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Conserved domains on  [gi|2173728245|gb|UIF29868|]
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HslU--HslV peptidase proteolytic subunit [Levilactobacillus brevis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 8-180 1.00e-99

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: 284.81  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEKViMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVELA 87
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  88 KQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGGI 167
Cdd:TIGR03692  80 KDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNY-ALAAARALLRNTDLSAEEIAREALKIAADI 158

                         170
                  ....*....|...
gi 2173728245 168 DIFTNENVISEEL 180
Cdd:TIGR03692 159 CIYTNHNITVEEL 171
 
Name Accession Description Interval E-value
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 8-180 1.00e-99

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: 284.81  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEKViMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVELA 87
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  88 KQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGGI 167
Cdd:TIGR03692  80 KDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNY-ALAAARALLRNTDLSAEEIAREALKIAADI 158

                         170
                  ....*....|...
gi 2173728245 168 DIFTNENVISEEL 180
Cdd:TIGR03692 159 CIYTNHNITVEEL 171
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
7-180 1.45e-99

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 284.25  E-value: 1.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   7 ATTICAVRHNGHNAMAGDGQVTMGEKViMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVEL 86
Cdd:PRK05456    1 GTTILAVRRNGKVAIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  87 AKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGG 166
Cdd:PRK05456   80 AKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNY-ALAAARALLENTDLSAEEIAEKALKIAAD 158

                         170
                  ....*....|....
gi 2173728245 167 IDIFTNENVISEEL 180
Cdd:PRK05456  159 ICIYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 5-180 1.25e-96

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 276.93  E-value: 1.25e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   5 FEATTICAVRHNGHNAMAGDGQVTMGeKVIMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAV 84
Cdd:COG5405     1 FHGTTILAVRKGGKVAIAGDGQVTLG-NTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  85 ELAKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIA 164
Cdd:COG5405    80 ELAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNY-ALAAARALLDHTDLDAEEIAREALEIA 158

                         170
                  ....*....|....*.
gi 2173728245 165 GGIDIFTNENVISEEL 180
Cdd:COG5405   159 ADICIYTNHNITVEEL 174
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 8-180 2.49e-92

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: 265.98  E-value: 2.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEkVIMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVELA 87
Cdd:cd01913     1 TTILAVRKNGKVVIAGDGQVTLGN-TVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  88 KQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGGI 167
Cdd:cd01913    80 KDWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNY-ALAAARALLDHTDLSAEEIARKALKIAADI 158

                         170
                  ....*....|...
gi 2173728245 168 DIFTNENVISEEL 180
Cdd:cd01913   159 CIYTNHNITVEEL 171
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-175 2.85e-26

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: 98.79  E-value: 2.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   7 ATTICAVRHNGHNAMAGDGQVTMGEKVIMKGTAHKIRRIYNNqVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQR----- 81
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDH-IGMAFAGLAADARTLVDRARAEAQLYRLRYGRpipve 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  82 --------AAVELAKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPddDILAIGSGGNFalAAATALHHHAKDMS- 152
Cdd:pfam00227  83 laariadlLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEY--KATAIGSGSQY--AYGVLEKLYRPDLTl 158

                         170       180
                  ....*....|....*....|....*
gi 2173728245 153 --AKEIAESAIHIAGGIDIFTNENV 175
Cdd:pfam00227 159 eeAVELAVKALKEAIDRDALSGGNI 183
 
Name Accession Description Interval E-value
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
 8-180 1.00e-99

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: 284.81  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEKViMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVELA 87
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  88 KQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGGI 167
Cdd:TIGR03692  80 KDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNY-ALAAARALLRNTDLSAEEIAREALKIAADI 158

                         170
                  ....*....|...
gi 2173728245 168 DIFTNENVISEEL 180
Cdd:TIGR03692 159 CIYTNHNITVEEL 171
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
7-180 1.45e-99

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 284.25  E-value: 1.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   7 ATTICAVRHNGHNAMAGDGQVTMGEKViMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVEL 86
Cdd:PRK05456    1 GTTILAVRRNGKVAIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  87 AKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGG 166
Cdd:PRK05456   80 AKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNY-ALAAARALLENTDLSAEEIAEKALKIAAD 158

                         170
                  ....*....|....
gi 2173728245 167 IDIFTNENVISEEL 180
Cdd:PRK05456  159 ICIYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
 5-180 1.25e-96

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 276.93  E-value: 1.25e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   5 FEATTICAVRHNGHNAMAGDGQVTMGeKVIMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAV 84
Cdd:COG5405     1 FHGTTILAVRKGGKVAIAGDGQVTLG-NTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  85 ELAKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIA 164
Cdd:COG5405    80 ELAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNY-ALAAARALLDHTDLDAEEIAREALEIA 158

                         170
                  ....*....|....*.
gi 2173728245 165 GGIDIFTNENVISEEL 180
Cdd:COG5405   159 ADICIYTNHNITVEEL 174
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 8-180 2.49e-92

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: 265.98  E-value: 2.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEkVIMKGTAHKIRRIYNNQVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQRAAVELA 87
Cdd:cd01913     1 TTILAVRKNGKVVIAGDGQVTLGN-TVMKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  88 KQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPDDDILAIGSGGNFaLAAATALHHHAKDMSAKEIAESAIHIAGGI 167
Cdd:cd01913    80 KDWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNY-ALAAARALLDHTDLSAEEIARKALKIAADI 158

                         170
                  ....*....|...
gi 2173728245 168 DIFTNENVISEEL 180
Cdd:cd01913   159 CIYTNHNITVEEL 171
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 8-175 2.74e-27

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: 101.03  E-value: 2.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEkVIMKGTAHKIRRIYNNqVVVGFAGSVADAFNLEEKFEGQLNEYS------GNLQR 81
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGL-LVASSTVEKIFKIDDH-IGCAFAGLAADAQTLVERLRKEAQLYRlrygepIPVEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  82 AAVELAKQWRSD-QALQKLEALLIVMDKDE-----MLLVSGSGEVIAPddDILAIGSGGNFalAAATALHHHAKDMS--- 152
Cdd:cd01906    79 LAKLLANLLYEYtQSLRPLGVSLLVAGVDEeggpqLYSVDPSGSYIEY--KATAIGSGSQY--ALGILEKLYKPDMTlee 154

                         170       180
                  ....*....|....*....|...
gi 2173728245 153 AKEIAESAIHIAGGIDIFTNENV 175
Cdd:cd01906   155 AIELALKALKSALERDLYSGGNI 177
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-175 2.85e-26

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: 98.79  E-value: 2.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   7 ATTICAVRHNGHNAMAGDGQVTMGEKVIMKGTAHKIRRIYNNqVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQR----- 81
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDH-IGMAFAGLAADARTLVDRARAEAQLYRLRYGRpipve 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  82 --------AAVELAKQWRSDQALQKLEALLIVMDKDEMLLVSGSGEVIAPddDILAIGSGGNFalAAATALHHHAKDMS- 152
Cdd:pfam00227  83 laariadlLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEY--KATAIGSGSQY--AYGVLEKLYRPDLTl 158

                         170       180
                  ....*....|....*....|....*
gi 2173728245 153 --AKEIAESAIHIAGGIDIFTNENV 175
Cdd:pfam00227 159 eeAVELAVKALKEAIDRDALSGGNI 183
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 8-163 5.95e-16

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: 71.27  E-value: 5.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEkVIMKGTAHKIRRIYNNqVVVGFAGSVADAFNLEEKFEGQLNEYS------GNLQR 81
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGL-PVAGSPVIKIGKNEDG-IAWGLAGLAADAQTLVRRLREALQLYRlrygepISVVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245  82 AAVELAKQWRSDQALQKLEALLIVMDKDEM----LLVSGSGEVIApDDDILAIGSGGNFalAAATALHHHAKDMSAKEIA 157
Cdd:cd01901    79 LAKELAKLLQVYTQGRPFGVNLIVAGVDEGggnlYYIDPSGPVIE-NPGAVATGSRSQR--AKSLLEKLYKPDMTLEEAV 155


                  ....*.
gi 2173728245 158 ESAIHI 163
Cdd:cd01901   156 ELALKA 161
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-76 9.15e-06

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: 43.97  E-value: 9.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGeKVIMKGTAHKIRRIyNNQVVVGFAGSVADAFNLEEKFEGQLNEYS 76
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAG-SLVASRNFDKIFKI-SDNILLGTAGSAADTQALTRLLKRNLRLYE 67
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 7-136 1.63e-05

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 43.60  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   7 ATTICAVRHNGHNAMAGDGQVTMGeKVIMKGTAHKIRRIYNNqVVVGFAGSVADAFNLEE--KFEGQLNEYSgNLQRAAV 84
Cdd:COG0638    35 GTTTVGIKTKDGVVLAADRRATMG-NLIASKSIEKIFKIDDH-IGVAIAGLVADARELVRlaRVEAQLYELR-YGEPISV 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173728245  85 E-LAK------QWRSDQALQKLEALLIV--MDKDEMLLVS--GSGEVIapDDDILAIGSGGNF 136
Cdd:COG0638   112 EgLAKllsdllQGYTQYGVRPFGVALLIggVDDGGPRLFStdPSGGLY--EEKAVAIGSGSPF 172
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-136 9.27e-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: 38.36  E-value: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   8 TTICAVRHNGHNAMAGDGQVTMGEKVIMKgTAHKIRRIYNNqVVVGFAGSVADAFNLEEKFEGQLNEYSGNLQR-----A 82
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANR-VTDKLTQLHDR-IYCCRSGSAADTQAIADYVRYYLDMHSIELGEpplvkT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173728245  83 AVELAK----QWRSDqalqkLEALLIVMDKDEML-----LVSGSGEVIapDDDILAIGSGGNF 136
Cdd:cd03762    79 AASLFKnlcyNYKEM-----LSAGIIVAGWDEQNggqvySIPLGGMLI--RQPFAIGGSGSTY 134
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 6-136 3.19e-03

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: 36.99  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173728245   6 EATTICAVRHNGHNAMAGDGQVTMGEKVimkgTAHKIRRIY--NNQVVVGFAGSVADA------FNLE----EKFEGQLN 73
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMI----ASRDVEKVYptDEYSAVGIAGTAGLAielvrlFQVElehyEKIEGVPL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2173728245  74 EYSGNLQRaaveLAKQWRSD--QALQKLEALLIVMDKDemlLVSGSGEVIAPD--------DDILAIGSGGNF 136
Cdd:TIGR03690  77 TLDGKANR----LAAMVRGNlpAAMQGLAVVPLLAGYD---LDAGAGRIFSYDvtggryeeRGYHAVGSGSVF 142
 
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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