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Conserved domains on  [gi|24586402|ref|NP_524837|]
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proteasome alpha1 subunit, isoform B [Drosophila melanogaster]

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 ...
 8-218 7.91e-145

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: 403.54  E-value: 7.91e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   8 GFDRHITIFSPEGRLYQVEYAFKAIAQENITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  88 RSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24586402 168 VGAKTLEANSYLEKKYKPN----LSEEKAIQLAISCLSSVLAIDFKPNGIEIGVV 218
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 ...
 8-218 7.91e-145

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: 403.54  E-value: 7.91e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   8 GFDRHITIFSPEGRLYQVEYAFKAIAQENITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  88 RSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24586402 168 VGAKTLEANSYLEKKYKPN----LSEEKAIQLAISCLSSVLAIDFKPNGIEIGVV 218
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-240 1.93e-71

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 218.55  E-value: 1.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402    6 SAGFDRHITIFSPEGRLYQVEYAFKAIAQeNITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKR-GTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   86 DSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMvLIAYDNEIGPSVYKTDPAGYFSGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVAL-LIAGVDDGGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586402  166 CSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVVSKSDPTFRILDEREIEEHLTKI 240
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKL 239
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-218 7.47e-60

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: 187.00  E-value: 7.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402    38 TTVALKSGDCAVVATQKKVTEKNIV--PETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDvLC 115
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATRGSKLlsKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   116 RRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQL 195
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVEL 164

                         170       180
                  ....*....|....*....|....
gi 24586402   196 AISCLSSVLAID-FKPNGIEIGVV 218
Cdd:pfam00227 165 AVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-232 5.21e-58

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 183.81  E-value: 5.21e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAiAQENITTVALKSGDCAVVATQKKVTEKN-IVPETVTHLFRITKDIGCA 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREA-VKRGTTTVGIKTKDGVVLAADRRATMGNlIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  80 MTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAeMRPLGCSMVLIAYDNEiGPSVYKTDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586402 160 FSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSvlAID---FKPNGIEIGVVSKSdpTFRILDERE 232
Cdd:COG0638 158 LYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYS--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 9.66e-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: 55.20  E-value: 9.66e-11
                           10        20
                   ....*....|....*....|...
gi 24586402      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 ...
 8-218 7.91e-145

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: 403.54  E-value: 7.91e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   8 GFDRHITIFSPEGRLYQVEYAFKAIAQENITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADS 87
Cdd:cd03754   1 GFDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  88 RSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACS 167
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24586402 168 VGAKTLEANSYLEKKYKPN----LSEEKAIQLAISCLSSVLAIDFKPNGIEIGVV 218
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-218 7.07e-118

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: 334.80  E-value: 7.07e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   9 FDRHITIFSPEGRLYQVEYAFKAIAQEnITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADSR 88
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNG-STAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  89 SQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSV 168
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24586402 169 GAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVV 218
Cdd:cd01911 160 GKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-240 1.93e-71

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 218.55  E-value: 1.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402    6 SAGFDRHITIFSPEGRLYQVEYAFKAIAQeNITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIA 85
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKR-GTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   86 DSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMvLIAYDNEIGPSVYKTDPAGYFSGFKA 165
Cdd:PRK03996  86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVAL-LIAGVDDGGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586402  166 CSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVVSKSDPTFRILDEREIEEHLTKI 240
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKKFRKLSVEEIEKYLEKL 239
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 38-218 1.18e-63

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: 196.56  E-value: 1.18e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIV-PETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCR 116
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIADINQVYTQnaEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLA 196
Cdd:cd01906  82 LLANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 24586402 197 ISCLSSVLAIDF-KPNGIEIGVV 218
Cdd:cd01906 160 LKALKSALERDLySGGNIEVAVI 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 2.70e-62

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: 194.09  E-value: 2.70e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   8 GFDRHITIFSPEGRLYQVEYAFKAIAQeNITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADS 87
Cdd:cd03756   1 GYDRAITVFSPDGRLYQVEYAREAVKR-GTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  88 RSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMvLIAYDNEIGPSVYKTDPAGYFSGFKACS 167
Cdd:cd03756  80 RVLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVAL-LIAGVDDGGPRLFETDPSGAYNEYKATA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24586402 168 VGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVVS 219
Cdd:cd03756 159 IGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 38-218 7.47e-60

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: 187.00  E-value: 7.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402    38 TTVALKSGDCAVVATQKKVTEKNIV--PETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDvLC 115
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATRGSKLlsKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   116 RRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQL 195
Cdd:pfam00227  85 ARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVEL 164

                         170       180
                  ....*....|....*....|....
gi 24586402   196 AISCLSSVLAID-FKPNGIEIGVV 218
Cdd:pfam00227 165 AVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-232 5.21e-58

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 183.81  E-value: 5.21e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   1 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAiAQENITTVALKSGDCAVVATQKKVTEKN-IVPETVTHLFRITKDIGCA 79
Cdd:COG0638   1 MQPSQQSSYDRAITIFSPDGRLYQVEYAREA-VKRGTTTVGIKTKDGVVLAADRRATMGNlIASKSIEKIFKIDDHIGVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  80 MTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAeMRPLGCSMVLIAYDNEiGPSVYKTDPAGY 159
Cdd:COG0638  80 IAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586402 160 FSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSvlAID---FKPNGIEIGVVSKSdpTFRILDERE 232
Cdd:COG0638 158 LYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYS--AAErdsASGDGIDVAVITED--GFRELSEEE 229
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-237 3.35e-55

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: 176.36  E-value: 3.35e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  13 ITIFSPEGRLYQVEYAFKAIAQeNITTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADSRSQVQ 92
Cdd:cd03750   5 LTTFSPSGKLVQIEYALAAVSS-GAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  93 KARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMvLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKT 172
Cdd:cd03750  84 KARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSL-LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNY 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586402 173 LEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVVSKsDPTFRILDEREIEEHL 237
Cdd:cd03750 163 SNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGE-TKGFRLLTPAEIKDYL 226
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-218 7.82e-54

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: 172.53  E-value: 7.82e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   9 FDRHITIFSPEGRLYQVEYAFKAIAQENiTTVALKSGDCAVVATQKKVTEKNIVPETVTH-LFRITKDIGCAMTGRIADS 87
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAG-TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEkIYKIDDHIACAVAGITSDA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  88 RSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACS 167
Cdd:cd03752  82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24586402 168 VGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVL-AIDFKPNGIEIGVV 218
Cdd:cd03752 162 IGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMdSTKLTSEKLEFATL 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-218 1.59e-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: 166.38  E-value: 1.59e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   9 FDRHITIFSPEGRLYQVEYAFKAIAQENiTTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADSR 88
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGT-TAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  89 SQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSV 168
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24586402 169 GAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVlaIDFKPNGIEIGVV 218
Cdd:cd03755 160 GRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEV--VQSGSKNIELAVM 207
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-244 2.66e-49

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 162.33  E-value: 2.66e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402    1 MSRGssagFDRHITIFSPEGRLYQVEYAFKAIAQENITtVALKSGDCAVVATQKKVTEKNIVP-ETVTHLFRITKDIGCA 79
Cdd:PTZ00246   1 MSRR----YDSRTTTFSPEGRLYQVEYALEAINNASLT-VGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   80 MTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDNEIGPSVYKTDPAGY 159
Cdd:PTZ00246  76 VAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  160 FSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDF-KPNGIEIGVVSKSD----PTFRILDEREIE 234
Cdd:PTZ00246 156 YSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILSHGEtdgePIQKMLSEKEIA 235

                        250
                 ....*....|
gi 24586402  235 EHLTKIAEKD 244
Cdd:PTZ00246 236 ELLKKVTQEY 245
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-193 3.58e-49

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: 160.52  E-value: 3.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   7 AGFDRHITIFSPEGRLYQVEYAFKAIaqENI-TTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIA 85
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAV--ENSgTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  86 DSRSQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDnEIGPSVYKTDPAGYFSGFKA 165
Cdd:cd03751  80 DGRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYD-SDGPQLYMIEPSGVSYGYFG 158

                       170       180
                ....*....|....*....|....*...
gi 24586402 166 CSVGAKTLEANSYLEKKYKPNLSEEKAI 193
Cdd:cd03751 159 CAIGKGKQAAKTELEKLKFSELTCREAV 186
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-218 9.20e-47

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: 154.42  E-value: 9.20e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   9 FDRHITIFSPEGRLYQVEYAFKAIAQENiTTVALKSGDCAVVATQKKVTEKNIVPETVTHLFRITKDIGCAMTGRIADSR 88
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  89 SQVQKARYEAANFRYKYGYEMPVDVLCRRIADI----NQVYTQNAEM-RPLGCSMvLIAYDNEIGPSVYKTDPAGYFSGF 163
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLalqfGEGDDGKKAMsRPFGVAL-LIAGVDENGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24586402 164 KACSVGAKTLEANSYLEKKYKPNLSEEKAIQLAISCLSSVLAIDFKPNGIEIGVV 218
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-218 2.05e-42

