYitVEDKKFRKL 220
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-197 2.35e-75

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: 227.60  E-value: 2.35e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDaDGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKATAIG 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 46254554 165 RWANTVREFFEKAYSDhEVTTKcDAIKLAMRAL 197
Cdd:cd03756 161 SGRQAVTEFLEKEYKE-DMSLE-EAIELALKAL 191
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-197 1.35e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 198.06  E-value: 1.35e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   1 MSSRYGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEK-SSVSEMQEDRTVRKISMLDRHVALAFAGLT 79
Cdd:COG0638   5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRrATMGNLIASKSIEKIFKIDDHIGVAIAGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  80 ADARILINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQcNGRRPFGISCLIGGIDADGsARLFHTEPSGIFHEYK 159
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEK 162

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 46254554 160 ATATGRWANTVREFFEKAYSDhEVTTKcDAIKLAMRAL 197
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYRE-DLSLD-EAVELALRAL 198
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-213 1.18e-61

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 191.63  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    28 VRKGSTAVGVRGANCVVLGVEK--SSVSEMQEDRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVT 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKraTRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   106 LEyITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATGRWANTVREFFEKAYsdHEVTT 185
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY--RPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 46254554   186 KCDAIKLAMRALLEVTQ---MSQMRLEVAVL 213
Cdd:pfam00227 158 LEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-230 9.59e-54

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: 172.89  E-value: 9.59e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSaRLFHTEPSGIFHEYKATATG 164
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGP-YLYQVDPSGSYFTWKATAIG 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46254554 165 RWANTVREFFEKAYS-DHEVTtkcDAIKLAMRALLEV--TQMSQMRLEVAVLENGKPMKMLDsvvISEI 230
Cdd:cd03750 160 KNYSNAKTFLEKRYNeDLELE---DAIHTAILTLKEGfeGQMTEKNIEIGICGETKGFRLLT---PAEI 222
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.43e-53

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: 170.98  E-value: 4.43e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGR-----RPFGISCLIGGIDADGsARLFHTEPSGIFHEYK 159
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFHTDPSGTFTRCD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46254554 160 ATATGRWANTVREFFEKAYsdHEVTTKCDAIKLAMRALLEVTQ--MSQMRLEVAVL 213
Cdd:cd03753 160 AKAIGSGSEGAQSSLQEKY--HKDMTLEEAEKLALSILKQVMEekLNSTNVELATV 213
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-213 1.19e-52

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: 169.84  E-value: 1.19e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   3 SRYGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEM-QEDRTVRKISMLDRHVALAFAGLTAD 81
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLlDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  82 ARILINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKAT 161
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46254554 162 ATGRWANTVREFFEKAYSDhEVTTKcDAIKLAMRAL---LEVTQMSQMRLEVAVL 213
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKD-DMTLE-EALALAVKVLsktMDSTKLTSEKLEFATL 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-213 5.64e-50

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: 161.89  E-value: 5.64e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  32 STAVGVRGANCVVLGVEKSSVSEMQE-DRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVTLEYIT 110
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554 111 RYLAQLKQKYTQcnGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATGRWANTVREFFEKAYsdHEVTTKCDAI 190
Cdd:cd01906  81 KLLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY--KPDMTLEEAI 156

                       170       180
                ....*....|....*....|....*.
gi 46254554 191 KLAMRALLEVTQ---MSQMRLEVAVL 213
Cdd:cd01906 157 ELALKALKSALErdlYSGGNIEVAVI 182
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-213 2.47e-49

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: 161.30  E-value: 2.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  10 TIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEdrTVRKISMLDRHVALAFAGLTADARILINRG 89
Cdd:cd03749   6 TTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSS--YQKKIFKVDDHIGIAIAGLTADARVLSRYM 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  90 QVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGsARLFHTEPSGIFHEYKATATGRWANT 169
Cdd:cd03749  84 RQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPSGNYFEYKATSIGARSQS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 46254554 170 VREFFEKAYSDHEVTTKCDAIKLAMRALLEVTQ----MSQMRLEVAVL 213
Cdd:cd03749 163 ARTYLERHFEEFEDCSLEELIKHALRALRETLPgeqeLTIKNVSIAIV 210
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-243 7.10e-49

