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Conserved domains on  [gi|24654389|ref|NP_725669|]
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proteasome alpha5 subunit, isoform A [Drosophila melanogaster]

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 ...
 8-222 1.74e-150

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: 417.51  E-value: 1.74e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDsgDSDGAAAMSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGE--GDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24654389 168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTM 222
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 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 ...
 8-222 1.74e-150

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: 417.51  E-value: 1.74e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDsgDSDGAAAMSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGE--GDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24654389 168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTM 222
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-243 1.63e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.40  E-value: 1.63e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHG---GV----RPFGVALLIAGVDDGGPRLFETDPSGAYLEY 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654389  168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMT-KEREFYMFTKEEVEQHIKNI 243
Cdd:PRK03996 163 KATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-235 7.21e-88

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: 259.50  E-value: 7.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389     8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHG---GV----RPFGVALLIAGVDDGGPRLFETDPSGALLEY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654389   168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMT-KEREFYMFTKEE 235
Cdd:TIGR03633 156 KATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITvEDKKFRKLSVEE 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-235 3.81e-73

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 222.33  E-value: 3.81e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRIT-SPLMVPSTVEKIVEVDKHIGCATSGLMAD 84
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  85 ARTLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTF 164
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG--------VRPFGVALLIGGVDDGGPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24654389 165 VRHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEE-KLNSTNVEVMTMTKErEFYMFTKEE 235
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITED-GFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-219 7.03e-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: 184.69  E-value: 7.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    31 IKLGSTAIGICTPEGVVLAVEKRIT--SPLMVPSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMS 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   109 IESCAQAVSTLAIQFGDSGdsdgaaamSRPFGVAILFAGI-EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLF 187
Cdd:pfam00227  81 VELAARIADLLQAYTQYSG--------RRPFGVSLLIAGYdEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 24654389   188 RPDLTLDEAIDISLNTLKQVME-EKLNSTNVEV 219
Cdd:pfam00227 153 RPDLTLEEAVELAVKALKEAIDrDALSGGNIEV 185
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 1.86e-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: 1.86e-11
                           10        20
                   ....*....|....*....|...
gi 24654389      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 ...
 8-222 1.74e-150

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: 417.51  E-value: 1.74e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDsgDSDGAAAMSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGE--GDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24654389 168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTM 222
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 5.81e-110

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: 314.77  E-value: 5.81e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdgaaaMSRPFGVAILFAGI-EAGQPQLWHMDPSGTFVR 166
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYG-------GVRPFGVSLLIAGYdEEGGPQLYQTDPSGTYFG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24654389 167 HGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEV 219
Cdd:cd01911 154 YKATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEI 206
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-243 1.63e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.40  E-value: 1.63e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHG---GV----RPFGVALLIAGVDDGGPRLFETDPSGAYLEY 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24654389  168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMT-KEREFYMFTKEEVEQHIKNI 243
Cdd:PRK03996 163 KATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-235 7.21e-88

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: 259.50  E-value: 7.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389     8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHG---GV----RPFGVALLIAGVDDGGPRLFETDPSGALLEY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24654389   168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMT-KEREFYMFTKEE 235
Cdd:TIGR03633 156 KATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITvEDKKFRKLSVEE 224
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 1.21e-81

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: 243.39  E-value: 1.21e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHG---GV----RPFGVALLIAGVDDGGPRLFETDPSGAYNEY 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24654389 168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEV 219
Cdd:cd03756 155 KATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEI 206
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-235 3.81e-73

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 222.33  E-value: 3.81e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRIT-SPLMVPSTVEKIVEVDKHIGCATSGLMAD 84
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  85 ARTLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTF 164
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG--------VRPFGVALLIGGVDDGGPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24654389 165 VRHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEE-KLNSTNVEVMTMTKErEFYMFTKEE 235
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITED-GFRELSEEE 229
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-240 1.88e-61

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: 192.54  E-value: 1.88e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGdsdGAaamsRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH 167
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSG---GV----RPFGVSLLIAGWDEGGPYLYQVDPSGSYFTW 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654389 168 GAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMTKEREFYMFTKEEVEQHI 240
Cdd:cd03750 154 KATAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-222 4.08e-60

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: 188.34  E-value: 4.08e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGDsdgaaamSRPFGVAILFAGIEA-GQPQLWHMDPSGTFVR 166
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGG-------VRPFGISTLIVGFDPdGTPRLYQTDPSGTYSA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24654389 167 HGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEekLNSTNVEVMTM 222
Cdd:cd03755 154 WKANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQ--SGSKNIELAVM 207
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-222 9.30e-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: 9.30e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  35 STAIGICTPEGVVLAVEKRITSPLMV-PSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCA 113
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 114 QAVSTLAIQFGDSGdsdgaaamsRPFGVAILFAGI-EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLT 192
Cdd:cd01906  81 KLLANLLYEYTQSL---------RPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMT 151

