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Conserved domains on  [gi|767998215|ref|XP_011524120|]
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proteasome subunit alpha-type 8 isoform X1 [Homo sapiens]

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

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 ...
 9-193 1.64e-122

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: 345.89  E-value: 1.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03755   31 VGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFA------GLTADARVLINRARLECQSHRLTVEDPVTVEY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd03755  105 ITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEE--MTRDD 182

                        170       180
                 ....*....|....*....|....*
gi 767998215 169 AIKLAIKALLEVVQSGGKNIELAII 193
Cdd:cd03755  183 TIKLAIKALLEVVQSGSKNIELAVM 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 ...
 9-193 1.64e-122

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: 345.89  E-value: 1.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03755   31 VGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFA------GLTADARVLINRARLECQSHRLTVEDPVTVEY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd03755  105 ITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEE--MTRDD 182

                        170       180
                 ....*....|....*....|....*
gi 767998215 169 AIKLAIKALLEVVQSGGKNIELAII 193
Cdd:cd03755  183 TIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
9-211 3.74e-65

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 201.99  E-value: 3.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:PRK03996  40 VGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASA------GLVADARVLIDRARVEAQINRLTYGEPIGVET 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:PRK03996 114 LTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKED--LSLEE 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767998215 169 AIKLAIKALLEVVQSGGK--NIELAIIR-RNQPLKMFSAKEVELYV 211
Cdd:PRK03996 191 AIELALKALAKANEGKLDpeNVEIAYIDvETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 9-193 4.14e-64

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: 197.40  E-value: 4.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215    9 VGIRGTNIVVLGVEKKSVA--KLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTV 86
Cdd:pfam00227   8 VGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFA------GLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   87 EyITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASD 166
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPD--LTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 767998215  167 SEAIKLAIKALLEVVQ---SGGKNIELAII 193
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 9-193 4.62e-59

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: 185.55  E-value: 4.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215    9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:TIGR03633  33 VGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATS------GLVADARVLIDRARIEAQINRLTYGEPIDVET 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:TIGR03633 107 LAKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGALLEYKATAIGAGRQAVTEFLEKEYRED--LSLDE 183

                         170       180
                  ....*....|....*....|....*..
gi 767998215  169 AIKLAIKALLEVVQSG--GKNIELAII 193
Cdd:TIGR03633 184 AIELALKALYSAVEDKltPENVEVAYI 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-197 2.01e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 163.78  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVA-KLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:COG0638   39 VGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIA------GLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQSnGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:COG0638  113 GLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYRED--LSLD 188

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767998215 168 EAIKLAIKALLEVVQS---GGKNIELAIIRRNQ 197
Cdd:COG0638  189 EAVELALRALYSAAERdsaSGDGIDVAVITEDG 221
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 1.64e-122

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: 345.89  E-value: 1.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03755   31 VGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFA------GLTADARVLINRARLECQSHRLTVEDPVTVEY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd03755  105 ITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEE--MTRDD 182

                        170       180
                 ....*....|....*....|....*
gi 767998215 169 AIKLAIKALLEVVQSGGKNIELAII 193
Cdd:cd03755  183 TIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 6.44e-87

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: 255.83  E-value: 6.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd01911   31 VGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVA------GLTADARVLVNRARVEAQNYRYTYGEPIPVEV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd01911  105 LVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKD--LTLEE 182

                        170       180
                 ....*....|....*....|....*..
gi 767998215 169 AIKLAIKALLEVVQSG--GKNIELAII 193
Cdd:cd01911  183 AIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
9-211 3.74e-65

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 201.99  E-value: 3.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:PRK03996  40 VGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASA------GLVADARVLIDRARVEAQINRLTYGEPIGVET 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:PRK03996 114 LTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKED--LSLEE 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767998215 169 AIKLAIKALLEVVQSGGK--NIELAIIR-RNQPLKMFSAKEVELYV 211
Cdd:PRK03996 191 AIELALKALAKANEGKLDpeNVEIAYIDvETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 9-193 4.14e-64

