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Conserved domains on  [gi|23489885|gb|EAA21790|]
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proteasome subunit alpha type 4 [Plasmodium yoelii yoelii]

Protein Classification

PTZ00246 family protein( domain architecture ID 11488288)

PTZ00246 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 1.47e-169

proteasome subunit alpha; Provisional


:

Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 467.41  E-value: 1.47e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    1 MARRYDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLN 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   81 ADANILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWF 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  161 ATAIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYLSNK--DGKVIQKYLTEKEIAELIKI 238
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGetDGEPIQKMLSEKEIAELLKK 240


                 ....*...
gi 23489885  239 YTQQNVKK 246
Cdd:PTZ00246 241 VTQEYAKE 248
 
Name Accession Description Interval E-value
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 1.47e-169

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 467.41  E-value: 1.47e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    1 MARRYDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLN 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   81 ADANILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWF 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  161 ATAIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYLSNK--DGKVIQKYLTEKEIAELIKI 238
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGetDGEPIQKMLSEKEIAELLKK 240


                 ....*...
gi 23489885  239 YTQQNVKK 246
Cdd:PTZ00246 241 VTQEYAKE 248
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 8.13e-149

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: 413.28  E-value: 8.13e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   3 RRYDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNAD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  83 ANILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFAT 162
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23489885 163 AIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYL 215
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-220 3.94e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 196.90  E-value: 3.94e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADK-VFISKLINkANNFEKIYKIDDHIFCGVAGLNADA 83
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRrATMGNLIA-SKSIEKIFKIDDHIGVAIAGLVADA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  84 NILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGgLRPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGWFATA 163
Cdd:COG0638  88 RELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAVA 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23489885 164 IGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYLSnKDG 220
Cdd:COG0638 166 IGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVIT-EDG 221
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-215 1.20e-61

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 191.63  E-value: 1.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    28 INNASITIGIITNDGVILGADK--VFISKLINKaNNFEKIYKIDDHIFCGVAGLNADANILINQSRLYAQRYLYNYNDVE 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKraTRGSKLLSK-DTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   106 PVAqLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMTL 185
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 23489885   186 QEGLLLAIKTLAKSTDSEIPKCEKIELAYL 215
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 4.27e-10

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 53.27  E-value: 4.27e-10
                           10        20
                   ....*....|....*....|...
gi 23489885      5 YDSRTTTFSPEGRLYQVEYALEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-246 1.47e-169

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 467.41  E-value: 1.47e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    1 MARRYDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLN 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   81 ADANILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWF 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  161 ATAIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYLSNK--DGKVIQKYLTEKEIAELIKI 238
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGetDGEPIQKMLSEKEIAELLKK 240


                 ....*...
gi 23489885  239 YTQQNVKK 246
Cdd:PTZ00246 241 VTQEYAKE 248
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-215 8.13e-149

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: 413.28  E-value: 8.13e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   3 RRYDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNAD 82
Cdd:cd03752   1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  83 ANILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFAT 162
Cdd:cd03752  81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23489885 163 AIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYL 215
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 2.07e-109

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: 313.61  E-value: 2.07e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNfEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAI 164
Cdd:cd01911  80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 23489885 165 GTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIpKCEKIELAYL 215
Cdd:cd01911 160 GKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-237 1.38e-87

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 259.38  E-value: 1.38e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLInKANNFEKIYKIDDHIFCGVAGLNADAN 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLI-EPSSIEKIFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKeGYQLYHTDPSGNYSGWFATAI 164
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23489885  165 GTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEiPKCEKIELAYLSNKDGKViqKYLTEKEIAELIK 237
Cdd:PRK03996 168 GAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGK-LDPENVEIAYIDVETKKF--RKLSVEEIEKYLE 237
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 1.45e-80

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: 240.70  E-value: 1.45e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLInKANNFEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLV-EPESIEKIYKIDDHVGAATSGLVADAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGyQLYHTDPSGNYSGWFATAI 164
Cdd:cd03756  81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGP-RLFETDPSGAYNEYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 23489885 165 GTNNLTASSILKQEWKKDMTLQEGLLLAIKTLaKSTDSEIPKCEKIELAYLS 216
Cdd:cd03756 160 GSGRQAVTEFLEKEYKEDMSLEEAIELALKAL-YAALEENETPENVEIAYVT 210
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-202 5.48e-64

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: 198.36  E-value: 5.48e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINkANNFEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQD-PRTVRKICMLDDHVCLAFAGLTADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAI 164
Cdd:cd03755  80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23489885 165 GTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDS 202
Cdd:cd03755 160 GRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQS 197
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 34-215 5.83e-64

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: 197.33  E-value: 5.83e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  34 TIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADANILINQSRLYAQRYLYNYNDVEPVAQLVVQ 113
Cdd:cd01906   3 IVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 114 ICDIKQSYTQYggLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMTLQEGLLLAI 193
Cdd:cd01906  83 LANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 23489885 194 KTLAKSTDSEIPKCEKIELAYL 215
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-220 3.94e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 196.90  E-value: 3.94e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADK-VFISKLINkANNFEKIYKIDDHIFCGVAGLNADA 83
Cdd:COG0638   9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRrATMGNLIA-SKSIEKIFKIDDHIGVAIAGLVADA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  84 NILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGgLRPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGWFATA 163
Cdd:COG0638  88 RELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYG-VRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAVA 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23489885 164 IGTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAYLSnKDG 220
Cdd:COG0638 166 IGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVIT-EDG 221
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-196 1.90e-62

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: 194.48  E-value: 1.90e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKaNNFEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEP-SSVEKIMEIDDHIGCAMSGLIADAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGL-----RPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGW 159
Cdd:cd03753  80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVD-ENGPQLFHTDPSGTFTRC 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23489885 160 FATAIGTNNLTASSILKQEWKKDMTLQEGLLLAIKTL 196
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSIL 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-215 1.20e-61

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 191.63  E-value: 1.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885    28 INNASITIGIITNDGVILGADK--VFISKLINKaNNFEKIYKIDDHIFCGVAGLNADANILINQSRLYAQRYLYNYNDVE 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKraTRGSKLLSK-DTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   106 PVAqLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMTL 185
Cdd:pfam00227  80 PVE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 23489885   186 QEGLLLAIKTLAKSTDSEIPKCEKIELAYL 215
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-204 2.48e-58

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: 184.45  E-value: 2.48e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  10 TTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKaNNFEKIYKIDDHIFCGVAGLNADANILINQ 89
Cdd:cd03750   6 TTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDE-SSVHKVEQITPHIGMVYSGMGPDFRVLVKK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  90 SRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKeGYQLYHTDPSGNYSGWFATAIGTNNL 169
Cdd:cd03750  85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEG-GPYLYQVDPSGSYFTWKATAIGKNYS 163

                       170       180       190
                ....*....|....*....|....*....|....*
gi 23489885 170 TASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEI 204
Cdd:cd03750 164 NAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQM 198
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-214 3.45e-54

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: 173.62  E-value: 3.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLINKANNfEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADGR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGWFATAI 164
Cdd:cd03751  83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYD-SDGPQLYMIEPSGVSYGYFGCAI 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23489885 165 GTNNLTASSILKQEWKKDMTLQEGLLLAIKTLAKSTDSEIPKCEKIELAY 214
Cdd:cd03751 162 GKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDEIKDKAFELELSW 211
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-203 4.00e-54

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 173.25  E-value: 4.00e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASITIGIITNDGVILGADKVFISKLinkANNFEKIYKIDDHIFCGVAGLNADAN 84
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  85 ILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKeGYQLYHTDPSGNYSGWFATAI 164
Cdd:cd03749  78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23489885 165 GTNNLTASSILKQEWK--KDMTLQEGLLLAIKTLAKSTDSE 203
Cdd:cd03749 157 GARSQSARTYLERHFEefEDCSLEELIKHALRALRETLPGE 197
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 2.44e-51

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 166.26  E-value: 2.44e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885   5 YDSRTTTFSPEGRLYQVEYALEAINNASIT-IGIITNDGVILGADKVFISKLINkANNFEKIYKIDDHIFCGVAGLNADA 83
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGLTsVAVRGKDCAVVVTQKKVPDKLID-PSTVTHLFRITDEIGCVMTGMIADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  84 NILINQSRLYAQRYLYNYNDVEPVAQLVVQICDIKQSYTQYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATA 163
Cdd:cd03754  81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23489885 164 IGTNNLTASSILKQEWKKD----MTLQEGLLLAIKTLaKSTDSEIPKCEKIELA 213
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKpdliESYEETVELAISCL-QTVLSTDFKATEIEVG 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 34-196 3.79e-44

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 146.39  E-value: 3.79e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  34 TIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADANILINQSRLYAQRYLYNYNDVEPVAQLVVQ 113
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 114 ICDIKQSYTQyggLRPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGW-FATAIGTNNLTASSILKQEWKKDMTLQEGLLLA 192
Cdd:cd01901  83 LAKLLQVYTQ---GRPFGVNLIVAGVD-EGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELA 158


                ....
gi 23489885 193 IKTL 196
Cdd:cd01901 159 LKAL 162
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-202 5.10e-30

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: 110.61  E-value: 5.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  34 TIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNAD----ANILINQSRLYAQRYLYNYNdVEPVAQ 109
Cdd:cd01912   3 IVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADtqalTRLLKRNLRLYELRNGRELS-VKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 110 LVVQICDIKQSYtqygglrPYGVSFLIAGYDTKEGYQLYHTDPSGNY-SGWFAtAIGTNNLTASSILKQEWKKDMTLQEg 188
Cdd:cd01912  82 LLSNILYSYRGF-------PYYVSLIVGGVDKGGGPFLYYVDPLGSLiEAPFV-ATGSGSKYAYGILDRGYKPDMTLEE- 152

                       170
                ....*....|....
gi 23489885 189 lllAIKTLAKSTDS 202
Cdd:cd01912 153 ---AVELVKKAIDS 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-196 9.36e-22

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: 88.85  E-value: 9.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  34 TIGIITNDGVILGADK-----VFISklinkANNFEKIYKIDDHIFCGVAGLNADA----NILINQSRLYAQRYlYNYNDV 104
Cdd:cd03764   3 TVGIVCKDGVVLAADKrasmgNFIA-----SKNVKKIFQIDDKIAMTIAGSVGDAqslvRILKAEARLYELRR-GRPMSI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 105 EPVAQLVVQIcdikqsyTQYGGLRPYGVSFLIAGYDtKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMT 184
Cdd:cd03764  77 KALATLLSNI-------LNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMT 148

                       170
                ....*....|..
gi 23489885 185 LQEGLLLAIKTL 196
Cdd:cd03764 149 VEEAKKLAIRAI 160
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-194 1.39e-17

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: 78.01  E-value: 1.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  35 IGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADANilinQSRLYAQR--YLYNY-NDVEPVAQLV 111
Cdd:cd03758   5 IGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRL----QFAEYIQKniQLYKMrNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 112 VqicdikqSYTQ---YGGLR---PYGVSFLIAGYDTKEGYQLYHTDPSGN----------YSGWFATaigtnnltasSIL 175
Cdd:cd03758  81 A-------NFTRrelAESLRsrtPYQVNLLLAGYDKVEGPSLYYIDYLGTlvkvpyaahgYGAYFCL----------SIL 143

                       170
                ....*....|....*....
gi 23489885 176 KQEWKKDMTLQEGLLLAIK 194
Cdd:cd03758 144 DRYYKPDMTVEEALELMKK 162
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-197 2.59e-17

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: 77.24  E-value: 2.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  33 ITI-GIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADANILIN--QSRLYAQRYLYNYndvEPVAQ 109
Cdd:cd03763   1 TTIvGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNmiSSNLELHRLNTGR---KPRVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 110 LVVQIcdIKQSYTQYGGLrpYGVSFLIAGYDTKeGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMTLQEGL 189
Cdd:cd03763  78 TALTM--LKQHLFRYQGH--IGAALVLGGVDYT-GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAK 152


                ....*...
gi 23489885 190 LLAIKTLA 197
Cdd:cd03763 153 KLVCEAIE 160
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 4.27e-10

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 53.27  E-value: 4.27e-10
                           10        20
                   ....*....|....*....|...
gi 23489885      5 YDSRTTTFSPEGRLYQVEYALEA 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 7.02e-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: 52.74  E-value: 7.02e-10
                          10        20
                  ....*....|....*....|...
gi 23489885     5 YDSRTTTFSPEGRLYQVEYALEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-197 1.70e-08

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 52.61  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  35 IGIITNDGVILGAD-KVFISKLI-NKANNfeKIYKIDDHIFCGVAGLNADANILINQSRLYAQRYLYNYND---VEPVAQ 109
Cdd:cd03762   4 IAVEYDGGVVLGADsRTSTGSYVaNRVTD--KLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEpplVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 110 LVVQICdikqsytqYGGLRPYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKDMTLQEGL 189
Cdd:cd03762  82 LFKNLC--------YNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECI 153


                ....*...
gi 23489885 190 LLAIKTLA 197
Cdd:cd03762 154 KFVKNALS 161
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-192 2.15e-07

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: 49.55  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  34 TIGIITNDGVILGAD-----KVFISklinkANNFEKIYKIDDHIFCGVAGLNADA----NILINQSRLYAQRYlynyNDV 104
Cdd:cd03761   3 TLAFIFQGGVIVAVDsrataGSYIA-----SQTVKKVIEINPYLLGTMAGGAADCqyweRVLGRECRLYELRN----KER 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 105 EPVAQLVVQICDIKQSYtqygglRPYGVSF--LIAGYDtKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSILKQEWKKD 182
Cdd:cd03761  74 ISVAAASKLLSNMLYQY------KGMGLSMgtMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYD 146

                       170
                ....*....|
gi 23489885 183 MTLQEGLLLA 192
Cdd:cd03761 147 LSVEEAYDLA 156
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 28-187 4.75e-06

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: 46.10  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  28 INNASITIGIITNDGVILGAD-KVFISKLINKANNfEKIYKIDDHIFCGVAGLNADANILinQSRLYAQRYLYNYND--- 103
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDtRLSEGYSILSRDS-PKIFKLTDKCVLGSSGFQADILAL--TKRLKARIKMYKYSHnke 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885 104 --VEPVAQLVvqicdikqSYTQYGglR---PYGVSFLIAGYDTKEGYQLYHTDPSGNYSGWFATAIGTNNLTASSIL-KQ 177
Cdd:cd03757  82 msTEAIAQLL--------STILYS--RrffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLdNQ 151

                       170
                ....*....|
gi 23489885 178 EWKKDMTLQE 187
Cdd:cd03757 152 VGRKNQNNVE 161
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-187 2.89e-05

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 43.71  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  35 IGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADA-------NILINQSRL--------------Y 93
Cdd:cd03760   6 IAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFqylkrllDQLVIDDEClddghslspkeihsY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  94 AQRYLYNY-NDVEPV-AQLVVqicdikqsytqyGGLRPYGVSFLiaGYDTKEGyqLYHTDPSgnysgwFATAIGtnNLTA 171
Cdd:cd03760  86 LTRVLYNRrSKMNPLwNTLVV------------GGVDNEGEPFL--GYVDLLG--TAYEDPH------VATGFG--AYLA 141

                       170
                ....*....|....*...
gi 23489885 172 SSILKQEWKK--DMTLQE 187
Cdd:cd03760 142 LPLLREAWEKkpDLTEEE 159
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-142 3.12e-05

proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239728  Cd Length: 195  Bit Score: 43.39  E-value: 3.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489885  30 NASITIGIITNDGVILGADKVFISKLINKANNFEKIYKIDDHIFCGVAGLNADANILinqsrlyAQRYLYNYN------- 102
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTL-------AQKLRFRVNlyrlree 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 23489885 103 -DVEP--VAQLVVQICdikqsYTQYGGlrPYGVSFLIAGYDTK 142
Cdd:cd03759  75 rEIKPktFSSLISSLL-----YEKRFG--PYFVEPVVAGLDPD 110
 
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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