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Conserved domains on  [gi|442628090|ref|NP_001260511|]
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proteasome beta4 subunit, isoform B [Drosophila melanogaster]

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 ...
 1-192 5.80e-122

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: 342.64  E-value: 5.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   1 METLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRES 80
Cdd:cd03758    1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  81 AHFTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:cd03758   81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442628090 161 KKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:cd03758  161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 5.80e-122

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: 342.64  E-value: 5.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   1 METLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRES 80
Cdd:cd03758    1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  81 AHFTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:cd03758   81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442628090 161 KKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:cd03758  161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 3-183 4.81e-51

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: 162.74  E-value: 4.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090    3 TLLGIKGPDFVMLAADTTH-ARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESA 81
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRAtRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   82 HFTRKNLAEYLRS-RTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:pfam00227  86 RIADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 442628090  161 KKCIAEIQKRLVVNLKNFTVAVV 183
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-192 2.59e-17

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 76.72  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAh 82
Cdd:COG0638   37 TTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 ftrKNLAEYLRSRTPYQVFMF-----VAGYDpNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAY 157
Cdd:COG0638  116 ---KLLSDLLQGYTQYGVRPFgvallIGGVD-DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442628090 158 DVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 3-164 1.97e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 46.91  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGydlsPRESAH 82
Cdd:PTZ00488  41 TTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNG----ELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLAEYLRSRTPYQVFM--FVAGYDpNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:PTZ00488 117 AASKILANIVWNYKGMGLSMgtMICGWD-KKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLG 195


                 ....
gi 442628090 161 KKCI 164
Cdd:PTZ00488 196 RRAI 199
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 5.80e-122

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: 342.64  E-value: 5.80e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   1 METLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRES 80
Cdd:cd03758    1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  81 AHFTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:cd03758   81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442628090 161 KKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:cd03758  161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-192 4.47e-70

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: 211.15  E-value: 4.47e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   2 ETLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESA 81
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  82 HFTRKNLAEYLrsRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFK 161
Cdd:cd01912   81 NLLSNILYSYR--GFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 442628090 162 KCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:cd01912  159 KAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 3-183 9.64e-53

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: 166.90  E-value: 9.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAH 82
Cdd:cd01906    2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFKK 162
Cdd:cd01906   82 LLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                        170       180
                 ....*....|....*....|.
gi 442628090 163 CIAEIQKRLVVNLKNFTVAVV 183
Cdd:cd01906  162 ALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 3-183 4.81e-51

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: 162.74  E-value: 4.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090    3 TLLGIKGPDFVMLAADTTH-ARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESA 81
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRAtRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   82 HFTRKNLAEYLRS-RTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:pfam00227  86 RIADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 442628090  161 KKCIAEIQKRLVVNLKNFTVAVV 183
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 3-166 8.15e-31

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: 110.56  E-value: 8.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAH 82
Cdd:cd01901    2 TSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLAEYLRSRtPYQVFMFVAGYDPNaGPELTFIDYLANAL-PVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFK 161
Cdd:cd01901   82 ELAKLLQVYTQGR-PFGVNLIVAGVDEG-GGNLYYIDPSGPVIeNPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                 ....*
gi 442628090 162 KCIAE 166
Cdd:cd01901  160 KALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-192 1.53e-21

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: 86.92  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAH 82
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FtrknLAEYLRSR--TPYQVFMFVAGYDPNaGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:cd03764   82 L----LSNILNSSkyFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442628090 161 KKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:cd03764  157 IRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 3-192 2.59e-17

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 76.72  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAh 82
Cdd:COG0638   37 TTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 ftrKNLAEYLRSRTPYQVFMF-----VAGYDpNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAY 157
Cdd:COG0638  116 ---KLLSDLLQGYTQYGVRPFgvallIGGVD-DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442628090 158 DVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLE 192
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-189 4.53e-17

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: 75.76  E-value: 4.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAH 82
Cdd:cd03757   10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLaeYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYD---------RYWHPNITQ 153
Cdd:cd03757   90 LLSTIL--YSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPLSL 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 442628090 154 AEAYDVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVR 189
Cdd:cd03757  168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-193 1.18e-14

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: 69.14  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADT-----THARSiivmkEDQNKIHKVSDSLLISTVGESGDTEQFTEFI-SKNIALYKMRNGYDLS 76
Cdd:cd03760    4 SVIAIKYKDGVIIAADTlgsygSLARF-----KNVERIFKVGDNTLLGASGDYADFQYLKRLLdQLVIDDECLDDGHSLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  77 PresahftrKNLAEYL-------RSR-TPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWH 148
Cdd:cd03760   79 P--------KEIHSYLtrvlynrRSKmNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWE 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 442628090 149 --PNITQAEAYDVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLEP 193
Cdd:cd03760  151 kkPDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-188 3.04e-14

