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Conserved domains on  [gi|2043688461|pdb|6ZOU|L]
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Chain L, Proteasome subunit beta type-6

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-222 3.10e-109

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: 312.27  E-value: 3.10e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        2 FNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNd 81
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       82 KKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYE 161
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6ZOU_L      162 pgtngkvkKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD 222
Cdd:cd03757 160 --------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-222 3.10e-109

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: 312.27  E-value: 3.10e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        2 FNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNd 81
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       82 KKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYE 161
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6ZOU_L      162 pgtngkvkKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD 222
Cdd:cd03757 160 --------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-207 1.23e-44

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: 147.33  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L          7 DNGGTILGIAGEDFAVLAGDTRNITDYSINSRYE-PKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDK--- 82
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPipv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L         83 KLSiNSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEP 162
Cdd:pfam00227  82 ELA-ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE------KLYRP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
6ZOU_L        163 GtngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIV 207
Cdd:pfam00227 155 D-----------LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-218 5.05e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.70  E-value: 5.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHnDKKLSINS 88
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRY-GEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       89 AARNIQHLLYG---KRFFPYYVHTIIAGLDEDGkGAVYSFDPVGSYEREQCRAGGAAASLIMPFLdnqvnfKNQYEPGtn 165
Cdd:COG0638 114 LAKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVL------EKEYRED-- 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
6ZOU_L      166 gkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYE 218
Cdd:COG0638 185 ---------LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
9-222 6.78e-07

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 48.29  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L         9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEpKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHnDKKLSINS 88
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITSPLIEPSSIE-KIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTY-GEPIGVET 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        89 AARNI-----QHLLY-GKRffPYYVHTIIAGLDeDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNqvNFKNQyep 162
Cdd:PRK03996 114 LTKKIcdhkqQYTQHgGVR--PFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEK--NYKED--- 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       163 gtngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVgDGLEILIVTKDGvrKEFYELKRD 222
Cdd:PRK03996 186 ------------LSLEEAIELALKALAKANEGKLDP-ENVEIAYIDVET--KKFRKLSVE 230
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-222 3.10e-109

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: 312.27  E-value: 3.10e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        2 FNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNd 81
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       82 KKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYE 161
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
6ZOU_L      162 pgtngkvkKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD 222
Cdd:cd03757 160 --------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-216 8.77e-58

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: 180.72  E-value: 8.77e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       10 GTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSA 89
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNG-RELSVKAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       90 ARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEPGtngkvk 169
Cdd:cd01912  80 ANLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILD------RGYKPD------ 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
6ZOU_L      170 kplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEF 216
Cdd:cd01912 148 -----MTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-207 1.23e-44

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: 147.33  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L          7 DNGGTILGIAGEDFAVLAGDTRNITDYSINSRYE-PKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDK--- 82
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPipv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L         83 KLSiNSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEP 162
Cdd:pfam00227  82 ELA-ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE------KLYRP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
6ZOU_L        163 GtngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIV 207
Cdd:pfam00227 155 D-----------LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 10-207 1.30e-42

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: 141.86  E-value: 1.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       10 GTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSA 89
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYG-EPIPVEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       90 ARNIQHLLYGKRF--FPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEPGtngk 167
Cdd:cd01906  80 AKLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILE------KLYKPD---- 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
6ZOU_L      168 vkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIV 207
Cdd:cd01906 150 -------MTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 9-218 5.05e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.70  E-value: 5.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHnDKKLSINS 88
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRY-GEPISVEG 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       89 AARNIQHLLYG---KRFFPYYVHTIIAGLDEDGkGAVYSFDPVGSYEREQCRAGGAAASLIMPFLdnqvnfKNQYEPGtn 165
Cdd:COG0638 114 LAKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVL------EKEYRED-- 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
6ZOU_L      166 gkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYE 218
Cdd:COG0638 185 ---------LSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEE 228
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-216 8.34e-31

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: 111.96  E-value: 8.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       11 TILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSAA 90
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRG-RPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       91 RNIQHLLYGKRFFPYYVHTIIAGLDEDGkGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEPGtngkvkk 170
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE------DEYKED------- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
6ZOU_L      171 plkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEF 216
Cdd:cd03764 147 ----MTVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKELE 188
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-212 2.12e-23

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: 92.69  E-value: 2.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        8 NGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSIN 87
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREE-REIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       88 SAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVG--SYEREQCRAGGAAASLiMPFLDnqvnfkNQYEPGtn 165
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcpSIPSDFVVSGTASEQL-YGMCE------SLWRPD-- 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
6ZOU_L      166 gkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGV 212
Cdd:cd03759 152 ---------MEPDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 10-190 9.02e-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: 90.15  E-value: 9.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       10 GTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSA 89
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYG-EPISVVAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       90 ARNIQHLLYGKRF-FPYYVHTIIAGLDEDGkGAVYSFDPVGSY-EREQCRAGGAAASLIMPFLDNQVNFKnqyepgtngk 167
Cdd:cd01901  80 AKELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPViENPGAVATGSRSQRAKSLLEKLYKPD---------- 148

                       170       180
                ....*....|....*....|...
6ZOU_L      168 vkkplkyLSVEEVIKLVRDSFTS 190
Cdd:cd01901 149 -------MTLEEAVELALKALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-216 2.26e-16

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: 73.80  E-value: 2.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       11 TILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKKLsINSAA 90
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPL-VKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       91 RNIQHLLYGKRFFpYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEPGtngkvkk 170
Cdd:cd03762  81 SLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVD------ANYKPG------- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
6ZOU_L      171 plkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEF 216
Cdd:cd03762 147 ----MTLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-214 1.27e-13

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: 66.84  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       11 TILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSAA 90
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNG-YELSPKAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       91 RNIQHLL--YGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYEPGtngkv 168
Cdd:cd03758  82 NFTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILD------RYYKPD----- 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
6ZOU_L      169 kkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRK 214
Cdd:cd03758 151 ------MTVEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRD 190
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-184 2.15e-13

proteasome alpha 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 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 66.31  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        7 DNGGTILGIAGEDFAVLAGDtRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKkLSI 86
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVE-KKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEP-IPV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       87 NSAARNI--------QHllYGKRffPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNfkn 158
Cdd:cd01911 103 EVLVKRIadlaqvytQY--GGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYK--- 175

                       170       180
                ....*....|....*....|....*.
6ZOU_L      159 qyepgtngkvkkplKYLSVEEVIKLV 184
Cdd:cd01911 176 --------------KDLTLEEAIKLA 187
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-158 3.45e-12

proteasome_alpha_type_1. 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: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 63.08  E-value: 3.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        7 DNGGTILGIAGEDFAVLAGDTRNITDYSinsRYEPKVFDCGDNIVMSANGFAADGDALVKRFKN---SVKW-YHFDHNDK 82
Cdd:cd03749  25 KQGSATVGLKSKTHAVLVALKRATSELS---SYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQeclNYRFvYDSPIPVS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       83 KLSI---NSAARNIQHllYGKRffPYYVHTIIAGLDEDGKgAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQV-NFKN 158
Cdd:cd03749 102 RLVSkvaEKAQINTQR--YGRR--PYGVGLLIAGYDESGP-HLFQTCPSGNYFEYKATSIGARSQSARTYLERHFeEFED 176
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-208 8.94e-09

proteasome_alpha_archeal. 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: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 53.49  E-value: 8.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEpKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHnDKKLSINS 88
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKRITSKLVEPESIE-KIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTY-GEPIDVEV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       89 AARNI-----QHLLYGK-RffPYYVHTIIAGLDEDGKgAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKnqyep 162
Cdd:cd03756 106 LVKKIcdlkqQYTQHGGvR--PFGVALLIAGVDDGGP-RLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKED----- 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
6ZOU_L      163 gtngkvkkplkyLSVEEVIKLVRDSFTSATERhIQVGDGLEILIVT 208
Cdd:cd03756 178 ------------MSLEEAIELALKALYAALEE-NETPENVEIAYVT 210
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 9-213 2.79e-08

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: 51.80  E-value: 2.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRniTDYSINSRYE--PKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKKLSI 86
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTL--GSYGSLARFKnvERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       87 NSAARNIQHLLYGKR--FFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLdnqvnfKNQYEPGT 164
Cdd:cd03760  80 KEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLL------REAWEKKP 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
6ZOU_L      165 NgkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVR 213
Cdd:cd03760 154 D---------LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-151 4.36e-08

proteasome_alpha_type_7. 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: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 51.60  E-value: 4.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRNITDYSiNSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKkLSINS 88
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVAKLQ-DPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDP-VTVEY 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6ZOU_L       89 AARNIQHLLY------GKRffPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLD 151
Cdd:cd03755 105 ITRYIAGLQQrytqsgGVR--PFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLE 171
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-131 1.04e-07

