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Conserved domains on  [gi|490182788|ref|WP_004081403|]
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MULTISPECIES: ATP-dependent protease subunit HslV [Thermotoga]

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;
5-176 1.25e-119

ATP-dependent protease subunit HslV;


:

Pssm-ID: 235477  Cd Length: 172  Bit Score: 335.10  E-value: 1.25e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   5 GTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELA 84
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  85 KDWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEIC 164
Cdd:PRK05456  81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                        170
                 ....*....|..
gi 490182788 165 IYTNQNIVIEEV 176
Cdd:PRK05456 161 IYTNHNITIEEL 172
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
5-176 1.25e-119

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 335.10  E-value: 1.25e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   5 GTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELA 84
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  85 KDWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEIC 164
Cdd:PRK05456  81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                        170
                 ....*....|..
gi 490182788 165 IYTNQNIVIEEV 176
Cdd:PRK05456 161 IYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 3-176 6.06e-118

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 330.86  E-value: 6.06e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   3 FHGTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVE 82
Cdd:COG5405    1 FHGTTILAVRKGGKVAIAGDGQVTLGNTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  83 LAKDWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGE 162
Cdd:COG5405   81 LAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLDAEEIAREALEIAAD 160

                        170
                 ....*....|....
gi 490182788 163 ICIYTNQNIVIEEV 176
Cdd:COG5405  161 ICIYTNHNITVEEL 174
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 6-176 3.74e-111

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: 313.70  E-value: 3.74e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788    6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELAK 85
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   86 DWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEICI 165
Cdd:TIGR03692  81 DWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLRNTDLSAEEIAREALKIAADICI 160

                         170
                  ....*....|.
gi 490182788  166 YTNQNIVIEEV 176
Cdd:TIGR03692 161 YTNHNITVEEL 171
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 6-176 7.44e-104

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: 295.26  E-value: 7.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELAK 85
Cdd:cd01913    1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  86 DWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEICI 165
Cdd:cd01913   81 DWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLSAEEIARKALKIAADICI 160

                        170
                 ....*....|.
gi 490182788 166 YTNQNIVIEEV 176
Cdd:cd01913  161 YTNHNITVEEL 171
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 3-176 1.45e-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: 109.58  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788    3 FHGTTILVVRRNGQTVMGGDGQVTFGSTVL-KGNARKVRKLGEgKVLAGFAGSVADAMTLFDRFEAKLREW----GGNLT 77
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLsKDTVEKIFKIDD-HIGMAFAGLAADARTLVDRARAEAQLYrlryGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   78 ---------KAAVELAKDWRTDRVLRRLEALLLVADKENIFIISGNGEVIqpDDDAAAIGSGGPYALAAAKALLR--NTD 146
Cdd:pfam00227  81 velaariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYI--EYKATAIGSGSQYAYGVLEKLYRpdLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 490182788  147 LSAREIVEKAMTIAGEICIYTNQNIVIEEV 176
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
5-176 1.25e-119

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 335.10  E-value: 1.25e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   5 GTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELA 84
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  85 KDWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEIC 164
Cdd:PRK05456  81 KDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTDLSAEEIAEKALKIAADIC 160

                        170
                 ....*....|..
gi 490182788 165 IYTNQNIVIEEV 176
Cdd:PRK05456 161 IYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 3-176 6.06e-118

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 330.86  E-value: 6.06e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   3 FHGTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVE 82
Cdd:COG5405    1 FHGTTILAVRKGGKVAIAGDGQVTLGNTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  83 LAKDWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGE 162
Cdd:COG5405   81 LAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLDAEEIAREALEIAAD 160

                        170
                 ....*....|....
gi 490182788 163 ICIYTNQNIVIEEV 176
Cdd:COG5405  161 ICIYTNHNITVEEL 174
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 6-176 3.74e-111

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: 313.70  E-value: 3.74e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788    6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELAK 85
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   86 DWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEICI 165
Cdd:TIGR03692  81 DWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLRNTDLSAEEIAREALKIAADICI 160

                         170
                  ....*....|.
gi 490182788  166 YTNQNIVIEEV 176
Cdd:TIGR03692 161 YTNHNITVEEL 171
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 6-176 7.44e-104

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: 295.26  E-value: 7.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGKVLAGFAGSVADAMTLFDRFEAKLREWGGNLTKAAVELAK 85
Cdd:cd01913    1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  86 DWRTDRVLRRLEALLLVADKENIFIISGNGEVIQPDDDAAAIGSGGPYALAAAKALLRNTDLSAREIVEKAMTIAGEICI 165
Cdd:cd01913   81 DWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDHTDLSAEEIARKALKIAADICI 160

