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Conserved domains on  [gi|6755198|ref|NP_036098|]
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proteasome subunit alpha type-6 isoform 1 [Mus musculus]

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 2.45e-163

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: 450.15  E-value: 2.45e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6755198  168 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 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 2.45e-163

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: 450.15  E-value: 2.45e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6755198  168 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 220
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-239 4.21e-73

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 222.79  E-value: 4.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198     6 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    86 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755198   166 TAAGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHL 239
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNY--KEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 36-220 1.36e-56

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: 178.92  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198     36 GLTSVAVRGKDCAVIVTQKKVP--DKLLDSSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 113
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    114 LCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQ 193
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 6755198    194 TVETAITCLSTVLSID-FKPSEIEVGVV 220
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 2.10e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.16  E-value: 2.10e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITESIGCV 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   80 MTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMILIGIDEEqGPQVYKCDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755198  160 YCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSID-FKPSEIEVGVVTVEnpKFRILTEAE 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 5.19e-11

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: 55.97  E-value: 5.19e-11
                           10        20
                   ....*....|....*....|...
gi 6755198       9 FDRHITIFSPEGRLYQVEYAFKA 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 2.45e-163

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: 450.15  E-value: 2.45e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6755198  168 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 220
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 3.02e-128

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: 361.38  E-value: 3.02e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADSR 88
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGS-TAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6755198  169 GVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVV 220
Cdd:cd01911 160 GKGSQEAKTFLEKRYKK--DLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-239 4.21e-73

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 222.79  E-value: 4.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198     6 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    86 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755198   166 TAAGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHL 239
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNY--KEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-222 5.44e-65

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: 201.02  E-value: 5.44e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    8 GFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADS 87
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKRGT-TALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03756  80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKATA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6755198  168 AGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTV 222
Cdd:cd03756 159 IGSGRQAVTEFLEKEY--KEDMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 38-220 1.92e-64

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: 198.49  E-value: 1.92e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   38 TSVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198  117 RIADISQVYTQnaEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVE 196
Cdd:cd01906  82 LLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP--DMTLEEAIE 157

                       170       180
                ....*....|....*....|....*
gi 6755198  197 TAITCLSTVLSIDF-KPSEIEVGVV 220
Cdd:cd01906 158 LALKALKSALERDLySGGNIEVAVI 182
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-239 4.21e-63

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: 196.77  E-value: 4.21e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   13 ITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADSRSQVQ 92
Cdd:cd03750   5 LTTFSPSGKLVQIEYALAAVSSGA-PSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   93 RARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATAAGVKQ 172
Cdd:cd03750  84 KARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTWKATAIGKNY 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755198  173 TESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTvENPKFRILTEAEIDAHL 239
Cdd:cd03750 163 SNAKTFLEKRYNE--DLELEDAIHTAILTLKEGFEGQMTEKNIEIGICG-ETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 8.79e-57

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: 180.24  E-value: 8.79e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTH-LFKITESIGCVMTGMTADS 87
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEkIYKIDDHIACAVAGITSDA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03752  82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6755198  168 AGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLS-TVLSIDFKPSEIEVGVV 220
Cdd:cd03752 162 IGNNNQAAQSLLKQDYKD--DMTLEEALALAVKVLSkTMDSTKLTSEKLEFATL 213
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 36-220 1.36e-56

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: 178.92  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198     36 GLTSVAVRGKDCAVIVTQKKVP--DKLLDSSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 113
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    114 LCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQ 193
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 6755198    194 TVETAITCLSTVLSID-FKPSEIEVGVV 220
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 2.10e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.16  E-value: 2.10e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITESIGCV 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   80 MTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMILIGIDEEqGPQVYKCDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755198  160 YCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSID-FKPSEIEVGVVTVEnpKFRILTEAE 234
Cdd:COG0638 158 LYEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRALYSAAERDsASGDGIDVAVITED--GFRELSEEE 229
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-217 6.13e-50

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: 162.53  E-value: 6.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    9 FDRHITIFSPEGRLYQVEYAFKAINQGgLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADSR 88
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKG-TTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6755198  169 GVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEV 217
Cdd:cd03755 160 GRNSKTVREFLEKNYKE--EMTRDDTIKLAIKALLEVVQSGSKNIELAV 206
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-220 6.47e-50

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: 162.45  E-value: 6.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    7 AGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTAD 86
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSG-TAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   87 SRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKAT 166
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755198  167 AAGVKQTESTSFLEKKVKKkfdwtfEQTVETAITCLSTVL-----SIDFKPSEIEVGVV 220
Cdd:cd03751 160 AIGKGKQAAKTELEKLKFS------ELTCREAVKEAAKIIyivhdEIKDKAFELELSWV 212
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 2.68e-48

