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Conserved domains on  [gi|2043688459|pdb|6ZOU|J]
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Chain J, Proteasome subunit beta type-4

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 ...
 1-194 5.28e-97

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: 279.47  E-value: 5.28e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        1 MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       81 SSFVRQELAKSIRSRRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYD-KVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159

                       170       180       190
                ....*....|....*....|....*....|....
6ZOU_J      161 LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDD 194
Cdd:cd03758 160 MKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 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 ...
 1-194 5.28e-97

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: 279.47  E-value: 5.28e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        1 MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       81 SSFVRQELAKSIRSRRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYD-KVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159

                       170       180       190
                ....*....|....*....|....*....|....
6ZOU_J      161 LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDD 194
Cdd:cd03758 160 MKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 4-184 3.00e-56

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: 176.22  E-value: 3.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J          4 ILGIRVQDSVILASSKAVTRGISVLKDSD-DKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSS 82
Cdd:pfam00227   7 IVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAAR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         83 FVRQELAKSIRS-RRPYQVNVLIGGYDKKkNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLL 161
Cdd:pfam00227  87 IADLLQAYTQYSgRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
6ZOU_J        162 KLCVQELEKRMPMDFKGVIVKIV 184
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 4-194 5.60e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 102.15  E-value: 5.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSf 83
Cdd:COG0638  38 TVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAK- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 vrqELAKSIRSR-----RPYQVNVLIGGYDkkKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGL 158
Cdd:COG0638 117 ---LLSDLLQGYtqygvRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*.
6ZOU_J      159 DLLKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDD 194
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELSE 227
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 5-160 1.34e-12

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 64.24  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         5 LGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSFv 84
Cdd:PTZ00488  43 LAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI- 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6ZOU_J        85 rqeLAKSIRSRRPYQVNV--LIGGYDKKknKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL 160
Cdd:PTZ00488 122 ---LANIVWNYKGMGLSMgtMICGWDKK--GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDL 194
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-194 5.28e-97

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: 279.47  E-value: 5.28e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        1 MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAV 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       81 SSFVRQELAKSIRSRRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYD-KVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159

                       170       180       190
                ....*....|....*....|....*....|....
6ZOU_J      161 LKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDD 194
Cdd:cd03758 160 MKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-192 1.31e-63

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: 194.58  E-value: 1.31e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd01912   3 IVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 VRQELAKsiRSRRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKL 163
Cdd:cd01912  83 LSNILYS--YRGFPYYVSLIVGGVD-KGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKK 159

                       170       180
                ....*....|....*....|....*....
6ZOU_J      164 CVQELEKRMPMDFKGVIVKIVDKDGIRQV 192
Cdd:cd01912 160 AIDSAIERDLSSGGGVDVAVITKDGVEEL 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 4-184 3.00e-56

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: 176.22  E-value: 3.00e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J          4 ILGIRVQDSVILASSKAVTRGISVLKDSD-DKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSS 82
Cdd:pfam00227   7 IVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAAR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         83 FVRQELAKSIRS-RRPYQVNVLIGGYDKKkNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLL 161
Cdd:pfam00227  87 IADLLQAYTQYSgRRPFGVSLLIAGYDED-GGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
6ZOU_J        162 KLCVQELEKRMPMDFKGVIVKIV 184
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 4-184 8.48e-51

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: 161.89  E-value: 8.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd01906   3 IVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 VRQELAKSIRSRRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKL 163
Cdd:cd01906  83 LANLLYEYTQSLRPLGVSLLVAGVD-EEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                       170       180
                ....*....|....*....|.
6ZOU_J      164 CVQELEKRMPMDFKGVIVKIV 184
Cdd:cd01906 162 ALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 4-167 3.05e-36

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: 124.43  E-value: 3.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 VRQELAkSIRSRRPYQVNVLIGGYDkkKNKPELYQIDYLGTKVELPYG-AHGYSGFYTFSLLDHHYRPDMTTEEGLDLLK 162
Cdd:cd01901  83 LAKLLQ-VYTQGRPFGVNLIVAGVD--EGGGNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....*
6ZOU_J      163 LCVQE 167
Cdd:cd01901 160 KALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-193 1.15e-31

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: 113.12  E-value: 1.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 vrqeLAKSIRSRR--PYQVNVLIGGYDkkKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLL 161
Cdd:cd03764  83 ----LSNILNSSKyfPYIVQLLIGGVD--EEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLA 156

