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Conserved domains on  [gi|68303565|ref|NP_001020268|]
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proteasome subunit alpha-type 8 isoform 3 [Homo sapiens]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-175 1.27e-116

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


The actual alignment was detected with superfamily member cd03755:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 207  Bit Score: 330.48  E-value: 1.27e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRgkdcvvlgvekksvaklqdprtvrkicmlddhvclafaGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSGGKNIELAII 175
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 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 ...
 5-175 1.27e-116

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: 330.48  E-value: 1.27e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRgkdcvvlgvekksvaklqdprtvrkicmlddhvclafaGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSGGKNIELAII 175
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-193 2.58e-74

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 224.33  E-value: 2.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKtkdgvvlavdkritspliepssiekifkiddhigaasaGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSGGK--NIELAIIR-RNQPLKMFSAKEVELYV 193
Cdd:PRK03996 169 AGRDTVMEFLEKNYKED--LSLEEAIELALKALAKANEGKLDpeNVEIAYIDvETKKFRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-175 2.93e-68

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: 208.27  E-value: 2.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565     5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKtkdgvvlavdkritsklvepssiekifkiddhigaatsGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGALLEYKATAIG 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 68303565   127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSG--GKNIELAII 175
Cdd:TIGR03633 162 AGRQAVTEFLEKEYRED--LSLDEAIELALKALYSAVEDKltPENVEVAYI 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-179 1.14e-53

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 171.48  E-value: 1.14e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   1 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR---------------------------------------GLT 41
Cdd:COG0638   5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKtkdgvvlaadrratmgnliasksiekifkiddhigvaiaGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  42 ADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSnGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWK 121
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEK 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68303565 122 ANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQS---GGKNIELAIIRRNQ 179
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYRED--LSLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG 221
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 33-175 6.63e-48

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: 155.42  E-value: 6.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    33 TAVGIRGLTADARVVINRARVECQSHKLTVEDPVTVEyITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTD 112
Cdd:pfam00227  46 IGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQID 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68303565   113 PSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQ---SGGKNIELAII 175
Cdd:pfam00227 125 PSGSYIEYKATAIGSGSQYAYGVLEKLYRPD--LTLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 2.61e-11

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: 55.97  E-value: 2.61e-11
                           10        20
                   ....*....|....*....|...
gi 68303565      5 YDRAITVFSPDGHLFQVEYAQEA 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 ...
 5-175 1.27e-116

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: 330.48  E-value: 1.27e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRgkdcvvlgvekksvaklqdprtvrkicmlddhvclafaGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSGGKNIELAII 175
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-175 3.34e-88

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: 258.53  E-value: 3.34e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKgkdgvvlavekkvtsklldpssvekifkiddhigcavaGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIG 126
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSG--GKNIELAII 175
Cdd:cd01911 161 KGSQEAKTFLEKRYKKD--LTLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-193 2.58e-74

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 224.33  E-value: 2.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKtkdgvvlavdkritspliepssiekifkiddhigaasaGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYLEYKATAIG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSGGK--NIELAIIR-RNQPLKMFSAKEVELYV 193
Cdd:PRK03996 169 AGRDTVMEFLEKNYKED--LSLEEAIELALKALAKANEGKLDpeNVEIAYIDvETKKFRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-175 2.93e-68

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: 208.27  E-value: 2.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565     5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKtkdgvvlavdkritsklvepssiekifkiddhigaatsGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGALLEYKATAIG 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 68303565   127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSG--GKNIELAII 175
Cdd:TIGR03633 162 AGRQAVTEFLEKEYRED--LSLDEAIELALKALYSAVEDKltPENVEVAYI 210
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-175 1.61e-67

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: 206.03  E-value: 1.61e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKckegvvlavdkritsklvepesiekiykiddhvgaatsGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYNEYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSG--GKNIELAII 175
Cdd:cd03756 161 SGRQAVTEFLEKEYKED--MSLEEAIELALKALYAALEENetPENVEIAYV 209
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-192 9.17e-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: 171.74  E-value: 9.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKaangvvlatekkvpsplidessvhkveqitphigmvysGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGG-PYLYQVDPSGSYFTWKATAIG 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68303565 127 RSAKTVREFLEKNYTEDAIASDseAIKLAIKALLEVV--QSGGKNIELAIIRRNQPLKMFSAKEVELY 192
Cdd:cd03750 160 KNYSNAKTFLEKRYNEDLELED--AIHTAILTLKEGFegQMTEKNIEIGICGETKGFRLLTPAEIKDY 225
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-179 1.14e-53

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 171.48  E-value: 1.14e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   1 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR---------------------------------------GLT 41
Cdd:COG0638   5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKtkdgvvlaadrratmgnliasksiekifkiddhigvaiaGLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  42 ADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSnGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWK 121
Cdd:COG0638  85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEK 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68303565 122 ANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQS---GGKNIELAIIRRNQ 179
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYRED--LSLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG 221
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-175 4.64e-48

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: 156.68  E-value: 4.64e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR------------------------------------GLTADARVVI 48
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKskthavlvalkratselssyqkkifkvddhigiaiaGLTADARVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  49 NRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRS 128
Cdd:cd03749  81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPSGNYFEYKATSIGAR 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 68303565 129 AKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGG----KNIELAII 175
Cdd:cd03749 160 SQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQeltiKNVSIAIV 210
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 33-175 6.63e-48

