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Conserved domains on  [gi|2274795559|ref|NP_001396621|]
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proteasome subunit alpha type-4 isoform 2 [Mus musculus]

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

Graphical summary

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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 ...
1-192 4.32e-134

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: 375.92  E-value: 4.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03752    23 MEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:cd03752   103 IPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKD-DM 181
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 161 TLKSALALAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:cd03752   182 TLEEALALAVKVLSKTMDSTKLTSEKLEFATL 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 ...
1-192 4.32e-134

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: 375.92  E-value: 4.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03752    23 MEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:cd03752   103 IPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKD-DM 181
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 161 TLKSALALAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:cd03752   182 TLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
1-213 1.73e-90

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 267.10  E-value: 1.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:PTZ00246   25 LEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeM 160
Cdd:PTZ00246  105 QPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKED-L 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2274795559 161 TLKSALALAVKVLNKTMDVSKLSAEKVEIATLTR--ESGKTVIRVLKQKEVEQLI 213
Cdd:PTZ00246  184 TLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
2-198 1.86e-61

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: 192.09  E-value: 1.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   2 EAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPI 81
Cdd:TIGR03633  24 EAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADARVLIDRARIEAQINRLTYGEPI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  82 PCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMT 161
Cdd:TIGR03633 103 DVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAIGAGRQAVTEFLEKEYRED-LS 180
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2274795559 162 LKSALALAVKVLNKTMDvSKLSAEKVEIATLTRESGK 198
Cdd:TIGR03633 181 LDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
6-192 4.91e-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: 189.70  E-value: 4.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   6 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 83
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  84 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLK 163
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 2274795559 164 SALALAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
2-195 8.34e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.93  E-value: 8.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   2 EAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQ 71
Cdd:COG0638    30 EAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGVAIAGLVADARELVRLARVEAQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  72 RYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSML 151
Cdd:COG0638   100 LYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVL 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2274795559 152 KQDYKEGeMTLKSALALAVKVLNKTMDVSKLSAEKVEIATLTRE 195
Cdd:COG0638   178 EKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-192 4.32e-134

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: 375.92  E-value: 4.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03752    23 MEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:cd03752   103 IPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKD-DM 181
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 161 TLKSALALAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:cd03752   182 TLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
1-213 1.73e-90

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 267.10  E-value: 1.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:PTZ00246   25 LEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeM 160
Cdd:PTZ00246  105 QPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKED-L 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2274795559 161 TLKSALALAVKVLNKTMDVSKLSAEKVEIATLTR--ESGKTVIRVLKQKEVEQLI 213
Cdd:PTZ00246  184 TLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-192 4.65e-89

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: 261.61  E-value: 4.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd01911    21 LEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:cd01911   100 IPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKK-DL 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 161 TLKSALALAVKVLNKTMDvSKLSAEKVEIATL 192
Cdd:cd01911   179 TLEEAIKLALKALKEVLE-EDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-213 4.56e-64

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 199.29  E-value: 4.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:PRK03996   30 REAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSI-EKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:PRK03996  109 IGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKE-DL 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2274795559 161 TLKSALALAVKVLNKTMDvSKLSAEKVEIATLTRESGKtvIRVLKQKEVEQLI 213
Cdd:PRK03996  187 SLEEAIELALKALAKANE-GKLDPENVEIAYIDVETKK--FRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
2-198 1.86e-61

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: 192.09  E-value: 1.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   2 EAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPI 81
Cdd:TIGR03633  24 EAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADARVLIDRARIEAQINRLTYGEPI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  82 PCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMT 161
Cdd:TIGR03633 103 DVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAIGAGRQAVTEFLEKEYRED-LS 180
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2274795559 162 LKSALALAVKVLNKTMDvSKLSAEKVEIATLTRESGK 198
Cdd:TIGR03633 181 LDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
2-193 2.89e-61

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: 191.00  E-value: 2.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   2 EAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPI 81
Cdd:cd03756    23 EAVKRGTTALGIKCKEGVVLAVDKRITSKLV-EPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  82 PCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMT 161
Cdd:cd03756   102 DVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKED-MS 179
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 162 LKSALALAVKVLNKTMDvSKLSAEKVEIATLT 193
Cdd:cd03756   180 LEEAIELALKALYAALE-ENETPENVEIAYVT 210
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
6-192 4.91e-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: 189.70  E-value: 4.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   6 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 83
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  84 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLK 163
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLE 159
                         170       180
                  ....*....|....*....|....*....
gi 2274795559 164 SALALAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
8-192 4.97e-59

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: 184.24  E-value: 4.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   8 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 87
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  88 TALCDIKQAYTQFggKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALA 167
Cdd:cd01906    81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD-MTLEEAIE 157
                         170       180
                  ....*....|....*....|....*
gi 2274795559 168 LAVKVLNKTMDVSKLSAEKVEIATL 192
Cdd:cd01906   158 LALKALKSALERDLYSGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
2-195 8.34e-51

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.93  E-value: 8.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   2 EAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQ 71
Cdd:COG0638    30 EAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGVAIAGLVADARELVRLARVEAQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  72 RYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSML 151
Cdd:COG0638   100 LYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVL 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2274795559 152 KQDYKEGeMTLKSALALAVKVLNKTMDVSKLSAEKVEIATLTRE 195
Cdd:COG0638   178 EKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
3-210 3.42e-49

