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Conserved domains on  [gi|15219317|ref|NP_178042|]
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N-terminal nucleophile aminohydrolases (Ntn hydrolases) superfamily protein [Arabidopsis thaliana]

Protein Classification

proteasome subunit alpha type-2( domain architecture ID 10132882)

proteasome subunit alpha type-2 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-2 (PSMA2) and Saccharomyces cerevisiae proteasome subunit alpha type-2 (Pre8p)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-232 1.66e-164

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: 453.32  E-value: 1.66e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219317 166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTDKVFRVLTPAEIDDYLA 232
Cdd:cd03750 161 NYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKDYLA 227
 
Name Accession Description Interval E-value
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-232 1.66e-164

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: 453.32  E-value: 1.66e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219317 166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTDKVFRVLTPAEIDDYLA 232
Cdd:cd03750 161 NYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKDYLA 227
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-235 5.16e-85

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 252.45  E-value: 5.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317    6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219317  166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTD-KVFRVLTPAEIDDYLAEVE 235
Cdd:PRK03996 170 GRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVEtKKFRKLSVEEIEKYLEKLL 240
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 32-213 5.93e-67

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: 204.72  E-value: 5.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317    32 GQTSLGIKASNGVVIATEKKLP--SILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVtQ 109
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV-E 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   110 LVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKG-PQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAI 188
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 15219317   189 HTAILTLKEGFEGE-ISSKNIEIGKI 213
Cdd:pfam00227 163 ELAVKALKEAIDRDaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-226 1.29e-60

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 189.97  E-value: 1.29e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   1 MGDSQ---YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLP-SILVDEASVQKIQHLTPNIGTVY 76
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  77 SGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGgVRPFGVSLLVAGYDDKGPQLYQVDPSGSYF 156
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219317 157 SWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEG-EISSKNIEIGKIGTDKvFRVLTPAE 226
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 1.07e-06

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: 44.02  E-value: 1.07e-06
                           10        20
                   ....*....|....*....|...
gi 15219317      6 YSFSLTTFSPSGKLVQIEHALTA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-232 1.66e-164

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: 453.32  E-value: 1.66e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219317 166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTDKVFRVLTPAEIDDYLA 232
Cdd:cd03750 161 NYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETKGFRLLTPAEIKDYLA 227
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-213 1.39e-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: 326.32  E-value: 1.39e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYD-DKGPQLYQVDPSGSYFSWKASAMG 164
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDeEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15219317 165 KNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKI 213
Cdd:cd01911 161 KGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-235 5.16e-85

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 252.45  E-value: 5.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317    6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:PRK03996  90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219317  166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTD-KVFRVLTPAEIDDYLAEVE 235
Cdd:PRK03996 170 GRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIDVEtKKFRKLSVEEIEKYLEKLL 240
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-213 8.56e-75

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: 225.67  E-value: 8.56e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGK 165
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15219317 166 NVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKI 213
Cdd:cd03756 162 GRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYV 209
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-210 3.04e-68

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: 208.76  E-value: 3.04e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   6 YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRV 85
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  86 LVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYD-DKGPQLYQVDPSGSYFSWKASAMG 164
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDpDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15219317 165 KNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGeiSSKNIEI 210
Cdd:cd03755 161 RNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQS--GSKNIEL 204
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 32-213 5.93e-67

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: 204.72  E-value: 5.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317    32 GQTSLGIKASNGVVIATEKKLP--SILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVtQ 109
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV-E 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   110 LVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKG-PQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAI 188
Cdd:pfam00227  83 LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162

                         170       180
                  ....*....|....*....|....*.
gi 15219317   189 HTAILTLKEGFEGE-ISSKNIEIGKI 213
Cdd:pfam00227 163 ELAVKALKEAIDRDaLSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 34-213 1.52e-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: 195.79  E-value: 1.52e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLPS-ILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVR 112
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSgLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 113 ETATVMQEFTQSggVRPFGVSLLVAGYD-DKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTA 191
Cdd:cd01906  82 LLANLLYEYTQS--LRPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 15219317 192 ILTLKEGFEGEISS-KNIEIGKI 213
Cdd:cd01906 160 LKALKSALERDLYSgGNIEVAVI 182
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-218 6.04e-62

