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Conserved domains on  [gi|1899858133|gb|QNQ29479|]
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ATP-dependent protease subunit HslV [Enterobacter roggenkampii]

Protein Classification

ATP-dependent protease subunit HslV( domain architecture ID 10012413)

ATP-dependent protease subunit HslV is the proteolytic component of the ATP-dependent protease HslVU, which catalyzes the ATP-dependent cleavage of peptide bonds with broad specificity during protein degradation

EC:  3.4.25.2
Gene Ontology:  GO:0051603|GO:0004298|GO:0046872|GO:0005839|GO:0009376
PubMed:  15037245

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
1-172 7.04e-133

ATP-dependent protease subunit HslV;


:

Pssm-ID: 235477  Cd Length: 172  Bit Score: 368.22  E-value: 7.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   1 MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELA 80
Cdd:PRK05456    1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDIC 160
Cdd:PRK05456   81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                         170
                  ....*....|..
gi 1899858133 161 IYTNHNHTIEEL 172
Cdd:PRK05456  161 IYTNHNITIEEL 172
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
1-172 7.04e-133

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 368.22  E-value: 7.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   1 MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELA 80
Cdd:PRK05456    1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDIC 160
Cdd:PRK05456   81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                         170
                  ....*....|..
gi 1899858133 161 IYTNHNHTIEEL 172
Cdd:PRK05456  161 IYTNHNITIEEL 172
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 2-172 1.89e-121

ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex of hexameric HslU active as a protein-unfolding ATPase and dodecameric HslV, the catalytic threonine protease. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274727  Cd Length: 171  Bit Score: 339.51  E-value: 1.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAK 81
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  82 DWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDICI 161
Cdd:TIGR03692  81 DWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLRNTDLSAEEIAREALKIAADICI 160

                         170
                  ....*....|.
gi 1899858133 162 YTNHNHTIEEL 172
Cdd:TIGR03692 161 YTNHNITVEEL 171
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 1-172 2.80e-121

ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444164  Cd Length: 174  Bit Score: 339.33  E-value: 2.80e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   1 MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELA 80
Cdd:COG5405     3 GTTILAVRKGGKVAIAGDGQVTLGNTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAVELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDIC 160
Cdd:COG5405    83 KDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLDAEEIAREALEIAADIC 162

                         170
                  ....*....|..
gi 1899858133 161 IYTNHNHTIEEL 172
Cdd:COG5405   163 IYTNHNITVEEL 174
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 2-172 5.60e-114

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: 320.68  E-value: 5.60e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAK 81
Cdd:cd01913     1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  82 DWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDICI 161
Cdd:cd01913    81 DWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLSAEEIARKALKIAADICI 160

                         170
                  ....*....|.
gi 1899858133 162 YTNHNHTIEEL 172
Cdd:cd01913   161 YTNHNITVEEL 171
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 2-172 5.52e-30

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: 108.04  E-value: 5.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTV-MKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQ--------GHL 72
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKI-DDHIGMAFAGLAADARTLVDRARAEAQLYRlrygrpipVEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  73 V-----KAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPenDLIAIGSGGPYAQAAARALL--ENTDMNA 145
Cdd:pfam00227  84 AariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEY--KATAIGSGSQYAYGVLEKLYrpDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 1899858133 146 RDIAVKALDIAGDICIYTNHNHTIEEL 172
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
1-172 7.04e-133

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 368.22  E-value: 7.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   1 MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELA 80
Cdd:PRK05456    1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDIC 160
Cdd:PRK05456   81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                         170
                  ....*....|..
gi 1899858133 161 IYTNHNHTIEEL 172
Cdd:PRK05456  161 IYTNHNITIEEL 172
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 2-172 1.89e-121

ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex of hexameric HslU active as a protein-unfolding ATPase and dodecameric HslV, the catalytic threonine protease. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274727  Cd Length: 171  Bit Score: 339.51  E-value: 1.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAK 81
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  82 DWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDICI 161
Cdd:TIGR03692  81 DWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLRNTDLSAEEIAREALKIAADICI 160

                         170
                  ....*....|.
gi 1899858133 162 YTNHNHTIEEL 172
Cdd:TIGR03692 161 YTNHNITVEEL 171
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 1-172 2.80e-121

ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444164  Cd Length: 174  Bit Score: 339.33  E-value: 2.80e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   1 MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELA 80
Cdd:COG5405     3 GTTILAVRKGGKVAIAGDGQVTLGNTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAVELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDIC 160
Cdd:COG5405    83 KDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLDAEEIAREALEIAADIC 162

                         170
                  ....*....|..
gi 1899858133 161 IYTNHNHTIEEL 172
Cdd:COG5405   163 IYTNHNITVEEL 174
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 2-172 5.60e-114

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: 320.68  E-value: 5.60e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAK 81
Cdd:cd01913     1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  82 DWRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYAQAAARALLENTDMNARDIAVKALDIAGDICI 161
Cdd:cd01913    81 DWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLSAEEIARKALKIAADICI 160

                         170
                  ....*....|.
gi 1899858133 162 YTNHNHTIEEL 172
Cdd:cd01913   161 YTNHNITVEEL 171
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 2-170 3.86e-37

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: 126.46  E-value: 3.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQ------GHLVKA 75
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKI-DDHIGCAFAGLAADAQTLVERLRKEAQLYRlrygepIPVEAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  76 AVELAKDWRTDRM-LRKLEALLAVA----DETASL-IITGNGDVIQPenDLIAIGSGGPYAQAAARALLEN--TDMNARD 147
Cdd:cd01906    80 AKLLANLLYEYTQsLRPLGVSLLVAgvdeEGGPQLySVDPSGSYIEY--KATAIGSGSQYALGILEKLYKPdmTLEEAIE 157