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 159.63  E-value: 2.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198     1 MSRGssagFDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITESIGCV 79
Cdd:PTZ00246   1 MSRR----YDSRTTTFSPEGRLYQVEYALEAINNASLT-VGILCKEGVILGADKPISSKLLDpGKINEKIYKIDSHIFCA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    80 MTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGY 159
Cdd:PTZ00246  76 VAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   160 YCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLS-TVLSIDFKPSEIEVGVVTVENPKF----RILTEAE 234
Cdd:PTZ00246 156 YSGWKATAIGQNNQTAQSILKQEWKE--DLTLEQGLLLAAKVLTkSMDSTSPKADKIEVGILSHGETDGepiqKMLSEKE 233

                        250
                 ....*....|..
gi 6755198   235 IDAHLVALAERD 246
Cdd:PTZ00246 234 IAELLKKVTQEY 245
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 1.16e-46

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: 154.37  E-value: 1.16e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    9 FDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVIVTQKKVPDKLldSSTVTHLFKITESIGCVMTGMTADSR 88
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSAT-VGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6755198  169 GVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSID--FKPSEIEVGVV 220
Cdd:cd03749 157 GARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEqeLTIKNVSIAIV 210
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 1.04e-44

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: 149.41  E-value: 1.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198    9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADSR 88
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADIS----QVYTQNAEM-RPLGCCMILIGIDEEqGPQVYKCDPAGYYCGF 163
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgEGDDGKKAMsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755198  164 KATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVV 220
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHK--DMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 38-204 6.59e-43

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: 142.92  E-value: 6.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   38 TSVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd01901   2 TSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198  117 RIADISQVYTQnaeMRPLGCCMILIGIDEEqGPQVYKCDPAG-YYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTV 195
Cdd:cd01901  82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGpVIENPGAVATGSRSQRAKSLLEKLYKP--DMTLEEAV 155


                ....*....
gi 6755198  196 ETAITCLST 204
Cdd:cd01901 156 ELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-203 1.48e-13

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: 66.70  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   38 TSVAVRGKDCAVIVTqkkvpDKLL------DSSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPV 111
Cdd:cd01912   2 TIVGIKGKDGVVLAA-----DTRAsagslvASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198  112 DMLCKRiadISQVYTQNAEMrPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGvkqTEST---SFLEKKVKKkfD 188
Cdd:cd01912  77 KAAANL---LSNILYSYRGF-PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATG---SGSKyayGILDRGYKP--D 147

                       170
                ....*....|....*
gi 6755198  189 WTFEQTVETAITCLS 203
Cdd:cd01912 148 MTLEEAVELVKKAID 162
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 9-31 1.79e-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: 56.97  E-value: 1.79e-11
                          10        20
                  ....*....|....*....|...
gi 6755198      9 FDRHITIFSPEGRLYQVEYAFKA 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 5.19e-11

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: 55.97  E-value: 5.19e-11
                           10        20
                   ....*....|....*....|...
gi 6755198       9 FDRHITIFSPEGRLYQVEYAFKA 31
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-205 1.57e-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: 56.11  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   32 INQGGlTSVAVRGKDCAVIVTQKKVPDK-LLDSSTVTHLFKITES--IGCvmTGMTADSRSQVQRARYEAANWKYKYGYE 108
Cdd:cd03757   5 TDNGG-TVLAIAGNDFAVIAGDTRLSEGySILSRDSPKIFKLTDKcvLGS--SGFQADILALTKRLKARIKMYKYSHNKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198  109 ipvdMLCKRIADISQV----------YTQNaemrplgccmILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSF 178
Cdd:cd03757  82 ----MSTEAIAQLLSTilysrrffpyYVFN----------ILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPL 147

                       170       180
                ....*....|....*....|....*..
gi 6755198  179 LEKKVKKKFDWTFEQTVETAITCLSTV 205
Cdd:cd03757 148 LDNQVGRKNQNNVERTPLSLEEAVSLV 174
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-223 7.10e-08

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: 51.10  E-value: 7.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198   38 TSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755198  117 RIADISQVYtqnaEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVE 196
Cdd:cd03764  82 LLSNILNSS----KYFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKE--DMTVEEAKK 154

                       170       180
                ....*....|....*....|....*...
gi 6755198  197 TAITCLSTVLSID-FKPSEIEVGVVTVE 223
Cdd:cd03764 155 LAIRAIKSAIERDsASGDGIDVVVITKD 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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