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 50.36  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        7 DNGGTILGIAGEDFAVLAGDtRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFK----NSVKWYHFDHNDK 82
Cdd:cd03751  28 ENSGTAIGIRCKDGVVLAVE-KLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRHLVSRAReeaeNYRDNYGTPIPVK 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
6ZOU_L       83 KLSiNSAARNIQ-HLLYGK-RffPYYVHTIIAGLDEDGkGAVYSFDPVGSY 131
Cdd:cd03751 107 VLA-DRVAMYMHaYTLYSSvR--PFGCSVLLGGYDSDG-PQLYMIEPSGVS 153
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
9-222 6.78e-07

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 48.29  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L         9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEpKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHnDKKLSINS 88
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITSPLIEPSSIE-KIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTY-GEPIGVET 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        89 AARNI-----QHLLY-GKRffPYYVHTIIAGLDeDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNqvNFKNQyep 162
Cdd:PRK03996 114 LTKKIcdhkqQYTQHgGVR--PFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEK--NYKED--- 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       163 gtngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVgDGLEILIVTKDGvrKEFYELKRD 222
Cdd:PRK03996 186 ------------LSLEEAIELALKALAKANEGKLDP-ENVEIAYIDVET--KKFRKLSVE 230
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-207 4.24e-06

proteasome_alpha_type_6. 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: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 46.07  E-value: 4.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDtRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDhNDKKLSINS 88
Cdd:cd03754  29 GLTSVAVRGKDCAVVVTQ-KKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYK-YGYEMPVDV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       89 AARNIQHL--LYGKRFF--PYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQvnFKnqyepgt 164
Cdd:cd03754 107 LAKRIADInqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAAGVKEQEATNFLEKK--LK------- 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
6ZOU_L      165 ngkvKKPLKYLSVEEVIKLVRDSFTSATERHIQvGDGLEILIV 207
Cdd:cd03754 178 ----KKPDLIESYEETVELAISCLQTVLSTDFK-ATEIEVGVV 215
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-143 2.99e-05

proteasome_alpha_type_5. 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: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 43.48  E-value: 2.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        9 GGTILGIAGEDFAVLAGDTRNITDYSINSRYEpKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKkLSINS 88
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSVE-KIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEP-MTVES 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
6ZOU_L       89 AARNIQHLL--YGKRFF-------PYYVHTIIAGLDEDGKgAVYSFDPVGSYEREQCRAGGAAA 143
Cdd:cd03753 105 VTQAVSDLAlqFGEGDDgkkamsrPFGVALLIAGVDENGP-QLFHTDPSGTFTRCDAKAIGSGS 167
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-207 4.29e-05

proteasome_alpha_type_4. 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: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 43.10  E-value: 4.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        8 NGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDkKLSIN 87
Cdd:cd03752  28 HAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQE-PIPVE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       88 SAARNI--------QHllYGKRffPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGG----AAASLImpfldnqvn 155
Cdd:cd03752 107 QLVQRLcdikqgytQY--GGLR--PFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGnnnqAAQSLL--------- 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
6ZOU_L      156 fKNQYEPGtngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIV 207
Cdd:cd03752 174 -KQDYKDD-----------MTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-212 5.98e-05

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


Pssm-ID: 239732  Cd Length: 189  Bit Score: 42.18  E-value: 5.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       11 TILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNdKKLSINSAA 90
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTG-RKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L       91 RNIQHLLygkrfFPYYVHT----IIAGLDEDGKgAVYSFDPVGSYEREQCRA--GGAAASLIMpfldnqvnFKNQYEPGt 164
Cdd:cd03763  81 TMLKQHL-----FRYQGHIgaalVLGGVDYTGP-HLYSIYPHGSTDKLPFVTmgSGSLAAMSV--------LEDRYKPD- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
6ZOU_L      165 ngkvkkplkyLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGV 212
Cdd:cd03763 146 ----------MTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGV 183
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-155 6.91e-03

proteasome_alpha_type_2. 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: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 36.53  E-value: 6.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZOU_L        7 DNGGTILGIAGEDFAVLAGDTRnITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDkKLSI 86
Cdd:cd03750  25 SSGAPSVGIKAANGVVLATEKK-VPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGE-PIPV 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6ZOU_L       87 NSAARNIQHLLY------GKRffPYYVHTIIAGLDEDGKgAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVN 155
Cdd:cd03750 103 SQLVREIASVMQeytqsgGVR--PFGVSLLIAGWDEGGP-YLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYN 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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