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Conserved domains on  [gi|7106389|ref|NP_036099|]
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proteasome subunit alpha type-7 isoform 1 [Mus musculus]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132902)

proteasome subunit alpha is a component of the proteasome complex that is involved in the proteolytic degradation of most intracellular proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 8.12e-158

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: 436.02  E-value: 8.12e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7106389  163 RGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 211
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 8.12e-158

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: 436.02  E-value: 8.12e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7106389  163 RGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 211
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-230 2.89e-97

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 284.03  E-value: 2.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANA 160
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106389   161 IGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSGGK--NIELA-VMRRDQPLKILNPEEIEKYVA 230
Cdd:PRK03996 167 IGAGRDTVMEFLEKNYKED-LSLEE-AIELALKALAKANEGKLDpeNVEIAyIDVETKKFRKLSVEEIEKYLE 237
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 1-224 2.77e-88

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: 260.66  E-value: 2.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389      1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANA 160
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106389    161 IGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQSG--GKNIELAVM-RRDQPLKILNPEE 224
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDL--SLDEAIELALKALYSAVEDKltPENVEVAYItVEDKKFRKLSVEE 224
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-211 1.86e-72

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: 219.36  E-value: 1.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     26 VKKGSTAVGVRGKDIVVLGVEKKSVA--KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVT 103
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    104 VEyITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAieT 183
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL--T 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 7106389    184 DDLTIKLVIKALLEVVQ---SGGKNIELAVM 211
Cdd:pfam00227 158 LEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-224 1.79e-71

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 218.09  E-value: 1.79e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTAD 79
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   80 ARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSnGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKAN 159
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAV 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106389  160 AIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQpLKILNPEE 224
Cdd:COG0638 165 AIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG-FRELSEEE 229
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 3-25 1.85e-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: 57.12  E-value: 1.85e-11
                           10        20
                   ....*....|....*....|...
gi 7106389       3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 8.12e-158

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: 436.02  E-value: 8.12e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7106389  163 RGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSGGKNIELAVM 211
Cdd:cd03755 161 RNSKTVREFLEKNYKEE--MTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 8.27e-119

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: 337.49  E-value: 8.27e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7106389  163 RGAKSVREFLEKNYTDDaiETDDLTIKLVIKALLEVVQSG--GKNIELAVM 211
Cdd:cd01911 161 KGSQEAKTFLEKRYKKD--LTLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-230 2.89e-97

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 284.03  E-value: 2.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANA 160
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKATA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106389   161 IGRGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSGGK--NIELA-VMRRDQPLKILNPEEIEKYVA 230
Cdd:PRK03996 167 IGAGRDTVMEFLEKNYKED-LSLEE-AIELALKALAKANEGKLDpeNVEIAyIDVETKKFRKLSVEEIEKYLE 237
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 1-224 2.77e-88

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: 260.66  E-value: 2.77e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389      1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANA 160
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106389    161 IGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQSG--GKNIELAVM-RRDQPLKILNPEE 224
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDL--SLDEAIELALKALYSAVEDKltPENVEVAYItVEDKKFRKLSVEE 224
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-210 1.52e-85

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: 253.41  E-value: 1.52e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKATAIG 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 7106389  163 RGAKSVREFLEKNYTDDaIETDDlTIKLVIKALLEVVQSG--GKNIELAV 210
Cdd:cd03756 161 SGRQAVTEFLEKEYKED-MSLEE-AIELALKALYAALEENetPENVEIAY 208
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-230 2.11e-77

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: 233.37  E-value: 2.11e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTWKATAIG 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  163 RGAKSVREFLEKNYTDDaIETDD--LTIKLVIKALLEvVQSGGKNIELAVMRRDQPLKILNPEEIEKYVA 230
Cdd:cd03750 160 KNYSNAKTFLEKRYNED-LELEDaiHTAILTLKEGFE-GQMTEKNIEIGICGETKGFRLLTPAEIKDYLA 227
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-211 1.86e-72

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: 219.36  E-value: 1.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     26 VKKGSTAVGVRGKDIVVLGVEKKSVA--KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVT 103
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    104 VEyITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAieT 183
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL--T 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 7106389    184 DDLTIKLVIKALLEVVQ---SGGKNIELAVM 211
Cdd:pfam00227 158 LEEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-224 1.79e-71

