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Conserved domains on  [gi|15223537|ref|NP_176040|]
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20S proteasome beta subunit G1 [Arabidopsis thaliana]

Protein Classification

proteasome subunit beta( domain architecture ID 10132923)

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_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-223 6.52e-118

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: 334.54  E-value: 6.52e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMWDDGNSLGPK 109
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 110 EIHNYLTRVMYNRRNKFNPLWNTLVLGGVKN-GKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHA--DLSFEDG 186
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15223537 187 VKLLEKCMRVLLYRDRSAINKLQIAKITEEGVTVSQP 223
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-223 6.52e-118

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: 334.54  E-value: 6.52e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMWDDGNSLGPK 109
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 110 EIHNYLTRVMYNRRNKFNPLWNTLVLGGVKN-GKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHA--DLSFEDG 186
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15223537 187 VKLLEKCMRVLLYRDRSAINKLQIAKITEEGVTVSQP 223
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-213 5.30e-41

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: 138.85  E-value: 5.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537    30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKN-IERVKAIGKHSLLGASGEISDFQEILRY------LDELTLNDNMwdd 102
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRaraeaqLYRLRYGRPI--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537   103 gnSLGPKEIHNYLTRVMYNRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLS 182
Cdd:pfam00227  80 --PVELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15223537   183 FEDGVKLLEKCMRVLLYRDRSAINKLQIAKI 213
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 31-218 3.33e-24

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: 95.35  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537    31 GTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLD-ELTLNDNMWddGNSLGPK 109
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKaEAKLYELRR--GRPMSVK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537   110 EIHNYLTRVMYNrrNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKL 189
Cdd:TIGR03634  79 ALATLLSNILNS--NRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKL 156

                         170       180
                  ....*....|....*....|....*....
gi 15223537   190 LEKCMRVLLYRDRSAINKLQIAKITEEGV 218
Cdd:TIGR03634 157 AVRAIKSAIERDVASGNGIDVAVITKDGV 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 30-219 4.42e-24

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 95.98  E-value: 4.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLdELTLNDNMWDDGNSLGPK 109
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA-RVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 110 EIHNYLTRVMY-NRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVK 188
Cdd:COG0638 113 GLAKLLSDLLQgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|.
gi 15223537 189 LLEKCMRVLLYRDRSAINKLQIAKITEEGVT 219
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFR 223
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-223 6.52e-118

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: 334.54  E-value: 6.52e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMWDDGNSLGPK 109
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 110 EIHNYLTRVMYNRRNKFNPLWNTLVLGGVKN-GKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHA--DLSFEDG 186
Cdd:cd03760  81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEEEA 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15223537 187 VKLLEKCMRVLLYRDRSAINKLQIAKITEEGVTVSQP 223
Cdd:cd03760 161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-220 1.98e-62

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: 193.81  E-value: 1.98e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  32 TSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMWDDGNsLGPKEI 111
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRE-LSVKAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 112 HNYLTRVMYNRRnkFNPLWNTLVLGGV-KNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKLL 190
Cdd:cd01912  80 ANLLSNILYSYR--GFPYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELV 157

                       170       180       190
                ....*....|....*....|....*....|
gi 15223537 191 EKCMRVLLYRDRSAINKLQIAKITEEGVTV 220
Cdd:cd01912 158 KKAIDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-213 2.72e-49

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: 159.97  E-value: 2.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  32 TSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMwDDGNSLGPKEI 111
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRL-RYGEPIPVEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 112 HNYLTRVMYNRRNKFNPLWNTLVLGGV-KNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKLL 190
Cdd:cd01906  80 AKLLANLLYEYTQSLRPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 15223537 191 EKCMRVLLYRDRSAINKLQIAKI 213
Cdd:cd01906 160 LKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-213 5.30e-41

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: 138.85  E-value: 5.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537    30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKN-IERVKAIGKHSLLGASGEISDFQEILRY------LDELTLNDNMwdd 102
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRaraeaqLYRLRYGRPI--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537   103 gnSLGPKEIHNYLTRVMYNRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLS 182
Cdd:pfam00227  80 --PVELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 15223537   183 FEDGVKLLEKCMRVLLYRDRSAINKLQIAKI 213
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-195 1.85e-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: 116.34  E-value: 1.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  32 TSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDELTLNDNMwDDGNSLGPKEI 111
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRL-RYGEPISVVAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 112 HNYLTRVMYNRRNKFnPLWNTLVLGGVKNGKSYLGMVSMIGVSFED-DHVATGFGNHLARPILRDEWHADLSFEDGVKLL 190
Cdd:cd01901  80 AKELAKLLQVYTQGR-PFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELA 158


                ....*
gi 15223537 191 EKCMR 195
Cdd:cd01901 159 LKALK 163
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 31-218 3.33e-24

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: 95.35  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537    31 GTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLD-ELTLNDNMWddGNSLGPK 109
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKaEAKLYELRR--GRPMSVK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537   110 EIHNYLTRVMYNrrNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKL 189
Cdd:TIGR03634  79 ALATLLSNILNS--NRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKL 156

                         170       180
                  ....*....|....*....|....*....
gi 15223537   190 LEKCMRVLLYRDRSAINKLQIAKITEEGV 218
Cdd:TIGR03634 157 AVRAIKSAIERDVASGNGIDVAVITKDGV 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 30-219 4.42e-24

