NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15233268|ref|NP_188850|]
View 

20S proteasome alpha subunit C1 [Arabidopsis thaliana]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132891)

proteasome subunit alpha belonging to the peptidase T1A family, is a component of the proteasome complex that is involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-4 and fungal proteasome subunit alpha type-3

Gene Ontology:  GO:0051603|GO:0005839
PubMed:  7682410|7697118|1317508|8882582

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 6.21e-163

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: 449.49  E-value: 6.21e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  83 ANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAA 162
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233268 163 AVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 6.21e-163

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: 449.49  E-value: 6.21e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  83 ANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAA 162
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233268 163 AVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-218 5.44e-122

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 347.22  E-value: 5.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIM 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   81 SDANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233268  161 AAAVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAevYLT 218
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVG--ILS 216
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-231 1.79e-91

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: 268.75  E-value: 1.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268     5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPS-SIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233268   165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDStSLTSEKLELAEVyltPSKTVKYHVHSPE 231
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVED-KLTPENVEVAYI---TVEDKKFRKLSVE 223
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-215 2.61e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 228.11  E-value: 2.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFgGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:COG0638  89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAI 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:COG0638 167 GSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVI 217
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-215 3.34e-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: 205.88  E-value: 3.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    30 NAGSAIGILSKDGVVLIGEKKVTSK-LLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVE 108
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   109 qLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEA 188
Cdd:pfam00227  83 -LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 15233268   189 VELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 9.38e-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: 55.20  E-value: 9.38e-11
                           10        20
                   ....*....|....*....|...
gi 15233268      5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 6.21e-163

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: 449.49  E-value: 6.21e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  83 ANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAA 162
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233268 163 AVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 1.49e-122

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: 347.12  E-value: 1.49e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPS-SVEKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTsLTSEKLELAEV 215
Cdd:cd01911 160 GKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEED-KKAKNIEIAVV 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-218 5.44e-122

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 347.22  E-value: 5.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIM 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   81 SDANILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233268  161 AAAVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAevYLT 218
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVG--ILS 216
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-237 1.05e-95

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 280.18  E-value: 1.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPS-SIEKIFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYLEYKATAI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233268  165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDStSLTSEKLELAEVyltPSKTVKYHVHSPESLTKLL 237
Cdd:PRK03996 168 GAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEG-KLDPENVEIAYI---DVETKKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 6.12e-92

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: 269.59  E-value: 6.12e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:cd03756  81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYNEYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTsLTSEKLELAEV 215
Cdd:cd03756 160 GSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEEN-ETPENVEIAYV 209
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-231 1.79e-91

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: 268.75  E-value: 1.79e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268     5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPS-SIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDD-GGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233268   165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDStSLTSEKLELAEVyltPSKTVKYHVHSPE 231
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVED-KLTPENVEVAYI---TVEDKKFRKLSVE 223
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-215 2.61e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 228.11  E-value: 2.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFgGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:COG0638  89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAI 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:COG0638 167 GSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVI 217
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 2.94e-73

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: 222.21  E-value: 2.94e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTkqgYTQFGGL--------RPFGVSFLFAGWDKhHGFQLYMSDPSGNY 156
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDL---ALQFGEGddgkkamsRPFGVALLIAGVDE-NGPQLFHTDPSGTF 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15233268 157 GGWKAAAVGANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTsLTSEKLELAEV 215
Cdd:cd03753 156 TRCDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEK-LNSTNVELATV 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-204 3.78e-72

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: 219.16  E-value: 3.78e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLlQTSTSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKL-QDPRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMDSTS 204
Cdd:cd03755 160 GRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGS 199
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-215 6.60e-71

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: 215.05  E-value: 6.60e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  32 GSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQLV 111
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 112 QSLCDTKQGYTQFggLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVEL 191
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                       170       180
                ....*....|....*....|....
gi 15233268 192 ALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:cd01906 159 ALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-215 3.34e-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: 205.88  E-value: 3.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268    30 NAGSAIGILSKDGVVLIGEKKVTSK-LLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVE 108
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   109 qLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEA 188
Cdd:pfam00227  83 -LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 15233268   189 VELALKVLTKTMDSTSLTSEKLELAEV 215
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-233 2.96e-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: 199.86  E-value: 2.96e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  10 TIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDANILINT 89
Cdd:cd03750   6 TTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDES-SVHKVEQITPHIGMVYSGMGPDFRVLVKK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  90 ARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAVGANNQ 169
Cdd:cd03750  85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKATAIGKNYS 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233268 170 AAQSILKQDYKDDATREEAVELALKVLTKTMDsTSLTSEKLELAEVYltpsKTVKYHVHSPESL 233
Cdd:cd03750 164 NAKTFLEKRYNEDLELEDAIHTAILTLKEGFE-GQMTEKNIEIGICG----ETKGFRLLTPAEI 222
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 1.34e-62

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: 195.20  E-value: 1.34e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLlqtSTSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDE-SGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15233268 165 GANNQAAQSILKQDYK--DDATREEAVELALKVLTKTMDSTS-LTSEKLELAEV 215
Cdd:cd03749 157 GARSQSARTYLERHFEefEDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIV 210
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-201 1.10e-59

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: 187.49  E-value: 1.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAGSAIGILSKDGVVLIGEKKVTSKLLQTStSAEKMYKIDDHVACAVAGIMSDAN 84
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPG-SNKRIFNVDRHIGIAVAGLLADGR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  85 ILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAV 164
Cdd:cd03751  83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDS-DGPQLYMIEPSGVSYGYFGCAI 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15233268 165 GANNQAAQSILKQDYKDDATREEAVELALKVLTKTMD 201
Cdd:cd03751 162 GKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHD 198
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 1.77e-59

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: 187.06  E-value: 1.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   5 YDSRTTIFSPEGRLYQVEYAMEAIGNAG-SAIGILSKDGVVLIGEKKVTSKLLQTSTsAEKMYKIDDHVACAVAGIMSDA 83
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPST-VTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  84 NILINTARVQAQRYTFMYQEPMPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAA 163
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15233268 164 VGANNQAAQSILKQDYKDD----ATREEAVELALKVLtKTMDSTSLTSEKLELAEV 215
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKpdliESYEETVELAISCL-QTVLSTDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-196 4.98e-47

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: 153.70  E-value: 4.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  32 GSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQLV 111
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 112 QSLCDTKQGYTQfggLRPFGVSFLFAGWDKHHGfQLYMSDPSGNYGGW-KAAAVGANNQAAQSILKQDYKDDATREEAVE 190
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVE 156


                ....*.
gi 15233268 191 LALKVL 196
Cdd:cd01901 157 LALKAL 162
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-213 2.76e-28

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: 105.99  E-value: 2.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  32 GSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVE--- 108
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKaaa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 109 QLVQSLCDTKQGYtqfgglrPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEA 188
Cdd:cd01912  81 NLLSNILYSYRGF-------PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEA 153

                       170       180
                ....*....|....*....|....*
gi 15233268 189 VELALKVLTKTMDSTSLTSEKLELA 213
Cdd:cd01912 154 VELVKKAIDSAIERDLSSGGGVDVA 178
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-204 1.22e-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: 104.64  E-value: 1.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  34 AIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQLVQS 113
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 114 LCDTKQGYTQFgglrPFGVSFLFAGWDKhHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVELAL 193
Cdd:cd03764  83 LSNILNSSKYF----PYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157

                       170
                ....*....|...
gi 15233268 194 KVLTKTM--DSTS 204
Cdd:cd03764 158 RAIKSAIerDSAS 170
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-191 1.70e-12

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: 64.14  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  33 SAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDanilintaRVQAQRYTfmyQEPMPVEQLvq 112
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGD--------RLQFAEYI---QKNIQLYKM-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 113 slcdtKQGYTQF-------------GGLR---PFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILK 176
Cdd:cd03758  70 -----RNGYELSpkaaanftrrelaESLRsrtPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILD 144

                       170
                ....*....|....*
gi 15233268 177 QDYKDDATREEAVEL 191
Cdd:cd03758 145 RYYKPDMTVEEALEL 159
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 9.38e-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: 55.20  E-value: 9.38e-11
                           10        20
                   ....*....|....*....|...
gi 15233268      5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 1.48e-10

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 54.66  E-value: 1.48e-10
                          10        20
                  ....*....|....*....|...
gi 15233268     5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-192 5.87e-10

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: 56.82  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  35 IGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQLVQSL 114
Cdd:cd03763   4 VGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTML 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 115 CDT---KQGYtqfgglrpFGVSFLFAGWDKHhGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVEL 191
Cdd:cd03763  84 KQHlfrYQGH--------IGAALVLGGVDYT-GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKL 154


                .
gi 15233268 192 A 192
Cdd:cd03763 155 V 155
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-197 5.31e-07

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


Pssm-ID: 239726  Cd Length: 212  Bit Score: 48.79  E-value: 5.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  30 NAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVEQ 109
Cdd:cd03757   7 NGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 110 LVQSLCDTKQGYTQFgglrPFGVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSIL---------KQDYK 180
Cdd:cd03757  87 IAQLLSTILYSRRFF----PYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLdnqvgrknqNNVER 162

                       170
                ....*....|....*..
gi 15233268 181 DDATREEAVELALKVLT 197
Cdd:cd03757 163 TPLSLEEAVSLVKDAFT 179
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-204 1.45e-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: 47.22  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  35 IGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPVE---QLV 111
Cdd:cd03762   4 IAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKtaaSLF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268 112 QSLCdtkqgYTQFGGLRpfgVSFLFAGWDKHHGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVEL 191
Cdd:cd03762  84 KNLC-----YNYKEMLS---AGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKF 155

                       170
                ....*....|....*
gi 15233268 192 ALKVLTKTM--DSTS 204
Cdd:cd03762 156 VKNALSLAMsrDGSS 170
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 28-191 1.76e-04

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 41.90  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268   28 IGNAGSAIGILSKDGVVLIGEKKVTSKLLQTSTSAEKMYKIDDHVACAVAGIMSDANILINTARVQAQRYTFMYQEPMPV 107
Cdd:PTZ00488  36 FAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233268  108 EQLVQSLCDTKQGYTQFGglrpFGVSFLFAGWDKHhGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREE 187
Cdd:PTZ00488 116 AAASKILANIVWNYKGMG----LSMGTMICGWDKK-GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEE 190


                 ....
gi 15233268  188 AVEL 191
Cdd:PTZ00488 191 AQDL 194
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 137-192 1.18e-03

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: 38.76  E-value: 1.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15233268 137 AGWDKHhGFQLYMSDPSGNYGGWKAAAVGANNQAAQSILKQDYKDDATREEAVELA 192
Cdd:cd03761 102 CGWDKT-GPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLA 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH