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Conserved domains on  [gi|79314743|ref|NP_001030838|]
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20S proteasome alpha subunit PAD1 [Arabidopsis thaliana]

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; similar to human proteasome subunit alpha type-7, -8 and fungal proteasome subunit alpha type-4

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_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 3.43e-151

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: 419.08  E-value: 3.43e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYtRIPALYQTDPSGTFSAWKANAT 163
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPD-GTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 79314743 164 GRNSNSIREFLEKNYKE-SAGQETVKLAIRALLEVVESGGKNIEVAVM 210
Cdd:cd03755 160 GRNSKTVREFLEKNYKEeMTRDDTIKLAIKALLEVVQSGSKNIELAVM 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 ...
 4-210 3.43e-151

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: 419.08  E-value: 3.43e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYtRIPALYQTDPSGTFSAWKANAT 163
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPD-GTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 79314743 164 GRNSNSIREFLEKNYKE-SAGQETVKLAIRALLEVVESGGKNIEVAVM 210
Cdd:cd03755 160 GRNSKTVREFLEKNYKEeMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-211 1.93e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.40  E-value: 1.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    1 MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKAD 80
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   81 ARVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPytRIPALYQTDPSGTFSAWKA 160
Cdd:PRK03996  87 ARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDD--GGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 79314743  161 NATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESGGK--NIEVAVMT 211
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKEDLSlEEAIELALKALAKANEGKLDpeNVEIAYID 218
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 4-211 2.94e-86

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: 255.27  E-value: 2.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743     4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDpyTRIPALYQTDPSGTFSAWKANAT 163
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79314743   164 GRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESG--GKNIEVAVMT 211
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSlDEAIELALKALYSAVEDKltPENVEVAYIT 211
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-212 4.93e-70

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 214.24  E-value: 4.93e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   1 MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTP-KLQDSRSARKIVSLDNHIALACAGLKA 79
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  80 DARVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSgGVRPFGLSTLIVGFDpyTRIPALYQTDPSGTFSAWK 159
Cdd:COG0638  86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEEK 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79314743 160 ANATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVES---GGKNIEVAVMTR 212
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYREDLSlDEAVELALRALYSAAERdsaSGDGIDVAVITE 219
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-210 6.83e-64

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: 197.40  E-value: 6.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    27 VRKGNAAVGVRGTDTVVLAVEKKST--PKLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVT 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   105 VEyITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAG- 183
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGG-PHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTl 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 79314743   184 QETVKLAIRALLEVVE---SGGKNIEVAVM 210
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 1.31e-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: 57.51  E-value: 1.31e-11
                           10        20
                   ....*....|....*....|...
gi 79314743      4 YDRAITVFSPDGHLFQVEYALEA 26
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 ...
 4-210 3.43e-151

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: 419.08  E-value: 3.43e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03755   1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYtRIPALYQTDPSGTFSAWKANAT 163
Cdd:cd03755  81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPD-GTPRLYQTDPSGTYSAWKANAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 79314743 164 GRNSNSIREFLEKNYKE-SAGQETVKLAIRALLEVVESGGKNIEVAVM 210
Cdd:cd03755 160 GRNSKTVREFLEKNYKEeMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 4.73e-113

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: 322.86  E-value: 4.73e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd01911   1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANAT 163
Cdd:cd01911  81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGG-PQLYQTDPSGTYFGYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 79314743 164 GRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESG--GKNIEVAVM 210
Cdd:cd01911 160 GKGSQEAKTFLEKRYKKDLTlEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-211 1.93e-93

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 274.40  E-value: 1.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    1 MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKAD 80
Cdd:PRK03996   7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   81 ARVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPytRIPALYQTDPSGTFSAWKA 160
Cdd:PRK03996  87 ARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDD--GGPRLFETDPSGAYLEYKA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 79314743  161 NATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESGGK--NIEVAVMT 211
Cdd:PRK03996 165 TAIGAGRDTVMEFLEKNYKEDLSlEEAIELALKALAKANEGKLDpeNVEIAYID 218
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 4-211 2.94e-86

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: 255.27  E-value: 2.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743     4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDpyTRIPALYQTDPSGTFSAWKANAT 163
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79314743   164 GRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESG--GKNIEVAVMT 211
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSlDEAIELALKALYSAVEDKltPENVEVAYIT 211
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-211 3.53e-84

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: 249.55  E-value: 3.53e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03756   2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTriPALYQTDPSGTFSAWKANAT 163
Cdd:cd03756  82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGG--PRLFETDPSGAYNEYKATAI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 79314743 164 GRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVESG--GKNIEVAVMT 211
Cdd:cd03756 160 GSGRQAVTEFLEKEYKEDMSlEEAIELALKALYAALEENetPENVEIAYVT 210
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-209 2.25e-70

