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Conserved domains on  [gi|2131918889|emb|CAG8433880|]
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8251_t:CDS:2 [Entrophospora candida]

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 ...
 5-212 3.39e-162

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: 446.42  E-value: 3.39e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDaNDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFD-PDGTPRLYQTDPSGTYSAWKANAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQTGAKNIEIAVM 212
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 ...
 5-212 3.39e-162

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: 446.42  E-value: 3.39e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDaNDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFD-PDGTPRLYQTDPSGTYSAWKANAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQTGAKNIEIAVM 212
Cdd:cd03755   160 GRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-215 2.20e-98

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 286.34  E-value: 2.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   1 MAGsYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSA 80
Cdd:PRK03996    7 QMG-YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  81 DARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWK 160
Cdd:PRK03996   86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYLEYK 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131918889 161 ANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ--TGAKNIEIAVMTND 215
Cdd:PRK03996  164 ATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVE 220
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-215 4.45e-93

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: 272.22  E-value: 4.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ--TGAKNIEIAVMTND 215
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEdkLTPENVEVAYITVE 213
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-220 3.60e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 226.95  E-value: 3.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   1 MAGSYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVL-KLQDPRTVRKIVMLDDHVCMAFAGLS 79
Cdd:COG0638     5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  80 ADARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSgGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAW 159
Cdd:COG0638    85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131918889 160 KANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ----TGaKNIEIAVMTNDAIIKV 220
Cdd:COG0638   162 KAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITEDGFREL 225
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-212 1.37e-71

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: 216.66  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  28 VRKGTCAVGVRGEDCVVLGVEKKSVL--KLQDPRTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVT 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 106 VEyITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDKvPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSK 185
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGG-PHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 2131918889 186 DETIKLAVKSLLEVVQ---TGAKNIEIAVM 212
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 5.23e-12

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: 58.28  E-value: 5.23e-12
                           10        20
                   ....*....|....*....|...
gi 2131918889    5 YDRALTVFSPDGHLFQVEYALEA 27
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 ...
 5-212 3.39e-162

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: 446.42  E-value: 3.39e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDaNDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFD-PDGTPRLYQTDPSGTYSAWKANAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQTGAKNIEIAVM 212
Cdd:cd03755   160 GRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-212 1.31e-121

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: 344.04  E-value: 1.31e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd01911     1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDaNDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd01911    81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYD-EEGGPQLYQTDPSGTYFGYKATAI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQTG--AKNIEIAVM 212
Cdd:cd01911   160 GKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-215 2.20e-98

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 286.34  E-value: 2.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   1 MAGsYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSA 80
Cdd:PRK03996    7 QMG-YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  81 DARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWK 160
Cdd:PRK03996   86 DARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYLEYK 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2131918889 161 ANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ--TGAKNIEIAVMTND 215
Cdd:PRK03996  164 ATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVE 220
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-215 4.45e-93

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: 272.22  E-value: 4.45e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ--TGAKNIEIAVMTND 215
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEdkLTPENVEVAYITVE 213
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-213 4.06e-91

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: 266.89  E-value: 4.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03756     2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03756    82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD--DGGPRLFETDPSGAYNEYKATAI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ--TGAKNIEIAVMT 213
Cdd:cd03756   160 GSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEenETPENVEIAYVT 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-220 3.60e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 226.95  E-value: 3.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   1 MAGSYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVL-KLQDPRTVRKIVMLDDHVCMAFAGLS 79
Cdd:COG0638     5 QQSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  80 ADARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSgGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAW 159
Cdd:COG0638    85 ADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD--DGGPRLFSTDPSGGLYEE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131918889 160 KANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQ----TGaKNIEIAVMTNDAIIKV 220
Cdd:COG0638   162 KAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITEDGFREL 225
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-215 1.26e-74

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: 225.66  E-value: 1.26e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03750     1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03750    81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD--EGGPYLYQVDPSGSYFTWKATAI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVV--QTGAKNIEIAVMTND 215
Cdd:cd03750   159 GKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFegQMTEKNIEIGICGET 211
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 28-212 1.37e-71

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: 216.66  E-value: 1.37e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  28 VRKGTCAVGVRGEDCVVLGVEKKSVL--KLQDPRTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVT 105
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 106 VEyITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDKvPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSK 185
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGG-PHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 2131918889 186 DETIKLAVKSLLEVVQ---TGAKNIEIAVM 212
Cdd:pfam00227 159 EEAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-212 6.81e-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: 207.97  E-value: 6.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQD-PRTVRKIVMLDDHVCMAFAGLSADAR 83
Cdd:cd03752     3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVAGITSDAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  84 VLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDKVpRLYQTDPSGIYSAWKANS 163
Cdd:cd03752    83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGF-QLYQSDPSGNYSGWKATA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2131918889 164 IGRSSKTVREFLEKNYKEGLSKDETIKLAVKSL---LEVVQTGAKNIEIAVM 212
Cdd:cd03752   162 IGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLsktMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-215 2.70e-64