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 218.09  E-value: 1.79e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTAD 79
Cdd:COG0638   7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   80 ARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSnGRRPFGISALIVGFDfDGTPRLYQTDPSGTYHAWKAN 159
Cdd:COG0638  87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAV 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106389  160 AIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQpLKILNPEE 224
Cdd:COG0638 165 AIGSGSPFARGVLEKEYREDL--SLDEAVELALRALYSAAERdsaSGDGIDVAVITEDG-FRELSEEE 229
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 6.21e-64

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: 198.33  E-value: 6.21e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGR-----RPFGISALIVGFDFDGtPRLYQTDPSGTYHAWK 157
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFHTDPSGTFTRCD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7106389  158 ANAIGRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS--GGKNIELAVM 211
Cdd:cd03753 160 AKAIGSGSEGAQSSLQEKYHKDM--TLEEAEKLALSILKQVMEEklNSTNVELATV 213
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-211 6.53e-63

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: 196.03  E-value: 6.53e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADAR 81
Cdd:cd03752   3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVAGITSDAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAI 161
Cdd:cd03752  83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAI 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7106389  162 GRGAKSVREFLEKNYTDDAI--ETDDLTIKLVIKAlLEVVQSGGKNIELAVM 211
Cdd:cd03752 163 GNNNQAAQSLLKQDYKDDMTleEALALAVKVLSKT-MDSTKLTSEKLEFATL 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 30-211 1.03e-60

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: 189.24  E-value: 1.03e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   30 STAVGVRGKDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYIT 108
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  109 RYIASLKQRYTQSngRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDaiETDDLTI 188
Cdd:cd01906  81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD--MTLEEAI 156

                       170       180
                ....*....|....*....|....*.
gi 7106389  189 KLVIKALLEVVQSG---GKNIELAVM 211
Cdd:cd01906 157 ELALKALKSALERDlysGGNIEVAVI 182
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-210 1.53e-60

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: 189.81  E-value: 1.53e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERtvRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIAGLTADARV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGtPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03749  79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPSGNYFEYKATSIG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7106389  163 RGAKSVREFLEKNYTDDAIETDDLTIKLVIKALLEVVQSGG----KNIELAV 210
Cdd:cd03749 158 ARSQSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQeltiKNVSIAI 209
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-199 1.16e-54

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 174.78  E-value: 1.16e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGtPRLYQTDPSGTYHAWKANAIG 162
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPSGVSYGYFGCAIG 162

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7106389  163 RGAKSVREFLEKnytddaIETDDLTIKLVIKALLEVV 199
Cdd:cd03751 163 KGKQAAKTELEK------LKFSELTCREAVKEAAKII 193
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 3-229 3.26e-54

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 175.04  E-value: 3.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389     3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDE-RTVRKICALDDNVCMAFAGLTADAR 81
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAI 161
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAI 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106389   162 GRGAKSVREFLEKNYTDDAieTDDLTIKLVIKALLEVVQS---GGKNIELAVMRRDQP-----LKILNPEEIEKYV 229
Cdd:PTZ00246 165 GQNNQTAQSILKQEWKEDL--TLEQGLLLAAKVLTKSMDStspKADKIEVGILSHGETdgepiQKMLSEKEIAELL 238
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-210 5.02e-52

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: 168.18  E-value: 5.02e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389    3 YDRAITVFSPDGHLFQVEYAQEAVKKGS-TAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADAR 81
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAI 161
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7106389  162 GRGAKSVREFLEKNY--TDDAIETDDLTIKLVIKALLEVVQSG--GKNIELAV 210
Cdd:cd03754 162 GVKEQEATNFLEKKLkkKPDLIESYEETVELAISCLQTVLSTDfkATEIEVGV 214
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 30-197 7.07e-41

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: 137.91  E-value: 7.07e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   30 STAVGVRGKDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYIT 108
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  109 RYIASLKQRYTQsngRRPFGISALIVGFDFDGtPRLYQTDPSGTYHAW-KANAIGRGAKSVREFLEKNYTDDaiETDDLT 187
Cdd:cd01901  81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD--MTLEEA 154

