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Conserved domains on  [gi|961079314|ref|XP_014767927|]
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proteasome subunit alpha type-5 [Octopus bimaculoides]

Protein Classification

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

proteasome subunit alpha type-5 is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-5 (PSMA5) and Saccharomyces cerevisiae proteasome subunit alpha type-5 (Pup2p)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 4.50e-153

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: 424.06  E-value: 4.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDDDADPGAMSRPFGVALLFAGIDEKGPQLFHMDPSGTFIQYDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961079314 168 KAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 4.50e-153

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: 424.06  E-value: 4.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDDDADPGAMSRPFGVALLFAGIDEKGPQLFHMDPSGTFIQYDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961079314 168 KAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-241 3.75e-99

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 288.66  E-value: 3.75e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAF---GdddadpGAmsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYtqhG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961079314 165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVT-REKNFQMFSKEDLKTIIEEI 241
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-233 2.48e-90

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: 265.67  E-value: 2.48e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALA---FGdddadpGAmsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQytqHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVTRE-KNFQMFSKED 233
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEdKKFRKLSVEE 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-233 1.57e-81

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 243.51  E-value: 1.57e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTC-PLIVASSIEKVLEIDSHIGCAMSGLVAD 84
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  85 SRTMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGdddadPGAMsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYT-----QYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEE-KLDSTNVEMATVTREKnFQMFSKED 233
Cdd:COG0638  161 EKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-220 4.79e-61

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: 190.09  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   31 IKLGSTAIGIQTNDGIVLAVEKRVTCPLIVAS--SIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMS 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSkdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  109 VEsVTQAVSNLALAFGdddadPGAMSRPFGVALLFAGIDEKG-PQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHK 187
Cdd:pfam00227  81 VE-LAARIADLLQAYT-----QYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 961079314  188 SMSLDNARKEALKILQQVME-EKLDSTNVEMATV 220
Cdd:pfam00227 155 DLTLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 8-30 2.82e-11

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 56.35  E-value: 2.82e-11
                           10        20
                   ....*....|....*....|...
gi 961079314     8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 4.50e-153

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: 424.06  E-value: 4.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDDDADPGAMSRPFGVALLFAGIDEKGPQLFHMDPSGTFIQYDA 167
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 961079314 168 KAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATV 220
Cdd:cd03753  161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 2.02e-114

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: 325.94  E-value: 2.02e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDddadpGAMSRPFGVALLFAGIDEK-GPQLFHMDPSGTFIQYD 166
Cdd:cd01911   81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQ-----YGGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 961079314 167 AKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATV 220
Cdd:cd01911  156 ATAIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
8-241 3.75e-99

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 288.66  E-value: 3.75e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAF---GdddadpGAmsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYtqhG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYLE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961079314 165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVT-REKNFQMFSKEDLKTIIEEI 241
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDvETKKFRKLSVEEIEKYLEKL 239
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 8-233 2.48e-90

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: 265.67  E-value: 2.48e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314    8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALA---FGdddadpGAmsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQytqHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGALLE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVTRE-KNFQMFSKED 233
Cdd:TIGR03633 155 YKATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYITVEdKKFRKLSVEE 224
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-221 1.27e-86

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: 255.72  E-value: 1.27e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALA---FGdddadpGAmsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:cd03756   82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQytqHG------GV--RPFGVALLIAGVDDGGPRLFETDPSGAYNE 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961079314 165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVT 221
Cdd:cd03756  154 YKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-233 1.57e-81

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 243.51  E-value: 1.57e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTC-PLIVASSIEKVLEIDSHIGCAMSGLVAD 84
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  85 SRTMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGdddadPGAMsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQ 164
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYT-----QYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 165 YDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEE-KLDSTNVEMATVTREKnFQMFSKED 233
Cdd:COG0638  161 EKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-220 5.57e-66

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


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 203.35  E-value: 5.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLI-VASSIEKVLEIDSHIGCAMSGLVAD 84
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLdQSFSSEKIYKIDDHIACAVAGITSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  85 SRTMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFgdddADPGAMsRPFGVALLFAGIDEK-GPQLFHMDPSGTFI 163
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGY----TQYGGL-RPFGVSFLYAGWDKHyGFQLYQSDPSGNYS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 961079314 164 QYDAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVME-EKLDSTNVEMATV 220
Cdd:cd03752  156 GWKATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDsTKLTSEKLEFATL 213
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-236 3.27e-64

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


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 199.47  E-value: 3.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03750    1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFgdddADPGAMsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQYDA 167
Cdd:cd03750   81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEY----TQSGGV-RPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961079314 168 KAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTNVEMATVTREKNFQMFSKEDLKT 236
Cdd:cd03750  156 TAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKD 224
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-220 1.15e-63

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 196.56  E-value: 1.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  35 STAIGIQTNDGIVLAVEKRVTCPLIVA-SSIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVT 113
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVAsSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 114 QAVSNLALAFGDDdadpgamSRPFGVALLFAGIDEK-GPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMSLD 192
Cdd:cd01906   81 KLLANLLYEYTQS-------LRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLE 153

                        170       180
                 ....*....|....*....|....*....
gi 961079314 193 NARKEALKILQQVMEEKLDS-TNVEMATV 220
Cdd:cd01906  154 EAIELALKALKSALERDLYSgGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-220 4.79e-61

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: 190.09  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   31 IKLGSTAIGIQTNDGIVLAVEKRVTCPLIVAS--SIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMS 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSkdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  109 VEsVTQAVSNLALAFGdddadPGAMSRPFGVALLFAGIDEKG-PQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHK 187
Cdd:pfam00227  81 VE-LAARIADLLQAYT-----QYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 961079314  188 SMSLDNARKEALKILQQVME-EKLDSTNVEMATV 220
Cdd:pfam00227 155 DLTLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-218 1.46e-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: 189.50  E-value: 1.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDDDAdpgamSRPFGVALLFAGIDEKG-PQLFHMDPSGTFIQYD 166
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGG-----VRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961079314 167 AKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEekLDSTNVEMA 218
Cdd:cd03755  156 ANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQ--SGSKNIELA 205
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-220 2.44e-57

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: 181.32  E-value: 2.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   6 SEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADS 85
Cdd:cd03751    2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  86 RTMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFgdddaDPGAMSRPFGVALLFAGIDEKGPQLFHMDPSGTFIQY 165
Cdd:cd03751   82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAY-----TLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961079314 166 DAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLD-STNVEMATV 220
Cdd:cd03751  157 FGCAIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDkAFELELSWV 212
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 8-241 1.58e-55

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 178.12  E-value: 1.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLI-VASSIEKVLEIDSHIGCAMSGLVADSR 86
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLdPGKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  87 TMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFgdddADPGAMsRPFGVALLFAGIDEK-GPQLFHMDPSGTFIQY 165
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSY----TQFGGL-RPFGVSFLFAGYDENlGYQLYHTDPSGNYSGW 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 166 DAKAIGSGSEGAQQALQDVYHKSMSLDNARKEALKILQQVMEEKLDSTN-VEMATVTREKN-----FQMFSKEDLKTIIE 239
Cdd:PTZ00246 160 KATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADkIEVGILSHGETdgepiQKMLSEKEIAELLK 239


                 ..
gi 961079314 240 EI 241
Cdd:PTZ00246 240 KV 241
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 7.17e-55

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: 175.17  E-value: 7.17e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTNDGIVLAVEKRVTCPLivASSIEKVLEIDSHIGCAMSGLVADSRT 87
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADARV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  88 MIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALA----FGdddadpgamSRPFGVALLFAGIDEKGPQLFHMDPSGTFI 163
Cdd:cd03749   79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQIntqrYG---------RRPYGVGLLIAGYDESGPHLFQTCPSGNYF 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961079314 164 QYDAKAIGSGSEGAQQALQDVYH--KSMSLDNARKEALKILQQVM--EEKLDSTNVEMATV 220
Cdd:cd03749  150 EYKATSIGARSQSARTYLERHFEefEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIV 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-220 6.96e-51

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: 165.10  E-value: 6.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314   8 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGIQTNDGIVLAVEKRVTCPLIVASSIEKVLEIDSHIGCAMSGLVADSR 86
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  87 TMIDRARVEAQNHWFTYNEKMSVESVTQAVSNLALAFGDDdadpgAMSRPFGVALLFAGID-EKGPQLFHMDPSGTFIQY 165
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQH-----AYMRPLGVSMILIGIDeELGPQLYKCDPAGYFAGY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 961079314 166 DAKAIGSGSEGAQQALQDVYHK----SMSLDNARKEALKILQQVMEEKLDSTNVEMATV 220
Cdd:cd03754  157 KATAAGVKEQEATNFLEKKLKKkpdlIESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-202 3.98e-44

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: 146.00  E-value: 3.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  35 STAIGIQTNDGIVLAVEKRVTCPLIVA-SSIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVT 113
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 114 QAVSNLALAFGDDdadpgamsRPFGVALLFAGIDEKGPQLFHMDPSGTFIQY-DAKAIGSGSEGAQQALQDVYHKSMSLD 192
Cdd:cd01901   81 KELAKLLQVYTQG--------RPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLE 152

                        170
                 ....*....|
gi 961079314 193 NARKEALKIL 202
Cdd:cd01901  153 EAVELALKAL 162
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-223 8.38e-37

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: 127.75  E-value: 8.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  36 TAIGIQTNDGIVLAVEKRVTCPLIVASS-IEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVTQ 114
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASMGNFIASKnVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 115 AVSNLALafgdddadpGAMSRPFGVALLFAGIDEKGPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMSLDNA 194
Cdd:cd03764   82 LLSNILN---------SSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 961079314 195 RKEALKILQQVMEEKLDS-TNVEMATVTRE 223
Cdd:cd03764  153 KKLAIRAIKSAIERDSASgDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 36-224 2.25e-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: 2.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  36 TAIGIQTNDGIVLAVEKRVTC-PLIVASSIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVTQ 114
Cdd:cd01912    2 TIVGIKGKDGVVLAADTRASAgSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 115 AVSNLaLAfgdddadpGAMSRPFGVALLFAGIDEK-GPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMSLDn 193
Cdd:cd01912   82 LLSNI-LY--------SYRGFPYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLE- 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 961079314 194 arkEALKILQQVMEEKLDS-----TNVEMATVTREK 224
Cdd:cd01912  152 ---EAVELVKKAIDSAIERdlssgGGVDVAVITKDG 184
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-194 6.06e-15

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: 70.74  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  36 TAIGIQTNDGIVLAVEKRVTC-PLIVASSIEKVLEIDSHIGCAMSGLVAD----SRTMidrARvEAQNHWFTYNEKMSVE 110
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAgSYIASQTVKKVIEINPYLLGTMAGGAADcqywERVL---GR-ECRLYELRNKERISVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 111 SVTQAVSNLALAFGDDDADPGAMsrpfgvallFAGIDEKGPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMS 190
Cdd:cd03761   78 AASKLLSNMLYQYKGMGLSMGTM---------ICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLS 148


                 ....
gi 961079314 191 LDNA 194
Cdd:cd03761  149 VEEA 152
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-194 4.92e-13

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 66.55  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  34 GSTAIGIQTNDGIVLAVEKRVTC-PLIVASSIEKVLEIDSHIGCAMSGLVAD----SRTMIDRARV-EAQNhwftyNEKM 107
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADcsfwERELAMQCRLyELRN-----GELI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 108 SVESVTQAVSNLALAFgdddadpgamsRPFGVAL--LFAGIDEKGPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVY 185
Cdd:PTZ00488 114 SVAAASKILANIVWNY-----------KGMGLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGF 182


                 ....*....
gi 961079314 186 HKSMSLDNA 194
Cdd:PTZ00488 183 KWDLNDEEA 191
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-207 3.22e-12

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: 63.01  E-value: 3.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  36 TAIGIQTNDGIVLAVEKRVTCPLIVAS-SIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVTQ 114
Cdd:cd03762    2 TIIAVEYDGGVVLGADSRTSTGSYVANrVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 115 AVSNLALAFGDDdadpgamsrpFGVALLFAGIDE-KGPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMSLDN 193
Cdd:cd03762   82 LFKNLCYNYKEM----------LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEE 151

                        170
                 ....*....|....
gi 961079314 194 ARKEALKILQQVME 207
Cdd:cd03762  152 CIKFVKNALSLAMS 165
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-196 3.58e-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: 62.98  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  36 TAIGIQTNDGIVLAVEKRVTCPLIVAS-SIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESVTQ 114
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEGPIVADkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 115 AVSNLALAFGdddadpGAMsrpfGVALLFAGIDEKGPQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQDVYHKSMSLDNA 194
Cdd:cd03763   82 MLKQHLFRYQ------GHI----GAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEA 151


                 ..
gi 961079314 195 RK 196
Cdd:cd03763  152 KK 153
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 8-30 2.79e-11

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 56.59  E-value: 2.79e-11
                          10        20
                  ....*....|....*....|...
gi 961079314    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 2.82e-11

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 56.35  E-value: 2.82e-11
                           10        20
                   ....*....|....*....|...
gi 961079314     8 YDRGVNTFSPEGRLFQVEYAIEA 30
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-206 7.99e-07

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 48.41  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  34 GSTAIGIQTNDGIVLAVEKRVTCPLIVASSIE-KVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESV 112
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSpKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 113 TQAVSNLalafgdddadpgAMSR---PFGVALLFAGIDEKG-PQLFHMDPSGTFIQYDAKAIGSGSEGAQQALQD-VYHK 187
Cdd:cd03757   88 AQLLSTI------------LYSRrffPYYVFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNqVGRK 155

                        170       180
                 ....*....|....*....|...
gi 961079314 188 SMSL----DNARKEALKILQQVM 206
Cdd:cd03757  156 NQNNvertPLSLEEAVSLVKDAF 178
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-193 3.53e-03

proteasome beta type-3 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: 239728  Cd Length: 195  Bit Score: 37.22  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314  34 GSTAIGIQTNDGIVLAVEKRVTCPLI-VASSIEKVLEIDSHIGCAMSGLVADSRTMIDRARVEAQNHWFTYNEKMSVESV 112
Cdd:cd03759    3 GGAVVAMAGKDCVAIASDLRLGVQQQtVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961079314 113 TQAVSNLALA--FGdddadpgamsrPFGVALLFAGIDEKG-PQLFHMDPSG--TFIQyDAKAIGSGSEGAQQALQDVYHK 187
Cdd:cd03759   83 SSLISSLLYEkrFG-----------PYFVEPVVAGLDPDGkPFICTMDLIGcpSIPS-DFVVSGTASEQLYGMCESLWRP 150


                 ....*.
gi 961079314 188 SMSLDN 193
Cdd:cd03759  151 DMEPDE 156
 
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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