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Conserved domains on  [gi|17508495|ref|NP_493271|]
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Proteasome subunit beta [Caenorhabditis elegans]

Protein Classification

proteasome subunit beta( domain architecture ID 10132938)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; such as Arabidopsis thaliana proteasome subunit beta type-7-A

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-235 1.32e-106

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: 307.20  E-value: 1.32e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGYIGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRALE 206
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17508495 207 AGMHGDNASGNSLNLVIIEPSETVFKGPI 235
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-235 1.32e-106

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: 307.20  E-value: 1.32e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGYIGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRALE 206
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17508495 207 AGMHGDNASGNSLNLVIIEPSETVFKGPI 235
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 43-224 2.79e-58

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: 184.31  E-value: 2.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495    43 TSTGTTIVAVAFKGGLVMGADSRATAGNIIADKH-CEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKAR 121
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   122 V----ITALRQAKQHLFNYQGYIGAYLLIGGVDPTG-PHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDE 196
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 17508495   197 AEKLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 39-224 1.49e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 145.29  E-value: 1.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  39 APKLTSTGTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGR 118
Cdd:COG0638  28 AREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 119 KARVITALRQAKQHLFNYQGY----IGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTK 194
Cdd:COG0638 108 PISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSL 187

                       170       180       190
                ....*....|....*....|....*....|
gi 17508495 195 DEAEKLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:COG0638 188 DEAVELALRALYSAAERDSASGDGIDVAVI 217
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 46-224 1.33e-39

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 136.19  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495    46 GTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITA 125
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   126 -------LRQAKQHLFNYQgyigayLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAE 198
Cdd:TIGR03634  81 atllsniLNSNRFFPFIVQ------LLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAK 154

                         170       180
                  ....*....|....*....|....*.
gi 17508495   199 KLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:TIGR03634 155 KLAVRAIKSAIERDVASGNGIDVAVI 180
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 46-221 1.32e-27

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 106.61  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   46 GTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITA 125
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  126 LRQAKQHLFNYQGY-IGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRA 204
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 17508495  205 LEAGMHGDNASGNSLNL 221
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-235 1.32e-106

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: 307.20  E-value: 1.32e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGYIGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRALE 206
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17508495 207 AGMHGDNASGNSLNLVIIEPSETVFKGPI 235
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 47-226 1.51e-65

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: 202.67  E-value: 1.51e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGY-IGAYLLIGGVDP-TGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRA 204
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|..
gi 17508495 205 LEAGMHGDNASGNSLNLVIIEP 226
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITK 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 43-224 2.79e-58

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: 184.31  E-value: 2.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495    43 TSTGTTIVAVAFKGGLVMGADSRATAGNIIADKH-CEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKAR 121
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   122 V----ITALRQAKQHLFNYQGYIGAYLLIGGVDPTG-PHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDE 196
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 17508495   197 AEKLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 47-224 9.01e-57

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: 180.00  E-value: 9.01e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGY---IGAYLLIGGVDP-TGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQ 202
Cdd:cd01906  81 KLLANLLYEYTQSlrpLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 17508495 203 RALEAGMHGDNASGNSLNLVII 224
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 39-224 1.49e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 145.29  E-value: 1.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  39 APKLTSTGTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGR 118
Cdd:COG0638  28 AREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 119 KARVITALRQAKQHLFNYQGY----IGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTK 194
Cdd:COG0638 108 PISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSL 187

                       170       180       190
                ....*....|....*....|....*....|
gi 17508495 195 DEAEKLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:COG0638 188 DEAVELALRALYSAAERDSASGDGIDVAVI 217
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 47-207 2.30e-41

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: 140.22  E-value: 2.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQ--GYIGAYLLIGGVDPTGPHLYMCSANGTTMAFP-FTAQGSGSYAAITILERDFKVDMTKDEAEKLVQR 203
Cdd:cd01901  81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
gi 17508495 204 ALEA 207
Cdd:cd01901 161 ALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 46-224 1.33e-39

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 136.19  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495    46 GTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITA 125
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   126 -------LRQAKQHLFNYQgyigayLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAE 198
Cdd:TIGR03634  81 atllsniLNSNRFFPFIVQ------LLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAK 154

