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Conserved domains on  [gi|182891590|gb|AAI64827|]
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Psma6a protein [Danio rerio]

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 2.03e-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: 450.53  E-value: 2.03e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADS 87
Cdd:cd03754    1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754   81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182891590 168 AGVKQTEATSFLEKKIKKKLDW--TFDQTVETAISCLSTVLAIDFKPSELEIGVV 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 2.03e-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: 450.53  E-value: 2.03e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADS 87
Cdd:cd03754    1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754   81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182891590 168 AGVKQTEATSFLEKKIKKKLDW--TFDQTVETAISCLSTVLAIDFKPSELEIGVV 220
Cdd:cd03754  161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-239 7.23e-75

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 227.02  E-value: 7.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   6 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  86 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182891590 166 TAAGVKQTEATSFLEKKIKKklDWTFDQTVETAISCLSTVLAIDFKPSELEIGVVTTEEPKFRILSESEIDTHL 239
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 36-220 1.96e-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: 180.84  E-value: 1.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   36 GLTSVAVRGKDCAVVITQRKVP--DKLLDSSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 113
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  114 LCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQ 193
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL--TLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 182891590  194 TVETAISCLSTVLAID-FKPSELEIGVV 220
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 1.27e-53

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 172.64  E-value: 1.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVP-DKLLDSSTVTHLFRITENIGCV 79
Cdd:COG0638    1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  80 MSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMIVVGVDEElGPQVYKCDPAGY 159
Cdd:COG0638   80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182891590 160 YCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQTVETAISCLSTvlAID---FKPSELEIGVVTTEepKFRILSESE 234
Cdd:COG0638  158 LYEEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYS--AAErdsASGDGIDVAVITED--GFRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 9-31 4.36e-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: 4.36e-11
                           10        20
                   ....*....|....*....|...
gi 182891590     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 2.03e-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: 450.53  E-value: 2.03e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   8 GFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADS 87
Cdd:cd03754    1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03754   81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182891590 168 AGVKQTEATSFLEKKIKKKLDW--TFDQTVETAISCLSTVLAIDFKPSELEIGVV 220
Cdd:cd03754  161 AGVKEQEATNFLEKKLKKKPDLieSYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 1.52e-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: 364.46  E-value: 1.52e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADSR 88
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGS-TAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd01911   80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 182891590 169 GVKQTEATSFLEKKIKKKLdwTFDQTVETAISCLSTVLAIDFKPSELEIGVV 220
Cdd:cd01911  160 GKGSQEAKTFLEKRYKKDL--TLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-239 7.23e-75

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 227.02  E-value: 7.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   6 SAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGT-TAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  86 DSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182891590 166 TAAGVKQTEATSFLEKKIKKklDWTFDQTVETAISCLSTVLAIDFKPSELEIGVVTTEEPKFRILSESEIDTHL 239
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-222 1.34e-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: 202.56  E-value: 1.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   8 GFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADS 87
Cdd:cd03756    1 GYDRAITVFSPDGRLYQVEYAREAVKRGT-TALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03756   80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182891590 168 AGVKQTEATSFLEKKIKKklDWTFDQTVETAISCLSTVLAIDFKPSELEIGVVTT 222
Cdd:cd03756  159 IGSGRQAVTEFLEKEYKE--DMSLEEAIELALKALYAALEENETPENVEIAYVTV 211
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 38-220 2.91e-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: 200.80  E-value: 2.91e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  38 TSVAVRGKDCAVVITQRKVPDKLLD-SSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd01906    2 TIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 117 RIADISQVYTQnaEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQTVE 196
Cdd:cd01906   82 LLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDM--TLEEAIE 157

                        170       180
                 ....*....|....*....|....*
gi 182891590 197 TAISCLSTVLAIDF-KPSELEIGVV 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 3.23e-64