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: 68.04  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAH 82
Cdd:cd03759    5 AVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLaeYLRSRTPYQVFMFVAGYDPNAGPELTFIDYL-ANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFK 161
Cdd:cd03759   85 LISSLL--YEKRFGPYFVEPVVAGLDPDGKPFICTMDLIgCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162

                        170       180
                 ....*....|....*....|....*..
gi 442628090 162 KCIAEIQKRLVVNLKNFTVAVVDKDGV 188
Cdd:cd03759  163 QALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-194 1.47e-12

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: 63.37  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGydlspRES-- 80
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTG-----RKPrv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  81 AHFTRKnLAEYLrsrTPYQ----VFMFVAGYDPNaGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEA 156
Cdd:cd03763   77 VTALTM-LKQHL---FRYQghigAALVLGGVDYT-GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEA 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442628090 157 YDVFKKCI-AEIQKRLVVNlKNFTVAVVDKDGVRDLEPI 194
Cdd:cd03763  152 KKLVCEAIeAGIFNDLGSG-SNVDLCVITKDGVEYLRNY 189
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-189 8.75e-07

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: 47.24  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAh 82
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 ftrKNLAEYLRSRTPYQVFM--FVAGYDPNaGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:cd03761   81 ---KLLSNMLYQYKGMGLSMgtMICGWDKT-GPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLA 156

                        170       180
                 ....*....|....*....|....*....
gi 442628090 161 KKCIAEIQKRLVVNLKNFTVAVVDKDGVR 189
Cdd:cd03761  157 RRAIYHATHRDAYSGGNVNLYHVREDGWR 185
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-183 1.63e-06

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: 46.67  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAAD--TTharSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFiSKNIAL-YKMRNGYDLSPRE 79
Cdd:cd01911   29 TAVGIKGKDGVVLAVEkkVT---SKLLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNR-ARVEAQnYRYTYGEPIPVEV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  80 SAhftrKNLAEYLRSRT------PYQVFMFVAGYDPNAGPEL-------TFIDYLANALpvnyaghGYGAIFASSIYDRY 146
Cdd:cd01911  105 LV----KRIADLAQVYTqyggvrPFGVSLLIAGYDEEGGPQLyqtdpsgTYFGYKATAI-------GKGSQEAKTFLEKR 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442628090 147 WHPNITQAEAYDVFKKCIAEIQKRlVVNLKNFTVAVV 183
Cdd:cd01911  174 YKKDLTLEEAIKLALKALKEVLEE-DKKAKNIEIAVV 209
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 3-164 1.97e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 46.91  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGydlsPRESAH 82
Cdd:PTZ00488  41 TTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNG----ELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  83 FTRKNLAEYLRSRTPYQVFM--FVAGYDpNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVF 160
Cdd:PTZ00488 117 AASKILANIVWNYKGMGLSMgtMICGWD-KKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLG 195


                 ....
gi 442628090 161 KKCI 164
Cdd:PTZ00488 196 RRAI 199
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-188 8.42e-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: 44.52  E-value: 8.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADT-THARSIIVMKEdQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESA 81
Cdd:cd03762    2 TIIAVEYDGGVVLGADSrTSTGSYVANRV-TDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090  82 HFTRKNLAEYlrsRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFK 161
Cdd:cd03762   81 SLFKNLCYNY---KEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVK 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 442628090 162 KCIAEIQKRL-----VVNLknftvAVVDKDGV 188
Cdd:cd03762  158 NALSLAMSRDgssggVIRL-----VIITKDGV 184
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-137 2.08e-03

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: 37.70  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628090   3 TLLGIKGPDFVMLAADTtHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFiSKNIAL-YKMRNGYDLSPRESA 81
Cdd:cd03756   30 TALGIKCKEGVVLAVDK-RITSKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDR-ARVEAQiHRLTYGEPIDVEVLV 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628090  82 hftrKNLAEYLRSRT------PYQVFMFVAGYDPNaGPEL-------TFIDYLANALpvnyaGHGYGAI 137
Cdd:cd03756  108 ----KKICDLKQQYTqhggvrPFGVALLIAGVDDG-GPRLfetdpsgAYNEYKATAI-----GSGRQAV 166
 
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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