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Conserved domains on  [gi|488286281|ref|WP_002357489|]
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MULTISPECIES: HslVU peptidase proteolytic subunit [Enterococcus]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
8-182 1.42e-115

ATP-dependent protease subunit HslV;


:

Pssm-ID: 235477  Cd Length: 172  Bit Score: 325.08  E-value: 1.42e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   8 STTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVEL 87
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  88 AQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFGDkeMPAKEIAKNALNIAA 167
Cdd:PRK05456  80 AKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTD--LSAEEIAEKALKIAA 157
                        170
                 ....*....|....*
gi 488286281 168 DICVFTNHNIIVEEL 182
Cdd:PRK05456 158 DICIYTNHNITIEEL 172
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
8-182 1.42e-115

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 325.08  E-value: 1.42e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   8 STTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVEL 87
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  88 AQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFGDkeMPAKEIAKNALNIAA 167
Cdd:PRK05456  80 AKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTD--LSAEEIAEKALKIAA 157
                        170
                 ....*....|....*
gi 488286281 168 DICVFTNHNIIVEEL 182
Cdd:PRK05456 158 DICIYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
6-182 2.45e-114

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 322.00  E-value: 2.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   6 FHSTTICAVEKDGKFAMAGDGQVTMGeSVVMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAV 85
Cdd:COG5405    1 FHGTTILAVRKGGKVAIAGDGQVTLG-NTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  86 ELAQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFgdKEMPAKEIAKNALNI 165
Cdd:COG5405   80 ELAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDH--TDLDAEEIAREALEI 157
                        170
                 ....*....|....*..
gi 488286281 166 AADICVFTNHNIIVEEL 182
Cdd:COG5405  158 AADICIYTNHNITVEEL 174
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
9-182 3.61e-113

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: 318.71  E-value: 3.61e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281    9 TTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVELA 88
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   89 QEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNfgDKEMPAKEIAKNALNIAAD 168
Cdd:TIGR03692  80 KDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLR--NTDLSAEEIAREALKIAAD 157
                         170
                  ....*....|....
gi 488286281  169 ICVFTNHNIIVEEL 182
Cdd:TIGR03692 158 ICIYTNHNITVEEL 171
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
9-182 8.29e-105

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: 297.95  E-value: 8.29e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVELA 88
Cdd:cd01913    1 TTILAVRKNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  89 QEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFgdKEMPAKEIAKNALNIAAD 168
Cdd:cd01913   80 KDWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDH--TDLSAEEIARKALKIAAD 157
                        170
                 ....*....|....
gi 488286281 169 ICVFTNHNIIVEEL 182
Cdd:cd01913  158 ICIYTNHNITVEEL 171
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
6-182 4.09e-32

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: 113.82  E-value: 4.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281    6 FHSTTICAVEKDGKFAMAGDGQVTMGESVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY----NGNLT 81
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKI-DDHIGMAFAGLAADARTLVDRARAEAQLYrlryGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   82 ---------RAAVELAQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDdgILAIGSGGNFALSAARAMKNFGDKE 152
Cdd:pfam00227  81 velaariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK--ATAIGSGSQYAYGVLEKLYRPDLTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 488286281  153 MPAKEIAKNALNIAADICVFTNHNIIVEEL 182
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
 
Name Accession Description Interval E-value
PRK05456 PRK05456
ATP-dependent protease subunit HslV;
8-182 1.42e-115

ATP-dependent protease subunit HslV;


Pssm-ID: 235477  Cd Length: 172  Bit Score: 325.08  E-value: 1.42e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   8 STTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVEL 87
Cdd:PRK05456   1 GTTILAVRRNGKVAIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEHQGNLLRAAVEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  88 AQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFGDkeMPAKEIAKNALNIAA 167
Cdd:PRK05456  80 AKDWRTDRYLRRLEAMLIVADKEHSLIISGNGDVIEPEDGIIAIGSGGNYALAAARALLENTD--LSAEEIAEKALKIAA 157
                        170
                 ....*....|....*
gi 488286281 168 DICVFTNHNIIVEEL 182
Cdd:PRK05456 158 DICIYTNHNITIEEL 172
HslV COG5405
ATP-dependent protease HslVU (ClpYQ), peptidase subunit [Posttranslational modification, ...
6-182 2.45e-114

