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Conserved domains on  [gi|354497813|ref|XP_003511013|]
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proteasome subunit alpha type-5 [Cricetulus griseus]

Protein Classification

proteasome subunit alpha type-5( domain architecture ID 10132896)

proteasome subunit alpha type-5 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-5 (PSMA5) and Saccharomyces cerevisiae proteasome subunit alpha type-5 (Pup2p)

Gene Ontology:  GO:0019773|GO:0043161
PubMed:  7682410|7697118|8882582|1317508

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 1.17e-155

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: 430.61  E-value: 1.17e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 354497813 168 RAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 1.17e-155

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: 430.61  E-value: 1.17e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 354497813 168 RAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-241 6.16e-98

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 285.57  E-value: 6.16e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKqqyTQHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354497813 165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQ-PGQNFHMFTKEELEEVIKDI 241
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-233 9.22e-89

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: 261.82  E-value: 9.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKqqyTQHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQ-PGQNFHMFTKEE 233
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITvEDKKFRKLSVEE 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-233 2.53e-74

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 225.02  E-value: 2.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRIT-SPLMEPSSIEKIVEIDAHIGCAMSGLIAD 84
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  85 AKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGeedadPGAMsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYT-----QYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEE-KLNATNIELATVQPGQnFHMFTKEE 233
Cdd:COG0638  161 EKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-220 8.15e-59

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: 184.31  E-value: 8.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   31 IKLGSTAIGIQTSEGVCLAVEKRIT--SPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMT 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  109 VESVTQAVSNLA--LQFGeedadpgaMSRPFGVALLFGGVDEKG-PQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVY 185
Cdd:pfam00227  81 VELAARIADLLQayTQYS--------GRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 354497813  186 HKSMTLKEAIKSSLIILKQVME-EKLNATNIELATV 220
Cdd:pfam00227 153 RPDLTLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 1.80e-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: 57.12  E-value: 1.80e-11
                           10        20
                   ....*....|....*....|...
gi 354497813     8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 1.17e-155

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: 430.61  E-value: 1.17e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 354497813 168 RAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 9.90e-115

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: 326.71  E-value: 9.90e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEdadpgAMSRPFGVALLFGGVDEK-GPQLFHMDPSGTFVQCD 166
Cdd:cd01911   81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQY-----GGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 354497813 167 ARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd01911  156 ATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-241 6.16e-98

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 285.57  E-value: 6.16e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKqqyTQHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354497813 165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQ-PGQNFHMFTKEELEEVIKDI 241
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-233 9.22e-89

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: 261.82  E-value: 9.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKqqyTQHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQ-PGQNFHMFTKEE 233
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITvEDKKFRKLSVEE 224
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 1.05e-84

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: 251.10  E-value: 1.05e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:cd03756   82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKqqyTQHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYNE 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 354497813 165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd03756  154 YKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYV 209
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-233 2.53e-74

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 225.02  E-value: 2.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRIT-SPLMEPSSIEKIVEIDAHIGCAMSGLIAD 84
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  85 AKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGeedadPGAMsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYT-----QYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 165 CDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEE-KLNATNIELATVQPGQnFHMFTKEE 233
Cdd:COG0638  161 EKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-220 3.64e-66

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: 203.73  E-value: 3.64e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPS-SIEKIVEIDAHIGCAMSGLIAD 84
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSfSSEKIYKIDDHIACAVAGITSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  85 AKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGeedadpGAmsRPFGVALLFGGVDEK-GPQLFHMDPSG 160
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKqgyTQYG------GL--RPFGVSFLYAGWDKHyGFQLYQSDPSG 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 354497813 161 TFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVME-EKLNATNIELATV 220
Cdd:cd03752  153 NYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDsTKLTSEKLEFATL 213
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-240 6.63e-64

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 198.70  E-value: 6.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03750    1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEdadpGAMsRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDA 167
Cdd:cd03750   81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQS----GGV-RPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 354497813 168 RAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEEleevIKD 240
Cdd:cd03750  156 TAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAE----IKD 224
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-218 3.04e-62

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: 193.73  E-value: 3.04e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDAdpgamSRPFGVALLFGGVDEKG-PQLFHMDPSGTFVQCD 166
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGG-----VRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 354497813 167 ARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEekLNATNIELA 218
Cdd:cd03755  156 ANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQ--SGSKNIELA 205
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-220 7.36e-60

