NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1938941383|pdb|6J2C|m]
View 

Chain m, Proteasome subunit alpha type-5

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 6.98e-129

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: 363.58  E-value: 6.98e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGaSGEERLMSRPFGVALLIAGHDAdDGYQLFHAEPSGTFYRY 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEG-DDGKKAMSRPFGVALLIAGVDE-NGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCI 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 6.98e-129

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: 363.58  E-value: 6.98e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGaSGEERLMSRPFGVALLIAGHDAdDGYQLFHAEPSGTFYRY 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEG-DDGKKAMSRPFGVALLIAGVDE-NGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCI 222
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-245 2.41e-88

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 262.08  E-value: 2.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGE--GAsgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTFY 165
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQhgGV--------RPFGVALLIAGVD-DGGPRLFETDPSGAYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       166 RYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDG-FKIYDNEKTAELIKELK 244
Cdd:PRK03996 161 EYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKkFRKLSVEEIEKYLEKLL 240


                 .
6J2C_m       245 E 245
Cdd:PRK03996 241 K 241
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-235 2.65e-82

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: 246.02  E-value: 2.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m          8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGE--GAsgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTFY 165
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQhgGV--------RPFGVALLIAGVD-DGGPRLFETDPSGALL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6J2C_m        166 RYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDG-FKIYDNEK 235
Cdd:TIGR03633 154 EYKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEDKkFRKLSVEE 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-234 1.26e-68

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 211.54  E-value: 1.26e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        6 SEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRAT-SPLLESDSIEKIVEIDRHIGCAMSGLTAD 84
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       85 ARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGAsgeerlmSRPFGVALLIAGHDaDDGYQLFHAEPSGTF 164
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-------VRPFGVALLIGGVD-DGGPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6J2C_m      165 YRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEE-KLDENNAQLSCITKqDGFKIYDNE 234
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITE-DGFRELSEE 228
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-219 1.34e-57

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 182.00  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         31 IKLGSTAIGIATKEGVVLGVEKRAT--SPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDIN 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        109 VEsLTQSVCDLALRFGEGASGeerlmsRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWH 188
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGR------RPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR 153

                         170       180       190
                  ....*....|....*....|....*....|..
6J2C_m        189 SSLTLKEAELLVLKILKQVME-EKLDENNAQL 219
Cdd:pfam00227 154 PDLTLEEAVELAVKALKEAIDrDALSGGNIEV 185
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 8.43e-10

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: 52.50  E-value: 8.43e-10
                           10        20
                   ....*....|....*....|...
6J2C_m           8 YDRGVSTFSPEGRLFQVEYSLEA 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 6.98e-129

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: 363.58  E-value: 6.98e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGaSGEERLMSRPFGVALLIAGHDAdDGYQLFHAEPSGTFYRY 167
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEG-DDGKKAMSRPFGVALLIAGVDE-NGPQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCI 222
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-216 4.04e-107

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: 308.22  E-value: 4.04e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGAsgeerlMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRY 167
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYG------GVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGY 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENN 216
Cdd:cd01911 155 KATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKN 203
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-245 2.41e-88

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 262.08  E-value: 2.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGE--GAsgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTFY 165
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQhgGV--------RPFGVALLIAGVD-DGGPRLFETDPSGAYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       166 RYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDG-FKIYDNEKTAELIKELK 244
Cdd:PRK03996 161 EYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVETKkFRKLSVEEIEKYLEKLL 240


                 .
6J2C_m       245 E 245
Cdd:PRK03996 241 K 241
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-235 2.65e-82

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: 246.02  E-value: 2.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m          8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGE--GAsgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTFY 165
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQhgGV--------RPFGVALLIAGVD-DGGPRLFETDPSGALL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6J2C_m        166 RYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDG-FKIYDNEK 235
Cdd:TIGR03633 154 EYKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEDKkFRKLSVEE 224
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-223 1.88e-79

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: 238.38  E-value: 1.88e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLA---LRFGeGAsgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTF 164
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKqqyTQHG-GV--------RPFGVALLIAGVD-DGGPRLFETDPSGAY 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
6J2C_m      165 YRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCIT 223
Cdd:cd03756 152 NEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-209 1.53e-69

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: 213.36  E-value: 1.53e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        6 SEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESD-SIEKIVEIDRHIGCAMSGLTAD 84
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSfSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       85 ARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASgeerlmSRPFGVALLIAGHDADDGYQLFHAEPSGTF 164
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGG------LRPFGVSFLYAGWDKHYGFQLYQSDPSGNY 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
6J2C_m      165 YRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVME 209
Cdd:cd03752 155 SGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMD 199
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-234 1.26e-68