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: 199.47  E-value: 3.23e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  13 ITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADSRSQVQ 92
Cdd:cd03750    5 LTTFSPSGKLVQIEYALAAVSSGA-PSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  93 RARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKATAAGVKQ 172
Cdd:cd03750   84 KARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEG-GPYLYQVDPSGSYFTWKATAIGKNY 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 182891590 173 TEATSFLEKKIKKKLDwtFDQTVETAISCLSTVLAIDFKPSELEIGVVtTEEPKFRILSESEIDTHL 239
Cdd:cd03750  163 SNAKTFLEKRYNEDLE--LEDAIHTAILTLKEGFEGQMTEKNIEIGIC-GETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-220 2.10e-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: 184.47  E-value: 2.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTH-LFRITENIGCVMSGMTADS 87
Cdd:cd03752    3 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEkIYKIDDHIACAVAGITSDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  88 RSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATA 167
Cdd:cd03752   82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 182891590 168 AGVKQTEATSFLEKKIKKKLdwTFDQTVETAISCLS-TVLAIDFKPSELEIGVV 220
Cdd:cd03752  162 IGNNNQAAQSLLKQDYKDDM--TLEEALALAVKVLSkTMDSTKLTSEKLEFATL 213
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 36-220 1.96e-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: 180.84  E-value: 1.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   36 GLTSVAVRGKDCAVVITQRKVP--DKLLDSSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDm 113
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  114 LCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQ 193
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL--TLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 182891590  194 TVETAISCLSTVLAID-FKPSELEIGVV 220
Cdd:pfam00227 161 AVELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-234 1.27e-53

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 172.64  E-value: 1.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVP-DKLLDSSTVTHLFRITENIGCV 79
Cdd:COG0638    1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREAVKRGT-TTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  80 MSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAeMRPLGCCMIVVGVDEElGPQVYKCDPAGY 159
Cdd:COG0638   80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182891590 160 YCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQTVETAISCLSTvlAID---FKPSELEIGVVTTEepKFRILSESE 234
Cdd:COG0638  158 LYEEKAVAIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYS--AAErdsASGDGIDVAVITED--GFRELSEEE 229
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-205 8.00e-51

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: 164.84  E-value: 8.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   9 FDRHITIFSPEGRLYQVEYAFKAINQGgLTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADSR 88
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKG-TTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd03755   80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 182891590 169 GVKQTEATSFLEKKIKKKLDwtFDQTVETAISCLSTV 205
Cdd:cd03755  160 GRNSKTVREFLEKNYKEEMT--RDDTIKLAIKALLEV 194
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-181 1.29e-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: 164.38  E-value: 1.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   7 AGFDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTAD 86
Cdd:cd03751    2 TGYDLSASTFSPDGRVFQVEYANKAVENSG-TAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  87 SRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKAT 166
Cdd:cd03751   81 GRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGC 159

                        170
                 ....*....|....*
gi 182891590 167 AAGVKQTEATSFLEK 181
Cdd:cd03751  160 AIGKGKQAAKTELEK 174
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 5.98e-49

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 161.56  E-value: 5.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   1 MSRGssagFDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVVITQRKVPDKLLD-SSTVTHLFRITENIGCV 79
Cdd:PTZ00246   1 MSRR----YDSRTTTFSPEGRLYQVEYALEAINNASLT-VGILCKEGVILGADKPISSKLLDpGKINEKIYKIDSHIFCA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  80 MSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDEELGPQVYKCDPAGY 159
Cdd:PTZ00246  76 VAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 160 YCGFKATAAGVKQTEATSFLEKKIKKklDWTFDQTVETAISCLSTVLAIDFKPSE-LEIGVVTTEEPKF----RILSESE 234
Cdd:PTZ00246 156 YSGWKATAIGQNNQTAQSILKQEWKE--DLTLEQGLLLAAKVLTKSMDSTSPKADkIEVGILSHGETDGepiqKMLSEKE 233

                        250
                 ....*....|..
gi 182891590 235 IDTHLMALTERD 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 3.04e-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: 153.22  E-value: 3.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   9 FDRHITIFSPEGRLYQVEYAFKAINQGGLTsVAVRGKDCAVVITQRKVPDKLldSSTVTHLFRITENIGCVMSGMTADSR 88
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSAT-VGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMIVVGVDeELGPQVYKCDPAGYYCGFKATAA 168
Cdd:cd03749   78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKATSI 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 182891590 169 GVKQTEATSFLEKKIKKKLDWTFDQTVETAISCLSTVLAID--FKPSELEIGVV 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 1.10e-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: 151.72  E-value: 1.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590   9 FDRHITIFSPEGRLYQVEYAFKAINQGGlTSVAVRGKDCAVVITQRKVPDKLLDSSTVTHLFRITENIGCVMSGMTADSR 88
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  89 SQVQRARYEAANWKYKYGYEIPVDMLCKRIADIS----QVYTQNAEM-RPLGCCMIVVGVDEElGPQVYKCDPAGYYCGF 163
Cdd:cd03753   80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgEGDDGKKAMsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 182891590 164 KATAAGVKQTEATSFLEKKIKKKLdwTFDQTVETAISCLSTVLAIDFKPSELEIGVV 220
Cdd:cd03753  159 DAKAIGSGSEGAQSSLQEKYHKDM--TLEEAEKLALSILKQVMEEKLNSTNVELATV 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 38-204 1.17e-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: 144.85  E-value: 1.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  38 TSVAVRGKDCAVVITQRKVPDKLLD-SSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd01901    2 TSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 117 RIADISQVYTQnaeMRPLGCCMIVVGVDEElGPQVYKCDPAG-YYCGFKATAAGVKQTEATSFLEKKIKKklDWTFDQTV 195
Cdd:cd01901   82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGpVIENPGAVATGSRSQRAKSLLEKLYKP--DMTLEEAV 155