                         170       180
                  ....*....|....*....|....*.
gi 17508495   199 KLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:TIGR03634 155 KLAVRAIKSAIERDVASGNGIDVAVI 180
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-229 1.80e-39

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: 135.84  E-value: 1.80e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITA- 125
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 126 ------LRQAKQHLFNYQgyigayLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEK 199
Cdd:cd03764  81 tllsniLNSSKYFPYIVQ------LLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKK 154

                       170       180       190
                ....*....|....*....|....*....|
gi 17508495 200 LVQRALEAGMHGDNASGNSLNLVIIEPSET 229
Cdd:cd03764 155 LAIRAIKSAIERDSASGDGIDVVVITKDGY 184
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-224 6.94e-39

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: 134.27  E-value: 6.94e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGYIGAYLLIGGVDPT-GPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRAL 205
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQnGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170
                ....*....|....*....
gi 17508495 206 EAGMHGDNASGNSLNLVII 224
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVII 179
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 47-227 1.03e-27

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: 105.40  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITAL 126
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 127 RQAKQHLFNYQGY---IGAylLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQR 203
Cdd:cd03761  81 KLLSNMLYQYKGMglsMGT--MICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                       170       180
                ....*....|....*....|....
gi 17508495 204 ALEAGMHGDNASGNSLNLVIIEPS 227
Cdd:cd03761 159 AIYHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 46-221 1.32e-27

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 106.61  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   46 GTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVITA 125
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  126 LRQAKQHLFNYQGY-IGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRA 204
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 17508495  205 LEAGMHGDNASGNSLNL 221
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 46-225 8.96e-21

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: 87.77  E-value: 8.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  46 GTTIVAVAFKGGLVMGADSRATAGNIIADKhCEKVHKLTESIYACGAGTAAD----LD------QVTKMLSG---NLRLL 112
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKRITSKLVEPES-IEKIYKIDDHVGAATSGLVADarvlIDrarveaQIHRLTYGepiDVEVL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 113 elntgrkARVITALRQA-KQHlfnyqGYI---GAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDF 188
Cdd:cd03756 107 -------VKKICDLKQQyTQH-----GGVrpfGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEY 174

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17508495 189 KVDMTKDEAEKLVQRALEAGMHgDNASGNSLNLVIIE 225
Cdd:cd03756 175 KEDMSLEEAIELALKALYAALE-ENETPENVEIAYVT 210
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-234 4.76e-20

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: 85.31  E-value: 4.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  45 TGTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRK----- 119
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHslspk 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 120 ------ARVITALRQAKQHLFNYqgyigayLLIGGVDPTG-PHLYMCSANGTTMAFPFTAQGSGSYAAITIL--ERDFKV 190
Cdd:cd03760  81 eihsylTRVLYNRRSKMNPLWNT-------LVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLreAWEKKP 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 17508495 191 DMTKDEAEKLVQRALEAGMHGDNASGNSLNLVIIEPSETVFKGP 234
Cdd:cd03760 154 DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-217 2.04e-18

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: 81.33  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  38 KAPKLtstGTTIVAVAFKGGLVMGADSRATAGNIIADkHCEKVHKLTESIYACGAGTAADldqvTKMLSgnlrllelntg 117
Cdd:cd01911  22 EAVKN---GSTAVGIKGKDGVVLAVEKKVTSKLLDPS-SVEKIFKIDDHIGCAVAGLTAD----ARVLV----------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 118 RKARVItalrqAKQHLFNYQGYI-------------------------GAYLLIGGVDP-TGPHLYMCSANGTTMAFPFT 171
Cdd:cd01911  83 NRARVE-----AQNYRYTYGEPIpvevlvkriadlaqvytqyggvrpfGVSLLIAGYDEeGGPQLYQTDPSGTYFGYKAT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17508495 172 AQGSGSYAAITILERDFKVDMTKDEAEKLVQRALEAGMHGDNASGN 217
Cdd:cd01911 158 AIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKN 203
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
46-232 2.09e-18