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: 160.95  E-value: 3.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   3 AIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSeKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 82
Cdd:cd03750    23 AVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVH-KVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  83 CEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKhYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTL 162
Cdd:cd03750   102 VSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNE-DLEL 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2274795559 163 KSALALAVKVLNKTMDVsKLSAEKVEIATLTRESGktvIRVLKQKEVE 210
Cdd:cd03750   180 EDAIHTAILTLKEGFEG-QMTEKNIEIGICGETKG---FRLLTPAEIK 223
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-192 5.43e-47

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: 154.44  E-value: 5.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03755    21 QEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTV-RKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEM 160
Cdd:cd03755   100 VTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKE-EM 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 161 TLKSALALAVKVLnktMDVSKLSAEKVEIATL 192
Cdd:cd03755   179 TRDDTIKLAIKAL---LEVVQSGSKNIELAVM 207
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-192 4.53e-41

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: 139.39  E-value: 4.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03753    21 IEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGK-----RPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDY 155
Cdd:cd03753   100 MTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKY 178
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2274795559 156 KEgEMTLKSALALAVKVLNKTMDvSKLSAEKVEIATL 192
Cdd:cd03753   179 HK-DMTLEEAEKLALSILKQVME-EKLNSTNVELATV 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
8-174 3.94e-39

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


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 132.90  E-value: 3.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   8 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 87
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  88 TALCDIKQAYTQFggkRPFGVSLLYIGWDKHYGfQLYQSDPSGNYGGW-KATCIGNNSAAAVSMLKQDYKEGeMTLKSAL 166
Cdd:cd01901    81 KELAKLLQVYTQG---RPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD-MTLEEAV 155

                  ....*...
gi 2274795559 167 ALAVKVLN 174
Cdd:cd01901   156 ELALKALK 163
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-192 7.56e-37

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: 128.56  E-value: 7.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERRNIHKLldeVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03749    21 MEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKE-GE 159
Cdd:cd03749    98 IPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEEfED 176
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2274795559 160 MTLKSALALAVKVLNKTM-DVSKLSAEKVEIATL 192
Cdd:cd03749   177 CSLEELIKHALRALRETLpGEQELTIKNVSIAIV 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
3-190 2.13e-30

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: 111.94  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   3 AIGHAG-TCLGILANDGVLLAAERRNIHKLLDEVFFSEkIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPI 81
Cdd:cd03754    24 AVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTH-LFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  82 PCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYK---EG 158
Cdd:cd03754   103 PVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAAGVKEQEATNFLEKKLKkkpDL 182
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2274795559 159 EMTLKSALALAVKVLnKTMDVSKLSAEKVEIA 190
Cdd:cd03754   183 IESYEETVELAISCL-QTVLSTDFKATEIEVG 213
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-190 4.80e-27

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: 103.13  E-value: 4.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   1 MEAIGHAGTCLGILANDGVLLAAERrNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEP 80
Cdd:cd03751    24 NKAVENSGTAIGIRCKDGVVLAVEK-LVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  81 IPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGN-NSAAAVSMLKQDYKegE 159
Cdd:cd03751   103 IPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGCAIGKgKQAAKTELEKLKFS--E 179
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2274795559 160 MTLKSALALAVKVLNKTMDVSKLSAEKVEIA 190
Cdd:cd03751   180 LTCREAVKEAAKIIYIVHDEIKDKAFELELS 210
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
9-195 1.91e-24

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: 95.78  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   9 TCLGILANDGVLLAAERRN------IHKLLDevffseKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 82
Cdd:cd03764     2 TTVGIVCKDGVVLAADKRAsmgnfiASKNVK------KIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  83 CEQLVTALCDIKQAYTQFggkrPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTL 162
Cdd:cd03764    76 IKALATLLSNILNSSKYF----PYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED-MTV 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2274795559 163 KSALALAVKVLNKTMDVSKLSAEKVEIATLTRE 195
Cdd:cd03764   150 EEAKKLAIRAIKSAIERDSASGDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
8-195 2.29e-19

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: 82.49  E-value: 2.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   8 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 87
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  88 TALCDIkQAYTQFGgkrPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALA 167
Cdd:cd01912    81 NLLSNI-LYSYRGF---PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD-MTLEEAVE 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 2274795559 168 LAVKVLNKTM--DVSklSAEKVEIATLTRE 195
Cdd:cd01912   156 LVKKAIDSAIerDLS--SGGGVDVAVITKD 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
9-171 1.33e-08

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: 52.97  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   9 TCLGILANDGVLLAAERRNIHkllDEVFFS---EKIYKLNEDMACSVAGITSDANVLTNELRliAQRYLLQYQ---EPip 82
Cdd:cd03763     2 TIVGVVFKDGVVLGADTRATE---GPIVADkncEKIHYIAPNIYCCGAGTAADTEAVTNMIS--SNLELHRLNtgrKP-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  83 ceQLVTALCDIKQAYTQFGGKrpFGVSLLYIGWDKhYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTL 162
Cdd:cd03763    75 --RVVTALTMLKQHLFRYQGH--IGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPD-MTE 148

                  ....*....
gi 2274795559 163 KSALALAVK 171
Cdd:cd03763   149 EEAKKLVCE 157
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
8-206 1.74e-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: 49.95  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559   8 GTCLGILANDGVLLAAERR-----NIHKLldevfFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 82
Cdd:cd03757     9 GTVLAIAGNDFAVIAGDTRlsegySILSR-----DSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274795559  83 CEQLVTALCDIkqAYtqfgGKR--PFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSML--------K 152
Cdd:cd03757    84 TEAIAQLLSTI--LY----SRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLdnqvgrknQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2274795559 153 QDYKEGEMTLKSALALAVKVLNKTMDVSKLSAEKVEIATLTRESGKTVIRVLKQ 206
Cdd:cd03757   158 NNVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRK 211
 
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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