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Conserved domains on  [gi|285812187|tpg|DAA08087|]
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TPA: proteasome core particle subunit alpha 1 [Saccharomyces cerevisiae S288C]

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 ...
 12-228 6.02e-123

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: 348.46  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 285812187 172 GPKQQEITTNLENHFKKSKidhINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVA 228
Cdd:cd03754  162 GVKEQEATNFLEKKLKKKP---DLIESYEETVELAISCLQTVLSTDFKATEIEVGVV 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 ...
 12-228 6.02e-123

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: 348.46  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 285812187 172 GPKQQEITTNLENHFKKSKidhINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVA 228
Cdd:cd03754  162 GVKEQEATNFLEKKLKKKP---DLIESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
12-245 3.49e-48

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 159.23  E-value: 3.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTT-AVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812187 172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKD--KFFTLSAENIEERL 245
Cdd:PRK03996 168 GAGRDTVMEFLEKNYK-------EDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVEtkKFRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 12-239 1.40e-45

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 152.03  E-value: 1.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   12 YDRHITIFSPEGRLYQVEYAFKATNQtNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKR-GTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKD--KFFTLSAE 239
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYR-------EDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEdkKFRKLSVE 223
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 42-227 1.14e-42

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: 143.48  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   42 SLAVRGKDCTVVISQKKVP--DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDvLAK 119
Cdd:pfam00227   7 IVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  120 RMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKkskiDHINEESW 199
Cdd:pfam00227  86 RIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR----PDLTLEEA 161

                         170       180
                  ....*....|....*....|....*...
gi 285812187  200 EKVVEFAITHMIDalGTEFSKNDLEVGV 227
Cdd:pfam00227 162 VELAVKALKEAID--RDALSGGNIEVAV 187
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-239 2.05e-33

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 120.64  E-value: 2.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQ--TninSLAVRGKDCTVVISQKKVP-DKLLDPTTVSYIFCISRTIGMVVNGPIP 88
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRgtT---TVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  89 DARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAyMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKA 168
Cdd:COG0638   86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285812187 169 TATGPKQQEITTNLENHFKKskidhinEESWEKVVEFAITHMIDAL-GTEFSKNDLEVGVATKDKFFTLSAE 239
Cdd:COG0638  164 VAIGSGSPFARGVLEKEYRE-------DLSLDEAVELALRALYSAAeRDSASGDGIDVAVITEDGFRELSEE 228
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 12-34 2.40e-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: 56.74  E-value: 2.40e-11
                           10        20
                   ....*....|....*....|...
gi 285812187    12 YDRHITIFSPEGRLYQVEYAFKA 34
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 ...
 12-228 6.02e-123

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: 348.46  E-value: 6.02e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 285812187 172 GPKQQEITTNLENHFKKSKidhINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVA 228
Cdd:cd03754  162 GVKEQEATNFLEKKLKKKP---DLIESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-227 1.89e-95

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: 278.56  E-value: 1.89e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTnINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNG-STAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd01911   80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 285812187 172 GPKQQEITTNLENHFKKskidhinEESWEKVVEFAITHMIDALGTEFSKNDLEVGV 227
Cdd:cd01911  160 GKGSQEAKTFLEKRYKK-------DLTLEEAIKLALKALKEVLEEDKKAKNIEIAV 208
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
12-245 3.49e-48

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 159.23  E-value: 3.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTT-AVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285812187 172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKD--KFFTLSAENIEERL 245
Cdd:PRK03996 168 GAGRDTVMEFLEKNYK-------EDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVEtkKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-229 1.77e-46

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: 154.03  E-value: 1.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQtNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKR-GTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03756   81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 285812187 172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVAT 229
Cdd:cd03756  160 GSGRQAVTEFLEKEYK-------EDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 12-239 1.40e-45

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 152.03  E-value: 1.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   12 YDRHITIFSPEGRLYQVEYAFKATNQtNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKR-GTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKD--KFFTLSAE 239
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYR-------EDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEdkKFRKLSVE 223
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 42-227 1.14e-42

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: 143.48  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187   42 SLAVRGKDCTVVISQKKVP--DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDvLAK 119
Cdd:pfam00227   7 IVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  120 RMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKkskiDHINEESW 199
Cdd:pfam00227  86 RIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR----PDLTLEEA 161

                         170       180
                  ....*....|....*....|....*...
gi 285812187  200 EKVVEFAITHMIDalGTEFSKNDLEVGV 227
Cdd:pfam00227 162 VELAVKALKEAID--RDALSGGNIEVAV 187
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-245 9.30e-42

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: 142.46  E-value: 9.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03750    1 YSFSLTTFSPSGKLVQIEYALAAVSSGAP-SVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03750   80 VLVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEG-GPYLYQVDPSGSYFTWKATAI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285812187 172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFT-LSAENIEERL 245
Cdd:cd03750  159 GKNYSNAKTFLEKRYN-------EDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRlLTPAEIKDYL 226
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-185 1.28e-41

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: 141.65  E-value: 1.28e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03751    4 YDLSASTFSPDGRVFQVEYANKAVENSGT-AIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03751   83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGCAI 161

                        170
                 ....*....|....
gi 285812187 172 GPKQQEITTNLENH 185
Cdd:cd03751  162 GKGKQAAKTELEKL 175
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 42-227 1.35e-39

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: 135.32  E-value: 1.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  42 SLAVRGKDCTVVISQKKVPDKLLD-PTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR 120
Cdd:cd01906    3 IVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187 121 MANLSQIYTQraYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKskidhinEESWE 200
Cdd:cd01906   83 LANLLYEYTQ--SLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP-------DMTLE 153

