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Conserved domains on  [gi|349577967|dbj|GAA23134|]
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K7_Pre4p [Saccharomyces cerevisiae Kyokai no. 7]

Protein Classification

proteasome subunit beta( domain architecture ID 10132923)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-236 2.54e-93

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


:

Pssm-ID: 239729  Cd Length: 197  Bit Score: 273.29  E-value: 2.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVT-ENAYDNPladaeE 118
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIdDECLDDG-----H 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 119 ALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDI 198
Cdd:cd03760   76 SLSPKEIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDL 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 349577967 199 pktTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd03760  156 ---TEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-236 2.54e-93

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 273.29  E-value: 2.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVT-ENAYDNPladaeE 118
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIdDECLDDG-----H 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 119 ALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDI 198
Cdd:cd03760   76 SLSPKEIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDL 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 349577967 199 pktTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd03760  156 ---TEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-233 8.80e-25

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: 97.25  E-value: 8.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967   38 IVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNG-VERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNplada 116
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRY----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  117 EEALEPSyIFEYLAT---VMYQRRSKMNPLWNaIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVD 193
Cdd:pfam00227  76 GRPIPVE-LAARIADllqAYTQYSGRRPFGVS-LLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 349577967  194 resdiPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAII 233
Cdd:pfam00227 154 -----PDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 40-237 1.55e-09

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 56.69  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL--EDLVTENAYDNPLAdae 117
Cdd:COG0638   34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLArvEAQLYELRYGEPIS--- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 118 ealepsyiFEYLAT----VMYQR-RSKMNPLWNAIIVAGVQSNGDQfLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVV 192
Cdd:COG0638  111 --------VEGLAKllsdLLQGYtQYGVRPFGVALLIGGVDDGGPR-LFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEY 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 349577967 193 DRESDIpKTTVQVAEEAIVNAMRvlyyRDARSSRNFSLAIIDKNT 237
Cdd:COG0638  182 REDLSL-DEAVELALRALYSAAE----RDSASGDGIDVAVITEDG 221
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-236 2.54e-93

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 273.29  E-value: 2.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVT-ENAYDNPladaeE 118
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIdDECLDDG-----H 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 119 ALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDI 198
Cdd:cd03760   76 SLSPKEIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDL 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 349577967 199 pktTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd03760  156 ---TEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 42-236 1.61e-49

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: 161.46  E-value: 1.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNpladaEEALE 121
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRN-----GRELS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 122 PSYIFEYLATVMYQRRSkmNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDresdiPKT 201
Cdd:cd01912   76 VKAAANLLSNILYSYRG--FPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYK-----PDM 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 349577967 202 TVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd01912  149 TLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKD 183
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 42-233 6.21e-40

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: 136.47  E-value: 6.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNpladaEEALE 121
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRY-----GEPIP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 122 PSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDresdiPKT 201
Cdd:cd01906   76 VEALAKLLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYK-----PDM 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 349577967 202 TVQVAEEAIVNAMRVLYYRDARSSRNFSLAII 233
Cdd:cd01906  151 TLEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-233 8.80e-25

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: 97.25  E-value: 8.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967   38 IVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNG-VERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNplada 116
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRY----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  117 EEALEPSyIFEYLAT---VMYQRRSKMNPLWNaIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVD 193
Cdd:pfam00227  76 GRPIPVE-LAARIADllqAYTQYSGRRPFGVS-LLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 349577967  194 resdiPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAII 233
Cdd:pfam00227 154 -----PDLTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 42-215 7.28e-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: 80.90  E-value: 7.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNpladaEEALE 121
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRY-----GEPIS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 122 PSYIFEYLATVMYQRRSkMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDresdiPKT 201
Cdd:cd01901   76 VVALAKELAKLLQVYTQ-GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYK-----PDM 149

                        170
                 ....*....|....
gi 349577967 202 TVQVAEEAIVNAMR 215
Cdd:cd01901  150 TLEEAVELALKALK 163
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 40-237 1.55e-09

