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Conserved domains on  [gi|156713442|ref|NP_001096137|]
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proteasome subunit alpha type-4 isoform 1 [Homo sapiens]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132891)

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

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

Graphical summary

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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 ...
 3-216 7.71e-157

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: 434.47  E-value: 7.71e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156713442 163 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-216 7.71e-157

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: 434.47  E-value: 7.71e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156713442 163 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-237 2.75e-112

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 323.34  E-value: 2.75e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  81 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156713442 161 ATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTR--ENGKTVIRVLKQKEVEQLI 237
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKED-LTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-222 1.06e-77

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: 234.47  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442    5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156713442  165 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGK 222
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYRED-LSLDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-219 1.68e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 198.45  E-value: 1.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMAC 74
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  75 SVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSG 154
Cdd:COG0638   79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSG 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156713442 155 NYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 219
Cdd:COG0638  157 GLYEEKAVAIGSGSPFARGVLEKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-216 1.25e-60

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: 1.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   30 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 107
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  108 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLK 187
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 156713442  188 SALALAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 3.75e-11

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 56.35  E-value: 3.75e-11
                           10        20
                   ....*....|....*....|...
gi 156713442     5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-216 7.71e-157

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: 434.47  E-value: 7.71e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   3 RRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 82
Cdd:cd03752    1 RRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  83 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 162
Cdd:cd03752   81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156713442 163 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:cd03752  161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-237 2.75e-112

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 323.34  E-value: 2.75e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   1 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 80
Cdd:PTZ00246   1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  81 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 160
Cdd:PTZ00246  81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156713442 161 ATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTR--ENGKTVIRVLKQKEVEQLI 237
Cdd:PTZ00246 161 ATAIGQNNQTAQSILKQEWKED-LTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 3.05e-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: 3.05e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd01911   80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156713442 165 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDvSKLSAEKVEIATL 216
Cdd:cd01911  160 GKGSQEAKTFLEKRYKK-DLTLEEAIKLALKALKEVLE-EDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-237 1.56e-81

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 244.74  E-value: 1.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:PRK03996  10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSI-EKIFKIDDHIGAASAGLVADAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:PRK03996  89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156713442 165 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGKtvIRVLKQKEVEQLI 237
Cdd:PRK03996 168 GAGRDTVMEFLEKNYKE-DLSLEEAIELALKALAKANE-GKLDPENVEIAYIDVETKK--FRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-222 1.06e-77

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: 234.47  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442    5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156713442  165 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGK 222
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYRED-LSLDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-217 2.24e-77

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: 232.99  E-value: 2.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLV-EPESIEKIYKIDDHVGAATSGLVADAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03756   81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156713442 165 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLT 217
Cdd:cd03756  160 GSGRQAVTEFLEKEYKED-MSLEEAIELALKALYAALE-ENETPENVEIAYVT 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-219 1.68e-63

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 198.45  E-value: 1.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERR----------NIhklldevffsEKIYKLNEDMAC 74
Cdd:COG0638    9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRatmgnliaskSI----------EKIFKIDDHIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  75 SVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKHyGFQLYQSDPSG 154
Cdd:COG0638   79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG-GPRLFSTDPSG 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156713442 155 NYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 219
Cdd:COG0638  157 GLYEEKAVAIGSGSPFARGVLEKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 2.42e-61

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: 192.19  E-value: 2.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTV-RKICMLDDHVCLAFAGLTADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03755   80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156713442 165 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLnktMDVSKLSAEKVEIATL 216
Cdd:cd03755  160 GRNSKTVREFLEKNYKE-EMTRDDTIKLAIKAL---LEVVQSGSKNIELAVM 207
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-216 1.25e-60

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: 1.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   30 HAGTCLGILANDGVLLAAERRNI--HKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPC 107
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTV-EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  108 EqLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLK 187
Cdd:pfam00227  82 E-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 156713442  188 SALALAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 10-234 2.73e-60

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: 190.23  E-value: 2.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  10 TIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSeKIYKLNEDMACSVAGITSDANVLTNE 89
Cdd:cd03750    6 TTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVH-KVEQITPHIGMVYSGMGPDFRVLVKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  90 LRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKhYGFQLYQSDPSGNYGGWKATCIGNNSA 169
Cdd:cd03750   85 ARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKATAIGKNYS 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156713442 170 AAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVsKLSAEKVEIATLTRENGktvIRVLKQKEVE 234
Cdd:cd03750  164 NAKTFLEKRYNE-DLELEDAIHTAILTLKEGFEG-QMTEKNIEIGICGETKG---FRLLTPAEIK 223
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-216 7.99e-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: 184.62  E-value: 7.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442 112 TALCDIKQAYTQFggKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALA 191
Cdd:cd01906   81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD-MTLEEAIE 157

                        170       180
                 ....*....|....*....|....*
gi 156713442 192 LAIKVLNKTMDVSKLSAEKVEIATL 216
Cdd:cd01906  158 LALKALKSALERDLYSGGNIEVAVI 182
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 1.46e-54

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: 175.22  E-value: 1.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGK-----RPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGW 159
Cdd:cd03753   80 TLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRC 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 156713442 160 KATCIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDvSKLSAEKVEIATL 216
Cdd:cd03753  159 DAKAIGSGSEGAQSSLQEKYHK-DMTLEEAEKLALSILKQVME-EKLNSTNVELATV 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-216 1.67e-52

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: 169.78  E-value: 1.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLldeVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03749   78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSI 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156713442 165 GNNSAAAVSMLKQDYKE-GEMTLKSALALAIKVLNKTM-DVSKLSAEKVEIATL 216
Cdd:cd03749  157 GARSQSARTYLERHFEEfEDCSLEELIKHALRALRETLpGEQELTIKNVSIAIV 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-214 1.14e-47

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: 157.40  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAG-TCLGILANDGVLLAAERRNIHKLLDEVFFSEkIYKLNEDMACSVAGITSDA 83
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTH-LFRITDEIGCVMTGMIADS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  84 NVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATC 163
Cdd:cd03754   81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156713442 164 IGNNSAAAVSMLKQDYK---EGEMTLKSALALAIKVLnKTMDVSKLSAEKVEIA 214
Cdd:cd03754  161 AGVKEQEATNFLEKKLKkkpDLIESYEETVELAISCL-QTVLSTDFKATEIEVG 213
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-214 4.45e-40

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: 137.80  E-value: 4.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442   5 YDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAErRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDAN 84
Cdd:cd03751    4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVE-KLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  85 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 164
Cdd:cd03751   83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD-GPQLYMIEPSGVSYGYFGCAI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156713442 165 GN-NSAAAVSMLKQDYKegEMTLKSALALAIKVLNKTMDVSKLSAEKVEIA 214
Cdd:cd03751  162 GKgKQAAKTELEKLKFS--ELTCREAVKEAAKIIYIVHDEIKDKAFELELS 210
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-198 6.74e-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: 133.29  E-value: 6.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442 112 TALCDIKQAYTQFggkRPFGVSLLYIGWDKHYGfQLYQSDPSGNYGGW-KATCIGNNSAAAVSMLKQDYKEGeMTLKSAL 190
Cdd:cd01901   81 KELAKLLQVYTQG---RPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD-MTLEEAV 155


                 ....*...
gi 156713442 191 ALAIKVLN 198
Cdd:cd01901  156 ELALKALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-219 2.85e-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: 2.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  33 TCLGILANDGVLLAAERRN------IHKLLDevffseKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 106
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRAsmgnfiASKNVK------KIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442 107 CEQLVTALCDIKQAYTQFggkrPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTL 186
Cdd:cd03764   76 IKALATLLSNILNSSKYF----PYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED-MTV 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 156713442 187 KSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 219
Cdd:cd03764  150 EEAKKLAIRAIKSAIERDSASGDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-219 7.34e-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: 81.72  E-value: 7.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  32 GTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLV 111
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442 112 TALCDIkQAYTQFGgkrPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALA 191
Cdd:cd01912   81 NLLSNI-LYSYRGF---PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD-MTLEEAVE 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 156713442 192 LAIKVLNKTM--DVSklSAEKVEIATLTRE 219
Cdd:cd01912  156 LVKKAIDSAIerDLS--SGGGVDVAVITKD 183
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 3.75e-11

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


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 56.35  E-value: 3.75e-11
                           10        20
                   ....*....|....*....|...
gi 156713442     5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 7.25e-11

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


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 55.43  E-value: 7.25e-11
                          10        20
                  ....*....|....*....|...
gi 156713442    5 YDSRTTIFSPEGRLYQVEYAMEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-195 1.65e-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: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  33 TCLGILANDGVLLAAERRNIHkllDEVFFS---EKIYKLNEDMACSVAGITSDANVLTNELRliAQRYLLQYQ---EPip 106
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATE---GPIVADkncEKIHYIAPNIYCCGAGTAADTEAVTNMIS--SNLELHRLNtgrKP-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442 107 ceQLVTALCDIKQAYTQFGGKrpFGVSLLYIGWDKhYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTL 186
Cdd:cd03763   75 --RVVTALTMLKQHLFRYQGH--IGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPD-MTE 148


                 ....*....
gi 156713442 187 KSALALAIK 195
Cdd:cd03763  149 EEAKKLVCE 157
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-175 4.94e-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: 49.18  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156713442  32 GTCLGILANDGVLLAAERR-----NIHKLldevfFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIP 106
Cdd:cd03757    9 GTVLAIAGNDFAVIAGDTRlsegySILSR-----DSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156713442 107 CEQLVTALCDIkqAYtqfgGKR--PFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSML 175
Cdd:cd03757   84 TEAIAQLLSTI--LY----SRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLL 148
 
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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