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 211.54  E-value: 1.26e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        6 SEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRAT-SPLLESDSIEKIVEIDRHIGCAMSGLTAD 84
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       85 ARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGAsgeerlmSRPFGVALLIAGHDaDDGYQLFHAEPSGTF 164
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-------VRPFGVALLIGGVD-DGGPRLFSTDPSGGL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6J2C_m      165 YRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEE-KLDENNAQLSCITKqDGFKIYDNE 234
Cdd:COG0638 159 YEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITE-DGFRELSEE 228
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-253 1.25e-62

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 197.00  E-value: 1.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE-SDSIEKIVEIDRHIGCAMSGLTADAR 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDpGKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        87 SMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASgeerlmSRPFGVALLIAGHDADDGYQLFHAEPSGTFYR 166
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGG------LRPFGVSFLFAGYDENLGYQLYHTDPSGNYSG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       167 YNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNA-QLSCITKQDG-----FKIYDNEKTAELI 240
Cdd:PTZ00246 159 WKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKiEVGILSHGETdgepiQKMLSEKEIAELL 238

                        250
                 ....*....|...
6J2C_m       241 KELKEKEAAESPE 253
Cdd:PTZ00246 239 KKVTQEYAKENTN 251
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-209 7.41e-59

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: 185.64  E-value: 7.41e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEgaSGEerlmSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRY 167
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQ--SGG----VRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAW 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVME 209
Cdd:cd03755 155 KANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQ 196
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-219 1.34e-57

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 182.00  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m         31 IKLGSTAIGIATKEGVVLGVEKRAT--SPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDIN 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        109 VEsLTQSVCDLALRFGEGASGeerlmsRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWH 188
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGR------RPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYR 153

                         170       180       190
                  ....*....|....*....|....*....|..
6J2C_m        189 SSLTLKEAELLVLKILKQVME-EKLDENNAQL 219
Cdd:pfam00227 154 PDLTLEEAVELAVKALKEAIDrDALSGGNIEV 185
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-213 6.72e-56

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: 177.30  E-value: 6.72e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       35 STAIGIATKEGVVLGVEKRATSPLLE-SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLT 113
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      114 QSVCDLALRFgegasgeeRLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTL 193
Cdd:cd01906  81 KLLANLLYEY--------TQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTL 152

                       170       180
                ....*....|....*....|
6J2C_m      194 KEAELLVLKILKQVMEEKLD 213
Cdd:cd01906 153 EEAIELALKALKSALERDLY 172
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-215 8.52e-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: 178.24  E-value: 8.52e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        6 SEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADA 85
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       86 RSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASgeerlmSRPFGVALLIAGHDaDDGYQLFHAEPSGTFY 165
Cdd:cd03751  82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSS------VRPFGCSVLLGGYD-SDGPQLYMIEPSGVSY 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
6J2C_m      166 RYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDEN 215
Cdd:cd03751 155 GYFGCAIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKA 204
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-216 1.86e-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: 174.79  E-value: 1.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLleSDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADARV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRfgegasGEERLMSRPFGVALLIAGHDaDDGYQLFHAEPSGTFYRY 167
Cdd:cd03749  79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQI------NTQRYGRRPYGVGLLIAGYD-ESGPHLFQTCPSGNYFEY 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHS--SLTLKEAELLVLKILKQVM--EEKLDENN 216
Cdd:cd03749 152 KATSIGARSQSARTYLERHFEEfeDCSLEELIKHALRALRETLpgEQELTIKN 204
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-230 1.59e-51

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: 167.50  E-value: 1.59e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARS 87
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       88 MIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEgaSGEerlmSRPFGVALLIAGHDaDDGYQLFHAEPSGTFYRY 167
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQ--SGG----VRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTW 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
6J2C_m      168 NAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKI 230
Cdd:cd03750 154 KATAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRL 216
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-212 1.66e-40

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: 138.91  E-value: 1.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        8 YDRGVSTFSPEGRLFQVEYSLEAIKLGS-TAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADAR 86
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       87 SMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASgeerlMsRPFGVALLIAGHDADDGYQLFHAEPSGTFYR 166
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAY-----M-RPLGVSMILIGIDEELGPQLYKCDPAGYFAG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
6J2C_m      167 YNAKAIGSGSEGAQAELLNEWHS----SLTLKEAELLVLKILKQVMEEKL 212
Cdd:cd03754 156 YKATAAGVKEQEATNFLEKKLKKkpdlIESYEETVELAISCLQTVLSTDF 205
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-205 3.99e-39