                       170       180       190
                ....*....|....*....|....*....|.
gi 24654389 193 LDEAIDISLNTLKQVMEEKLNS-TNVEVMTM 222
Cdd:cd01906 152 LEEAIELALKALKSALERDLYSgGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-219 7.03e-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: 184.69  E-value: 7.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    31 IKLGSTAIGICTPEGVVLAVEKRIT--SPLMVPSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMS 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   109 IESCAQAVSTLAIQFGDSGdsdgaaamSRPFGVAILFAGI-EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLF 187
Cdd:pfam00227  81 VELAARIADLLQAYTQYSG--------RRPFGVSLLIAGYdEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 24654389   188 RPDLTLDEAIDISLNTLKQVME-EKLNSTNVEV 219
Cdd:pfam00227 153 RPDLTLEEAVELAVKALKEAIDrDALSGGNIEV 185
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-222 4.06e-58

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 183.32  E-value: 4.06e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMAD 84
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSfSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  85 ARTLIERARVECQNHWFVYNERMSIESCAQAVSTLA---IQFGDsgdsdgaaamSRPFGVAILFAGIEAG-QPQLWHMDP 160
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKqgyTQYGG----------LRPFGVSFLYAGWDKHyGFQLYQSDP 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24654389 161 SGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVME-EKLNSTNVEVMTM 222
Cdd:cd03752 151 SGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDsTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-244 9.26e-55

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 176.20  E-value: 9.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMADAR 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGkINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   87 TLIERARVECQNHWFVYNERmsiescaQAVSTLAIQFGDSGDSDGAAAMSRPFGVAILFAGIEAGQP-QLWHMDPSGTFV 165
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEP-------QPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGyQLYHTDPSGNYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  166 RHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTN-VEVMTMTKEREFY-----MFTKEEVEQH 239
Cdd:PTZ00246 158 GWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADkIEVGILSHGETDGepiqkMLSEKEIAEL 237


                 ....*
gi 24654389  240 IKNIA 244
Cdd:PTZ00246 238 LKKVT 242
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-197 1.10e-52

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: 169.38  E-value: 1.10e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADA 85
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  86 RTLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGDsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTFV 165
Cdd:cd03751  82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSS-------VRPFGCSVLLGGYDSDGPQLYMIEPSGVSY 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 24654389 166 RHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAI 197
Cdd:cd03751 155 GYFGCAIGKGKQAAKTELEKLKFSELTCREAV 186
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 6.39e-52

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: 167.47  E-value: 6.39e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLmvPSTVEKIVEVDKHIGCATSGLMADART 87
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADARV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  88 LIERARVECQNHWFVYNERMSIESCAQAVSTLA---IQFgdSGdsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTF 164
Cdd:cd03749  79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAqinTQR--YG--------RRPYGVGLLIAGYDESGPHLFQTCPSGNY 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 165 VRHGAKAIGSGSEGAQQNLQ---DLFrPDLTLDEAIDISLNTLKQVM--EEKLNSTNVEV 219
Cdd:cd03749 149 FEYKATSIGARSQSARTYLErhfEEF-EDCSLEELIKHALRALRETLpgEQELTIKNVSI 207
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-219 5.77e-46

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: 152.39  E-value: 5.77e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADAR 86
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  87 TLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSgdsdgaAAMsRPFGVAILFAGI-EAGQPQLWHMDPSGTFV 165
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQH------AYM-RPLGVSMILIGIdEELGPQLYKCDPAGYFA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24654389 166 RHGAKAIGSGSEGAQQNLQDLFRPD----LTLDEAIDISLNTLKQVMEEKLNSTNVEV 219
Cdd:cd03754 155 GYKATAAGVKEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDFKATEIEV 212
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-205 6.84e-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: 140.22  E-value: 6.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  35 STAIGICTPEGVVLAVEKRITSPLMVP-STVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCA 113
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 114 QAVSTLAIQFGDsgdsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRH-GAKAIGSGSEGAQQNLQDLFRPDLT 192
Cdd:cd01901  81 KELAKLLQVYTQ----------GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMT 150

                       170
                ....*....|...
gi 24654389 193 LDEAIDISLNTLK 205
Cdd:cd01901 151 LEEAVELALKALK 163
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 36-225 3.09e-32

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: 116.39  E-value: 3.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQ 114
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASAGSLVASrNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 115 AVSTlaIQFGDSGDsdgaaamsrPFGVAILFAGI-EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTL 193
Cdd:cd01912  82 LLSN--ILYSYRGF---------PYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTL 150

                       170       180       190
                ....*....|....*....|....*....|...
gi 24654389 194 DEAIDISLNTLKQVMEEKLNS-TNVEVMTMTKE 225
Cdd:cd01912 151 EEAVELVKKAIDSAIERDLSSgGGVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-225 2.93e-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: 111.19  E-value: 2.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQ 114
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASMGNFIASkNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 115 AVSTLAIQFGdsgdsdgaaamSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTLD 194
Cdd:cd03764  82 LLSNILNSSK-----------YFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVE 150

                       170       180       190
                ....*....|....*....|....*....|..
gi 24654389 195 EAIDISLNTLKQVMEEKLNS-TNVEVMTMTKE 225
Cdd:cd03764 151 EAKKLAIRAIKSAIERDSASgDGIDVVVITKD 182
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-225 1.17e-13

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: 67.67  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  34 GSTAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESC 112
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSrDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 113 AQAVSTLAIQ---FgdsgdsdgaaamsrPFGVAILFAGI-EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQ-------- 180
Cdd:cd03757  88 AQLLSTILYSrrfF--------------PYYVFNILAGIdEEGKGVVYSYDPVGSYERETYSAGGSASSLIQplldnqvg 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24654389 181 -QNLQDLFRPDLTLDEAIDIslntLKQVME---EKLNST--NVEVMTMTKE 225
Cdd:cd03757 154 rKNQNNVERTPLSLEEAVSL----VKDAFTsaaERDIYTgdSLEIVIITKD 200
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-199 1.89e-13

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: 66.50  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITSPLMVPS-TVEKIVEVDKHIGCATSGLMADArTLIER--ARvECQNHWFVYNERMSIESC 112
Cdd:cd03761   2 TTLAFIFQGGVIVAVDSRATAGSYIASqTVKKVIEINPYLLGTMAGGAADC-QYWERvlGR-ECRLYELRNKERISVAAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 113 AQAVSTLAIQFGDSGDSdgaaamsrpfgVAILFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLT 192
Cdd:cd03761  80 SKLLSNMLYQYKGMGLS-----------MGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLS 148


                ....*..
gi 24654389 193 LDEAIDI 199
Cdd:cd03761 149 VEEAYDL 155
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 8-30 1.37e-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: 1.37e-11
                          10        20
                  ....*....|....*....|...
gi 24654389     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 1.86e-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: 1.86e-11
                           10        20
                   ....*....|....*....|...
gi 24654389      8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-226 4.22e-11

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: 59.90  E-value: 4.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITS-PLMVPSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQ 114
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEgPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 115 AVSTLAIQFGDSgdsdgaaamsrpFGVAILFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTLD 194
Cdd:cd03763  82 MLKQHLFRYQGH------------IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEE 149

                       170       180       190
                ....*....|....*....|....*....|...
gi 24654389 195 EAIDISLNTLKQVMEEKLNS-TNVEVMTMTKER 226
Cdd:cd03763 150 EAKKLVCEAIEAGIFNDLGSgSNVDLCVITKDG 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-199 2.01e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.45  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389   34 GSTAIGICTPEGVVLAVEKRITS-PLMVPSTVEKIVEVDKHIGCATSGLMADA----RTLIERARV-ECQNhwfvyNERM 107
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCsfweRELAMQCRLyELRN-----GELI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  108 SIESCAQAVSTLAIQFGDSGDSDGAaamsrpfgvaiLFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLF 187
Cdd:PTZ00488 114 SVAAASKILANIVWNYKGMGLSMGT-----------MICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGF 182

                        170
                 ....*....|..
gi 24654389  188 RPDLTLDEAIDI 199
Cdd:PTZ00488 183 KWDLNDEEAQDL 194
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-225 5.73e-08

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: 51.43  E-value: 5.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITSPLMV-PSTVEKIVEVDKHIGCATSGLMADARTLIERarVECQNHWFVY--NERMSIESC 112
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVlKDDEDKIYKLSDHKLMACSGEAGDRLQFAEY--IQKNIQLYKMrnGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 113 AQAV-STLAiqfgDSGDSDGaaamsrPFGVAILFAGIEA-GQPQLWHMDPSGTF--VRHGAKaiGSGSEGAQQNLQDLFR 188
Cdd:cd03758  81 ANFTrRELA----ESLRSRT------PYQVNLLLAGYDKvEGPSLYYIDYLGTLvkVPYAAH--GYGAYFCLSILDRYYK 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24654389 189 PDLTLDEAIDIslntLKQVMEE-----KLNSTNVEVMTMTKE 225
Cdd:cd03758 149 PDMTVEEALEL----MKKCIKElkkrfIINLPNFTVKVVDKD 186
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-209 9.30e-08

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: 50.69  E-value: 9.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389  36 TAIGICTPEGVVLAVEKRITSPLMVPSTV-EKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQ 114
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANRVtDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654389 115 AVSTLAIQFGDSgdsdgaaamsrpfgvaiLFAGI------EAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFR 188
Cdd:cd03762  82 LFKNLCYNYKEM-----------------LSAGIivagwdEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYK 144

                       170       180
                ....*....|....*....|.
gi 24654389 189 PDLTLDEAIDISLNTLKQVME 209
Cdd:cd03762 145 PGMTLEECIKFVKNALSLAMS 165
 
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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