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Conserved domains on  [gi|74212039|dbj|BAE40184|]
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unnamed protein product [Mus musculus]

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 ...
 1-141 9.31e-101

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: 288.88  E-value: 9.31e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd03755  69 LAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPS 148

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 141
Cdd:cd03755 149 GTYSAWKANAIGRNSKTVREFLEKNYKEE--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 ...
 1-141 9.31e-101

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: 288.88  E-value: 9.31e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd03755  69 LAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPS 148

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 141
Cdd:cd03755 149 GTYSAWKANAIGRNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
2-160 1.80e-57

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 180.03  E-value: 1.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039    2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSG 81
Cdd:PRK03996  79 ASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   82 TYHAWKANAIGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSGGK--NIELA-VMRRDQPLKILNPEEIEKY 158
Cdd:PRK03996 158 AYLEYKATAIGAGRDTVMEFLEKNYKED-LSLEE-AIELALKALAKANEGKLDpeNVEIAyIDVETKKFRKLSVEEIEKY 235


                 ..
gi 74212039  159 VA 160
Cdd:PRK03996 236 LE 237
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-141 2.08e-52

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: 165.43  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039     1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEyITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:pfam00227  48 MAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPS 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74212039    81 GTYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQ---SGGKNIELAVM 141
Cdd:pfam00227 127 GSYIEYKATAIGSGSQYAYGVLEKLYRPDL--TLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-154 1.02e-49

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: 159.74  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039     2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSG 81
Cdd:TIGR03633  72 ATSGLVADARVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSG 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74212039    82 TYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQSG--GKNIELAVM-RRDQPLKILNPEE 154
Cdd:TIGR03633 151 ALLEYKATAIGAGRQAVTEFLEKEYREDL--SLDEAIELALKALYSAVEDKltPENVEVAYItVEDKKFRKLSVEE 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-154 9.87e-40

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 134.50  E-value: 9.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSnGRRPFGISALIVGFDfDGTPRLYQTDPS 80
Cdd:COG0638  78 VAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPS 155

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQpLKILNPEE 154
Cdd:COG0638 156 GGLYEEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG-FRELSEEE 229
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-141 9.31e-101

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: 288.88  E-value: 9.31e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd03755  69 LAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPS 148

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 141
Cdd:cd03755 149 GTYSAWKANAIGRNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-141 1.00e-69

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: 209.99  E-value: 1.00e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd01911  69 CAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPS 148

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSG--GKNIELAVM 141
Cdd:cd01911 149 GTYFGYKATAIGKGSQEAKTFLEKRYKKD--LTLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
2-160 1.80e-57

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 180.03  E-value: 1.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039    2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSG 81
Cdd:PRK03996  79 ASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   82 TYHAWKANAIGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSGGK--NIELA-VMRRDQPLKILNPEEIEKY 158
Cdd:PRK03996 158 AYLEYKATAIGAGRDTVMEFLEKNYKED-LSLEE-AIELALKALAKANEGKLDpeNVEIAyIDVETKKFRKLSVEEIEKY 235


                 ..
gi 74212039  159 VA 160
Cdd:PRK03996 236 LE 237
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-141 2.08e-52

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: 165.43  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039     1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEyITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:pfam00227  48 MAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPS 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74212039    81 GTYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQ---SGGKNIELAVM 141
Cdd:pfam00227 127 GSYIEYKATAIGSGSQYAYGVLEKLYRPDL--TLEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-154 1.02e-49

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: 159.74  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039     2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSG 81
Cdd:TIGR03633  72 ATSGLVADARVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSG 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74212039    82 TYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQSG--GKNIELAVM-RRDQPLKILNPEE 154
Cdd:TIGR03633 151 ALLEYKATAIGAGRQAVTEFLEKEYREDL--SLDEAIELALKALYSAVEDKltPENVEVAYItVEDKKFRKLSVEE 224
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-160 1.28e-49

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: 159.79  E-value: 1.28e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPS 80
Cdd:cd03750  69 MVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPS 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaIETDD--LTIKLVIKALLEvVQSGGKNIELAVMRRDQPLKILNPEEIEKY 158
Cdd:cd03750 148 GSYFTWKATAIGKNYSNAKTFLEKRYNED-LELEDaiHTAILTLKEGFE-GQMTEKNIEIGICGETKGFRLLTPAEIKDY 225


                ..
gi 74212039 159 VA 160
Cdd:cd03750 226 LA 227
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-140 7.63e-48

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: 154.80  E-value: 7.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSG 81
Cdd:cd03756  71 ATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSG 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74212039  82 TYHAWKANAIGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSG--GKNIELAV 140
Cdd:cd03756 150 AYNEYKATAIGSGRQAVTEFLEKEYKED-MSLEE-AIELALKALYAALEENetPENVEIAY 208
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 1-141 3.69e-45

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: 146.87  E-value: 3.69e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSngRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd01906  43 CAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPS 120

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSG---GKNIELAVM 141
Cdd:cd01906 121 GSYIEYKATAIGSGSQYALGILEKLYKPD--MTLEEAIELALKALKSALERDlysGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-154 9.87e-40

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 134.50  E-value: 9.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSnGRRPFGISALIVGFDfDGTPRLYQTDPS 80
Cdd:COG0638  78 VAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPS 155

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQpLKILNPEE 154
Cdd:COG0638 156 GGLYEEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG-FRELSEEE 229
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-141 9.41e-36

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: 123.61  E-value: 9.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSG 81
Cdd:cd03752  73 AVAGITSDANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSG 152

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74212039  82 TYHAWKANAIGRGAKSVREFLEKNYTDDAI--ETDDLTIKLVIKAlLEVVQSGGKNIELAVM 141
Cdd:cd03752 153 NYSGWKATAIGNNNQAAQSLLKQDYKDDMTleEALALAVKVLSKT-MDSTKLTSEKLEFATL 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-140 4.05e-34

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: 119.70  E-value: 4.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGtPRLYQTDPS 80
Cdd:cd03749  67 IAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPS 145

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDAIETDDLTIKLVIKALLEVVQSGG----KNIELAV 140
Cdd:cd03749 146 GNYFEYKATSIGARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQeltiKNVSIAI 209
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-141 2.87e-33

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: 117.44  E-value: 2.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGR-----RPFGISALIVGFDFDGtPRLYQ 76
Cdd:cd03753  70 AMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFH 148

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74212039  77 TDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS--GGKNIELAVM 141
Cdd:cd03753 149 TDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDM--TLEEAEKLALSILKQVMEEklNSTNVELATV 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 2-159 3.08e-32

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 115.72  E-value: 3.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039    2 AFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSG 81
Cdd:PTZ00246  75 AVAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   82 TYHAWKANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQP-----LKILNPE 153
Cdd:PTZ00246 155 NYSGWKATAIGQNNQTAQSILKQEWKEDL--TLEQGLLLAAKVLTKSMDStspKADKIEVGILSHGETdgepiQKMLSEK 232


                 ....*.
gi 74212039  154 EIEKYV 159
Cdd:PTZ00246 233 EIAELL 238
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-127 2.47e-28

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: 103.24  E-value: 2.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQsngRRPFGISALIVGFDFDGtPRLYQTDPS 80
Cdd:cd01901  43 WGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYIDPS 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 74212039  81 GTYHAW-KANAIGRGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLE 127
Cdd:cd01901 119 GPVIENpGAVATGSRSQRAKSLLEKLYKPD--MTLEEAVELALKALKS 164
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-129 1.33e-24

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: 95.04  E-value: 1.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGtPRLYQTDPS 80
Cdd:cd03751  72 IAVAGLLADGRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPS 150

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKnytddaIETDDLTIKLVIKALLEVV 129
Cdd:cd03751 151 GVSYGYFGCAIGKGKQAAKTELEK------LKFSELTCREAVKEAAKII 193
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-140 9.42e-24

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: 92.68  E-value: 9.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   5 GLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYH 84
Cdd:cd03754  75 GMIADSRSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFA 154

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039  85 AWKANAIGRGAKSVREFLEKNY--TDDAIETDDLTIKLVIKALLEVVQSG--GKNIELAV 140
Cdd:cd03754 155 GYKATAAGVKEQEATNFLEKKLkkKPDLIESYEETVELAISCLQTVLSTDfkATEIEVGV 214
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-144 1.97e-14

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: 67.47  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYtqsnGRRPFGISALIVGFDFDGTPRLYQTDPS 80
Cdd:cd01912  43 LGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANLLSNILYSY----RGFPYYVSLIVGGVDKGGGPFLYYVDPL 118

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039  81 GTYHawKAN--AIGRGAKSVREFLEKNYTDDaIETDDLtIKLVIKALLEV----VQSGGkNIELAVMRRD 144
Cdd:cd01912 119 GSLI--EAPfvATGSGSKYAYGILDRGYKPD-MTLEEA-VELVKKAIDSAierdLSSGG-GVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-144 6.66e-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: 55.34  E-value: 6.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74212039   1 MAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLkqryTQSNGRRPFGISALIVGFDFDGtPRLYQTDPS 80
Cdd:cd03764  43 MTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNI----LNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPL 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74212039  81 GTYHAWKANAIGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQ---SGGKNIELAVMRRD 144
Cdd:cd03764 118 GSIIEDKYTATGSGSPYAYGVLEDEYKED-MTVEE-AKKLAIRAIKSAIErdsASGDGIDVVVITKD 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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