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Conserved domains on  [gi|2441536692|pdb|7QXX|g]
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Chain g, Proteasome subunit alpha type-6

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 ...
 7-219 1.19e-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: 450.92  E-value: 1.19e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        7 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADS 86
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 166
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      167 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 219
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 ...
 7-219 1.19e-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: 450.92  E-value: 1.19e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        7 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADS 86
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 166
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      167 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 219
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-238 1.98e-73

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 223.56  E-value: 1.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g         5 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTA 84
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        85 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKA 164
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7QXX_g       165 TAAGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHL 238
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNY--KEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 35-219 2.52e-57

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: 180.46  E-value: 2.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g         35 GLTSVAVRGKDCAVIVTQKKVP--DKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 112
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        113 LCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQ 192
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLTLEE 160

                         170       180
                  ....*....|....*....|....*...
7QXX_g        193 TVETAITCLSTVLSID-FKPSEIEVGVV 219
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-233 2.19e-49

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 161.85  E-value: 2.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        1 SRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITENIGCVM 79
Cdd:COG0638   2 QPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       80 TGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMILIGIDEEqGPQVYKCDPAGYY 159
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      160 CGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSID-FKPSEIEVGVVTVEnpKFRILTEAE 233
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRALYSAAERDsASGDGIDVAVITED--GFRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 4.83e-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: 4.83e-11
                           10        20
                   ....*....|....*....|...
7QXX_g           8 FDRHITIFSPEGRLYQVEYAFKA 30
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 ...
 7-219 1.19e-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: 450.92  E-value: 1.19e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        7 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADS 86
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 166
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      167 AGVKQTESTSFLEKKVKKKFDW--TFEQTVETAITCLSTVLSIDFKPSEIEVGVV 219
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 8.16e-129

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: 362.53  E-value: 8.16e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        8 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSR 87
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGS-TAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       88 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAA 167
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
7QXX_g      168 GVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVV 219
Cdd:cd01911 160 GKGSQEAKTFLEKRYKK--DLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-238 1.98e-73

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 223.56  E-value: 1.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g         5 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTA 84
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        85 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKA 164
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7QXX_g       165 TAAGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHL 238
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNY--KEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-221 1.73e-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: 202.18  E-value: 1.73e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        7 GFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADS 86
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKRGT-TALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATA 166
Cdd:cd03756  80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKATA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      167 AGVKQTESTSFLEKKVkkKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTV 221
Cdd:cd03756 159 IGSGRQAVTEFLEKEY--KEDMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 37-219 3.90e-65

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: 200.41  E-value: 3.90e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       37 TSVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 115
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g      116 RIADISQVYTQnaEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVE 195
Cdd:cd01906  82 LLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP--DMTLEEAIE 157

                       170       180
                ....*....|....*....|....*
7QXX_g      196 TAITCLSTVLSIDF-KPSEIEVGVV 219
Cdd:cd01906 158 LALKALKSALERDLySGGNIEVAVI 182
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-238 1.65e-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: 197.93  E-value: 1.65e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       12 ITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQ 91
Cdd:cd03750   5 LTTFSPSGKLVQIEYALAAVSSGA-PSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       92 RARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATAAGVKQ 171
Cdd:cd03750  84 KARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTWKATAIGKNY 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7QXX_g      172 TESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTvENPKFRILTEAEIDAHL 238
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 ...
 8-219 9.28e-58

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: 182.55  E-value: 9.28e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        8 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTH-LFKITENIGCVMTGMTADS 86
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEkIYKIDDHIACAVAGITSDA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 166
Cdd:cd03752  82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
7QXX_g      167 AGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLS-TVLSIDFKPSEIEVGVV 219
Cdd:cd03752 162 IGNNNQAAQSLLKQDYKD--DMTLEEALALAVKVLSkTMDSTKLTSEKLEFATL 213
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 35-219 2.52e-57

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: 180.46  E-value: 2.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g         35 GLTSVAVRGKDCAVIVTQKKVP--DKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 112
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        113 LCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQ 192
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLTLEE 160

                         170       180
                  ....*....|....*....|....*...
7QXX_g        193 TVETAITCLSTVLSID-FKPSEIEVGVV 219
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-216 1.53e-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: 164.07  E-value: 1.53e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        8 FDRHITIFSPEGRLYQVEYAFKAINQGgLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSR 87
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKG-TTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       88 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAA 167
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
7QXX_g      168 GVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEV 216
Cdd:cd03755 160 GRNSKTVREFLEKNYKE--EMTRDDTIKLAIKALLEVVQSGSKNIELAV 206
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-219 2.91e-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: 163.22  E-value: 2.91e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        6 AGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTAD 85
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSG-TAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       86 SRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKAT 165
Cdd:cd03751  81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
7QXX_g      166 AAGVKQTESTSFLEKKVKKkfdwtfEQTVETAITCLSTVL-----SIDFKPSEIEVGVV 219
Cdd:cd03751 160 AIGKGKQAAKTELEKLKFS------ELTCREAVKEAAKIIyivhdEIKDKAFELELSWV 212
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-233 2.19e-49