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: 186.55  E-value: 7.36e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  35 STAIGIQTSEGVCLAVEKRITSPLME-PSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVT 113
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 114 QAVSNLALQFGEEdadpgamSRPFGVALLFGGVDEK-GPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLK 192
Cdd:cd01906   81 KLLANLLYEYTQS-------LRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLE 153

                        170       180
                 ....*....|....*....|....*....
gi 354497813 193 EAIKSSLIILKQVMEE-KLNATNIELATV 220
Cdd:cd01906  154 EAIELALKALKSALERdLYSGGNIEVAVI 182
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-241 7.61e-59

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 186.60  E-value: 7.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSI-EKIVEIDAHIGCAMSGLIADAK 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKInEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  87 TLIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFGEedadpgamSRPFGVALLFGGVDEK-GPQLFHMDPSGTF 162
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKqsyTQFGG--------LRPFGVSFLFAGYDENlGYQLYHTDPSGNY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 163 VQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKL-NATNIELATVQPGQN-----FHMFTKEELEE 236
Cdd:PTZ00246 157 SGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILSHGETdgepiQKMLSEKEIAE 236


                 ....*
gi 354497813 237 VIKDI 241
Cdd:PTZ00246 237 LLKKV 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-220 8.15e-59

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: 184.31  E-value: 8.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   31 IKLGSTAIGIQTSEGVCLAVEKRIT--SPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMT 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  109 VESVTQAVSNLA--LQFGeedadpgaMSRPFGVALLFGGVDEKG-PQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVY 185
Cdd:pfam00227  81 VELAARIADLLQayTQYS--------GRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 354497813  186 HKSMTLKEAIKSSLIILKQVME-EKLNATNIELATV 220
Cdd:pfam00227 153 RPDLTLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-220 1.61e-56

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: 179.40  E-value: 1.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADA 85
Cdd:cd03751    2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  86 KTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDAdpgamSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQC 165
Cdd:cd03751   82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSS-----VRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 354497813 166 DARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEE-KLNATNIELATV 220
Cdd:cd03751  157 FGCAIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEiKDKAFELELSWV 212
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 2.10e-54

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: 173.63  E-value: 2.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLmePSSIEKIVEIDAHIGCAMSGLIADAKT 87
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADARV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  88 LIDKARVETQNHWFTYNETMTVESVTQAVSNLA---LQFgeedadpgAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQ 164
Cdd:cd03749   79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAqinTQR--------YGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 165 CDARAIGSASEGAQSSLQEVYH--KSMTLKEAIKSSLIILKQVM--EEKLNATNIELATV 220
Cdd:cd03749  151 YKATSIGARSQSARTYLERHFEefEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIV 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 1.25e-47

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: 156.63  E-value: 1.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAK 86
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  87 TLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEdadpgAMSRPFGVALLFGGVD-EKGPQLFHMDPSGTFVQC 165
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQH-----AYMRPLGVSMILIGIDeELGPQLYKCDPAGYFAGY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 354497813 166 DARAIGSASEGAQSSLQEVYHK----SMTLKEAIKSSLIILKQVMEEKLNATNIELATV 220
Cdd:cd03754  157 KATAAGVKEQEATNFLEKKLKKkpdlIESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-203 4.41e-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: 140.61  E-value: 4.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  35 STAIGIQTSEGVCLAVEKRITSPLMEP-SSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVT 113
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 114 QAVSNLALQFGEedadpgamSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQC-DARAIGSASEGAQSSLQEVYHKSMTLK 192
Cdd:cd01901   81 KELAKLLQVYTQ--------GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLE 152

                        170
                 ....*....|.
gi 354497813 193 EAIKSSLIILK 203
Cdd:cd01901  153 EAVELALKALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-237 9.30e-30

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: 109.65  E-value: 9.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKRIT-SPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQ 114
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 115 AVSNLALQFGeedadpgamSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEA 194
Cdd:cd03764   82 LLSNILNSSK---------YFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 354497813 195 IKSSLIILKQVMEEKL-NATNIELATVqpgqnfhmfTKEELEEV 237
Cdd:cd03764  153 KKLAIRAIKSAIERDSaSGDGIDVVVI---------TKDGYKEL 187
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 36-208 2.95e-29