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: 155.42  E-value: 6.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    33 TAVGIRGLTADARVVINRARVECQSHKLTVEDPVTVEyITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTD 112
Cdd:pfam00227  46 IGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQID 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68303565   113 PSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQ---SGGKNIELAII 175
Cdd:pfam00227 125 PSGSYIEYKATAIGSGSQYAYGVLEKLYRPD--LTLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-175 1.29e-46

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 152.89  E-value: 1.29e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   3 SRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGI---------------------------------------RGLTAD 43
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGIlakdgivlaaekkvtsklldqsfssekiykiddhiacavAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  44 ARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKAN 123
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 68303565 124 AIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKAL---LEVVQSGGKNIELAII 175
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDD--MTLEEALALAVKVLsktMDSTKLTSEKLEFATL 213
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-175 1.12e-45

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: 150.57  E-value: 1.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKtkegvvlavekritsplmepssvekimeiddhigcamsGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGR-----RPFGISALIVGFDDDGiSRLYQTDPSGTYHAWK 121
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFHTDPSGTFTRCD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 68303565 122 ANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQS--GGKNIELAII 175
Cdd:cd03753 160 AKAIGSGSEGAQSSLQEKYHKD--MTLEEAEKLALSILKQVMEEklNSTNVELATV 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-190 1.91e-43

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 146.15  E-value: 1.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565    1 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGI---------------------------------------RGLT 41
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGIlckegvilgadkpissklldpgkinekiykidshifcavAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   42 ADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWK 121
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68303565  122 ANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQS---GGKNIELAIIRRNQP-----LKMFSAKEVE 190
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKED--LTLEQGLLLAAKVLTKSMDStspKADKIEVGILSHGETdgepiQKMLSEKEIA 235
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-175 7.04e-42

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: 139.55  E-value: 7.04e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  32 STAVGIRGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSngRRPFGISALIVGFDDDGISRLYQT 111
Cdd:cd01906  40 HIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSV 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68303565 112 DPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQSG---GKNIELAII 175
Cdd:cd01906 118 DPSGSYIEYKATAIGSGSQYALGILEKLYKPD--MTLEEAIELALKALKSALERDlysGGNIEVAVI 182
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-175 4.74e-39

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: 133.51  E-value: 4.74e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGS-TAVGIR--------------------------------------GLTADAR 45
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRgkdcavvvtqkkvpdklidpstvthlfritdeigcvmtGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  46 VVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAI 125
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 68303565 126 GRSAKTVREFLEKNY--TEDAIASDSEAIKLAIKALLEVVQSG--GKNIELAII 175
Cdd:cd03754 162 GVKEQEATNFLEKKLkkKPDLIESYEETVELAISCLQTVLSTDfkATEIEVGVV 215
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-162 5.17e-33

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


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 117.77  E-value: 5.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565   5 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIR--------------------------------------GLTADARV 46
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRckdgvvlaveklvtsklyepgsnkrifnvdrhigiavaGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  47 VINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIG 126
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPSGVSYGYFGCAIG 162

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 68303565 127 RSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEV 162
Cdd:cd03751 163 KGKQAAKTELEKLKFSE--LTCREAVKEAAKIIYIV 196
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 33-161 1.14e-24

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: 94.77  E-value: 1.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  33 TAVGIRGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQsngRRPFGISALIVGFDDDGiSRLYQTD 112
Cdd:cd01901  41 IAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYID 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 68303565 113 PSGTYHAW-KANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLE 161
Cdd:cd01901 117 PSGPVIENpGAVATGSRSQRAKSLLEKLYKPD--MTLEEAVELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-178 4.65e-12

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


Pssm-ID: 238893  Cd Length: 189  Bit Score: 62.08  E-value: 4.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  32 STAVGIRGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYtqsnGRRPFGISALIVGFDDDGISRLYQT 111
Cdd:cd01912  40 NILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANLLSNILYSY----RGFPYYVSLIVGGVDKGGGPFLYYV 115

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68303565 112 DPSGTYHawKAN--AIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEV----VQSGGkNIELAIIRRN 178
Cdd:cd01912 116 DPLGSLI--EAPfvATGSGSKYAYGILDRGYKPD--MTLEEAVELVKKAIDSAierdLSSGG-GVDVAVITKD 183
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 1.14e-11

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 56.97  E-value: 1.14e-11
                          10        20
                  ....*....|....*....|...
gi 68303565     5 YDRAITVFSPDGHLFQVEYAQEA 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 2.61e-11

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: 55.97  E-value: 2.61e-11
                           10        20
                   ....*....|....*....|...
gi 68303565      5 YDRAITVFSPDGHLFQVEYAQEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-178 1.65e-10

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: 58.03  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68303565  34 AVGIRGLTADARVVINRARVECQSHKLTVEDPVTVeyitRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDP 113
Cdd:cd03764  42 AMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSI----KALATLLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDP 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68303565 114 SGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSEAIKLAIKALLEVVQ---SGGKNIELAIIRRN 178
Cdd:cd03764 117 LGSIIEDKYTATGSGSPYAYGVLEDEYKED--MTVEEAKKLAIRAIKSAIErdsASGDGIDVVVITKD 182
 
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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