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: 133.67  E-value: 3.99e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       35 STAIGIATKEGVVLGVEKRATSPLLE-SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLT 113
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      114 QSVCDLALRFGEGasgeerlmsRPFGVALLIAGHDaDDGYQLFHAEPSGTFYRY-NAKAIGSGSEGAQAELLNEWHSSLT 192
Cdd:cd01901  81 KELAKLLQVYTQG---------RPFGVNLIVAGVD-EGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMT 150

                       170
                ....*....|...
6J2C_m      193 LKEAELLVLKILK 205
Cdd:cd01901 151 LEEAVELALKALK 163
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 36-209 1.47e-23

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: 94.05  E-value: 1.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRAT-SPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQ 114
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      115 SVCDLALRFGEGasgeerlmsrPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLK 194
Cdd:cd01912  82 LLSNILYSYRGF----------PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLE 151

                       170
                ....*....|....*
6J2C_m      195 EAELLVLKILKQVME 209
Cdd:cd01912 152 EAVELVKKAIDSAIE 166
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-232 4.56e-19

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: 81.92  E-value: 4.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRAT-SPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTq 114
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      115 svcdlalrfgegasgeeRLMS--------RPFGVALLIAGHDaDDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNE 186
Cdd:cd03764  81 -----------------TLLSnilnsskyFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDE 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
6J2C_m      187 WHSSLTLKEAELLVLKILKQVMEEKLDE-NNAQLSCITKqDGFKIYD 232
Cdd:cd03764 143 YKEDMTVEEAKKLAIRAIKSAIERDSASgDGIDVVVITK-DGYKELE 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-200 3.94e-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: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRATS-PLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQ 114
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEgPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      115 SVCDLALRFGEGasgeerlmsrpFGVALLIAGHDAdDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLK 194
Cdd:cd03763  82 MLKQHLFRYQGH-----------IGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEE 149


                ....*.
6J2C_m      195 EAELLV 200
Cdd:cd03763 150 EAKKLV 155
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 8-30 4.39e-10

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: 53.51  E-value: 4.39e-10
                          10        20
                  ....*....|....*....|...
6J2C_m          8 YDRGVSTFSPEGRLFQVEYSLEA 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 8.43e-10

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: 52.50  E-value: 8.43e-10
                           10        20
                   ....*....|....*....|...
6J2C_m           8 YDRGVSTFSPEGRLFQVEYSLEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-209 1.78e-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: 55.69  E-value: 1.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRATS-PLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQ 114
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTgSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      115 SVCDLALRFgegasgEERLMSrpfgvALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLK 194
Cdd:cd03762  82 LFKNLCYNY------KEMLSA-----GIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLE 150

                       170
                ....*....|....*
6J2C_m      195 EAELLVLKILKQVME 209
Cdd:cd03762 151 ECIKFVKNALSLAMS 165
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-196 1.26e-06

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: 47.62  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRATS-PLLESDSIEKIVEIDRHIGCAMSGLTADA----RSMIEHARtaavTHNLYYDEDINVE 110
Cdd:cd03761   2 TTLAFIFQGGVIVAVDSRATAgSYIASQTVKKVIEINPYLLGTMAGGAADCqyweRVLGRECR----LYELRNKERISVA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      111 SLTQSVCDLALRF-GEGASgeerlmsrpfgVALLIAGHDaDDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHS 189
Cdd:cd03761  78 AASKLLSNMLYQYkGMGLS-----------MGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRY 145


                ....*..
6J2C_m      190 SLTLKEA 196
Cdd:cd03761 146 DLSVEEA 152
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-210 6.89e-06

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: 45.65  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       36 TAIGIATKEGVVLGVEKRAT-SPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHartaaVTHNL-YYDEDINVESLT 113
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAArSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEY-----IQKNIqLYKMRNGYELSP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m      114 QSvcdlALRF--GEGAsgeERLMSR-PFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSS 190
Cdd:cd03758  78 KA----AANFtrRELA---ESLRSRtPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPD 150

                       170       180
                ....*....|....*....|
6J2C_m      191 LTLKEAellvLKILKQVMEE 210
Cdd:cd03758 151 MTVEEA----LELMKKCIKE 166
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-199 1.47e-05

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 44.98  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m        34 GSTAIGIATKEGVVLGVEKRATS-PLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESL 112
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6J2C_m       113 TQSVCDLALRFgegasgeerlmsRPFGVAL--LIAGHDaDDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSS 190
Cdd:PTZ00488 119 SKILANIVWNY------------KGMGLSMgtMICGWD-KKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWD 185


                 ....*....
6J2C_m       191 LTLKEAELL 199
Cdd:PTZ00488 186 LNDEEAQDL 194
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH