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Conserved domains on  [gi|1050392572|gb|OCT94763|]
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hypothetical protein XELAEV_18012453mg [Xenopus laevis]

Protein Classification

proteasome subunit beta( domain architecture ID 10132911)

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_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 3.36e-129

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: 361.13  E-value: 3.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   1 MEYLIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758     1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELL 160
Cdd:cd03758    81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050392572 161 KKCIAELQKRFILSLPSFTVRVIDKDGIHDLES 193
Cdd:cd03758   161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 3.36e-129

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: 361.13  E-value: 3.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   1 MEYLIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758     1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELL 160
Cdd:cd03758    81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050392572 161 KKCIAELQKRFILSLPSFTVRVIDKDGIHDLES 193
Cdd:cd03758   161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 1.28e-54

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: 171.98  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADT-VCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADKrATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 TRRNLADYLRS-RTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLKK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
gi 1050392572 163 CIAELQKRFILSLPSFTVRVI 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 1.13e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 104.07  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADT-VCANSIIrMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:COG0638    39 VGIKTKDGVVLAADRrATMGNLI-ASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 trrnLADYLRSRT-----PYHVNLLLAGYDEhEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVE 158
Cdd:COG0638   118 ----LSDLLQGYTqygvrPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050392572 159 LLKKCIAELQKRFILSLPSFTVRVIDKDGIHDLE 192
Cdd:COG0638   193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-187 2.08e-11

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 61.16  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  13 VLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADYL 92
Cdd:PTZ00488   51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  93 RSRTPYHVNL--LLAGYDEhEGPSLYYMDYLAA-LAKTRFAAhGYGAYLTLSILDRYYKPDLTREEAVELLKKCIAELQK 169
Cdd:PTZ00488  127 WNYKGMGLSMgtMICGWDK-KGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATF 204

                         170
                  ....*....|....*...
gi 1050392572 170 RFILSLPSFTVRVIDKDG 187
Cdd:PTZ00488  205 RDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 3.36e-129

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: 361.13  E-value: 3.36e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   1 MEYLIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758     1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELL 160
Cdd:cd03758    81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050392572 161 KKCIAELQKRFILSLPSFTVRVIDKDGIHDLES 193
Cdd:cd03758   161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-192 5.56e-82

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: 241.58  E-value: 5.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   2 EYLIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAA 81
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  82 NFTRRNLADYLRsrTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLK 161
Cdd:cd01912    81 NLLSNILYSYRG--FPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1050392572 162 KCIAELQKRFILSLPSFTVRVIDKDGIHDLE 192
Cdd:cd01912   159 KAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 3-183 1.74e-62

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: 191.55  E-value: 1.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   3 YLIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAN 82
Cdd:cd01906     2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  83 FTRRNLADYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLKK 162
Cdd:cd01906    82 LLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                         170       180
                  ....*....|....*....|.
gi 1050392572 163 CIAELQKRFILSLPSFTVRVI 183
Cdd:cd01906   162 ALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 1.28e-54

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: 171.98  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADT-VCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADKrATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 TRRNLADYLRS-RTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLKK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
gi 1050392572 163 CIAELQKRFILSLPSFTVRVI 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-166 4.90e-39

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: 131.36  E-value: 4.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:cd01901     4 VAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRNLADYLRSRtPYHVNLLLAGYDEhEGPSLYYMDYLAALAK-TRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLKKC 163
Cdd:cd01901    84 AKLLQVYTQGR-PFGVNLIVAGVDE-GGGNLYYIDPSGPVIEnPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALKA 161


                  ...
gi 1050392572 164 IAE 166
Cdd:cd01901   162 LKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-192 1.01e-27

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: 103.10  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADT-VCANSIIRMKQdVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03764     4 VGIVCKDGVVLAADKrASMGNFIASKN-VKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 trrnLADYLRSR--TPYHVNLLLAGYDEhEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELLK 161
Cdd:cd03764    83 ----LSNILNSSkyFPYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1050392572 162 KCIAELQKRFILSLPSFTVRVIDKDGIHDLE 192
Cdd:cd03764   158 RAIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 1.13e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 104.07  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADT-VCANSIIrMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:COG0638    39 VGIKTKDGVVLAADRrATMGNLI-ASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 trrnLADYLRSRT-----PYHVNLLLAGYDEhEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVE 158
Cdd:COG0638   118 ----LSDLLQGYTqygvrPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050392572 159 LLKKCIAELQKRFILSLPSFTVRVIDKDGIHDLE 192
Cdd:COG0638   193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 3.27e-24

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: 94.17  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCA-NSIIRMKqDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMR-NGYELSPTAAAN 82
Cdd:cd03760     6 IAIKYKDGVIIAADTLGSyGSLARFK-NVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLdDGHSLSPKEIHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  83 FTRRNLadY-LRSR-TPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYY--KPDLTREEAVE 158
Cdd:cd03760    85 YLTRVL--YnRRSKmNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWekKPDLTEEEARA 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1050392572 159 LLKKCIAELQKRFILSLPSFTVRVIDKDGIH 189
Cdd:cd03760   163 LIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 6.93e-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: 91.17  E-value: 6.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:cd03757    12 LAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRNLadYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILD---------RYYKPDLTREE 155
Cdd:cd03757    92 STIL--YSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPLSLEE 169

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050392572 156 AVELLKKCIAELQKRFILSLPSFTVRVIDKDGIH 189
Cdd:cd03757   170 AVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-188 1.26e-18

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: 79.59  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   4 LIGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03759     6 VVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  84 TRRNLadYLRSRTPYHVNLLLAGYDEHEGPSLYYMDYLAALAKTR-FAAHGYGAYLTLSILDRYYKPDLTREEAVELLKK 162
Cdd:cd03759    86 ISSLL--YEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYGMCESLWRPDMEPDELFETISQ 163

                         170       180
                  ....*....|....*....|....*.
gi 1050392572 163 CIAELQKRFILSLPSFTVRVIDKDGI 188
Cdd:cd03759   164 ALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-165 7.53e-15

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: 69.18  E-value: 7.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   4 LIGIQGNDFVLVAADT-VCANSII--RMKqdvDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03762     3 IIAVEYDGGVVLGADSrTSTGSYVanRVT---DKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  81 ANFTRrNLADYLRSRTPYHVnlLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELL 160
Cdd:cd03762    80 ASLFK-NLCYNYKEMLSAGI--IVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFV 156


                  ....*
gi 1050392572 161 KKCIA 165
Cdd:cd03762   157 KNALS 161
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-166 6.10e-14

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: 67.08  E-value: 6.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRmKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAnft 84
Cdd:cd01911    31 VGIKGKDGVVLAVEKKVTSKLLD-PSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLV--- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 rRNLADYLRSRT------PYHVNLLLAGYDEHEGPSLYYMD----YLAALAktrfAAHGYGAYLTLSILDRYYKPDLTRE 154
Cdd:cd01911   107 -KRIADLAQVYTqyggvrPFGVSLLIAGYDEEGGPQLYQTDpsgtYFGYKA----TAIGKGSQEAKTFLEKRYKKDLTLE 181

                         170
                  ....*....|..
gi 1050392572 155 EAVELLKKCIAE 166
Cdd:cd01911   182 EAIKLALKALKE 193
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-165 3.90e-13

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: 64.91  E-value: 3.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYElSPTAAANft 84
Cdd:cd03763     4 VGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRK-PRVVTAL-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 rRNLADYLrsrTPYH----VNLLLAGYDeHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVELL 160
Cdd:cd03763    81 -TMLKQHL---FRYQghigAALVLGGVD-YTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLV 155


                  ....*
gi 1050392572 161 KKCIA 165
Cdd:cd03763   156 CEAIE 160
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-187 2.08e-11

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 61.16  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  13 VLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADYL 92
Cdd:PTZ00488   51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  93 RSRTPYHVNL--LLAGYDEhEGPSLYYMDYLAA-LAKTRFAAhGYGAYLTLSILDRYYKPDLTREEAVELLKKCIAELQK 169
Cdd:PTZ00488  127 WNYKGMGLSMgtMICGWDK-KGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATF 204

                         170
                  ....*....|....*...
gi 1050392572 170 RFILSLPSFTVRVIDKDG 187
Cdd:PTZ00488  205 RDAYSGGAINLYHMQKDG 222
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-187 4.68e-10

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: 56.48  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  13 VLVAADT--VCANSIirMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLAD 90
Cdd:cd03761    12 VIVAVDSraTAGSYI--ASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  91 YlrSRTPYHVNLLLAGYDeHEGPSLYYMDYLAA-LAKTRFAAhGYGAYLTLSILDRYYKPDLTREEAVELLKKCIAELQK 169
Cdd:cd03761    90 Y--KGMGLSMGTMICGWD-KTGPGLYYVDSDGTrLKGDLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATH 165

                         170
                  ....*....|....*...
gi 1050392572 170 RFILSLPSFTVRVIDKDG 187
Cdd:cd03761   166 RDAYSGGNVNLYHVREDG 183
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-159 5.00e-09

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: 53.89  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYkmRNGYElSPTAAANFT 84
Cdd:cd03752    33 LGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRY--LYSYQ-EPIPVEQLV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRnLADYLRSRT------PYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVE 158
Cdd:cd03752   110 QR-LCDIKQGYTqygglrPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALA 188


                  .
gi 1050392572 159 L 159
Cdd:cd03752   189 L 189
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-159 9.61e-09

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: 53.10  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRmKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGyelSPTAAANFT 84
Cdd:cd03756    32 LGIKCKEGVVLAVDKRITSKLVE-PESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYG---EPIDVEVLV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRnLADYLRSRT------PYHVNLLLAGYDEHeGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVE 158
Cdd:cd03756   108 KK-ICDLKQQYTqhggvrPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIE 185


                  .
gi 1050392572 159 L 159
Cdd:cd03756   186 L 186
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-166 8.91e-08

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 50.62  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQDVDKMFKMSEKILLLCVGEAGDtvqfAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:PTZ00246   35 VGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTAD----ANILINQCRLYAQRYRYTYGEPQPVEQL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRNLADYLRSRT------PYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEAVE 158
Cdd:PTZ00246  111 VVQICDLKQSYTqfgglrPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLL 190


                  ....*...
gi 1050392572 159 LLKKCIAE 166
Cdd:PTZ00246  191 LAAKVLTK 198
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-167 2.31e-07

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 49.28  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAadtVCANSIIRMKQD--VDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRngYELSPTAAan 82
Cdd:cd03755    31 VGVRGKDCVVLG---VEKKSVAKLQDPrtVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLT--VEDPVTVE-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  83 FTRRNLADYLRSRT------PYHVNLLLAGYDEHEGPSLYYMDYLAALAKTRFAAHGYGAYLTLSILDRYYKPDLTREEA 156
Cdd:cd03755   104 YITRYIAGLQQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDT 183

                         170
                  ....*....|.
gi 1050392572 157 VELLKKCIAEL 167
Cdd:cd03755   184 IKLAIKALLEV 194
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-163 9.53e-07

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 47.23  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKqDVDKMFKMSEKILLLCVGEAGDT---VQFAEYIQKNvqlYKMRNGYELSPTAAA 81
Cdd:cd03754    33 VAVRGKDCAVVVTQKKVPDKLIDPS-TVTHLFRITDEIGCVMTGMIADSrsqVQRARYEAAE---FKYKYGYEMPVDVLA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  82 nftrRNLADYLRSRT------PYHVNLLLAGYDEHEGPSLYYMD---YLAAlaktrFAAHGYGAYLT--LSILDRYYKPD 150
Cdd:cd03754   109 ----KRIADINQVYTqhaymrPLGVSMILIGIDEELGPQLYKCDpagYFAG-----YKATAAGVKEQeaTNFLEKKLKKK 179

                         170
                  ....*....|....*..
gi 1050392572 151 ----LTREEAVELLKKC 163
Cdd:cd03754   180 pdliESYEETVELAISC 196
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-166 1.02e-05

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: 44.64  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVcANSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQ----LYKMRNGYELSPTA- 79
Cdd:cd03753    31 IGIKTKEGVVLAVEKR-ITSPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQnhrfTYNEPMTVESVTQAv 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  80 ---AANFTRRNLADYLRSRtPYHVNLLLAGYDEhEGPSLYYMD----YLAALAKtrfaAHGYGAYLTLSILDRYYKPDLT 152
Cdd:cd03753   110 sdlALQFGEGDDGKKAMSR-PFGVALLIAGVDE-NGPQLFHTDpsgtFTRCDAK----AIGSGSEGAQSSLQEKYHKDMT 183

                         170
                  ....*....|....*...
gi 1050392572 153 REEA----VELLKKCIAE 166
Cdd:cd03753   184 LEEAeklaLSILKQVMEE 201
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-159 4.65e-05

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 42.51  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCANSIIRMKQdVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGyelSPTAAANFT 84
Cdd:PRK03996   40 VGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYG---EPIGVETLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRnLADYLRSRT------PYHVNLLLAGYDEHeGPSLY-------YMDYLAAlaktrfaAHGYGAYLTLSILDRYYKPDL 151
Cdd:PRK03996  116 KK-ICDHKQQYTqhggvrPFGVALLIAGVDDG-GPRLFetdpsgaYLEYKAT-------AIGAGRDTVMEFLEKNYKEDL 186


                  ....*...
gi 1050392572 152 TREEAVEL 159
Cdd:PRK03996  187 SLEEAIEL 194
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-164 4.05e-03

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: 36.87  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572   5 IGIQGNDFVLVAADTVCAnSIIRMKQDVDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYkmRNGYElSPTAAANFT 84
Cdd:cd03751    34 IGIRCKDGVVLAVEKLVT-SKLYEPGSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENY--RDNYG-TPIPVKVLA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050392572  85 RRnLADYLRSRT------PYHVNLLLAGYDEHeGPSLYYMD--------YLAALAKTRFAAhgygayltLSILDRYYKPD 150
Cdd:cd03751   110 DR-VAMYMHAYTlyssvrPFGCSVLLGGYDSD-GPQLYMIEpsgvsygyFGCAIGKGKQAA--------KTELEKLKFSE 179

                         170
                  ....*....|....
gi 1050392572 151 LTREEAVELLKKCI 164
Cdd:cd03751   180 LTCREAVKEAAKII 193
 
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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