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: 215.26  E-value: 2.25e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03750   1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTriPALYQTDPSGTFSAWKANAT 163
Cdd:cd03750  81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGG--PYLYQVDPSGSYFTWKATAI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 79314743 164 GRNSNSIREFLEKNYKESAGQE-TVKLAIRALLEVVESG--GKNIEVAV 209
Cdd:cd03750 159 GKNYSNAKTFLEKRYNEDLELEdAIHTAILTLKEGFEGQmtEKNIEIGI 207
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-212 4.93e-70

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 214.24  E-value: 4.93e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   1 MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTP-KLQDSRSARKIVSLDNHIALACAGLKA 79
Cdd:COG0638   6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  80 DARVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSgGVRPFGLSTLIVGFDpyTRIPALYQTDPSGTFSAWK 159
Cdd:COG0638  86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEEK 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79314743 160 ANATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVES---GGKNIEVAVMTR 212
Cdd:COG0638 163 AVAIGSGSPFARGVLEKEYREDLSlDEAVELALRALYSAAERdsaSGDGIDVAVITE 219
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-200 4.25e-68

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: 208.74  E-value: 4.25e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   3 RYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQD-SRSARKIVSLDNHIALACAGLKADA 81
Cdd:cd03752   2 RYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVAGITSDA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  82 RVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRIpALYQTDPSGTFSAWKAN 161
Cdd:cd03752  82 NILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGF-QLYQSDPSGNYSGWKAT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 79314743 162 ATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVES 200
Cdd:cd03752 161 AIGNNNQAAQSLLKQDYKDDMTlEEALALAVKVLSKTMDS 200
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-210 6.83e-64

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: 197.40  E-value: 6.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    27 VRKGNAAVGVRGTDTVVLAVEKKST--PKLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVT 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   105 VEyITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAG- 183
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGG-PHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTl 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 79314743   184 QETVKLAIRALLEVVE---SGGKNIEVAVM 210
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 5.94e-61

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: 190.63  E-value: 5.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03753   1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGV-----RPFGLSTLIVGFDPYTriPALYQTDPSGTFSAW 158
Cdd:cd03753  81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG--PQLFHTDPSGTFTRC 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79314743 159 KANATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVES--GGKNIEVAVM 210
Cdd:cd03753 159 DAKAIGSGSEGAQSSLQEKYHKDMTlEEAEKLALSILKQVMEEklNSTNVELATV 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-209 1.64e-59

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: 187.11  E-value: 1.64e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLqdSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03749   1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL--SSYQKKIFKVDDHIGIAIAGLTADARV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDpyTRIPALYQTDPSGTFSAWKANAT 163
Cdd:cd03749  79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD--ESGPHLFQTCPSGNYFEYKATSI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 79314743 164 GRNSNSIREFLEKN---YKESAGQETVKLAIRALLEVVESGG----KNIEVAV 209
Cdd:cd03749 157 GARSQSARTYLERHfeeFEDCSLEELIKHALRALRETLPGEQeltiKNVSIAI 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 3-212 1.58e-58

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 185.83  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743    3 RYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQD-SRSARKIVSLDNHIALACAGLKADA 81
Cdd:PTZ00246   4 RYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDpGKINEKIYKIDSHIFCAVAGLTADA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   82 RVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRIpALYQTDPSGTFSAWKAN 161
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGY-QLYHTDPSGNYSGWKAT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 79314743  162 ATGRNSNSIREFLEKNYKESAG-QETVKLAIRALLEVVES---GGKNIEVAVMTR 212
Cdd:PTZ00246 163 AIGQNNQTAQSILKQEWKEDLTlEQGLLLAAKVLTKSMDStspKADKIEVGILSH 217
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 33-210 1.65e-56

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: 178.07  E-value: 1.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  33 AVGVRGTDTVVLAVEKKSTPKLQD-SRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTVEYITRY 111
Cdd:cd01906   3 IVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 112 IAGLQQKYTQSggVRPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAG-QETVKLA 190
Cdd:cd01906  83 LANLLYEYTQS--LRPLGVSLLVAGVDEEGG-PQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTlEEAIELA 159

                       170       180
                ....*....|....*....|...
gi 79314743 191 IRALLEVVESG---GKNIEVAVM 210
Cdd:cd01906 160 LKALKSALERDlysGGNIEVAVI 182
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-197 2.74e-51

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: 165.92  E-value: 2.74e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARV 83
Cdd:cd03751   4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  84 LINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTriPALYQTDPSGTFSAWKANAT 163
Cdd:cd03751  84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG--PQLYMIEPSGVSYGYFGCAI 161

                       170       180       190
                ....*....|....*....|....*....|....*
gi 79314743 164 GRNSNSIREFLEK-NYKESAGQETVKLAIRALLEV 197
Cdd:cd03751 162 GKGKQAAKTELEKlKFSELTCREAVKEAAKIIYIV 196
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-209 4.21e-50