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: 108.30  E-value: 2.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKRIT-SPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQ 114
Cdd:cd01912    2 TIVGIKGKDGVVLAADTRASaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 115 AVSNLALQFGEEdadpgamsrPFGVALLFGGVDEK-GPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKE 193
Cdd:cd01912   82 LLSNILYSYRGF---------PYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEE 152

                        170
                 ....*....|....*
gi 354497813 194 AIKssliILKQVMEE 208
Cdd:cd01912  153 AVE----LVKKAIDS 163
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-196 2.99e-12

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: 63.37  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKRITS-PLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQ 114
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEgPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 115 AVSNLALQFGeedadpGAMsrpfGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEA 194
Cdd:cd03763   82 MLKQHLFRYQ------GHI----GAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEA 151


                 ..
gi 354497813 195 IK 196
Cdd:cd03763  152 KK 153
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 8-30 1.45e-11

Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 57.36  E-value: 1.45e-11
                          10        20
                  ....*....|....*....|...
gi 354497813    8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 1.80e-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: 57.12  E-value: 1.80e-11
                           10        20
                   ....*....|....*....|...
gi 354497813     8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-195 1.68e-10

proteasome beta type-5 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: 239730  Cd Length: 188  Bit Score: 58.41  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKRITS-PLMEPSSIEKIVEIDAHIGCAMSGLIADA---KTLIDKarvETQNHWFTYNETMTVES 111
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAgSYIASQTVKKVIEINPYLLGTMAGGAADCqywERVLGR---ECRLYELRNKERISVAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 112 VTQAVSNLALQFGEEDADPGAMsrpfgvallFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTL 191
Cdd:cd03761   79 ASKLLSNMLYQYKGMGLSMGTM---------ICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSV 149


                 ....
gi 354497813 192 KEAI 195
Cdd:cd03761  150 EEAY 153
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-196 2.95e-09

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: 54.92  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKRITS-PLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQ 114
Cdd:cd03762    2 TIIAVEYDGGVVLGADSRTSTgSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 115 AVSNLALQFGEEdadpgamsrpFGVALLFGGVDE-KGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKE 193
Cdd:cd03762   82 LFKNLCYNYKEM----------LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEE 151


                 ...
gi 354497813 194 AIK 196
Cdd:cd03762  152 CIK 154
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-194 5.82e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.99  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  34 GSTAIGIQTSEGVCLAVEKRITS-PLMEPSSIEKIVEIDAHIGCAMSGLIADA----KTLIDKARV-ETQNhwftyNETM 107
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCsfweRELAMQCRLyELRN-----GELI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 108 TVESVTQAVSNLALQFgeedadpgamsRPFGVAL--LFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVY 185
Cdd:PTZ00488 114 SVAAASKILANIVWNY-----------KGMGLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGF 182


                 ....*....
gi 354497813 186 HKSMTLKEA 194
Cdd:PTZ00488 183 KWDLNDEEA 191
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-208 3.14e-07

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: 49.12  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  36 TAIGIQTSEGVCLAVEKritsplMEPSSI-------EKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMT 108
Cdd:cd03758    3 TLIGIKGKDFVILAADT------SAARSIlvlkddeDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 109 VESVTQAV-SNLA--LQfgeedadpgamSR-PFGVALLFGGVDEK-GPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQE 183
Cdd:cd03758   77 PKAAANFTrRELAesLR-----------SRtPYQVNLLLAGYDKVeGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR 145

                        170       180
                 ....*....|....*....|....*
gi 354497813 184 VYHKSMTLKEAIKssliILKQVMEE 208
Cdd:cd03758  146 YYKPDMTVEEALE----LMKKCIKE 166
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-196 5.83e-07

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: 48.79  E-value: 5.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813  34 GSTAIGIQTSEGVCLAVEKRITSPLMEPSSIE-KIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESV 112
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSpKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354497813 113 TQAVSNLALQ---FgeedadpgamsrPFGVALLFGGVDEKG-PQLFHMDPSGTFVQCDARAIGSASEGAQSSL------- 181
Cdd:cd03757   88 AQLLSTILYSrrfF------------PYYVFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLdnqvgrk 155

                        170
                 ....*....|....*..
gi 354497813 182 --QEVYHKSMTLKEAIK 196
Cdd:cd03757  156 nqNNVERTPLSLEEAVS 172
 
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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