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 161.85  E-value: 2.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        1 SRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITENIGCVM 79
Cdd:COG0638   2 QPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       80 TGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMILIGIDEEqGPQVYKCDPAGYY 159
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7QXX_g      160 CGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSID-FKPSEIEVGVVTVEnpKFRILTEAE 233
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRALYSAAERDsASGDGIDVAVITED--GFRELSEEE 229
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-245 3.25e-48

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 159.63  E-value: 3.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g         8 FDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITENIGCVMTGMTADS 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLT-VGILCKEGVILGADKPISSKLLDpGKINEKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        87 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATA 166
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       167 AGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLS-TVLSIDFKPSEIEVGVVTVENPKF----RILTEAEIDAHLVAL 241
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKE--DLTLEQGLLLAAKVLTkSMDSTSPKADKIEVGILSHGETDGepiqKMLSEKEIAELLKKV 241


                 ....
7QXX_g       242 AERD 245
Cdd:PTZ00246 242 TQEY 245
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 6.41e-47

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: 154.76  E-value: 6.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        8 FDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVIVTQKKVPDKLldSSTVTHLFKITENIGCVMTGMTADSR 87
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSAT-VGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       88 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDeEQGPQVYKCDPAGYYCGFKATAA 167
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
7QXX_g      168 GVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSID--FKPSEIEVGVV 219
Cdd:cd03749 157 GARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEqeLTIKNVSIAIV 210
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 3.82e-45

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: 150.18  E-value: 3.82e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g        8 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSR 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       88 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADIS----QVYTQNAEM-RPLGCCMILIGIDEEqGPQVYKCDPAGYYCGF 162
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgEGDDGKKAMsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
7QXX_g      163 KATAAGVKQTESTSFLEKKVKKkfDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVV 219
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHK--DMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 37-203 1.58e-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: 144.46  E-value: 1.58e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       37 TSVAVRGKDCAVIVTQKKVPDKLLD-SSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 115
Cdd:cd01901   2 TSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g      116 RIADISQVYTQnaeMRPLGCCMILIGIDEEqGPQVYKCDPAG-YYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTV 194
Cdd:cd01901  82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGpVIENPGAVATGSRSQRAKSLLEKLYKP--DMTLEEAV 155


                ....*....
7QXX_g      195 ETAITCLST 203
Cdd:cd01901 156 ELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 37-202 3.37e-14

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: 68.62  E-value: 3.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       37 TSVAVRGKDCAVIVTqkkvpDKLL------DSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPV 110
Cdd:cd01912   2 TIVGIKGKDGVVLAA-----DTRAsagslvASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g      111 DMLCKRiadISQVYTQNAEMrPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGvkqTEST---SFLEKKVKKkfD 187
Cdd:cd01912  77 KAAANL---LSNILYSYRGF-PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATG---SGSKyayGILDRGYKP--D 147

                       170
                ....*....|....*
7QXX_g      188 WTFEQTVETAITCLS 202
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 ...
 8-30 1.77e-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: 1.77e-11
                          10        20
                  ....*....|....*....|...
7QXX_g          8 FDRHITIFSPEGRLYQVEYAFKA 30
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 ...
 8-30 4.83e-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: 4.83e-11
                           10        20
                   ....*....|....*....|...
7QXX_g           8 FDRHITIFSPEGRLYQVEYAFKA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-204 2.96e-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: 55.34  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       31 INQGGlTSVAVRGKDCAVIVTQKKVPDK-LLDSSTVTHLFKITEN--IGCvmTGMTADSRSQVQRARYEAANWKYKYGYE 107
Cdd:cd03757   5 TDNGG-TVLAIAGNDFAVIAGDTRLSEGySILSRDSPKIFKLTDKcvLGS--SGFQADILALTKRLKARIKMYKYSHNKE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g      108 ipvdMLCKRIADISQV----------YTQNaemrplgccmILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSF 177
Cdd:cd03757  82 ----MSTEAIAQLLSTilysrrffpyYVFN----------ILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPL 147

                       170       180
                ....*....|....*....|....*..
7QXX_g      178 LEKKVKKKFDWTFEQTVETAITCLSTV 204
Cdd:cd03757 148 LDNQVGRKNQNNVERTPLSLEEAVSLV 174
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 37-222 2.04e-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: 52.64  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       37 TSVAVRGKDCAVIVTQKKVP-DKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 115
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g      116 RIADISQVYtqnaEMRPLGCCMILIGIDEEqGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKkfDWTFEQTVE 195
Cdd:cd03764  82 LLSNILNSS----KYFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKE--DMTVEEAKK 154

                       170       180
                ....*....|....*....|....*...
7QXX_g      196 TAITCLSTVLSID-FKPSEIEVGVVTVE 222
Cdd:cd03764 155 LAIRAIKSAIERDsASGDGIDVVVITKD 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 68-157 3.63e-03

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 37.20  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7QXX_g       68 LFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGyEIPvdmLCKRIADISQ--VYtQNAEMrpLGCCMILIGIDEE 145
Cdd:cd03762  34 LTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELG-EPP---LVKTAASLFKnlCY-NYKEM--LSAGIIVAGWDEQ 106

                        90
                ....*....|..
7QXX_g      146 QGPQVYKCDPAG 157
Cdd:cd03762 107 NGGQVYSIPLGG 118
 
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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