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 81.80  E-value: 2.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   46 GTTIVAVAFKGGLVMGADSRATAGNIIADKhCEKVHKLTESIYACGAGTAADldqvtkmlsgnlrllelntgrkARVIT- 124
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVAD----------------------ARVLId 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  125 -ALRQAKQHLFNY-----------------QGY--------IGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSY 178
Cdd:PRK03996  93 rARVEAQINRLTYgepigvetltkkicdhkQQYtqhggvrpFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17508495  179 AAITILERDFKVDMTKDEAEKLVQRALEAGMHgDNASGNSLNLVIIEPSETVFK 232
Cdd:PRK03996 173 TVMEFLEKNYKEDLSLEEAIELALKALAKANE-GKLDPENVEIAYIDVETKKFR 225
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 48-203 2.04e-13

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 67.23  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  48 TIVAVAFKGGLVMGADSRATAGnIIADKHCE-KVHKLTESIYACGAGTAADLDQVTKMLSGNLRL------LELNTGRKA 120
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARS-ILVLKDDEdKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLykmrngYELSPKAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 121 RVI-----TALRQAKQhlfnYQgyigAYLLIGGVDP-TGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTK 194
Cdd:cd03758  82 NFTrrelaESLRSRTP----YQ----VNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTV 153


                ....*....
gi 17508495 195 DEAEKLVQR 203
Cdd:cd03758 154 EEALELMKK 162
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-224 3.99e-12

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: 63.82  E-value: 3.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  43 TSTGTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRK--- 119
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEmst 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 120 ---ARVITALRQAKQhLFNYQgyigAYLLIGGVDPTG-PHLYMCSANGTTMAFPFTAQGSGSYAAITILE---------R 186
Cdd:cd03757  85 eaiAQLLSTILYSRR-FFPYY----VFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnN 159

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17508495 187 DFKVDMTKDEAEKLVQRALEAGMHGDNASGNSLNLVII 224
Cdd:cd03757 160 VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVII 197
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-209 2.40e-11

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: 61.58  E-value: 2.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  38 KAPKLtstGTTIVAVAFKGGLVMGADSRATAGNIIADKhCEKVHKLTESIYACGAGTAADLDQvtkmlsgnlrLLElntg 117
Cdd:cd03753  22 EAIKL---GSTAIGIKTKEGVVLAVEKRITSPLMEPSS-VEKIMEIDDHIGCAMSGLIADART----------LID---- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 118 rKARVitalrQAKQHLFNYQGYI------------------------------GAYLLIGGVDPTGPHLYMCSANGTTMA 167
Cdd:cd03753  84 -HARV-----EAQNHRFTYNEPMtvesvtqavsdlalqfgegddgkkamsrpfGVALLIAGVDENGPQLFHTDPSGTFTR 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17508495 168 FPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQRALEAGM 209
Cdd:cd03753 158 CDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVM 199
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 46-205 2.58e-11

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: 61.61  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  46 GTTIVAVAFKGGLVMGADSRATAgNIIADKHCEKVHKLTESIYACGAGTAADLdqvtkmlsgnlRLLeLNtgrKARVita 125
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADA-----------RVL-IN---RARL--- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 126 lrQAKQHLFNYQG-----YIGAYL--------------------LIGGVDPTG-PHLYMCSANGTTMAFPFTAQGSGSYA 179
Cdd:cd03755  88 --ECQSHRLTVEDpvtveYITRYIaglqqrytqsggvrpfgistLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKT 165

                       170       180
                ....*....|....*....|....*.
gi 17508495 180 AITILERDFKVDMTKDEAEKLVQRAL 205
Cdd:cd03755 166 VREFLEKNYKEEMTRDDTIKLAIKAL 191
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 46-209 4.04e-11

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: 61.21  E-value: 4.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  46 GTTIVAVAfKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADldqvTKMLSGNLRLlelntgrkarvita 125
Cdd:cd03752  30 GTCLGILA-KDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD----ANILINYARL-------------- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 126 lrQAKQHLFNY-----------------QGY--------IGAYLLIGGVDPT-GPHLYMCSANGTTMAFPFTAQGSGSYA 179
Cdd:cd03752  91 --IAQRYLYSYqepipveqlvqrlcdikQGYtqygglrpFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQA 168

                       170       180       190
                ....*....|....*....|....*....|
gi 17508495 180 AITILERDFKVDMTKDEAEKLVQRALEAGM 209
Cdd:cd03752 169 AQSLLKQDYKDDMTLEEALALAVKVLSKTM 198
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-213 1.33e-09

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


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 56.53  E-value: 1.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  38 KAPKLtstGTTIVAVAFKGGLVMGADSRATagNIIADkHCEKVHKLTESIYACGAGTAADldqvTKMLSGNLRLLELN-- 115
Cdd:cd03749  22 EAVKQ---GSATVGLKSKTHAVLVALKRAT--SELSS-YQKKIFKVDDHIGIAIAGLTAD----ARVLSRYMRQECLNyr 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 116 --------TGRKARVITALRQAKQHLFNYQGYiGAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERD 187
Cdd:cd03749  92 fvydspipVSRLVSKVAEKAQINTQRYGRRPY-GVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERH 170

                       170       180
                ....*....|....*....|....*...
gi 17508495 188 FKV--DMTKDEAEKLVQRALEAGMHGDN 213
Cdd:cd03749 171 FEEfeDCSLEELIKHALRALRETLPGEQ 198
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 44-213 2.98e-07

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: 50.01  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  44 STGTTIVAVAFKGGLVMGADSRATagNIIADKHC-EKVHKLTESIYACGAGTAADLdqvtkmlsgnlRLLeLNTGRKarv 122
Cdd:cd03750  25 SSGAPSVGIKAANGVVLATEKKVP--SPLIDESSvHKVEQITPHIGMVYSGMGPDF-----------RVL-VKKARK--- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 123 italrQAKQHLFNYQGYI-------------------------GAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGS 177
Cdd:cd03750  88 -----IAQQYYLVYGEPIpvsqlvreiasvmqeytqsggvrpfGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNY 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17508495 178 YAAITILERDFKVDMTKDEAeklVQRAL-------EAGMHGDN 213
Cdd:cd03750 163 SNAKTFLEKRYNEDLELEDA---IHTAIltlkegfEGQMTEKN 202
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 50-258 6.69e-07

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 49.47  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495   50 VAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARV---ITAL 126
Cdd:PTZ00246  35 VGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVeqlVVQI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  127 RQAKQHLFNYQGY--IGAYLLIGGVDPT-GPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDFKVDMTKDEAEKLVQR 203
Cdd:PTZ00246 115 CDLKQSYTQFGGLrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAK 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17508495  204 ALEAGMHGDNASGNSLNLVIIEPSETVFKgPIVpEFCKRPEPNDLVYKFQAGATK 258
Cdd:PTZ00246 195 VLTKSMDSTSPKADKIEVGILSHGETDGE-PIQ-KMLSEKEIAELLKKVTQEYAK 247
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 5.90e-06

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: 45.70  E-value: 5.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  44 STGTTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACGAGTAADLDQVTKMLSGNLRLLELNTGRKARVI 123
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 124 TALRQAKQHLfnYQGYIGAYL---LIGGVDPTG-PhlYMCSAN--GTTM-AFPFTAQGSGSYAAITILERDFKVDMTKDE 196
Cdd:cd03759  81 TFSSLISSLL--YEKRFGPYFvepVVAGLDPDGkP--FICTMDliGCPSiPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17508495 197 AEKLVQRALEAGMHGDNASGNSLNLVIIEPSETVFK 232
Cdd:cd03759 157 LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTR 192
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-203 1.70e-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: 41.88  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495  39 APKLTSTGTTIVAVAFKGGLVMGADsratagNIIADKHCEK-----VHKLTESIYACGAGTAADLDQVTKMLSGNLRLLE 113
Cdd:cd03751  23 ANKAVENSGTAIGIRCKDGVVLAVE------KLVTSKLYEPgsnkrIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508495 114 LNTGRKA--RVITALRQAKQHLFNYQGYI---GAYLLIGGVDPTGPHLYMCSANGTTMAFPFTAQGSGSYAAITILERDF 188
Cdd:cd03751  97 DNYGTPIpvKVLADRVAMYMHAYTLYSSVrpfGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLK 176

                       170
                ....*....|....*
gi 17508495 189 KVDMTKDEAEKLVQR 203
Cdd:cd03751 177 FSELTCREAVKEAAK 191
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 47-97 2.08e-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: 37.94  E-value: 2.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508495  47 TTIVAVAFKGGLVMGADSRATAGNIIADKHCEKVHKLTESIYACG-AGTAAD 97
Cdd:cd01913   1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGfAGSTAD 52
 
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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