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


Pssm-ID: 444164  Cd Length: 174  Bit Score: 322.00  E-value: 2.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   6 FHSTTICAVEKDGKFAMAGDGQVTMGeSVVMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAV 85
Cdd:COG5405    1 FHGTTILAVRKGGKVAIAGDGQVTLG-NTVMKHNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYSGNLTRAAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  86 ELAQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFgdKEMPAKEIAKNALNI 165
Cdd:COG5405   80 ELAKDWRTDRYLRRLEAMLIVADKEHILLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDH--TDLDAEEIAREALEI 157
                        170
                 ....*....|....*..
gi 488286281 166 AADICVFTNHNIIVEEL 182
Cdd:COG5405  158 AADICIYTNHNITVEEL 174
ATP_dep_HslV TIGR03692
ATP-dependent protease HslVU, peptidase subunit; The ATP-dependent protease HslVU, a complex ...
9-182 3.61e-113

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: 318.71  E-value: 3.61e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281    9 TTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVELA 88
Cdd:TIGR03692   1 TTILAVRRNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVLAGFAGSTADAFTLFERFEAKLEEYQGNLTRAAVELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   89 QEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNfgDKEMPAKEIAKNALNIAAD 168
Cdd:TIGR03692  80 KDWRTDRYLRRLEAMLIVADKETSLLISGTGDVIEPDDGIAAIGSGGNYALAAARALLR--NTDLSAEEIAREALKIAAD 157
                         170
                  ....*....|....
gi 488286281  169 ICVFTNHNIIVEEL 182
Cdd:TIGR03692 158 ICIYTNHNITVEEL 171
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
9-182 8.29e-105

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: 297.95  E-value: 8.29e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGESVvMKGTAKKVRRIYNDEVVVGFAGSVADAFTLEEKFEGKLNEYNGNLTRAAVELA 88
Cdd:cd01913    1 TTILAVRKNGKVVIAGDGQVTLGNTV-MKGNARKVRRLYNGKVIAGFAGSTADAFTLFERFEAKLEQYPGNLLRAAVELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  89 QEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDDGILAIGSGGNFALSAARAMKNFgdKEMPAKEIAKNALNIAAD 168
Cdd:cd01913   80 KDWRTDRYLRRLEAMLIVADKEHTLLISGNGDVIEPDDGIAAIGSGGNYALAAARALLDH--TDLSAEEIARKALKIAAD 157
                        170
                 ....*....|....
gi 488286281 169 ICVFTNHNIIVEEL 182
Cdd:cd01913  158 ICIYTNHNITVEEL 171
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
9-180 9.02e-35

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: 120.29  E-value: 9.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGeSVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY------NGNLTR 82
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSG-LLVASSTVEKIFKI-DDHIGCAFAGLAADAQTLVERLRKEAQLYrlrygePIPVEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  83 AAVELAQEWRT-QQSMQKLEAMLIVM-----NKEEMLLVSGTGEVITPDdgILAIGSGGNFALSAARAMKNFGDKEMPAK 156
Cdd:cd01906   79 LAKLLANLLYEyTQSLRPLGVSLLVAgvdeeGGPQLYSVDPSGSYIEYK--ATAIGSGSQYALGILEKLYKPDMTLEEAI 156
                        170       180
                 ....*....|....*....|....
gi 488286281 157 EIAKNALNIAADICVFTNHNIIVE 180
Cdd:cd01906  157 ELALKALKSALERDLYSGGNIEVA 180
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
6-182 4.09e-32

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: 113.82  E-value: 4.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281    6 FHSTTICAVEKDGKFAMAGDGQVTMGESVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY----NGNLT 81
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKI-DDHIGMAFAGLAADARTLVDRARAEAQLYrlryGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   82 ---------RAAVELAQEWRTQQSMQKLEAMLIVMNKEEMLLVSGTGEVITPDdgILAIGSGGNFALSAARAMKNFGDKE 152
Cdd:pfam00227  81 velaariadLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK--ATAIGSGSQYAYGVLEKLYRPDLTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 488286281  153 MPAKEIAKNALNIAADICVFTNHNIIVEEL 182
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
9-165 2.10e-19