                       170
                ....*....|
gi 7106389  188 IKLVIKALLE 197
Cdd:cd01901 155 VELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-214 7.53e-22

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: 89.04  E-value: 7.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   31 TAVGVRGKDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITR 109
Cdd:cd01912   2 TIVGIKGKDGVVLAADTRASAgSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  110 YIASLKQRYtqsnGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHawKAN--AIGRGAKSVREFLEKNYTDDaIETDDLt 187
Cdd:cd01912  82 LLSNILYSY----RGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLI--EAPfvATGSGSKYAYGILDRGYKPD-MTLEEA- 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 7106389  188 IKLVIKALLEV----VQSGGkNIELAVMRRD 214
Cdd:cd01912 154 VELVKKAIDSAierdLSSGG-GVDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-214 6.98e-18

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: 78.45  E-value: 6.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   31 TAVGVRGKDIVVLGVEKK-SVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITR 109
Cdd:cd03764   2 TTVGIVCKDGVVLAADKRaSMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  110 YIASLkqryTQSNGRRPFGISALIVGFDFDGtPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDaIETDDlTIK 189
Cdd:cd03764  82 LLSNI----LNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED-MTVEE-AKK 154

                       170       180
                ....*....|....*....|....*...
gi 7106389  190 LVIKALLEVVQ---SGGKNIELAVMRRD 214
Cdd:cd03764 155 LAIRAIKSAIErdsASGDGIDVVVITKD 182
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 3-25 9.05e-12

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: 57.74  E-value: 9.05e-12
                          10        20
                  ....*....|....*....|...
gi 7106389      3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 3-25 1.85e-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: 57.12  E-value: 1.85e-11
                           10        20
                   ....*....|....*....|...
gi 7106389       3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-214 1.18e-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: 53.35  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   31 TAVGVRGKDIVVLGVEKKS-----VAklqdERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVE 105
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRAtegpiVA----DKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  106 YITRYIASLKQRYtqsNGrrpfGISA-LIV-GFDFDGtPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAieT 183
Cdd:cd03763  78 TALTMLKQHLFRY---QG----HIGAaLVLgGVDYTG-PHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDM--T 147

                       170       180       190
                ....*....|....*....|....*....|....*
gi 7106389  184 DDLTIKLVIKALLEVVQ----SGGkNIELAVMRRD 214
Cdd:cd03763 148 EEEAKKLVCEAIEAGIFndlgSGS-NVDLCVITKD 181
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-198 1.27e-06

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 47.58  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   31 TAVGVRGKDIVVL---GVEKKSVAKLQDErtVRKICALDDNVCMAFAGLTADarivinraRVEcqshrltvedpvTVEYI 107
Cdd:cd03758   3 TLIGIKGKDFVILaadTSAARSILVLKDD--EDKIYKLSDHKLMACSGEAGD--------RLQ------------FAEYI 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389  108 TRYIA--SLKQRYTQSN----------------GRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVR 169
Cdd:cd03758  61 QKNIQlyKMRNGYELSPkaaanftrrelaeslrSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCL 140

                       170       180
                ....*....|....*....|....*....
gi 7106389  170 EFLEKNYTDDaIETDDlTIKLVIKALLEV 198
Cdd:cd03758 141 SILDRYYKPD-MTVEE-ALELMKKCIKEL 167
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 29-172 1.93e-05

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: 44.17  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   29 GSTAVGVRGKDIVVLGVEKK-SVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYI 107
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRlSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106389  108 TRYIASLkqRYtqsnGRR--PFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFL 172
Cdd:cd03757  88 AQLLSTI--LY----SRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLL 148
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 29-142 1.50e-03

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


Pssm-ID: 239728  Cd Length: 195  Bit Score: 38.38  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106389   29 GSTAVGVRGKDIVV------LGVEKKSVAKLQDertvrKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPV 102
Cdd:cd03759   3 GGAVVAMAGKDCVAiasdlrLGVQQQTVSTDFQ-----KVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREI 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7106389  103 TVEYITRYIASL--KQRYTqsngrrPFGISALIVGFDFDGTP 142
Cdd:cd03759  78 KPKTFSSLISSLlyEKRFG------PYFVEPVVAGLDPDGKP 113
 
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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