                 ....*....
gi 182891590 196 ETAISCLST 204
Cdd:cd01901  156 ELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-203 2.68e-15

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: 71.71  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  38 TSVAVRGKDCAVVITqrkvpDKLL------DSSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPV 111
Cdd:cd01912    2 TIVGIKGKDGVVLAA-----DTRAsagslvASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 112 DMLCKRiadISQVYTQNAEMrPLGCCMIVVGVDEELGPQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKIKKKLdwTF 191
Cdd:cd01912   77 KAAANL---LSNILYSYRGF-PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDM--TL 150

                        170
                 ....*....|..
gi 182891590 192 DQTVETAISCLS 203
Cdd:cd01912  151 EEAVELVKKAID 162
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 9-31 1.51e-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: 57.36  E-value: 1.51e-11
                          10        20
                  ....*....|....*....|...
gi 182891590    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 4.36e-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: 4.36e-11
                           10        20
                   ....*....|....*....|...
gi 182891590     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 ...
 32-200 1.25e-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: 56.50  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  32 INQGGlTSVAVRGKDCAVVITQ-RKVPDKLLDSSTVTHLFRITEN--IGCvmSGMTADSRSQVQRARYEAANWKYKYGYE 108
Cdd:cd03757    5 TDNGG-TVLAIAGNDFAVIAGDtRLSEGYSILSRDSPKIFKLTDKcvLGS--SGFQADILALTKRLKARIKMYKYSHNKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 109 ipvdMLCKRIADISQV----------YTQNaemrplgccmIVVGVDEELGPQVYKCDPAGYYCGFKATAAGVKQTEATSF 178
Cdd:cd03757   82 ----MSTEAIAQLLSTilysrrffpyYVFN----------ILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPL 147

                        170       180
                 ....*....|....*....|....*
gi 182891590 179 LEKKIKKKLDWTFDQ---TVETAIS 200
Cdd:cd03757  148 LDNQVGRKNQNNVERtplSLEEAVS 172
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-231 1.56e-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: 53.03  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  38 TSVAVRGKDCAVVITQRKVP-DKLLDSSTVTHLFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCK 116
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590 117 RIADISQVYtqnaEMRPLGCCMIVVGVDEElGPQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKIKKKLdwTFDQTVE 196
Cdd:cd03764   82 LLSNILNSS----KYFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDM--TVEEAKK 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 182891590 197 TAISCLSTVLAID-FKPSELEIGVVTTEEpkFRILS 231
Cdd:cd03764  155 LAIRAIKSAIERDsASGDGIDVVVITKDG--YKELE 188
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 69-158 4.62e-05

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


Pssm-ID: 239731  Cd Length: 188  Bit Score: 42.98  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  69 LFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGyEIPvdmLCKRIADISQ--VYtQNAEMrpLGCCMIVVGVDEE 146
Cdd:cd03762   34 LTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELG-EPP---LVKTAASLFKnlCY-NYKEM--LSAGIIVAGWDEQ 106

                         90
                 ....*....|..
gi 182891590 147 LGPQVYKCDPAG 158
Cdd:cd03762  107 NGGQVYSIPLGG 118
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 69-201 6.04e-03

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


Pssm-ID: 239732  Cd Length: 189  Bit Score: 36.79  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182891590  69 LFRITENIGCVMSGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNaemrpLGCCMIVVGVDEElG 148
Cdd:cd03763   34 IHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTMLKQHLFRYQGH-----IGAALVLGGVDYT-G 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 182891590 149 PQVYKCDPAGYYCGFKATAAGVKQTEATSFLEKKikkkldWTFDQTVETAISC 201
Cdd:cd03763  108 PHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDR------YKPDMTEEEAKKL 154
 
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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