                         170       180
                  ....*....|....*....|...
gi 1899858133 148 IAVKALDIAGDICIYTNHNHTIE 170
Cdd:cd01906   158 LALKALKSALERDLYSGGNIEVA 180
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 2-172 5.52e-30

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: 108.04  E-value: 5.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTV-MKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQ--------GHL 72
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKI-DDHIGMAFAGLAADARTLVDRARAEAQLYRlrygrpipVEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  73 V-----KAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVIQPenDLIAIGSGGPYAQAAARALL--ENTDMNA 145
Cdd:pfam00227  84 AariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEY--KATAIGSGSQYAYGVLEKLYrpDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 1899858133 146 RDIAVKALDIAGDICIYTNHNHTIEEL 172
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 2-155 1.71e-25

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: 95.92  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQ------GHLVKA 75
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKN-EDGIAWGLAGLAADAQTLVRRLREALQLYRlrygepISVVAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  76 AVELAKDWRTDRMLRKLEALLAVADETA----SLIITGNGDVIQPEnDLIAIGSGGPYAQAAARALLEN--TDMNARDIA 149
Cdd:cd01901    80 AKELAKLLQVYTQGRPFGVNLIVAGVDEgggnLYYIDPSGPVIENP-GAVATGSRSQRAKSLLEKLYKPdmTLEEAVELA 158


                  ....*.
gi 1899858133 150 VKALDI 155
Cdd:cd01901   159 LKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-163 9.46e-11

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: 57.84  E-value: 9.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQGH-----LVKAA 76
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKI-SDNILLGTAGSAADTQALTRLLKRNLRLYELRngrelSVKAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  77 VELAKdwrtdRML-RKLEALLavadeTASLIITG--------------NGDVIqpENDLIAIGSGGPYAQAAARALLENt 141
Cdd:cd01912    80 ANLLS-----NILySYRGFPY-----YVSLIVGGvdkgggpflyyvdpLGSLI--EAPFVATGSGSKYAYGILDRGYKP- 146

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1899858133 142 DMN---ARDIAVKALDIAG----------DICIYT 163
Cdd:cd01912   147 DMTleeAVELVKKAIDSAIerdlssgggvDVAVIT 181
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 2-158 7.98e-10

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 55.54  E-value: 7.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMH---QGHL--VKAA 76
Cdd:COG0638    36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKI-DDHIGVAIAGLVADARELVRLARVEAQLYelrYGEPisVEGL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  77 VELAKD---WRTDRMLRKLEALLAVA---DETASLIIT-GNGDVIqpENDLIAIGSGGPYaqaaARALLE---NTDMN-- 144
Cdd:COG0638   115 AKLLSDllqGYTQYGVRPFGVALLIGgvdDGGPRLFSTdPSGGLY--EEKAVAIGSGSPF----ARGVLEkeyREDLSld 188

                         170
                  ....*....|....*
gi 1899858133 145 -ARDIAVKALDIAGD 158
Cdd:COG0638   189 eAVELALRALYSAAE 203
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-153 1.70e-07

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: 48.79  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFerKLEMHQGHL-------VK 74
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQI-DDKIAMTIAGSVGDAQSLVRIL--KAEARLYELrrgrpmsIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  75 AAVELAKD-WRTDRMLRKL-EALLAVADETASLIITGN--GDVIqpENDLIAIGSGGPYAQaaarALLE---NTDMN--- 144
Cdd:cd03764    78 ALATLLSNiLNSSKYFPYIvQLLIGGVDEEGPHLYSLDplGSII--EDKYTATGSGSPYAY----GVLEdeyKEDMTvee 151


                  ....*....
gi 1899858133 145 ARDIAVKAL 153
Cdd:cd03764   152 AKKLAIRAI 160
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 2-158 1.81e-07

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 48.94  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEmhqgHLVK-AAVELA 80
Cdd:TIGR03690   3 TTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPT-DEYSAVGIAGTAGLAIELVRLFQVELE----HYEKiEGVPLT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  81 KDWRTDR---MLRK-----LEALLAVADETASLIITGNGDVIQ--------PENDLIAIGSGGPYAQAAARALLENtDMN 144
Cdd:TIGR03690  78 LDGKANRlaaMVRGnlpaaMQGLAVVPLLAGYDLDAGAGRIFSydvtggryEERGYHAVGSGSVFAKGALKKLYSP-DLD 156

                         170
                  ....*....|....*..
gi 1899858133 145 ARD---IAVKALDIAGD 158
Cdd:TIGR03690 157 EDDalrVAVEALYDAAD 173
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-69 2.07e-05

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: 42.95  E-value: 2.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMHQ 69
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYI-APNIYCCGAGTAADTEAVTNMISSNLELHR 67
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-81 6.82e-05

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: 41.44  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAFTLFELFERKLEMH-----QGHLVKAA 76
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQL-HDRIYCCRSGSAADTQAIADYVRYYLDMHsielgEPPLVKTA 79


                  ....*
gi 1899858133  77 VELAK 81
Cdd:cd03762    80 ASLFK 84
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 2-130 3.08e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 39.97  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133   2 TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLyNDKVIAGFAGGTADAftlfELFERKL-------EMHQGHL-- 72
Cdd:PTZ00488   40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEI-NPTLLGTMAGGAADC----SFWERELamqcrlyELRNGELis 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899858133  73 VKAAVELAKD--WRTDRMLRKLEALLAVADETASLIITGNGDVIQPENDLIAIGSGGPYA 130
Cdd:PTZ00488  115 VAAASKILANivWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYA 174
 
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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