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 56.69  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL--EDLVTENAYDNPLAdae 117
Cdd:COG0638   34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLArvEAQLYELRYGEPIS--- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 118 ealepsyiFEYLAT----VMYQR-RSKMNPLWNAIIVAGVQSNGDQfLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVV 192
Cdd:COG0638  111 --------VEGLAKllsdLLQGYtQYGVRPFGVALLIGGVDDGGPR-LFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEY 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 349577967 193 DRESDIpKTTVQVAEEAIVNAMRvlyyRDARSSRNFSLAIIDKNT 237
Cdd:COG0638  182 REDLSL-DEAVELALRALYSAAE----RDSASGDGIDVAVITEDG 221
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-236 1.95e-09

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: 55.72  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLEdlVTENAYDnplADAEEALE 121
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILK--AEARLYE---LRRGRPMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 122 PSYIFEYLATVMYQrrSKMNPLWNAIIVAGVQSNGDQfLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDIpKT 201
Cdd:cd03764   76 IKALATLLSNILNS--SKYFPYIVQLLIGGVDEEGPH-LYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTV-EE 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 349577967 202 TVQVAEEAIVNAMRvlyyRDARSSRNFSLAIIDKN 236
Cdd:cd03764  152 AKKLAIRAIKSAIE----RDSASGDGIDVVVITKD 182
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-236 2.03e-08

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 53.02  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  40 TGTSVISMKYDNGVIIAADN-LGSYGSLLRFNgVERLIPVGDNTVVGISGDISDMQHIERLLEDLVteNAYDnplADAEE 118
Cdd:cd03759    2 NGGAVVAMAGKDCVAIASDLrLGVQQQTVSTD-FQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRV--NLYR---LREER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 119 ALEPSYIFEYLATVMYQRRskMNPLWNAIIVAGVQSNGDQFLRYVNLLG-VTYSSPTLATGFGAH----MANPLLRKVVD 193
Cdd:cd03759   76 EIKPKTFSSLISSLLYEKR--FGPYFVEPVVAGLDPDGKPFICTMDLIGcPSIPSDFVVSGTASEqlygMCESLWRPDME 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 349577967 194 resdiPKTTVQVAEEAIVNAMRvlyyRDARSSRNFSLAIIDKN 236
Cdd:cd03759  154 -----PDELFETISQALLSAVD----RDALSGWGAVVYIITKD 187
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-236 2.32e-05

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


Pssm-ID: 239727  Cd Length: 193  Bit Score: 44.11  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  43 SVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQH----IERLLEDLVTENAYD-NPLADAe 117
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQfaeyIQKNIQLYKMRNGYElSPKAAA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 118 ealepSYIFEYLATvmYQRRSKmnPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLrkvvDRESD 197
Cdd:cd03758   82 -----NFTRRELAE--SLRSRT--PYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSIL----DRYYK 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 349577967 198 iPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd03758  149 -PDMTVEEALELMKKCIKELKKRFIINLPNFTVKVVDKD 186
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 41-236 4.11e-05

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 43.40  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  41 GTSVISMKYDNGVIIAADN--LGSYGSLLRFNgvERLIPVGDNTVVGISGDISDMQHIERLLEDLVTENAYDNPLADAEE 118
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTrlSEGYSILSRDS--PKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 119 AlepsyIFEYLATVMYQRRSkmNPLWNAIIVAGVQSNGDQFLRYVNLLG----VTYSsptlATGFGAHMANPLLRKVVDR 194
Cdd:cd03757   86 A-----IAQLLSTILYSRRF--FPYYVFNILAGIDEEGKGVVYSYDPVGsyerETYS----AGGSASSLIQPLLDNQVGR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 349577967 195 ES----DIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKN 236
Cdd:cd03757  155 KNqnnvERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKD 200
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-96 4.50e-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: 42.98  E-value: 4.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHI 96
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAI 55
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-236 7.49e-04

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 39.54  E-value: 7.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967  42 TSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLL--EDLVTENAYDNPLADAEEA 119
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLgrECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577967 120 lepsyifEYLATVMYQRRSkMNpLWNAIIVAGVQSNGDQfLRYVNLLGVTYSSPTLATGFGahmaNPLLRKVVDRESDIP 199
Cdd:cd03761   81 -------KLLSNMLYQYKG-MG-LSMGTMICGWDKTGPG-LYYVDSDGTRLKGDLFSVGSG----STYAYGVLDSGYRYD 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 349577967 200 KTTvqvaEEAIVNAMRVLY---YRDARSSRNFSLAIIDKN 236
Cdd:cd03761  147 LSV----EEAYDLARRAIYhatHRDAYSGGNVNLYHVRED 182
 
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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