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Conserved domains on  [gi|1061214199|ref|NP_001317602|]
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proteasome subunit alpha type-4 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 ...
 3-169 5.40e-130

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 cd03752:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 213  Bit Score: 362.82  E-value: 5.40e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752     1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160


                  ....*..
gi 1061214199 163 CIGNNSA 169
Cdd:cd03752   161 AIGNNNQ 167
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-169 5.40e-130

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: 362.82  E-value: 5.40e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752     1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160


                  ....*..
gi 1061214199 163 CIGNNSA 169
Cdd:cd03752   161 AIGNNNQ 167
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-168 5.25e-91

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 265.56  E-value: 5.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 80
Cdd:PTZ00246    1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  81 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 160
Cdd:PTZ00246   81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160


                  ....*...
gi 1061214199 161 ATCIGNNS 168
Cdd:PTZ00246  161 ATAIGQNN 168
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-165 1.97e-64

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: 197.10  E-value: 1.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160


                  .
gi 1061214199 165 G 165
Cdd:TIGR03633 161 G 161
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-168 8.55e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 162.62  E-value: 8.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMAC 74
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  75 SVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSG 154
Cdd:COG0638    79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSG 156

                         170
                  ....*....|....
gi 1061214199 155 NYGGWKATCIGNNS 168
Cdd:COG0638   157 GLYEEKAVAIGSGS 170
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-168 2.87e-49

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: 157.34  E-value: 2.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  30 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 107
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061214199 108 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNS 168
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGS 141
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 2.30e-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: 55.58  E-value: 2.30e-11
                           10        20
                   ....*....|....*....|...
gi 1061214199    5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-169 5.40e-130

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: 362.82  E-value: 5.40e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752     1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160


                  ....*..
gi 1061214199 163 CIGNNSA 169
Cdd:cd03752   161 AIGNNNQ 167
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-168 1.99e-96

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


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 277.79  E-value: 1.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd01911     1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd01911    80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159


                  ....
gi 1061214199 165 GNNS 168
Cdd:cd01911   160 GKGS 163
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-168 5.25e-91

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 265.56  E-value: 5.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 80
Cdd:PTZ00246    1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  81 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 160
Cdd:PTZ00246   81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160


                  ....*...
gi 1061214199 161 ATCIGNNS 168
Cdd:PTZ00246  161 ATAIGQNN 168
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-168 3.72e-66

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 201.99  E-value: 3.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVffS-EKIYKLNEDMACSVAGITSDA 83
Cdd:PRK03996   10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPS--SiEKIFKIDDHIGAASAGLVADA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  84 NVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATC 163
Cdd:PRK03996   88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATA 166


                  ....*
gi 1061214199 164 IGNNS 168
Cdd:PRK03996  167 IGAGR 171
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-165 9.50e-66

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: 199.86  E-value: 9.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03756     2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLV-EPESIEKIYKIDDHVGAATSGLVADAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03756    81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAI 159


                  .
gi 1061214199 165 G 165
Cdd:cd03756   160 G 160
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-165 1.97e-64

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: 197.10  E-value: 1.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160


                  .
gi 1061214199 165 G 165
Cdd:TIGR03633 161 G 161
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-168 4.03e-56

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: 175.97  E-value: 4.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  10 TIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSeKIYKLNEDMACSVAGITSDANVLTNE 89
Cdd:cd03750     6 TTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVH-KVEQITPHIGMVYSGMGPDFRVLVKK 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061214199  90 LRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKhYGFQLYQSDPSGNYGGWKATCIGNNS 168
Cdd:cd03750    85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKATAIGKNY 162
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-168 1.30e-55

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: 174.09  E-value: 1.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTV-RKICMLDDHVCLAFAGLTADAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03755    80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159


                  ....
gi 1061214199 165 GNNS 168
Cdd:cd03755   160 GRNS 163
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-168 8.55e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 162.62  E-value: 8.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMAC 74
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  75 SVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSG 154
Cdd:COG0638    79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSG 156

                         170
                  ....*....|....
gi 1061214199 155 NYGGWKATCIGNNS 168
Cdd:COG0638   157 GLYEEKAVAIGSGS 170
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-168 1.06e-50

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 161.69  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLldeVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03749    78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSI 156


                  ....
gi 1061214199 165 GNNS 168
Cdd:cd03749   157 GARS 160
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-168 2.87e-49

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: 157.34  E-value: 2.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  30 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 107
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061214199 108 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNS 168
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGS 141
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-168 1.56e-47

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: 152.65  E-value: 1.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1061214199 112 TALCDIKQAYTQFggKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNS 168
Cdd:cd01906    81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGS 135
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-166 5.13e-45

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: 147.38  E-value: 5.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAG-TCLGILANDGVLLAAERRNIHKLLDEVFFSEkIYKLNEDMACSVAGITSDA 83
Cdd:cd03754     2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTH-LFRITDEIGCVMTGMIADS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  84 NVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATC 163
Cdd:cd03754    81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160


                  ...
gi 1061214199 164 IGN 166
Cdd:cd03754   161 AGV 163
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-168 1.29e-43

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: 143.63  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGK-----RPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGW 159
Cdd:cd03753    80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158


                  ....*....
gi 1061214199 160 KATCIGNNS 168
Cdd:cd03753   159 DAKAIGSGS 167
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-165 4.73e-39

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: 132.02  E-value: 4.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAErRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03751     4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVE-KLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03751    83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGCAI 161


                  .
gi 1061214199 165 G 165
Cdd:cd03751   162 G 162
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-168 3.87e-32

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: 112.87  E-value: 3.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1061214199 112 TALCDIKQAYTQFggkRPFGVSLLYIGWDKHYGfQLYQSDPSGNYGGW-KATCIGNNS 168
Cdd:cd01901    81 KELAKLLQVYTQG---RPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENpGAVATGSRS 134
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-154 1.62e-15

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: 70.36  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  33 TCLGILANDGVLLAAERRN------IHKLLDevffseKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 106
Cdd:cd03764     2 TTVGIVCKDGVVLAADKRAsmgnfiASKNVK------KIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1061214199 107 CEQLVTALCDIKQAYTQFggkrPFGVSLLYIGWDKHyGFQLYQSDPSG 154
Cdd:cd03764    76 IKALATLLSNILNSSKYF----PYIVQLLIGGVDEE-GPHLYSLDPLG 118
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-156 3.93e-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: 66.70  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1061214199 112 TALCDIkQAYTQFGgkrPFGVSLLYIGWDKHYGFQLYQSDPSGNY 156
Cdd:cd01912    81 NLLSNI-LYSYRGF---PYYVSLIVGGVDKGGGPFLYYVDPLGSL 121
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 2.30e-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: 55.58  E-value: 2.30e-11
                           10        20
                   ....*....|....*....|...
gi 1061214199    5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 4.10e-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: 54.66  E-value: 4.10e-11
                          10        20
                  ....*....|....*....|...
gi 1061214199   5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-169 2.18e-07

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


Pssm-ID: 239726  Cd Length: 212  Bit Score: 48.79  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214199  32 GTCLGILANDGVLLAAERR-----NIHKLldevfFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 106
Cdd:cd03757     9 GTVLAIAGNDFAVIAGDTRlsegySILSR-----DSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1061214199 107 CEQLVTALCDIkqAYtqfgGKR--PFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSA 169
Cdd:cd03757    84 TEAIAQLLSTI--LY----SRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASS 142
 
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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