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Conserved domains on  [gi|17562788|ref|NP_506571|]
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Proteasome subunit alpha type-6 [Caenorhabditis elegans]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132899)

proteasome subunit alpha is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-6 (PSMA6) and Saccharomyces cerevisiae proteasome subunit alpha type-1 (Slc1p)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 6.06e-130

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: 365.79  E-value: 6.06e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   8 GFDRHITIFSPEGRVYQVEYAFKAINSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDA 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  88 KFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17562788 168 VGVKQLPATSFLEKKIKKKSE--LTSTEAIELAIEALQTSLGIDVRSKDLEVVVV 220
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
 
Name Accession Description Interval E-value
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 6.06e-130

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: 365.79  E-value: 6.06e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   8 GFDRHITIFSPEGRVYQVEYAFKAINSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDA 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  88 KFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17562788 168 VGVKQLPATSFLEKKIKKKSE--LTSTEAIELAIEALQTSLGIDVRSKDLEVVVV 220
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-242 1.56e-58

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 185.42  E-value: 1.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788    6 SAGFDRHITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIP 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   86 DAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDeKGPEVYRVDPAGYYRGMKG 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562788  166 VSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKDLEVVVVTKDNSKFTKLTSDQVEHHLNQI 242
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKL 239
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-220 2.76e-49

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: 160.04  E-value: 2.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788    38 TAVAVKGADAAVIAVQKRVP--DSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELlA 115
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVEL-A 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   116 KKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKkiKKKSELTSTEAI 195
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 17562788   196 ELAIEALQTSLGIDVRS-KDLEVVVV 220
Cdd:pfam00227 163 ELAVKALKEAIDRDALSgGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 2.59e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 153.76  E-value: 2.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   1 MSRGSSAGFDRHITIFSPEGRVYQVEYAFKAInSTNLTAVAVKGADAAVIAVQKRVPDS-LIVADTVTSVYQISQSVGCC 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAV-KRGTTTVGIKTKDGVVLAADRRATMGnLIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  80 AIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAeMRSLGCALLFISYDDEkGPEVYRVDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562788 160 YRGMKGVSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKD-LEVVVVTKDnsKFTKLTSDQ 234
Cdd:COG0638 158 LYEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRALYSAAERDSASGDgIDVAVITED--GFRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 9-31 3.35e-10

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 53.65  E-value: 3.35e-10
                           10        20
                   ....*....|....*....|...
gi 17562788      9 FDRHITIFSPEGRVYQVEYAFKA 31
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 6.06e-130

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: 365.79  E-value: 6.06e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   8 GFDRHITIFSPEGRVYQVEYAFKAINSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDA 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  88 KFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17562788 168 VGVKQLPATSFLEKKIKKKSE--LTSTEAIELAIEALQTSLGIDVRSKDLEVVVV 220
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 2.11e-100

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: 290.88  E-value: 2.11e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   9 FDRHITIFSPEGRVYQVEYAFKAINSTnLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAK 88
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNG-STAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  89 FQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSV 168
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17562788 169 GVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKDLEVVVV 220
Cdd:cd01911 160 GKGSQEAKTFLEKRYKK--DLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-242 1.56e-58

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 185.42  E-value: 1.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788    6 SAGFDRHITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIP 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   86 DAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDeKGPEVYRVDPAGYYRGMKG 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562788  166 VSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKDLEVVVVTKDNSKFTKLTSDQVEHHLNQI 242
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKL 239
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-221 2.86e-51

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: 165.97  E-value: 2.86e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   8 GFDRHITIFSPEGRVYQVEYAFKAINStNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDA 87
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKR-GTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  88 KFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDeKGPEVYRVDPAGYYRGMKGVS 167
Cdd:cd03756  80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYNEYKATA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17562788 168 VGVKQLPATSFLEKKIkkKSELTSTEAIELAIEALQTSLGIDVRSKDLEVVVVT 221
Cdd:cd03756 159 IGSGRQAVTEFLEKEY--KEDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 38-220 4.61e-51

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: 164.59  E-value: 4.61e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDSLIVAD-TVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAK 116
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVASsTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 117 KMADLNQYYTQnaEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKKseLTSTEAIE 196
Cdd:cd01906  82 LLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD--MTLEEAIE 157

                       170       180
                ....*....|....*....|....*
gi 17562788 197 LAIEALQTSLGIDVRS-KDLEVVVV 220
Cdd:cd01906 158 LALKALKSALERDLYSgGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-220 2.76e-49

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: 160.04  E-value: 2.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788    38 TAVAVKGADAAVIAVQKRVP--DSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELlA 115
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVEL-A 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   116 KKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKkiKKKSELTSTEAI 195
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 17562788   196 ELAIEALQTSLGIDVRS-KDLEVVVV 220
Cdd:pfam00227 163 ELAVKALKEAIDRDALSgGNIEVAVI 188
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-239 3.50e-48

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: 158.64  E-value: 3.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  13 ITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIK 92
Cdd:cd03750   5 LTTFSPSGKLVQIEYALAAVSSGA-PSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  93 RAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYdDEKGPEVYRVDPAGYYRGMKGVSVGVKQ 172
Cdd:cd03750  84 KARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGW-DEGGPYLYQVDPSGSYFTWKATAIGKNY 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562788 173 LPATSFLEKKIKKKSELtsTEAIELAIEALQTSLGIDVRSKDLEVVVVTKDNsKFTKLTSDQVEHHL 239
Cdd:cd03750 163 SNAKTFLEKRYNEDLEL--EDAIHTAILTLKEGFEGQMTEKNIEIGICGETK-GFRLLTPAEIKDYL 226
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 2.59e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 153.76  E-value: 2.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   1 MSRGSSAGFDRHITIFSPEGRVYQVEYAFKAInSTNLTAVAVKGADAAVIAVQKRVPDS-LIVADTVTSVYQISQSVGCC 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAV-KRGTTTVGIKTKDGVVLAADRRATMGnLIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  80 AIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAeMRSLGCALLFISYDDEkGPEVYRVDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562788 160 YRGMKGVSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKD-LEVVVVTKDnsKFTKLTSDQ 234
Cdd:COG0638 158 LYEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRALYSAAERDSASGDgIDVAVITED--GFRELSEEE 229
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-217 1.77e-44

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: 148.58  E-value: 1.77e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   7 AGFDRHITIFSPEGRVYQVEYAFKAI-NSTnlTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIP 85
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVeNSG--TAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  86 DAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEkGPEVYRVDPAGYYRGMKG 165
Cdd:cd03751  80 DGRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17562788 166 VSVGVKQLPATSFLEKkiKKKSELTSTEAIELAIEALQTSLGiDVRSKDLEV 217
Cdd:cd03751 159 CAIGKGKQAAKTELEK--LKFSELTCREAVKEAAKIIYIVHD-EIKDKAFEL 207
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-236 1.33e-42

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: 144.03  E-value: 1.33e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   9 FDRHITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLIvaDTVTS---VYQISQSVGCCAIGMIP 85
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILAKDGIVLAAEKKVTSKLL--DQSFSsekIYKIDDHIACAVAGITS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  86 DAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKG 165
Cdd:cd03752  80 DANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17562788 166 VSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALqtslgidvrSKDLEVvvvtkdnskfTKLTSDQVE 236
Cdd:cd03752 160 TAIGNNNQAAQSLLKQDYKD--DMTLEEALALAVKVL---------SKTMDS----------TKLTSEKLE 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 1.90e-37

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 131.90  E-value: 1.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788    1 MSRGssagFDRHITIFSPEGRVYQVEYAFKAINSTNLTaVAVKGADAAVIAVQKRVPDSLI-VADTVTSVYQISQSVGCC 79
Cdd:PTZ00246   1 MSRR----YDSRTTTFSPEGRLYQVEYALEAINNASLT-VGILCKEGVILGADKPISSKLLdPGKINEKIYKIDSHIFCA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   80 AIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGY 159
Cdd:PTZ00246  76 VAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  160 YRGMKGVSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKD-LEVVVVTKDNSKF----TKLTSDQ 234
Cdd:PTZ00246 156 YSGWKATAIGQNNQTAQSILKQEWKE--DLTLEQGLLLAAKVLTKSMDSTSPKADkIEVGILSHGETDGepiqKMLSEKE 233

                        250
                 ....*....|..
gi 17562788  235 VEHHLNQIANRD 246
Cdd:PTZ00246 234 IAELLKKVTQEY 245
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 3.27e-37

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: 129.76  E-value: 3.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   9 FDRHITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAK 88
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  89 FQIKRAQGEAASWKYKNGYDMPCELLAKKMADL-----NQYYTQNAEMRSLGCALLFISYdDEKGPEVYRVDPAGYYRGM 163
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLalqfgEGDDGKKAMSRPFGVALLIAGV-DENGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17562788 164 KGVSVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSLGIDVRSKDLEVVVV 220
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHK--DMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 3.87e-35

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: 124.40  E-value: 3.87e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   9 FDRHITIFSPEGRVYQVEYAFKAInSTNLTAVAVKGADAAVIAVQKRVPDSLIVADTVTSVYQISQSVGCCAIGMIPDAK 88
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAV-RKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  89 FQIKRAQGEAASwkYKNGYDMP--CELLAKKMADLNQYYTQNAEMRSLGCALLFISYDDEKGPEVYRVDPAGYYRGMKGV 166
Cdd:cd03755  80 VLINRARLECQS--HRLTVEDPvtVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKAN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17562788 167 SVGVKQLPATSFLEKKIKKksELTSTEAIELAIEALQTSlgIDVRSKDLEVVVV 220
Cdd:cd03755 158 AIGRNSKTVREFLEKNYKE--EMTRDDTIKLAIKALLEV--VQSGSKNIELAVM 207
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 4.93e-35

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: 124.33  E-value: 4.93e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788   9 FDRHITIFSPEGRVYQVEYAFKAINSTNlTAVAVKGADAAVIAVQKRVPDSLivADTVTSVYQISQSVGCCAIGMIPDAK 88
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGS-ATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  89 FQIKRAQGEAASWKYKNGYDMPCELLAKKMADLNQYYTQNAEMRSLGCALLFISYdDEKGPEVYRVDPAGYYRGMKGVSV 168
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGY-DESGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17562788 169 GVKQLPATSFLEKKIKKKSELTSTEAIELAIEALQTSL--GIDVRSKDLEVVVV 220
Cdd:cd03749 157 GARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIV 210
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 38-204 9.95e-33

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: 116.73  E-value: 9.95e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDSLIVAD-TVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAK 116
Cdd:cd01901   2 TSVAIKGKGGVVLAADKRLSSGLPVAGsPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 117 KMADLNQYYTQnaeMRSLGCALLFISYdDEKGPEVYRVDPAG-YYRGMKGVSVGVKQLPATSFLEKKIKKKseLTSTEAI 195
Cdd:cd01901  82 ELAKLLQVYTQ---GRPFGVNLIVAGV-DEGGGNLYYIDPSGpVIENPGAVATGSRSQRAKSLLEKLYKPD--MTLEEAV 155


                ....*....
gi 17562788 196 ELAIEALQT 204
Cdd:cd01901 156 ELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-223 2.72e-16

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: 74.40  E-value: 2.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDSLIVADTVTS-VYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAK 116
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASAGSLVASRNFDkIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 117 KMADLnQYYTQNAemrSLGCALLFISYDDEKGPEVYRVDPAG-YYRGmKGVSVGVKQLPATSFLEKKIKKKseLTSTEAI 195
Cdd:cd01912  82 LLSNI-LYSYRGF---PYYVSLIVGGVDKGGGPFLYYVDPLGsLIEA-PFVATGSGSKYAYGILDRGYKPD--MTLEEAV 154