                        170       180
                 ....*....|....*....|....*...
gi 285812187 201 KVVEFAITHMIDALGTEFSKND-LEVGV 227
Cdd:cd01906  154 EAIELALKALKSALERDLYSGGnIEVAV 181
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-189 1.57e-38

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: 133.63  E-value: 1.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVS-YIFCISRTIGMVVNGPIPDA 90
Cdd:cd03752    3 YDSRTTIFSPEGRLYQVEYAMEAISHAGT-CLGILAKDGIVLAAEKKVTSKLLDQSFSSeKIYKIDDHIACAVAGITSDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  91 RNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATA 170
Cdd:cd03752   82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATA 161

                        170
                 ....*....|....*....
gi 285812187 171 TGPKQQEITTNLENHFKKS 189
Cdd:cd03752  162 IGNNNQAAQSLLKQDYKDD 180
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-227 1.02e-36

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: 128.95  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLldpttVSY---IFCISRTIGMVVNGPIP 88
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSA-TVGLKSKTHAVLVALKRATSEL-----SSYqkkIFKVDDHIGIAIAGLTA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  89 DARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDeELGPSIYKTDPAGYYVGYKA 168
Cdd:cd03749   75 DARVLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEYKA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285812187 169 TATGPKQQEITTNLENHFkkskidhinEESWEKVVEFAITHMIDALGT------EFSKNDLEVGV 227
Cdd:cd03749  154 TSIGARSQSARTYLERHF---------EEFEDCSLEELIKHALRALREtlpgeqELTIKNVSIAI 209
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-227 7.34e-35

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 124.01  E-value: 7.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTT-AVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATAT 171
Cdd:cd03755   80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 285812187 172 GPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALgtEFSKNDLEVGV 227
Cdd:cd03755  160 GRNSKTVREFLEKNYK-------EEMTRDDTIKLAIKALLEVV--QSGSKNIELAV 206
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-239 2.05e-33

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 120.64  E-value: 2.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQ--TninSLAVRGKDCTVVISQKKVP-DKLLDPTTVSYIFCISRTIGMVVNGPIP 88
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRgtT---TVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  89 DARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAyMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGYKA 168
Cdd:COG0638   86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 285812187 169 TATGPKQQEITTNLENHFKKskidhinEESWEKVVEFAITHMIDAL-GTEFSKNDLEVGVATKDKFFTLSAE 239
Cdd:COG0638  164 VAIGSGSPFARGVLEKEYRE-------DLSLDEAVELALRALYSAAeRDSASGDGIDVAVITEDGFRELSEE 228
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 12-252 4.22e-33

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 120.73  E-value: 4.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATNQTNInSLAVRGKDCTVVISQKKVPDKLLDP-TTVSYIFCISRTIGMVVNGPIPDA 90
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASL-TVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  91 RNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATA 170
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187 171 TGPKQQEITTNLENHFKkskidhiNEESWEKVVEFAITHMIDALGTEFSKND-LEVGVATKDKF------FTLSAENIEE 243
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWK-------EDLTLEQGLLLAAKVLTKSMDSTSPKADkIEVGILSHGETdgepiqKMLSEKEIAE 236


                 ....*....
gi 285812187 244 RLVAIAEQD 252
Cdd:PTZ00246 237 LLKKVTQEY 245
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-189 7.69e-33

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: 118.98  E-value: 7.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  12 YDRHITIFSPEGRLYQVEYAFKATnQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDAR 91
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAI-KLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  92 NAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIY-----TQRAYMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGY 166
Cdd:cd03753   80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFgegddGKKAMSRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158

                        170       180
                 ....*....|....*....|...
gi 285812187 167 KATATGPKQQEITTNLENHFKKS 189
Cdd:cd03753  159 DAKAIGSGSEGAQSSLQEKYHKD 181
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 41-214 4.26e-25

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: 97.08  E-value: 4.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  41 NSLAVRGKDCTVVISQKKVPDKLLDP-TTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAK 119
Cdd:cd01901    2 TSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187 120 RMANLSQIYTQrayMRPLGVILTFVSVDEElGPSIYKTDPAGYYVGY-KATATGPKQQEITTNLENHFKKskidhinees 198
Cdd:cd01901   82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEG-GGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKP---------- 147

                        170
                 ....*....|....*.
gi 285812187 199 wEKVVEFAITHMIDAL 214
Cdd:cd01901  148 -DMTLEEAVELALKAL 162
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 12-34 5.13e-12

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: 58.52  E-value: 5.13e-12
                          10        20
                  ....*....|....*....|...
gi 285812187   12 YDRHITIFSPEGRLYQVEYAFKA 34
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 ...
 12-34 2.40e-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: 56.74  E-value: 2.40e-11
                           10        20
                   ....*....|....*....|...
gi 285812187    12 YDRHITIFSPEGRLYQVEYAFKA 34
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-172 6.72e-05

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: 42.62  E-value: 6.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812187  72 IFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANlsqIYTQRAYMrPLGVILTFVSVDEElG 151
Cdd:cd03764   34 IFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSN---ILNSSKYF-PYIVQLLIGGVDEE-G 108

                         90       100
                 ....*....|....*....|.
gi 285812187 152 PSIYKTDPAGYYVGYKATATG 172
Cdd:cd03764  109 PHLYSLDPLGSIIEDKYTATG 129
 
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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