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: 197.40  E-value: 4.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215    9 VGIRGTNIVVLGVEKKSVA--KLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTV 86
Cdd:pfam00227   8 VGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFA------GLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   87 EyITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASD 166
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPD--LTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 767998215  167 SEAIKLAIKALLEVVQ---SGGKNIELAII 193
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 9-193 4.62e-59

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: 185.55  E-value: 4.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215    9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:TIGR03633  33 VGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATS------GLVADARVLIDRARIEAQINRLTYGEPIDVET 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:TIGR03633 107 LAKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGALLEYKATAIGAGRQAVTEFLEKEYRED--LSLDE 183

                         170       180
                  ....*....|....*....|....*..
gi 767998215  169 AIKLAIKALLEVVQSG--GKNIELAII 193
Cdd:TIGR03633 184 AIELALKALYSAVEDKltPENVEVAYI 210
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 7.37e-59

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: 184.84  E-value: 7.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03756   32 LGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATS------GLVADARVLIDRARVEAQIHRLTYGEPIDVEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd03756  106 LVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG-PRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKED--MSLEE 182

                        170       180
                 ....*....|....*....|....*..
gi 767998215 169 AIKLAIKALLEVVQSG--GKNIELAII 193
Cdd:cd03756  183 AIELALKALYAALEENetPENVEIAYV 209
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-210 4.52e-58

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: 183.29  E-value: 4.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03750   31 VGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYS------GMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDse 168
Cdd:cd03750  105 LVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGG-PYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELED-- 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767998215 169 AIKLAIKALLEVV--QSGGKNIELAIIRRNQPLKMFSAKEVELY 210
Cdd:cd03750  182 AIHTAILTLKEGFegQMTEKNIEIGICGETKGFRLLTPAEIKDY 225
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 9-193 1.24e-55

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 175.38  E-value: 1.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQD-ERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:cd01906    4 VGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFA------GLAADAQTLVERLRKEAQLYRLRYGEPIPVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQSngRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:cd01906   78 ALAKLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD--MTLE 153

                        170       180
                 ....*....|....*....|....*....
gi 767998215 168 EAIKLAIKALLEVVQSG---GKNIELAII 193
Cdd:cd01906  154 EAIELALKALKSALERDlysGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-197 2.01e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 163.78  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVA-KLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:COG0638   39 VGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIA------GLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQSnGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:COG0638  113 GLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYRED--LSLD 188

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767998215 168 EAIKLAIKALLEVVQS---GGKNIELAIIRRNQ 197
Cdd:COG0638  189 EAVELALRALYSAAERdsaSGDGIDVAVITEDG 221
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 2.64e-45

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: 150.19  E-value: 2.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQD-ERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:cd03752   33 LGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVA------GITSDANILINYARLIAQRYLYSYQEPIPVE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:cd03752  107 QLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDD--MTLE 184

                        170       180
                 ....*....|....*....|....*....
gi 767998215 168 EAIKLAIKAL---LEVVQSGGKNIELAII 193
Cdd:cd03752  185 EALALAVKVLsktMDSTKLTSEKLEFATL 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 7.69e-42

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: 141.27  E-value: 7.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERtvRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03749   31 VGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIA------GLTADARVLSRYMRQECLNYRFVYDSPIPVSR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSE 168
Cdd:cd03749  103 LVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEEFEDCSLEE 181

                        170       180
                 ....*....|....*....|....*....
gi 767998215 169 AIKLAIKALLEVVQSGG----KNIELAII 193
Cdd:cd03749  182 LIKHALRALRETLPGEQeltiKNVSIAIV 210
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 7.36e-40

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: 136.31  E-value: 7.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03753   31 IGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMS------GLIADARTLIDHARVEAQNHRFTYNEPMTVES 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGR-----RPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDai 163
Cdd:cd03753  105 VTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKD-- 181

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767998215 164 ASDSEAIKLAIKALLEVVQS--GGKNIELAII 193
Cdd:cd03753  182 MTLEEAEKLALSILKQVMEEklNSTNVELATV 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 9-208 4.01e-39

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 135.75  E-value: 4.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDE-RTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:PTZ00246  35 VGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVA------GLTADANILINQCRLYAQRYRYTYGEPQPVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:PTZ00246 109 QLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKED--LTLE 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767998215 168 EAIKLAIKALLEVVQS---GGKNIELAIIRRNQP-----LKMFSAKEVE 208
Cdd:PTZ00246 187 QGLLLAAKVLTKSMDStspKADKIEVGILSHGETdgepiQKMLSEKEIA 235
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 9-179 1.39e-34

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: 120.96  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQD-ERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:cd01901    4 VAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLA------GLAADAQTLVRRLREALQLYRLRYGEPISVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYTQsngRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAW-KANAIGRSAKTVREFLEKNYTEDaiASD 166
Cdd:cd01901   78 ALAKELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD--MTL 151

                        170
                 ....*....|...
gi 767998215 167 SEAIKLAIKALLE 179
Cdd:cd01901  152 EEAVELALKALKS 164
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-193 4.45e-32

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: 116.18  E-value: 4.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVcmaFAVLTifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03754   33 VAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEI---GCVMT---GMIADSRSQVQRARYEAAEFKYKYGYEMPVDV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNY--TEDAIASD 166
Cdd:cd03754  107 LAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAAGVKEQEATNFLEKKLkkKPDLIESY 186

                        170       180
                 ....*....|....*....|....*....
gi 767998215 167 SEAIKLAIKALLEVVQSG--GKNIELAII 193
Cdd:cd03754  187 EETVELAISCLQTVLSTDfkATEIEVGVV 215
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-180 1.28e-31

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: 115.07  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVEY 88
Cdd:cd03751   34 IGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVA------GLLADGRHLVSRAREEAENYRDNYGTPIPVKV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  89 ITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDSE 168
Cdd:cd03751  108 LADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSE--LTCRE 184

                        170
                 ....*....|..
gi 767998215 169 AIKLAIKALLEV 180
Cdd:cd03751  185 AVKEAAKIIYIV 196
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-196 2.79e-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: 76.71  E-value: 2.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKKSVA-KLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVE 87
Cdd:cd01912    4 VGIKGKDGVVLAADTRASAgSLVASRNFDKIFKISDNILLGTA------GSAADTQALTRLLKRNLRLYELRNGRELSVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 YITRFIATLKQKYtqsnGRRPFGISALIVGFDDDGISRLYQTDPSGTYHawKAN--AIGRSAKTVREFLEKNYTEDaiAS 165
Cdd:cd01912   78 AAANLLSNILYSY----RGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLI--EAPfvATGSGSKYAYGILDRGYKPD--MT 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767998215 166 DSEAIKLAIKALLEV----VQSGGkNIELAIIRRN 196
Cdd:cd01912  150 LEEAVELVKKAIDSAierdLSSGG-GVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 9-196 9.30e-17

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


Pssm-ID: 239733  Cd Length: 188  Bit Score: 75.37  E-value: 9.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215   9 VGIRGTNIVVLGVEKK-SVAKLQDERTVRKICALDDHVCMAFAvltifiGLTADARVVINRARVECQSHKLTVEDPVTVe 87
Cdd:cd03764    4 VGIVCKDGVVLAADKRaSMGNFIASKNVKKIFQIDDKIAMTIA------GSVGDAQSLVRILKAEARLYELRRGRPMSI- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998215  88 yitRFIATLKQKYTQSNGRRPFGISALIVGFDDDGiSRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDaiASDS 167
Cdd:cd03764   77 ---KALATLLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED--MTVE 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767998215 168 EAIKLAIKALLEVVQ---SGGKNIELAIIRRN 196
Cdd:cd03764  151 EAKKLAIRAIKSAIErdsASGDGIDVVVITKD 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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