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: 192.95  E-value: 6.04e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   4 SQYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEA-SVQKIQHLTPNIGTVYSGMGPD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSfSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  83 FRVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDK-GPQLYQVDPSGSYFSWKAS 161
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15219317 162 AMGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLkegfegeisSKNIEIGKIGTDKV 218
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVL---------SKTMDSTKLTSEKL 208
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-226 1.29e-60

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 189.97  E-value: 1.29e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   1 MGDSQ---YSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLP-SILVDEASVQKIQHLTPNIGTVY 76
Cdd:COG0638   1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  77 SGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGgVRPFGVSLLVAGYDDKGPQLYQVDPSGSYF 156
Cdd:COG0638  81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVDDGGPRLFSTDPSGGLY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219317 157 SWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEG-EISSKNIEIGKIGTDKvFRVLTPAE 226
Cdd:COG0638 160 EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDG-FRELSEEE 229
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-213 4.43e-59

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: 185.62  E-value: 4.43e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  12 TFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSR 91
Cdd:cd03753   7 TFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHAR 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  92 KQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGV-----RPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKN 166
Cdd:cd03753  87 VEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15219317 167 VSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKI 213
Cdd:cd03753 167 SEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-188 6.63e-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: 180.17  E-value: 6.63e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   4 SQYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDF 83
Cdd:cd03751   2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  84 RVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAM 163
Cdd:cd03751  82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAI 161

                       170       180
                ....*....|....*....|....*
gi 15219317 164 GKNVSNAKTFLEKRYTEDMELDDAI 188
Cdd:cd03751 162 GKGKQAAKTELEKLKFSELTCREAV 186
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-211 6.94e-54

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: 172.42  E-value: 6.94e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  10 LTTFSPSGKLVQIEHALTAVG-SGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVR 88
Cdd:cd03754   6 ITIFSPEGRLYQVEYAFKAVKnAGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSRSQVQ 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  89 KSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDD-KGPQLYQVDPSGSYFSWKASAMGKNV 167
Cdd:cd03754  86 RARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEeLGPQLYKCDPAGYFAGYKATAAGVKE 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15219317 168 SNAKTFLEKRYTED----MELDDAIHTAILTLKEGFEGEISSKNIEIG 211
Cdd:cd03754 166 QEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDFKATEIEVG 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 11-214 3.32e-53

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: 170.55  E-value: 3.32e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  11 TTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILvdeASVQ-KIQHLTPNIGTVYSGMGPDFRVLVRK 89
Cdd:cd03749   6 TTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQkKIFKVDDHIGIAIAGLTADARVLSRY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  90 SRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSN 169
Cdd:cd03749  83 MRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15219317 170 AKTFLEKRYT--EDMELDDAIHTAILTLKEGF--EGEISSKNIEIGKIG 214
Cdd:cd03749 163 ARTYLERHFEefEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIVG 211
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-234 5.48e-52

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 168.88  E-value: 5.48e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317    5 QYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEA-SVQKIQHLTPNIGTVYSGMGPDF 83
Cdd:PTZ00246   4 RYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGkINEKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   84 RVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDK-GPQLYQVDPSGSYFSWKASA 162
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219317  163 MGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEI-SSKNIEIGKIGTDK-----VFRVLTPAEIDDYLAEV 234
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILSHGEtdgepIQKMLSEKEIAELLKKV 241
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 34-197 5.54e-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: 145.23  E-value: 5.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLPS-ILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVR 112
Cdd:cd01901   2 TSVAIKGKGGVVLAADKRLSSgLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 113 ETATVMQEFTQsggVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSW-KASAMGKNVSNAKTFLEKRYTEDMELDDAIHTA 191
Cdd:cd01901  82 ELAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELA 158


                ....*.
gi 15219317 192 ILTLKE 197
Cdd:cd01901 159 LKALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-216 9.85e-27

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: 101.56  E-value: 9.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLP-SILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVtqlvR 112
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSI----K 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 113 ETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTAI 192
Cdd:cd03764  78 ALATLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157

                       170       180
                ....*....|....*....|....*
gi 15219317 193 LTLKEGFEGEISSKN-IEIGKIGTD 216
Cdd:cd03764 158 RAIKSAIERDSASGDgIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-221 1.27e-24

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: 95.97  E-value: 1.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLP-SILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVR 112
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 113 ETATVMQEFtQSGgvrPFGVSLLVAGYDDK-GPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTA 191
Cdd:cd01912  82 LLSNILYSY-RGF---PYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELV 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 15219317 192 ILTLKEGFEGEISS-KNIEIGKIGTDKVFRV 221
Cdd:cd01912 158 KKAIDSAIERDLSSgGGVDVAVITKDGVEEL 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-218 2.01e-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: 63.76  E-value: 2.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVI-----ATEkklpSILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEqYLRLYKEpipvt 108
Cdd:cd03763   2 TIVGVVFKDGVVLgadtrATE----GPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLE-LHRLNTG----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 109 QLVR-ETATVM--QE-FTQSGGVrpfGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMEL 184
Cdd:cd03763  72 RKPRvVTALTMlkQHlFRYQGHI---GAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTE 148

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15219317 185 DDAIHTAILTLKEGFEGEI-SSKNIEIGKIGTDKV 218
Cdd:cd03763 149 EEAKKLVCEAIEAGIFNDLgSGSNVDLCVITKDGV 183
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-197 7.86e-10

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: 56.44  E-value: 7.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLP-SILVDEASVQKIQHLTPNIGTVYSGMGPD---FRVLVRKSrkqaeqyLRLYK--EPIPV 107
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAArSILVLKDDEDKIYKLSDHKLMACSGEAGDrlqFAEYIQKN-------IQLYKmrNGYEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 108 TqlVRETAtvmqEFTQ---SGGVR---PFGVSLLVAGYDDK-GPQLYQVDPSGSYFS--WKASAMGKNVSNAktFLEKRY 178
Cdd:cd03758  76 S--PKAAA----NFTRrelAESLRsrtPYQVNLLLAGYDKVeGPSLYYIDYLGTLVKvpYAAHGYGAYFCLS--ILDRYY 147

                       170
                ....*....|....*....
gi 15219317 179 TEDMELDDAIHTAILTLKE 197
Cdd:cd03758 148 KPDMTVEEALELMKKCIKE 166
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 11-187 4.53e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.99  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   11 TTFSPSG-KLVQIEHaltavgsGQTSLGIKASNGVVIATEKKLPS-ILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVR 88
Cdd:PTZ00488  24 TFDHGDAnKAIEFAH-------GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCSFWER 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317   89 KSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFtqsggvRPFGVSL--LVAGYDDKGPQLYQVDPSGSYFSWKASAMGKN 166
Cdd:PTZ00488  97 ELAMQCRLYELRNGELISVAAASKILANIVWNY------KGMGLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSG 170

                        170       180
                 ....*....|....*....|.
gi 15219317  167 VSNAKTFLEKRYTEDMELDDA 187
Cdd:PTZ00488 171 STYAYGVLDAGFKWDLNDEEA 191
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 1.07e-06

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: 44.02  E-value: 1.07e-06
                           10        20
                   ....*....|....*....|...
gi 15219317      6 YSFSLTTFSPSGKLVQIEHALTA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-188 1.38e-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: 47.24  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLPS-ILVDEASVQKIQHLTPNI-GTVySGMGPD----FRVLVRKSRKQaeqYLRlYKEPIPV 107
Cdd:cd03761   2 TTLAFIFQGGVIVAVDSRATAgSYIASQTVKKVIEINPYLlGTM-AGGAADcqywERVLGRECRLY---ELR-NKERISV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317 108 TQLVRETATVMQEFtqsggvRPFGVSL--LVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELD 185
Cdd:cd03761  77 AAASKLLSNMLYQY------KGMGLSMgtMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVE 150


                ...
gi 15219317 186 DAI 188
Cdd:cd03761 151 EAY 153
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 6-28 2.58e-06

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: 42.72  E-value: 2.58e-06
                          10        20
                  ....*....|....*....|...
gi 15219317     6 YSFSLTTFSPSGKLVQIEHALTA 28
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-188 6.21e-06

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: 45.29  E-value: 6.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219317  34 TSLGIKASNGVVIATEKKLP--SILVDEASvQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIpvtqLV 111
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTStgSYVANRVT-DKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPP----LV 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219317 112 RETATVMQEFTQSGGVRpFGVSLLVAGYDD-KGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAI 188
Cdd:cd03762  77 KTAASLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECI 153
 
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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