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Conserved domains on  [gi|398365453|ref|NP_014800|]
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proteasome core particle subunit beta 2 [Saccharomyces cerevisiae S288C]

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-219 3.25e-124

proteasome beta type-7 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: 239732  Cd Length: 189  Bit Score: 351.11  E-value: 3.25e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQ 189
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 398365453 190 AGIWNDLGSGSNVDVCVMEIGKdAEYLRNY 219
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDG-VEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 222-257 6.32e-15

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


:

Pssm-ID: 463597  Cd Length: 36  Bit Score: 66.65  E-value: 6.32e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 398365453  222 PNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQV 257
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVPLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-219 3.25e-124

proteasome beta type-7 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: 239732  Cd Length: 189  Bit Score: 351.11  E-value: 3.25e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQ 189
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 398365453 190 AGIWNDLGSGSNVDVCVMEIGKdAEYLRNY 219
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDG-VEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-207 7.52e-61

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 190.09  E-value: 7.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453   26 TSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKN-CAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPR 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  105 VVS----ALQMLKQHLFKYQGHIGAYLIVAGVDPTGS-HLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEE 179
Cdd:pfam00227  81 VELaariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 398365453  180 AIKLASDAIQAGIWNDLGSGSNVDVCVM 207
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 29-212 1.09e-42

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 143.50  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453   29 GTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSA 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  109 LQMLKQHLfkYQGHIGAY---LIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLAS 185
Cdd:TIGR03634  81 ATLLSNIL--NSNRFFPFivqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 398365453  186 DAIQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAV--ITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 23-212 7.21e-41

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 140.28  E-value: 7.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  23 PKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSRE 102
Cdd:COG0638   29 REAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PRVVSALQMLKQHLFKYQGH----IGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKE 178
Cdd:COG0638  109 ISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLD 188

                        170       180       190
                 ....*....|....*....|....*....|....
gi 398365453 179 EAIKLASDAIQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:COG0638  189 EAVELALRALYSAAERDSASGDGIDVAV--ITED 220
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-204 7.07e-28

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 107.00  E-value: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  13 NFLAENSHTQPKAT-----STGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQL 87
Cdd:PTZ00488  18 DFLAEYTFDHGDANkaiefAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  88 IGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGH-IGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAV 166
Cdd:PTZ00488  98 LAMQCRLYELRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGV 177

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 398365453 167 LESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDV 204
Cdd:PTZ00488 178 LDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 222-257 6.32e-15

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 66.65  E-value: 6.32e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 398365453  222 PNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQV 257
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVPLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-219 3.25e-124

proteasome beta type-7 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: 239732  Cd Length: 189  Bit Score: 351.11  E-value: 3.25e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQ 189
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 398365453 190 AGIWNDLGSGSNVDVCVMEIGKdAEYLRNY 219
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDG-VEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-212 1.66e-76

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: 230.02  E-value: 1.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQG-HIGAYLIVAGVDP-TGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDA 187
Cdd:cd01912   81 NLLSNILYSYRGfPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*
gi 398365453 188 IQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAV--ITKD 183
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 30-207 3.49e-63

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: 195.79  E-value: 3.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQ---GHIGAYLIVAGVDP-TGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLAS 185
Cdd:cd01906   81 KLLANLLYEYTqslRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                        170       180
                 ....*....|....*....|..
gi 398365453 186 DAIQAGIWNDLGSGSNVDVCVM 207
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-207 7.52e-61

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 190.09  E-value: 7.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453   26 TSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKN-CAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPR 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  105 VVS----ALQMLKQHLFKYQGHIGAYLIVAGVDPTGS-HLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEE 179
Cdd:pfam00227  81 VELaariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 398365453  180 AIKLASDAIQAGIWNDLGSGSNVDVCVM 207
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 30-190 2.52e-43

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: 144.46  E-value: 2.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQ--GHIGAYLIVAGVDPTGSHLFSIHAHGSTDVG-YYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASD 186
Cdd:cd01901   81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                 ....
gi 398365453 187 AIQA 190
Cdd:cd01901  161 ALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 29-212 1.09e-42

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 143.50  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453   29 GTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSA 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  109 LQMLKQHLfkYQGHIGAY---LIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLAS 185
Cdd:TIGR03634  81 ATLLSNIL--NSNRFFPFivqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 398365453  186 DAIQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAV--ITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 23-212 7.21e-41

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 140.28  E-value: 7.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  23 PKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSRE 102
Cdd:COG0638   29 REAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PRVVSALQMLKQHLFKYQGH----IGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKE 178
Cdd:COG0638  109 ISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLD 188

                        170       180       190
                 ....*....|....*....|....*....|....
gi 398365453 179 EAIKLASDAIQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:COG0638  189 EAVELALRALYSAAERDSASGDGIDVAV--ITED 220
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-212 3.21e-40

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: 137.38  E-value: 3.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLF--KYQGHIgAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDA 187
Cdd:cd03764   81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                        170       180
                 ....*....|....*....|....*
gi 398365453 188 IQAGIWNDLGSGSNVDVCVmeIGKD 212
Cdd:cd03764  160 IKSAIERDSASGDGIDVVV--ITKD 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-199 3.05e-38

proteasome beta type-6 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: 239731  Cd Length: 188  Bit Score: 132.35  E-value: 3.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQGHIGAYLIVAGVDPT-GSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAI 188
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDEQnGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170
                 ....*....|.
gi 398365453 189 QAGIWNDLGSG 199
Cdd:cd03762  161 SLAMSRDGSSG 171
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-207 1.12e-29

proteasome beta type-5 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: 239730  Cd Length: 188  Bit Score: 110.03  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSAL 109
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 110 QMLKQHLFKYQGH---IGAylIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASD 186
Cdd:cd03761   81 KLLSNMLYQYKGMglsMGT--MICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                        170       180
                 ....*....|....*....|.
gi 398365453 187 AIQAGIWNDLGSGSNVDVCVM 207
Cdd:cd03761  159 AIYHATHRDAYSGGNVNLYHV 179
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-204 7.07e-28

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 107.00  E-value: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  13 NFLAENSHTQPKAT-----STGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQL 87
Cdd:PTZ00488  18 DFLAEYTFDHGDANkaiefAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  88 IGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGH-IGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAV 166
Cdd:PTZ00488  98 LAMQCRLYELRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGV 177

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 398365453 167 LESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDV 204
Cdd:PTZ00488 178 LDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINL 215
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 26-207 6.84e-23

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: 93.09  E-value: 6.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  26 TSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRV 105
Cdd:cd03757    5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 106 VSALQMLKQHL-----FKYQghigAYLIVAGVDPTG-SHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLES-----HWK-- 172
Cdd:cd03757   85 EAIAQLLSTILysrrfFPYY----VFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvgrkNQNnv 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398365453 173 --QDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVM 207
Cdd:cd03757  161 erTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVII 197
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 25-209 2.08e-20

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: 86.23  E-value: 2.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  25 ATSTGTTIVGVKFNNGVVIAADTRSTQgPIVADKNCAKLHRISPKIWCAGAGTAADTEavtQLI--GSNIELHSLYTSRE 102
Cdd:cd03756   24 AVKRGTTALGIKCKEGVVLAVDKRITS-KLVEPESIEKIYKIDDHVGAATSGLVADAR---VLIdrARVEAQIHRLTYGE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PRVVSAL--------QMLKQHlfkyqGHI---GAYLIVAGVDPTGSHLFSIHAHGsTDVGYYL-SLGSGSLAAMAVLESH 170
Cdd:cd03756  100 PIDVEVLvkkicdlkQQYTQH-----GGVrpfGVALLIAGVDDGGPRLFETDPSG-AYNEYKAtAIGSGRQAVTEFLEKE 173

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 398365453 171 WKQDLTKEEAIKLASDAIQAGIwNDLGSGSNVDVCVMEI 209
Cdd:cd03756  174 YKEDMSLEEAIELALKALYAAL-EENETPENVEIAYVTV 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
25-206 3.95e-20

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 86.04  E-value: 3.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  25 ATSTGTTIVGVKFNNGVVIAADTRSTQgPIVADKNCAKLHRISPKIWCAGAGTAADTEavtQLI--GSNIELHSLYTSRE 102
Cdd:PRK03996  32 AVKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADAR---VLIdrARVEAQINRLTYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PRVVSAL--------QMLKQHlfkyqGHI---GAYLIVAGVDPTGSHLFSIHAHGsTDVGYY-LSLGSGSLAAMAVLESH 170
Cdd:PRK03996 108 PIGVETLtkkicdhkQQYTQH-----GGVrpfGVALLIAGVDDGGPRLFETDPSG-AYLEYKaTAIGAGRDTVMEFLEKN 181

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398365453 171 WKQDLTKEEAIKLASDAIqAGIWNDLGSGSNVDVCV 206
Cdd:PRK03996 182 YKEDLSLEEAIELALKAL-AKANEGKLDPENVEIAY 216
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-183 2.47e-18

proteasome beta type-2 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: 239727  Cd Length: 193  Bit Score: 80.32  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  31 TIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQ 110
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365453 111 MLKQHLFKY---QGHIGAYLIVAGVDP-TGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKL 183
Cdd:cd03758   83 FTRRELAESlrsRTPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-207 1.11e-17

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: 79.02  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTqgPIVADKNCA-KLHRISPKIWCAGAGTAADTEAVTQlIGSNIELHSLYTSRE 102
Cdd:cd01911   22 EAVKNGSTAVGIKGKDGVVLAVEKKVT--SKLLDPSSVeKIFKIDDHIGCAVAGLTADARVLVN-RARVEAQNYRYTYGE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 P----RVVSALQMLKQhlfKYQGHI-----GAYLIVAGVDP-TGSHLFSIHAHGSTdVGYY-LSLGSGSLAAMAVLESHW 171
Cdd:cd01911   99 PipveVLVKRIADLAQ---VYTQYGgvrpfGVSLLIAGYDEeGGPQLYQTDPSGTY-FGYKaTAIGKGSQEAKTFLEKRY 174

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398365453 172 KQDLTKEEAIKLASDAIQAGIWNDLgSGSNVDVCVM 207
Cdd:cd01911  175 KKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-211 3.27e-16

proteasome beta type-3 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: 239728  Cd Length: 195  Bit Score: 74.59  E-value: 3.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  27 STGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSRE--PR 104
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREikPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 105 VVSAL--QMLKQHLFkyqghiGAYL---IVAGVDPTGS-HLFSIHAHGSTDV-GYYLSLGSGSLAAMAVLESHWKQDLTK 177
Cdd:cd03759   81 TFSSLisSLLYEKRF------GPYFvepVVAGLDPDGKpFICTMDLIGCPSIpSDFVVSGTASEQLYGMCESLWRPDMEP 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 398365453 178 EEAIKLASDAIQAGIWNDLGSGSNVDVCVMEIGK 211
Cdd:cd03759  155 DELFETISQALLSAVDRDALSGWGAVVYIITKDK 188
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 28-206 8.65e-16

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 73.37  E-value: 8.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  28 TGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGS-NIELHSLYTSREPRVV 106
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQlVIDDECLDDGHSLSPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 107 SALQMLKQHLFKYQGHIGAY---LIVAGVDPTG-SHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHW--KQDLTKEEA 180
Cdd:cd03760   81 EIHSYLTRVLYNRRSKMNPLwntLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWekKPDLTEEEA 160

                        170       180
                 ....*....|....*....|....*.
gi 398365453 181 IKLASDAIQAGIWNDLGSGSNVDVCV 206
Cdd:cd03760  161 RALIEECMKVLYYRDARSINKYQIAV 186
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 222-257 6.32e-15

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 66.65  E-value: 6.32e-15
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 398365453  222 PNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQV 257
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVPLKLEVVEEVV 36
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-184 7.50e-10

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: 57.36  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTqligSNIELHS---LYTS 100
Cdd:cd03752   24 EAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILI----NYARLIAqryLYSY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 101 REPRVVSAL-QML---KQHLFKYQG--HIGAYLIVAGVDPT-GSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQ 173
Cdd:cd03752  100 QEPIPVEQLvQRLcdiKQGYTQYGGlrPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKD 179

                        170
                 ....*....|.
gi 398365453 174 DLTKEEAIKLA 184
Cdd:cd03752  180 DMTLEEALALA 190
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-184 1.00e-09

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: 56.96  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTQgPIVADKNCAKLHRISPKIWCAGAGTAADteAVTQLIGSNIEL-HSLYTSRE 102
Cdd:cd03753   22 EAIKLGSTAIGIKTKEGVVLAVEKRITS-PLMEPSSVEKIMEIDDHIGCAMSGLIAD--ARTLIDHARVEAqNHRFTYNE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PRVVSALQMLKQHLFKYQGH-----------IGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHW 171
Cdd:cd03753   99 PMTVESVTQAVSDLALQFGEgddgkkamsrpFGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKY 178