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 161.56  E-value: 7.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554    1 MSSRYGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEM-QEDRTVRKISMLDRHVALAFAGLT 79
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLlDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   80 ADARILINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYK 159
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  160 ATATGRWANTVREFFEKAYSdhEVTTKCDAIKLAMRAL---LEVTQMSQMRLEVAVLENGKP-----MKMLDSVVISEIV 231
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWK--EDLTLEQGLLLAAKVLtksMDSTSPKADKIEVGILSHGETdgepiQKMLSEKEIAELL 238

                        250
                 ....*....|....
gi 46254554  232 KIVQNE--KELQAK 243
Cdd:PTZ00246 239 KKVTQEyaKENTNN 252
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-165 7.16e-48

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 157.44  E-value: 7.16e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGSTAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARI 84
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  85 LINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGsARLFHTEPSGIFHEYKATATG 164
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPSGVSYGYFGCAIG 162


                .
gi 46254554 165 R 165
Cdd:cd03751 163 K 163
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-199 4.89e-37

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: 127.90  E-value: 4.89e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  32 STAVGVRGANCVVLGVEKSSVSEMQE-DRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVTLEYIT 110
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554 111 RYLAQLKQKYTQcngRRPFGISCLIGGIDADGsARLFHTEPSGIFHEY-KATATGRWANTVREFFEKAYsdHEVTTKCDA 189
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLY--KPDMTLEEA 154

                       170
                ....*....|
gi 46254554 190 IKLAMRALLE 199
Cdd:cd01901 155 VELALKALKS 164
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-212 1.03e-35

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: 126.19  E-value: 1.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554   5 YGRALTIFSPDGHLLQVEYAQEAVRKGS-TAVGVRGANCVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADAR 83
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  84 ILINRGQVECQSHRLNFENQVTLEYITRYLAQLKQKYTQCNGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATAT 163
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46254554 164 GRWANTVREFFEKAY---SDHEVTTKcDAIKLAMRALLEVTQMS--QMRLEVAV 212
Cdd:cd03754 162 GVKEQEATNFLEKKLkkkPDLIESYE-ETVELAISCLQTVLSTDfkATEIEVGV 214
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 33-214 7.03e-17

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: 75.94  E-value: 7.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  33 TAVGVRGANCVVLGVEK-SSVSEMQEDRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVTLEYITR 111
Cdd:cd01912   2 TIVGIKGKDGVVLAADTrASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554 112 YLAQLKQKYtqcnGRRPFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATGRWANTVREFFEKAYsdHEVTTKCDAIK 191
Cdd:cd01912  82 LLSNILYSY----RGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY--KPDMTLEEAVE 155

                       170       180
                ....*....|....*....|....*.
gi 46254554 192 LAMRALLEVTQ---MSQMRLEVAVLE 214
Cdd:cd01912 156 LVKKAIDSAIErdlSSGGGVDVAVIT 181
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-197 1.90e-14

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: 69.20  E-value: 1.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  33 TAVGVRGANCVVLGVEK-SSVSEMQEDRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVTLEYITR 111
Cdd:cd03764   2 TTVGIVCKDGVVLAADKrASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554 112 YLAQLkqkytqCNGRR--PFGISCLIGGIDADGsARLFHTEPSGIFHEYKATATGRWANTVREFFEKAYSDhEVTTKcDA 189
Cdd:cd03764  82 LLSNI------LNSSKyfPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKE-DMTVE-EA 152


                ....*...
gi 46254554 190 IKLAMRAL 197
Cdd:cd03764 153 KKLAIRAI 160
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 1.30e-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: 51.97  E-value: 1.30e-09
                          10        20
                  ....*....|....*....|...
gi 46254554     5 YGRALTIFSPDGHLLQVEYAQEA 27
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 ...
 5-27 1.89e-09

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 51.73  E-value: 1.89e-09
                           10        20
                   ....*....|....*....|...
gi 46254554      5 YGRALTIFSPDGHLLQVEYAQEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-164 2.31e-06

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


Pssm-ID: 239726  Cd Length: 212  Bit Score: 46.87  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46254554  31 GSTAVGVRGAN-CVVLGVEKSSVSEMQEDRTVRKISMLDRHVALAFAGLTADARILINRGQVECQSHRLNFENQVTLEYI 109
Cdd:cd03757   8 GGTVLAIAGNDfAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46254554 110 TRYLAqlkqkyTQCNGRR--PFGISCLIGGIDADGSARLFHTEPSGIFHEYKATATG 164
Cdd:cd03757  88 AQLLS------TILYSRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGG 138
 
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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