                        170
                 ....*....|.
gi 490182788 166 YTNQNIVIEEV 176
Cdd:cd01913  161 YTNHNITVEEL 171
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 6-176 6.78e-33

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: 115.28  E-value: 6.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEgKVLAGFAGSVADAMTLFDRFEAKLREWG------GNLTKA 79
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDD-HIGCAFAGLAADAQTLVERLRKEAQLYRlrygepIPVEAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  80 AVELAKDWRTDR-VLRRLEALLLVA--DKEN---IFIISGNGEVIQPddDAAAIGSGGPYALAAAKALLRN--TDLSARE 151
Cdd:cd01906   80 AKLLANLLYEYTqSLRPLGVSLLVAgvDEEGgpqLYSVDPSGSYIEY--KATAIGSGSQYALGILEKLYKPdmTLEEAIE 157

                        170       180
                 ....*....|....*....|....*
gi 490182788 152 IVEKAMTIAGEICIYTNQNIVIEEV 176
Cdd:cd01906  158 LALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 3-176 1.45e-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: 109.58  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788    3 FHGTTILVVRRNGQTVMGGDGQVTFGSTVL-KGNARKVRKLGEgKVLAGFAGSVADAMTLFDRFEAKLREW----GGNLT 77
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLsKDTVEKIFKIDD-HIGMAFAGLAADARTLVDRARAEAQLYrlryGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   78 ---------KAAVELAKDWRTDRVLRRLEALLLVADKENIFIISGNGEVIqpDDDAAAIGSGGPYALAAAKALLR--NTD 146
Cdd:pfam00227  81 velaariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYI--EYKATAIGSGSQYAYGVLEKLYRpdLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 490182788  147 LSAREIVEKAMTIAGEICIYTNQNIVIEEV 176
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 6-157 5.49e-23

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: 89.38  E-value: 5.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEGkVLAGFAGSVADAMTLFDRFEAKLREWGGNLTK------A 79
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDG-IAWGLAGLAADAQTLVRRLREALQLYRLRYGEpisvvaL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788  80 AVELAKDWRTDRVLRRLEALLLVADKE----NIFIISGNGEVIQpDDDAAAIGSGGPYALAAAKALLRN--TDLSAREIV 153
Cdd:cd01901   80 AKELAKLLQVYTQGRPFGVNLIVAGVDegggNLYYIDPSGPVIE-NPGAVATGSRSQRAKSLLEKLYKPdmTLEEAVELA 158


                 ....
gi 490182788 154 EKAM 157
Cdd:cd01901  159 LKAL 162
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 4-133 3.12e-06

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 45.52  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   4 HGTTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEgKVLAGFAGSVADAMTLFD--RFEAKLRE--WGGNLTka 79
Cdd:COG0638   34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDD-HIGVAIAGLVADARELVRlaRVEAQLYElrYGEPIS-- 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490182788  80 aVE-LAKD------WRTDRVLRRLEALLLVA--DKE--NIFIISGNGEVIQpdDDAAAIGSGGPY 133
Cdd:COG0638  111 -VEgLAKLlsdllqGYTQYGVRPFGVALLIGgvDDGgpRLFSTDPSGGLYE--EKAVAIGSGSPF 172
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-70 2.54e-05

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: 42.82  E-value: 2.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEgKVLAGFAGSVADAMTLFDRFEAKLR 70
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISD-NILLGTAGSAADTQALTRLLKRNLR 64
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-133 4.16e-04

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: 39.13  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEgKVLAGFAGSVADAMTLFDRFEAKLREWG-----GNLTKAA 80
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHD-RIYCCRSGSAADTQAIADYVRYYLDMHSielgePPLVKTA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490182788  81 VELAKD----WRTDrvlrrLEALLLVA--DKEN---IFIISGNGEVIQpdDDAAAIGSGGPY 133
Cdd:cd03762   80 ASLFKNlcynYKEM-----LSAGIIVAgwDEQNggqVYSIPLGGMLIR--QPFAIGGSGSTY 134
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-133 2.59e-03

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: 36.85  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490182788   6 TTILVVRRNGQTVMGGDGQVTFGSTVLKGNARKVRKLGEgKVLAGFAGSVADAMTLFD--RFEAKLRE--WGGNLT-KAA 80
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDD-KIAMTIAGSVGDAQSLVRilKAEARLYElrRGRPMSiKAL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490182788  81 VELAKDwrtdrVLR-------RLEALLLVADKE--NIFIISGNGEVIQpdDDAAAIGSGGPY 133
Cdd:cd03764   80 ATLLSN-----ILNsskyfpyIVQLLIGGVDEEgpHLYSLDPLGSIIE--DKYTATGSGSPY 134
 
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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