                        170
                 ....*....|...
gi 398365453 172 KQDLTKEEAIKLA 184
Cdd:cd03753  179 HKDMTLEEAEKLA 191
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-206 1.13e-09

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: 56.53  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTqGPIVADKNcaKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHS-LYTSRE 102
Cdd:cd03749   22 EAVKQGSATVGLKSKTHAVLVALKRAT-SELSSYQK--KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRfVYDSPI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 103 PrvvsaLQMLKQHL-FKYQGHI--------GAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWK- 172
Cdd:cd03749   99 P-----VSRLVSKVaEKAQINTqrygrrpyGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEe 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398365453 173 -QDLTKEEAIKLASDAIQAGIWND--LGSgSNVDVCV 206
Cdd:cd03749  174 fEDCSLEELIKHALRALRETLPGEqeLTI-KNVSIAI 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 24-184 1.99e-09

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 56.40  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHsLYTSREP 103
Cdd:PTZ00246  26 EAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRY-RYTYGEP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 104 RVVSALQM----LKQHLFKYQG--HIGAYLIVAGVDPT-GSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLT 176
Cdd:PTZ00246 105 QPVEQLVVqicdLKQSYTQFGGlrPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLT 184


                 ....*...
gi 398365453 177 KEEAIKLA 184
Cdd:PTZ00246 185 LEQGLLLA 192
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-223 4.47e-08

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: 52.32  E-value: 4.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTRSTQgPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREP 103
Cdd:cd03750   22 AAVSSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 104 RVvsalQMLKQHL------FKYQGHI---GAYLIVAGVDPTGSHLFSIHAHGStdvgYYL----SLGSGSLAAMAVLESH 170
Cdd:cd03750  101 PV----SQLVREIasvmqeYTQSGGVrpfGVSLLIAGWDEGGPYLYQVDPSGS----YFTwkatAIGKNYSNAKTFLEKR 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 398365453 171 WKQDLTKEEAIKLASDAIQAGIWNDLgSGSNVDVCVmeIGKDAEYLRnyLTPN 223
Cdd:cd03750  173 YNEDLELEDAIHTAILTLKEGFEGQM-TEKNIEIGI--CGETKGFRL--LTPA 220
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-188 6.05e-08

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: 51.90  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  24 KATSTGTTIVGVKFNNGVVIAADTrstqgpIVADK----NCAK-LHRISPKIWCAGAGTAADTEAV-------------- 84
Cdd:cd03751   25 KAVENSGTAIGIRCKDGVVLAVEK------LVTSKlyepGSNKrIFNVDRHIGIAVAGLLADGRHLvsrareeaenyrdn 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  85 ----------TQLIGSNIELHSLYTSREPrvvsalqmlkqhlfkyqghIGAYLIVAGVDPTGSHLFSIHAHGSTdVGYY- 153
Cdd:cd03751   99 ygtpipvkvlADRVAMYMHAYTLYSSVRP-------------------FGCSVLLGGYDSDGPQLYMIEPSGVS-YGYFg 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 398365453 154 LSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAI 188
Cdd:cd03751  159 CAIGKGKQAAKTELEKLKFSELTCREAVKEAAKII 193
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 30-186 7.16e-08

Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system that is the prokaryotic homolog of the proteasome. HslV is a dimer of hexamers (a dodecamer) that forms a central proteolytic chamber with active sites on the interior walls of the cavity. HslV shares significant sequence and structural similarity with the proteasomal beta-subunit and both are members of the Ntn-family of hydrolases. HslV has a nucleophilic threonine residue at its N-terminus that is exposed after processing of the propeptide and is directly involved in active site catalysis.


Pssm-ID: 238894  Cd Length: 171  Bit Score: 51.04  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453  30 TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISP-KIWCAGAGTAADTEAVTQLIGSNIELHSLYTSReprvvSA 108
Cdd:cd01913    1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNgKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLR-----AA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365453 109 LQMLKQ-HLFKYQGHIGAYLIVAgvDPTGSHLFSihahGSTDV----GYYLSLGSGS---LAAMAVLESHwkQDLTKEE- 179
Cdd:cd01913   76 VELAKDwRTDRYLRRLEAMLIVA--DKEHTLLIS----GNGDViepdDGIAAIGSGGnyaLAAARALLDH--TDLSAEEi 147

                        170
                 ....*....|
gi 398365453 180 ---AIKLASD 186
Cdd:cd01913  148 arkALKIAAD 157
 
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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