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 200.46  E-value: 2.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   1 MAGSYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDP-RTVRKIVMLDDHVCMAFAGLS 79
Cdd:PTZ00246    1 MSRRYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  80 ADARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDKVpRLYQTDPSGIYSAW 159
Cdd:PTZ00246   81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGY-QLYHTDPSGNYSGW 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2131918889 160 KANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQT---GAKNIEIAVMTND 215
Cdd:PTZ00246  160 KATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDStspKADKIEVGILSHG 218
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-211 2.06e-62

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: 194.05  E-value: 2.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRtvRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIAGLTADARV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03749    79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYD--ESGPHLFQTCPSGNYFEYKATSI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2131918889 165 GRSSKTVREFLEKNYK--EGLSKDETIKLAVKSLLEVVQTG----AKNIEIAV 211
Cdd:cd03749   157 GARSQSARTYLERHFEefEDCSLEELIKHALRALRETLPGEqeltIKNVSIAI 209
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-212 2.45e-62

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 194.09  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGV-----RPFGISTLIIGFDANDkvPRLYQTDPSGIYSAW 159
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG--PQLFHTDPSGTFTRC 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2131918889 160 KANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEVVQT--GAKNIEIAVM 212
Cdd:cd03753   159 DAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEklNSTNVELATV 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 32-212 6.46e-62

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: 191.55  E-value: 6.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  32 TCAVGVRGEDCVVLGVEKKSVLKLQD-PRTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTVEYIT 110
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 111 RYIAGVQQKYTQSggVRPFGISTLIIGFDANDKvPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSKDETIK 190
Cdd:cd01906    81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGG-PQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIE 157

                         170       180
                  ....*....|....*....|....*
gi 2131918889 191 LAVKSLLEVVQTGA---KNIEIAVM 212
Cdd:cd01906   158 LALKALKSALERDLysgGNIEVAVI 182
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-199 1.58e-53

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: 171.31  E-value: 1.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADARV 84
Cdd:cd03751     4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  85 LVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDkvPRLYQTDPSGIYSAWKANSI 164
Cdd:cd03751    84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG--PQLYMIEPSGVSYGYFGCAI 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2131918889 165 GRSSKTVREFLEKNYKEGLSKDETIKLAVKSLLEV 199
Cdd:cd03751   162 GKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIV 196
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-211 1.64e-53

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: 171.65  E-value: 1.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEAVRK-GTCAVGVRGEDCVVLGVEKKSVLKLQDPRTVRKIVMLDDHVCMAFAGLSADAR 83
Cdd:cd03754     2 FDRHITIFSPEGRLYQVEYAFKAVKNaGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  84 VLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYTQSGGVRPFGISTLIIGFDANDKvPRLYQTDPSGIYSAWKANS 163
Cdd:cd03754    82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELG-PQLYKCDPAGYFAGYKATA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2131918889 164 IGRSSKTVREFLEKNYKE----GLSKDETIKLAVKSLLEVVQTG--AKNIEIAV 211
Cdd:cd03754   161 AGVKEQEATNFLEKKLKKkpdlIESYEETVELAISCLQTVLSTDfkATEIEVGV 214
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 32-198 3.62e-42

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: 140.61  E-value: 3.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  32 TCAVGVRGEDCVVLGVEKKSVLKLQDP-RTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTVEYIT 110
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 111 RYIAGVQQKYTQsggVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAW-KANSIGRSSKTVREFLEKNYKEGLSKDETI 189
Cdd:cd01901    81 KELAKLLQVYTQ---GRPFGVNLIVAGVD--EGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAV 155


                  ....*....
gi 2131918889 190 KLAVKSLLE 198
Cdd:cd01901   156 ELALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-220 1.16e-24

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: 96.36  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  32 TCAVGVRGEDCVVLGVEKKS-----VLKlqdpRTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTV 106
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRAsagslVAS----RNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 107 EYITRYIAGVQQKYtQSGgvrPFGISTLIIGFDANDKvPRLYQTDPSGiySAWKAN--SIGRSSKTVREFLEKNYKEGLS 184
Cdd:cd01912    77 KAAANLLSNILYSY-RGF---PYYVSLIVGGVDKGGG-PFLYYVDPLG--SLIEAPfvATGSGSKYAYGILDRGYKPDMT 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2131918889 185 KDETIKLAVKSLLEV----VQTGaKNIEIAVMTNDAIIKV 220
Cdd:cd01912   150 LEEAVELVKKAIDSAierdLSSG-GGVDVAVITKDGVEEL 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-215 8.77e-21

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: 86.15  E-value: 8.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  32 TCAVGVRGEDCVVLGVEKKSVL-KLQDPRTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTVEYIT 110
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMgNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 111 RYIAGVqqkyTQSGGVRPFGISTLIIGFDanDKVPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSKDETIK 190
Cdd:cd03764    81 TLLSNI----LNSSKYFPYIVQLLIGGVD--EEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKK 154