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: 80.13  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGeSVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY------NGNLTR 82
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSG-LPVAGSPVIKIGKN-EDGIAWGLAGLAADAQTLVRRLREALQLYrlrygePISVVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  83 AAVELAQEWRTQQSMQKLEAMLIVMNKEEM----LLVSGTGEVITPDDGIlAIGSGGNFALSAARAMKNFGDKEMPAKEI 158
Cdd:cd01901   79 LAKELAKLLQVYTQGRPFGVNLIVAGVDEGggnlYYIDPSGPVIENPGAV-ATGSRSQRAKSLLEKLYKPDMTLEEAVEL 157

                 ....*..
gi 488286281 159 AKNALNI 165
Cdd:cd01901  158 ALKALKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
7-168 2.04e-07

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 48.99  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   7 HSTTICAVE-KDGkFAMAGDGQVTMGeSVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEE--KFEGKLNE--YNGNL- 80
Cdd:COG0638   34 RGTTTVGIKtKDG-VVLAADRRATMG-NLIASKSIEKIFKI-DDHIGVAIAGLVADARELVRlaRVEAQLYElrYGEPIs 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281  81 -----TRAAVELAQewRTQQSMQKLEAMLIV--MNKEEMLLVS--GTGEVItpDDGILAIGSGGNFALSAARamKNFgDK 151
Cdd:COG0638  111 veglaKLLSDLLQG--YTQYGVRPFGVALLIggVDDGGPRLFStdPSGGLY--EEKAVAIGSGSPFARGVLE--KEY-RE 183
                        170       180
                 ....*....|....*....|
gi 488286281 152 EMP---AKEIAKNALNIAAD 168
Cdd:COG0638  184 DLSldeAVELALRALYSAAE 203
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
9-76 1.45e-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: 46.28  E-value: 1.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGeSVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY 76
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAG-SLVASRNFDKIFKI-SDNILLGTAGSAADTQALTRLLKRNLRLY 66
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
7-168 2.21e-06

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: 46.24  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281    7 HSTTICAVEKDGKFAMAGDGQVTMGESVvmkgTAKKVRRIY--NDEVVVGFAGSVADA------FTLE----EKFEGKLN 74
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMI----ASRDVEKVYptDEYSAVGIAGTAGLAielvrlFQVElehyEKIEGVPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   75 EYNGNLTRAAVELAQEwrTQQSMQKLEAMLIVMNKEemlLVSGTGEVITPD--------DGILAIGSGGNFALSAARAMK 146
Cdd:TIGR03690  77 TLDGKANRLAAMVRGN--LPAAMQGLAVVPLLAGYD---LDAGAGRIFSYDvtggryeeRGYHAVGSGSVFAKGALKKLY 151
                         170       180
                  ....*....|....*....|..
gi 488286281  147 NFGDKEMPAKEIAKNALNIAAD 168
Cdd:TIGR03690 152 SPDLDEDDALRVAVEALYDAAD 173
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
9-90 1.14e-03

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: 37.97  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286281   9 TTICAVEKDGKFAMAGDGQVTMGESVVMKgTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEYN-----GNLTRA 83
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANR-VTDKLTQL-HDRIYCCRSGSAADTQAIADYVRYYLDMHSielgePPLVKT 78

                 ....*..
gi 488286281  84 AVELAQE 90
Cdd:cd03762   79 AASLFKN 85
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
9-76 4.54e-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: 36.46  E-value: 4.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488286281   9 TTICAVEKDGkFAMAGDGQVTMGeSVVMKGTAKKVRRIyNDEVVVGFAGSVADAFTLEEKFEGKLNEY 76
Cdd:cd03764    2 TTVGIVCKDG-VVLAADKRASMG-NFIASKNVKKIFQI-DDKIAMTIAGSVGDAQSLVRILKAEARLY 66
 
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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