                       170       180       190
                ....*....|....*....|....*....|..
6ZOU_J      162 KLCVQELEKRMPMDFKGVIVKIVDKDGIRQVD 193
Cdd:cd03764 157 IRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 4-194 5.60e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 102.15  E-value: 5.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSf 83
Cdd:COG0638  38 TVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAK- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 vrqELAKSIRSR-----RPYQVNVLIGGYDkkKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGL 158
Cdd:COG0638 117 ---LLSDLLQGYtqygvRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....*.
6ZOU_J      159 DLLKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDD 194
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELSE 227
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-189 1.52e-14

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: 68.41  E-value: 1.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd03762   3 IIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 VRqELAKSIRSRrpYQVNVLIGGYDKKkNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGldlLKL 163
Cdd:cd03762  83 FK-NLCYNYKEM--LSAGIIVAGWDEQ-NGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEEC---IKF 155

                       170       180
                ....*....|....*....|....*....
6ZOU_J      164 CVQELEKRMPMDFK--GVI-VKIVDKDGI 189
Cdd:cd03762 156 VKNALSLAMSRDGSsgGVIrLVIITKDGV 184
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-162 6.24e-14

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: 66.84  E-value: 6.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSF 83
Cdd:cd03763   3 IVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 VRQELAKsirsrrpYQ----VNVLIGGYDKkkNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLD 159
Cdd:cd03763  83 LKQHLFR-------YQghigAALVLGGVDY--TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKK 153


                ...
6ZOU_J      160 LLK 162
Cdd:cd03763 154 LVC 156
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-190 6.58e-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: 66.82  E-value: 6.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGiSVLKDSD-DKTRQLSPHTLMSFAGEAGDtvqfAEYIQANIQLYSIRE-----DYELSP 77
Cdd:cd03760   5 VIAIKYKDGVIIAADTLGSYG-SLARFKNvERIFKVGDNTLLGASGDYAD----FQYLKRLLDQLVIDDeclddGHSLSP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       78 QAVSSFvrqeLAKSIRSRR----PYQVNVLIGGYDKKKnKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYR--PD 151
Cdd:cd03760  80 KEIHSY----LTRVLYNRRskmnPLWNTLVVGGVDNEG-EPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkPD 154

                       170       180       190
                ....*....|....*....|....*....|....*....
6ZOU_J      152 MTTEEGLDLLKLCVQELEKRMPMDFKGVIVKIVDKDGIR 190
Cdd:cd03760 155 LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-189 3.51e-13

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: 64.96  E-value: 3.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVtrGISVLKDSDD--KTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVS 81
Cdd:cd03759   6 VVAMAGKDCVAIASDLRL--GVQQQTVSTDfqKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       82 SFVRQELAKsirsRR--PYQVNVLIGGYDkKKNKPELYQIDYLGTKVEL-PYGAHGYSGFYTFSLLDHHYRPDMTTEEGL 158
Cdd:cd03759  84 SLISSLLYE----KRfgPYFVEPVVAGLD-PDGKPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELF 158

                       170       180       190
                ....*....|....*....|....*....|.
6ZOU_J      159 DLLKLCVQELEKRMPMDFKGVIVKIVDKDGI 189
Cdd:cd03759 159 ETISQALLSAVDRDALSGWGAVVYIITKDKV 189
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 5-160 1.34e-12

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 64.24  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         5 LGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSFv 84
Cdd:PTZ00488  43 LAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI- 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6ZOU_J        85 rqeLAKSIRSRRPYQVNV--LIGGYDKKknKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDL 160
Cdd:PTZ00488 122 ---LANIVWNYKGMGLSMgtMICGWDKK--GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDL 194
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-160 3.71e-10

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: 56.96  E-value: 3.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTRGIsVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDyelSPQAVssfv 84
Cdd:cd03756  32 LGIKCKEGVVLAVDKRITSKL-VEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYG---EPIDV---- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       85 rQELAKSIRSR----------RPYQVNVLIGGYDKkkNKPELYQIDYLGTKVELPYGAHGySGFYTF-SLLDHHYRPDMT 153
Cdd:cd03756 104 -EVLVKKICDLkqqytqhggvRPFGVALLIAGVDD--GGPRLFETDPSGAYNEYKATAIG-SGRQAVtEFLEKEYKEDMS 179


                ....*..
6ZOU_J      154 TEEGLDL 160
Cdd:cd03756 180 LEEAIEL 186
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-172 4.34e-10