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: 143.20  E-value: 2.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402   9 FDRHITIFSPEGRLYQVEYAFKAIAQENITtVALKSGDCAVVATQKKVTEKniVPETVTHLFRITKDIGCAMTGRIADSR 88
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSAT-VGLKSKTHAVLVALKRATSE--LSSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  89 SQVQKARYEAANFRYKYGYEMPVDVLCRRIADINQVYTQNAEMRPLGCSMVLIAYDnEIGPSVYKTDPAGYFSGFKACSV 168
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24586402 169 GAKTLEANSYLEKKYK--PNLSEEKAIQLAISCLSSVLAIDFKPN--GIEIGVV 218
Cdd:cd03749 157 GARSQSARTYLERHFEefEDCSLEELIKHALRALRETLPGEQELTikNVSIAIV 210
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 38-202 2.91e-42

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: 141.38  E-value: 2.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIVP-ETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCR 116
Cdd:cd01901   2 TSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIADINQVYTQnaeMRPLGCSMVLIAYDNEiGPSVYKTDPAG-YFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQL 195
Cdd:cd01901  82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGpVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVEL 157


                ....*..
gi 24586402 196 AISCLSS 202
Cdd:cd01901 158 ALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-220 2.18e-19

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: 82.49  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIVPETVTH-LFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCR 116
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASAGSLVASRNFDkIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIAdiNQVYtQNAEMrPLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQLA 196
Cdd:cd01912  82 LLS--NILY-SYRGF-PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELV 157

                       170       180
                ....*....|....*....|....*..
gi 24586402 197 ISCLSSvlAID---FKPNGIEIGVVSK 220
Cdd:cd01912 158 KKAIDS--AIErdlSSGGGVDVAVITK 182
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-222 7.87e-15

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: 70.36  E-value: 7.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIV-PETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCR 116
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIaSKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIADI---NQVYTQNAEmrplgcsmVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAI 193
Cdd:cd03764  82 LLSNIlnsSKYFPYIVQ--------LLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAK 153

                       170       180       190
                ....*....|....*....|....*....|
gi 24586402 194 QLAISCLSSVLAID-FKPNGIEIGVVSKSD 222
Cdd:cd03764 154 KLAIRAIKSAIERDsASGDGIDVVVITKDG 183
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 9-31 2.58e-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: 56.59  E-value: 2.58e-11
                          10        20
                  ....*....|....*....|...
gi 24586402     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 9.66e-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: 55.20  E-value: 9.66e-11
                           10        20
                   ....*....|....*....|...
gi 24586402      9 FDRHITIFSPEGRLYQVEYAFKA 31
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 37-196 6.52e-10

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: 56.82  E-value: 6.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  37 ITTVALKSGDCAVVATQKKVTEKNIVPE-TVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLC 115
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 116 RRIADINQVYTQNaemrpLGCSMVLIAYDNEiGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQL 195
Cdd:cd03763  81 TMLKQHLFRYQGH-----IGAALVLGGVDYT-GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKL 154


                .
gi 24586402 196 A 196
Cdd:cd03763 155 V 155
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-196 8.63e-06

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: 45.33  E-value: 8.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEK-NIVPETVTHLFRITKDIGCAMTGRIADSRSQVQKARYEAANFRYKYGYEMPVDVLCR 116
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGySILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIADI------NQVYTQNaemrplgcsmVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGA----------KTLEANSYLE 180
Cdd:cd03757  90 LLSTIlysrrfFPYYVFN----------ILAGIDEEGKGVVYSYDPVGSYERETYSAGGSassliqplldNQVGRKNQNN 159

                       170
                ....*....|....*.
gi 24586402 181 KKYKPnLSEEKAIQLA 196
Cdd:cd03757 160 VERTP-LSLEEAVSLV 174
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-206 1.26e-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: 44.52  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIVPETVTH-LFRITKDIGCAMTGRIADSRSQVQKARYEAAnfryKYGYEMPVDVLCR 116
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDkLTQLHDRIYCCRSGSAADTQAIADYVRYYLD----MHSIELGEPPLVK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 117 RIADI--NQVYtQNAEMrpLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSEEKAIQ 194
Cdd:cd03762  78 TAASLfkNLCY-NYKEM--LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIK 154

                       170
                ....*....|..
gi 24586402 195 LAISCLSsvLAI 206
Cdd:cd03762 155 FVKNALS--LAM 164
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-200 2.45e-03

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 37.95  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402  38 TTVALKSGDCAVVATQKKVTEKNIV-PETVTHLFRITKDIGCAMTGRIADSrsqVQKARYEAAN---FRYKYGYEMPVdv 113
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVlKDDEDKIYKLSDHKLMACSGEAGDR---LQFAEYIQKNiqlYKMRNGYELSP-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586402 114 lcRRIAdiNQVYTQNAE-MR---PLGCSMVLIAYDNEIGPSVYKTDPAGYFSGFKACSVGAKTLEANSYLEKKYKPNLSE 189
Cdd:cd03758  78 --KAAA--NFTRRELAEsLRsrtPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTV 153

                       170
                ....*....|.
gi 24586402 190 EKAIQLAISCL 200
Cdd:cd03758 154 EEALELMKKCI 164
 
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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