                       170       180
                ....*....|....*....|....*....
gi 17562788 196 ELAIEALQTSLGIDVRSKD-LEVVVVTKD 223
Cdd:cd01912 155 ELVKKAIDSAIERDLSSGGgVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-223 1.96e-13

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: 66.51  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVP-DSLIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAK 116
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 117 KMADL---NQYYTQNAEmrslgcaLLFISYDDEkGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKKseLTSTE 193
Cdd:cd03764  82 LLSNIlnsSKYFPYIVQ-------LLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED--MTVEE 151

                       170       180       190
                ....*....|....*....|....*....|.
gi 17562788 194 AIELAIEALQTSLGIDVRSKD-LEVVVVTKD 223
Cdd:cd03764 152 AKKLAIRAIKSAIERDSASGDgIDVVVITKD 182
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 9-31 9.67e-11

Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 55.05  E-value: 9.67e-11
                          10        20
                  ....*....|....*....|...
gi 17562788     9 FDRHITIFSPEGRVYQVEYAFKA 31
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 9-31 3.35e-10

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 53.65  E-value: 3.35e-10
                           10        20
                   ....*....|....*....|...
gi 17562788      9 FDRHITIFSPEGRVYQVEYAFKA 31
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-223 2.44e-09

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: 55.73  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDS-LIVADTVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMPCELLAK 116
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGySILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 117 KMADL------NQYYTQNaemrslgcallFISYDDEKG-PEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKKS-- 187
Cdd:cd03757  90 LLSTIlysrrfFPYYVFN-----------ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNqn 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 17562788 188 -----ELTSTEAIELAIEALQTSLGIDVRSKD-LEVVVVTKD 223
Cdd:cd03757 159 nvertPLSLEEAVSLVKDAFTSAAERDIYTGDsLEIVIITKD 200
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-227 4.98e-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: 42.95  E-value: 4.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDSLIVAD-TVTSVYQISQSVGCCAIGMIPDAKFQIKRAQGEAASWKYKNGYDMP---CEL 113
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRvvtALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 114 LAKKMadLNQYytqnaeMRSLGCALLFISYDdEKGPEVYRVDPAGYYRGMKGVSVGVKQLPATSFLEKKIKKksELTSTE 193
Cdd:cd03763  82 MLKQH--LFRY------QGHIGAALVLGGVD-YTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKP--DMTEEE 150

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17562788 194 AIELAIEALqtSLGI--DVRS-KDLEVVVVTKDNSKF 227
Cdd:cd03763 151 AKKLVCEAI--EAGIfnDLGSgSNVDLCVITKDGVEY 185
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-223 2.12e-04

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: 41.03  E-value: 2.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788  38 TAVAVKGADAAVIAVQKRVPDSLIVA-DTVTSVYQISQSVGCCAIGMIPDA-KFQ--IKRaqgEAASWKYKNGYDMPCEL 113
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLkDDEDKIYKLSDHKLMACSGEAGDRlQFAeyIQK---NIQLYKMRNGYELSPKA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562788 114 LA----KKMADlnqyytqnaEMRS---LGCALLFISYDDEKGPEVYRVDpagYYRGMKGVSVGVKQLPA---TSFLEKKI 183
Cdd:cd03758  80 AAnftrRELAE---------SLRSrtpYQVNLLLAGYDKVEGPSLYYID---YLGTLVKVPYAAHGYGAyfcLSILDRYY 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17562788 184 KKKseLTSTEAIEL---AIEALQTSLGIDVRSkdLEVVVVTKD 223
Cdd:cd03758 148 KPD--MTVEEALELmkkCIKELKKRFIINLPN--FTVKVVDKD 186
 
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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