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 56.96  E-value: 4.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTRGIsVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQ----LYSIREDYELSPQAV 80
Cdd:cd03753  31 IGIKTKEGVVLAVEKRITSPL-MEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQnhrfTYNEPMTVESVTQAV 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       81 SS----FVRQELAKSIRSRrPYQVNVLIGGYDkkKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEE 156
Cdd:cd03753 110 SDlalqFGEGDDGKKAMSR-PFGVALLIAGVD--ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLEE 186

                       170
                ....*....|....*..
6ZOU_J      157 GLDL-LKLCVQELEKRM 172
Cdd:cd03753 187 AEKLaLSILKQVMEEKL 203
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-160 4.88e-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: 56.10  E-value: 4.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSFv 84
Cdd:cd03761   4 LAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKL- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       85 rqeLAKSIRSRRPYQVNV--LIGGYDKkkNKPELYQIDYLGTKVelpygaHGY-----SG-FYTFSLLDHHYRPDMTTEE 156
Cdd:cd03761  83 ---LSNMLYQYKGMGLSMgtMICGWDK--TGPGLYYVDSDGTRL------KGDlfsvgSGsTYAYGVLDSGYRYDLSVEE 151


                ....
6ZOU_J      157 GLDL 160
Cdd:cd03761 152 AYDL 155
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 3-173 3.44e-09

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 54.86  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         3 IILGIRVQDSVILASSKAVtrgISVLKD---SDDKTRQLSPHTLMSFAGEAGDtvqfAEYIQANIQLYSIREDYELS-PQ 78
Cdd:PTZ00246  33 LTVGILCKEGVILGADKPI---SSKLLDpgkINEKIYKIDSHIFCAVAGLTAD----ANILINQCRLYAQRYRYTYGePQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        79 AVSSFVRQ--ELAKSIRS---RRPYQVNVLIGGYDKKKNKpELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMT 153
Cdd:PTZ00246 106 PVEQLVVQicDLKQSYTQfggLRPFGVSFLFAGYDENLGY-QLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLT 184

                        170       180
                 ....*....|....*....|.
6ZOU_J       154 TEEGLDL-LKLCVQELEKRMP 173
Cdd:PTZ00246 185 LEQGLLLaAKVLTKSMDSTSP 205
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-177 6.00e-09

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: 53.60  E-value: 6.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTrgiSVLKDSDDKTR--QLSPHTLMSFAGEAGDT---VQFAEYIQANiqlYsiREDYElSPQA 79
Cdd:cd01911  31 VGIKGKDGVVLAVEKKVT---SKLLDPSSVEKifKIDDHIGCAVAGLTADArvlVNRARVEAQN---Y--RYTYG-EPIP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       80 VSSfvrqeLAKSI----------RSRRPYQVNVLIGGYDkKKNKPELYQIDylgtkvelPYGAhgYSGFYTFSL------ 143
Cdd:cd01911 102 VEV-----LVKRIadlaqvytqyGGVRPFGVSLLIAGYD-EEGGPQLYQTD--------PSGT--YFGYKATAIgkgsqe 165

                       170       180       190
                ....*....|....*....|....*....|....*...
6ZOU_J      144 ----LDHHYRPDMTTEEGLDLLKLCVQELekrMPMDFK 177
Cdd:cd01911 166 aktfLEKRYKKDLTLEEAIKLALKALKEV---LEEDKK 200
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-172 6.55e-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: 53.51  E-value: 6.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        3 IILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDtvqfaeyiqANI-----QLYSIRedYELS- 76
Cdd:cd03752  31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD---------ANIlinyaRLIAQR--YLYSy 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       77 --PQAVSSFVRQ-----ELAKSIRSRRPYQVNVLIGGYDKKKNKpELYQIDylgtkvelPYGahGYSGFYTF-------- 141
Cdd:cd03752 100 qePIPVEQLVQRlcdikQGYTQYGGLRPFGVSFLYAGWDKHYGF-QLYQSD--------PSG--NYSGWKATaignnnqa 168

                       170       180       190
                ....*....|....*....|....*....|...
6ZOU_J      142 --SLLDHHYRPDMTTEEGldlLKLCVQELEKRM 172
Cdd:cd03752 169 aqSLLKQDYKDDMTLEEA---LALAVKVLSKTM 198
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-190 1.31e-07

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


Pssm-ID: 239726  Cd Length: 212  Bit Score: 49.95  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSsf 83
Cdd:cd03757  11 VLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIA-- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       84 vrQELAKSIRSRR--PYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLD---------HHYRPDM 152
Cdd:cd03757  89 --QLLSTILYSRRffPYYVFNILAGID-EEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPL 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
6ZOU_J      153 TTEEGLDLLKLCVQELEKRmpmDFK---GVIVKIVDKDGIR 190
Cdd:cd03757 166 SLEEAVSLVKDAFTSAAER---DIYtgdSLEIVIITKDGIE 203
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-160 2.68e-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: 48.90  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        6 GIRVQDSVILASSKAvtrgiSVLKDSDDKTRQ----LSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVS 81
Cdd:cd03755  32 GVRGKDCVVLGVEKK-----SVAKLQDPRTVRkicmLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYIT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       82 SFVRQELAKSIRS--RRPYQVNVLIGGYDkKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLD 159
Cdd:cd03755 107 RYIAGLQQRYTQSggVRPFGISTLIVGFD-PDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTIK 185


                .
6ZOU_J      160 L 160
Cdd:cd03755 186 L 186
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-188 1.18e-06

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 47.32  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTrgiSVLKD--SDDKTRQLSPHTLMSFAGEAGD-TVQFAEYIQANIQLYSIREDYELSPQAVS 81
Cdd:cd03750  31 VGIKAANGVVLATEKKVP---SPLIDesSVHKVEQITPHIGMVYSGMGPDfRVLVKKARKIAQQYYLVYGEPIPVSQLVR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J       82 --SFVRQELAKSiRSRRPYQVNVLIGGYDKKknKPELYQIDylgtkvelPYGAH----------GYSGFYTFslLDHHYR 149
Cdd:cd03750 108 eiASVMQEYTQS-GGVRPFGVSLLIAGWDEG--GPYLYQVD--------PSGSYftwkataigkNYSNAKTF--LEKRYN 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
6ZOU_J      150 PDMTTEEGLDLLKLCVQE-LEKRmpMDFKGVIVKIVDKDG 188
Cdd:cd03750 175 EDLELEDAIHTAILTLKEgFEGQ--MTEKNIEIGICGETK 212
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-160 3.83e-06

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 45.98  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J         5 LGIRVQDSVILASSKavtRGISVL--KDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDyelSPQAVSS 82
Cdd:PRK03996  40 VGVKTKDGVVLAVDK---RITSPLiePSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYG---EPIGVET 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        83 fvrqeLAKSIRSR----------RPYQVNVLIGGYDKKknKPELYQIDYLGTKVElpYGAHGY-SGFYTF-SLLDHHYRP 150
Cdd:PRK03996 114 -----LTKKICDHkqqytqhggvRPFGVALLIAGVDDG--GPRLFETDPSGAYLE--YKATAIgAGRDTVmEFLEKNYKE 184

                        170
                 ....*....|
6ZOU_J       151 DMTTEEGLDL 160
Cdd:PRK03996 185 DLSLEEAIEL 194
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-127 1.42e-04

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


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 41.12  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        6 GIRVQDSVILAsskAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQAniQLYSIREDYElSPQAVSSFVR 85
Cdd:cd03749  32 GLKSKTHAVLV---ALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQ--ECLNYRFVYD-SPIPVSRLVS 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
6ZOU_J       86 QELAKSIR-----SRRPYQVNVLIGGYDKKknKPELYQIDYLGTKVE 127
Cdd:cd03749 106 KVAEKAQIntqryGRRPYGVGLLIAGYDES--GPHLFQTCPSGNYFE 150
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-120 3.22e-04

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: 39.96  E-value: 3.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        5 LGIRVQDSVILASSKAVTrgiSVL--KDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYiqANIQLYSIREDYElSPQAVss 82
Cdd:cd03751  34 IGIRCKDGVVLAVEKLVT---SKLyePGSNKRIFNVDRHIGIAVAGLLADGRHLVSR--AREEAENYRDNYG-TPIPV-- 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
6ZOU_J       83 fvrQELAKSI----------RSRRPYQVNVLIGGYDkkKNKPELYQID 120
Cdd:cd03751 106 ---KVLADRVamymhaytlySSVRPFGCSVLLGGYD--SDGPQLYMIE 148
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 4-96 5.95e-03

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


Pssm-ID: 238894  Cd Length: 171  Bit Score: 36.02  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_J        4 ILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSP-HTLMSFAGEAGDTVQFAEYIQANIQLYSiredYELSPQAVss 82
Cdd:cd01913   3 ILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNgKVIAGFAGSTADAFTLFERFEAKLEQYP----GNLLRAAV-- 76

                        90
                ....*....|....
6ZOU_J       83 fvrqELAKSIRSRR 96
Cdd:cd01913  77 ----ELAKDWRTDR 86
 
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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