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 95.98  E-value: 4.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLdELTLNDNMWDDGNSLGPK 109
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA-RVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 110 EIHNYLTRVMY-NRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVK 188
Cdd:COG0638 113 GLAKLLSDLLQgYTQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|.
gi 15223537 189 LLEKCMRVLLYRDRSAINKLQIAKITEEGVT 219
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFR 223
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-217 3.76e-23

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: 92.70  E-value: 3.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  32 TSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLD-ELTLNDNMWddGNSLGPKE 110
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKaEARLYELRR--GRPMSIKA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 111 IHNYLTRVMYNrrNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFEDGVKLL 190
Cdd:cd03764  79 LATLLSNILNS--SKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLA 156

                       170       180
                ....*....|....*....|....*..
gi 15223537 191 EKCMRVLLYRDRSAINKLQIAKITEEG 217
Cdd:cd03764 157 IRAIKSAIERDSASGDGIDVVVITKDG 183
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-193 5.08e-13

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: 65.68  E-value: 5.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  33 SIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQEILRYLDEltlndNM----WDDGNSLGP 108
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQK-----NIqlykMRNGYELSP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 109 KEIHNYLTRVM--YNRRNKfnPLWNTLVLGGV-KNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEWHADLSFED 185
Cdd:cd03758  78 KAAANFTRRELaeSLRSRT--PYQVNLLLAGYdKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEE 155


                ....*...
gi 15223537 186 GVKLLEKC 193
Cdd:cd03758 156 ALELMKKC 163
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-201 4.04e-11

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: 60.33  E-value: 4.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  30 TGTSIVAIKYKDGVLMASDMggSYGSTLRY--KNIERVKAIGKHSLLGASGEISDFQ---EILRY---LDELTLNDNMwd 101
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDL--RLGVQQQTvsTDFQKVFRIGDRLYIGLAGLATDVQtlaQKLRFrvnLYRLREEREI-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 102 dgnslGPKEIHNYLTRVMYNRRnkFNPLWNTLVLGGV-KNGKSYLGMVSMIG-VSFEDDHVATGFGNHLARPILRDEWHA 179
Cdd:cd03759  78 -----KPKTFSSLISSLLYEKR--FGPYFVEPVVAGLdPDGKPFICTMDLIGcPSIPSDFVVSGTASEQLYGMCESLWRP 150

                       170       180
                ....*....|....*....|..
gi 15223537 180 DLSFEDGVKLLEKCMRVLLYRD 201
Cdd:cd03759 151 DMEPDELFETISQALLSAVDRD 172
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 26-218 2.96e-10

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: 58.04  E-value: 2.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  26 YPYV-TGTSIVAIKYKDGVLMASD--MGGSYGSTLRykNIERVKAIGKHSLLGASGEISD---FQEILRYLDELTLNDNm 99
Cdd:cd03757   2 SPYTdNGGTVLAIAGNDFAVIAGDtrLSEGYSILSR--DSPKIFKLTDKCVLGSSGFQADilaLTKRLKARIKMYKYSH- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 100 wddGNSLGPKEIHNYLTRVMYNRRnkFNPLWNTLVLGGV-KNGKSYLGMVSMIGvSFEDD-HVATGFGNHLARPIL---- 173
Cdd:cd03757  79 ---NKEMSTEAIAQLLSTILYSRR--FFPYYVFNILAGIdEEGKGVVYSYDPVG-SYEREtYSAGGSASSLIQPLLdnqv 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15223537 174 -----RDEWHADLSFEDGVKLLEKCMRVLLYRDRSAINKLQIAKITEEGV 218
Cdd:cd03757 153 grknqNNVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGI 202
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-215 2.96e-06

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: 46.55  E-value: 2.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  31 GTSIVAIKYKDGVLMASDMggSYGSTLRYKN-IERVKAIGKHSLLGASGEISD------------FQEILRYlDELTLND 97
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDK--RITSKLVEPEsIEKIYKIDDHVGAATSGLVADarvlidrarveaQIHRLTY-GEPIDVE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  98 NMwddgnslgPKEIHNYltRVMYNRRNKFNPLWNTLVLGGVKNGKSYLGMVSMIGVSFEDDHVATGFGNHLARPILRDEW 177
Cdd:cd03756 105 VL--------VKKICDL--KQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEY 174

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15223537 178 HADLSFEDGVKLLEKCMrVLLYRDRSAINKLQIAKITE 215
Cdd:cd03756 175 KEDMSLEEAIELALKAL-YAALEENETPENVEIAYVTV 211
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-219 4.95e-06

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: 45.68  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537  32 TSIVAIKYKDGVLMASDMGGSYGSTLRYKNIERVKAIGKHSLLGASGEISDFQ---EILRY-LDELTLndnmwddgnSLG 107
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQaiaDYVRYyLDMHSI---------ELG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223537 108 P----KEIHNYLTRVMYNRRNKfnpLWNTLVLGG---VKNGKSYLgmVSMIGVSFEDDHVATGFGNHLARPILRDEWHAD 180
Cdd:cd03762  72 EpplvKTAASLFKNLCYNYKEM---LSAGIIVAGwdeQNGGQVYS--IPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPG 146

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15223537 181 LSFEDGVKLLEKCMRVLLYRDRSAINKLQIAKITEEGVT 219
Cdd:cd03762 147 MTLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVE 185
 
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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