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: 163.17  E-value: 4.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743   4 YDRAITVFSPDGHLFQVEYALEAVRKGN-AAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADAR 82
Cdd:cd03754   2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  83 VLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPyTRIPALYQTDPSGTFSAWKANA 162
Cdd:cd03754  82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDE-ELGPQLYKCDPAGYFAGYKATA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 79314743 163 TGRNSNSIREFLEKNYKESAG-----QETVKLAIRALLEVVESG--GKNIEVAV 209
Cdd:cd03754 161 AGVKEQEATNFLEKKLKKKPDliesyEETVELAISCLQTVLSTDfkATEIEVGV 214
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 33-196 1.23e-37

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: 129.44  E-value: 1.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  33 AVGVRGTDTVVLAVEKKSTPKLQD-SRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTVEYITRY 111
Cdd:cd01901   3 SVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 112 IAGLQQKYTQsggVRPFGLSTLIVGFDPYTriPALYQTDPSGTFSAW-KANATGRNSNSIREFLEKNYKESAG-QETVKL 189
Cdd:cd01901  83 LAKLLQVYTQ---GRPFGVNLIVAGVDEGG--GNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTlEEAVEL 157


                ....*..
gi 79314743 190 AIRALLE 196
Cdd:cd01901 158 ALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-212 1.67e-19

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


Pssm-ID: 238893  Cd Length: 189  Bit Score: 82.88  E-value: 1.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  34 VGVRGTDTVVLAVEKKSTP-KLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTVEYITRYI 112
Cdd:cd01912   4 VGIKGKDGVVLAADTRASAgSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANLL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 113 AGLQQKYtQSGgvrPFGLSTLIVGFDPYTRiPALYQTDPSGTFSawKAN--ATGRNSNSIREFLEKNYKE--SAgQETVK 188
Cdd:cd01912  84 SNILYSY-RGF---PYYVSLIVGGVDKGGG-PFLYYVDPLGSLI--EAPfvATGSGSKYAYGILDRGYKPdmTL-EEAVE 155

                       170       180
                ....*....|....*....|....*...
gi 79314743 189 LAIRALLEVVE----SGGkNIEVAVMTR 212
Cdd:cd01912 156 LVKKAIDSAIErdlsSGG-GVDVAVITK 182
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-212 4.77e-19

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: 81.53  E-value: 4.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  33 AVGVRGTDTVVLAVEKKST-PKLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTVEYITRY 111
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 112 IAGLqqkyTQSGGVRPFGLSTLIVGFDPYTriPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAG-QETVKLA 190
Cdd:cd03764  83 LSNI----LNSSKYFPYIVQLLIGGVDEEG--PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTvEEAKKLA 156

                       170       180
                ....*....|....*....|....*
gi 79314743 191 IRALLEVVE---SGGKNIEVAVMTR 212
Cdd:cd03764 157 IRAIKSAIErdsASGDGIDVVVITK 181
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 1.31e-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: 57.51  E-value: 1.31e-11
                           10        20
                   ....*....|....*....|...
gi 79314743      4 YDRAITVFSPDGHLFQVEYALEA 26
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 ...
 4-26 1.84e-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: 56.97  E-value: 1.84e-11
                          10        20
                  ....*....|....*....|...
gi 79314743     4 YDRAITVFSPDGHLFQVEYALEA 26
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-212 1.65e-05

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: 44.11  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  34 VGVRGTDTVVLAVEKKST--PKLQDsRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRL-TLEDPVTVEYITR 110
Cdd:cd03763   4 VGVVFKDGVVLGADTRATegPIVAD-KNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLnTGRKPRVVTALTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 111 yiagLQQK-YTQSGGVrpfGLSTLIVGFDPYTriPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAG-QETVK 188
Cdd:cd03763  83 ----LKQHlFRYQGHI---GAALVLGGVDYTG--PHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTeEEAKK 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 79314743 189 LAIRAllevVESG-------GKNIEVAVMTR 212
Cdd:cd03763 154 LVCEA----IEAGifndlgsGSNVDLCVITK 180
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-197 2.25e-04

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: 41.03  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  34 VGVRGTDTVVLA---VEKKSTPKLQDSrsARKIVSLDNHIALACAGLKAD---------ARVLINKARiecqsHRLTLED 101
Cdd:cd03758   5 IGIKGKDFVILAadtSAARSILVLKDD--EDKIYKLSDHKLMACSGEAGDrlqfaeyiqKNIQLYKMR-----NGYELSP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743 102 PVTVEYITRYIAglqqKYTQSGGvrPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKES 181
Cdd:cd03758  78 KAAANFTRRELA----ESLRSRT--PYQVNLLLAGYDKVEG-PSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPD 150

                       170
                ....*....|....*..
gi 79314743 182 -AGQETVKLAIRALLEV 197
Cdd:cd03758 151 mTVEEALELMKKCIKEL 167
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-174 2.77e-04

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: 40.71  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79314743  30 GNAAVGVRGTDTVVLAVEKK-STPKLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTveyi 108
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRlSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS---- 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79314743 109 TRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRiPALYQTDPSGTFSAWKANATGRNSNSIREFL 174
Cdd:cd03757  84 TEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGK-GVVYSYDPVGSYERETYSAGGSASSLIQPLL 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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