                         170       180
                  ....*....|....*....|....*....
gi 2131918889 191 LAVKSLLEVVQ----TGaKNIEIAVMTND 215
Cdd:cd03764   155 LAIRAIKSAIErdsaSG-DGIDVVVITKD 182
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 5-27 5.23e-12

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: 58.28  E-value: 5.23e-12
                           10        20
                   ....*....|....*....|...
gi 2131918889    5 YDRALTVFSPDGHLFQVEYALEA 27
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 5-27 1.03e-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: 57.36  E-value: 1.03e-11
                          10        20
                  ....*....|....*....|...
gi 2131918889   5 YDRALTVFSPDGHLFQVEYALEA 27
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-221 2.99e-10

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: 57.60  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  33 CAVGVRGEDCVVL---GVEKKSVLKLQDprTVRKIVMLDDHVCMAFAGLSAD---------ARVLVNKARiecqsHRLTV 100
Cdd:cd03758     3 TLIGIKGKDFVILaadTSAARSILVLKD--DEDKIYKLSDHKLMACSGEAGDrlqfaeyiqKNIQLYKMR-----NGYEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 101 EDPVTVEYITRYIAgvqqKYTQSGGvrPFGISTLIIGFDANDKvPRLYQTDPSGiySAWKAN--SIGRSSKTVREFLEKN 178
Cdd:cd03758    76 SPKAAANFTRRELA----ESLRSRT--PYQVNLLLAGYDKVEG-PSLYYIDYLG--TLVKVPyaAHGYGAYFCLSILDRY 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2131918889 179 YKEGLSKDETIKLAVKSLLE-----VVQTgaKNIEIAVMTNDAIIKVN 221
Cdd:cd03758   147 YKPDMTVEEALELMKKCIKElkkrfIINL--PNFTVKVVDKDGIRDLE 192
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-197 3.81e-09

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: 54.51  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  32 TCAVGVRGEDCVVLGVEKKSVlklQDP----RTVRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTVE 107
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRAT---EGPivadKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 108 YITRYIagVQQKYTQSGGVrpfGISTLIIGFDANDkvPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSKDE 187
Cdd:cd03763    78 TALTML--KQHLFRYQGHI---GAALVLGGVDYTG--PHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEE 150

                         170
                  ....*....|
gi 2131918889 188 TIKLAVKSLL 197
Cdd:cd03763   151 AKKLVCEAIE 160
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 3-196 2.11e-05

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 44.21  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889   3 GSYDRALTVFSPDGHLfQVEYAleavrKGTCAVGVRGEDCVVLGVEKKSVlklQDP----RTVRKIVMLDDHVCMAFAGL 78
Cdd:PTZ00488   17 GDFLAEYTFDHGDANK-AIEFA-----HGTTTLAFKYGGGIIIAVDSKAT---AGPyiasQSVKKVIEINPTLLGTMAGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  79 SADARVLVNKARIECQSHRLTVEDPVTVEYITRYIAGVQQKYtqsggvRPFGIS--TLIIGFDanDKVPRLYQTDPSGIY 156
Cdd:PTZ00488   88 AADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNY------KGMGLSmgTMICGWD--KKGPGLFYVDNDGTR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2131918889 157 SAWKANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKSL 196
Cdd:PTZ00488  160 LHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 60-195 2.54e-03

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 37.61  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  60 TVRKIVMLDDHVCMAFAGLSADA----RVLVnkarIECQSHRLTVEDPVTVEYITRYIAGVQQKYtqsggvRPFGIS--T 133
Cdd:cd03761    30 TVKKVIEINPYLLGTMAGGAADCqyweRVLG----RECRLYELRNKERISVAAASKLLSNMLYQY------KGMGLSmgT 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131918889 134 LIIGFDANDkvPRLYQTDPSGIYSAWKANSIGRSSKTVREFLEKNYKEGLSKDETIKLAVKS 195
Cdd:cd03761   100 MICGWDKTG--PGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-219 9.21e-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: 36.07  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889  31 GTCAVGVRGEDCVVLGVEKKSVLKLQDPRT-VRKIVMLDDHVCMAFAGLSADARVLVNKARIECQSHRLTVEDPVTVEYI 109
Cdd:cd03759     3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTdFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131918889 110 TRYIAGVQqkYTQSGGvrPFGISTLIIGFDANDKvPRLYQTDpsgiysawkanSIGRSSK--------TVREFL----EK 177
Cdd:cd03759    83 SSLISSLL--YEKRFG--PYFVEPVVAGLDPDGK-PFICTMD-----------LIGCPSIpsdfvvsgTASEQLygmcES 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2131918889 178 NYKEGLSKDETIKLAVKSLLEVVQTGA---KNIEIAVMTNDAIIK 219
Cdd:cd03759   147 LWRPDMEPDELFETISQALLSAVDRDAlsgWGAVVYIITKDKVTT 191
 
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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