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Conserved domains on  [gi|2567451157|ref|XP_058994570|]
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proteasome subunit beta type-4 isoform X1 [Mustela lutreola]

Protein Classification

proteasome subunit beta( domain architecture ID 10132923)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-247 1.09e-131

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 371.13  E-value: 1.09e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPR 131
Cdd:cd03760     1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRSKMNPLWNTMVIGGYAD-GESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQSEA 210
Cdd:cd03760    81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2567451157 211 RELVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGP 247
Cdd:cd03760   161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-247 1.09e-131

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 371.13  E-value: 1.09e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPR 131
Cdd:cd03760     1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRSKMNPLWNTMVIGGYAD-GESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQSEA 210
Cdd:cd03760    81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2567451157 211 RELVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGP 247
Cdd:cd03760   161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 50-237 1.34e-40

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: 139.24  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  50 MVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRN-ISRIMRVNDSTMLGASGDYADFQYLKQVLgQMVIDEELLGDGHSY 128
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRA-RAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 129 SPR--AIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLS 206
Cdd:pfam00227  80 PVElaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2567451157 207 QSEARELVERCMRVLYYRDARSYNRFQIATV 237
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 53-242 4.99e-16

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 74.17  E-value: 4.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  53 GTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVL-GQMVIDEelLGDGHSYSPR 131
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILkAEAKLYE--LRRGRPMSVK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRskMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLSQSEAR 211
Cdd:TIGR03634  79 ALATLLSNILNSNR--FFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLED--EYREDMSVEEAK 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2567451157 212 ELVERCMRVLYYRDARSYNRFQIATVTEKGV 242
Cdd:TIGR03634 155 KLAVRAIKSAIERDVASGNGIDVAVITKDGV 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 52-245 4.19e-15

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 72.87  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADfqylkqvlGQMVID--------EELLG 123
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVAD--------ARELVRlarveaqlYELRY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 124 dGHSYSPRAIHSWLTRAMYSR-RSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAqpllREVLEKQ 202
Cdd:COG0638   106 -GEPISVEGLAKLLSDLLQGYtQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFA----RGVLEKE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2567451157 203 --PVLSQSEARELVERCMRVLYYRDARSYNRFQIATVTEKGVEIE 245
Cdd:COG0638   181 yrEDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 18-228 3.16e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.45  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  18 PGQFYHIP-PTPGASLEPASSPYG-GPITRTqnpMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNdSTM 95
Cdd:PTZ00488    5 PEHFEHPPgAHPGDFLAEYTFDHGdANKAIE---FAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEIN-PTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  96 LGA-SGDYADFQYLKQVLGQMVIDEELLgDGHSYSPRAIHSWLTRAMYSRRSkMNPLWNTMVIGGYADGESfLGYVDMLG 174
Cdd:PTZ00488   81 LGTmAGGAADCSFWERELAMQCRLYELR-NGELISVAAASKILANIVWNYKG-MGLSMGTMICGWDKKGPG-LFYVDNDG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2567451157 175 VAYEAPSLATGYGAYLAQPLLREVLEKQpvLSQSEARELVERCMRVLYYRDARS 228
Cdd:PTZ00488  158 TRLHGNMFSCGSGSTYAYGVLDAGFKWD--LNDEEAQDLGRRAIYHATFRDAYS 209
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-247 1.09e-131

proteasome beta type-4 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: 239729  Cd Length: 197  Bit Score: 371.13  E-value: 1.09e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPR 131
Cdd:cd03760     1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRSKMNPLWNTMVIGGYAD-GESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQSEA 210
Cdd:cd03760    81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKPDLTEEEA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2567451157 211 RELVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGP 247
Cdd:cd03760   161 RALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 54-245 8.89e-67

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: 206.14  E-value: 8.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLgDGHSYSPRAI 133
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELR-NGRELSVKAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 134 HSWLTRAMYSRRSkmNPLWNTMVIGGY-ADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQpvLSQSEARE 212
Cdd:cd01912    80 ANLLSNILYSYRG--FPYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD--MTLEEAVE 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2567451157 213 LVERCMRVLYYRDARSYNRFQIATVTEKGVEIE 245
Cdd:cd01912   156 LVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 54-237 1.01e-50

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: 164.98  E-value: 1.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLgDGHSYSPRAI 133
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLR-YGEPIPVEAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 134 HSWLTRAMYSRRSKMNPLWNTMVIGGY-ADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQpvLSQSEARE 212
Cdd:cd01906    80 AKLLANLLYEYTQSLRPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD--MTLEEAIE 157

                         170       180
                  ....*....|....*....|....*
gi 2567451157 213 LVERCMRVLYYRDARSYNRFQIATV 237
Cdd:cd01906   158 LALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 50-237 1.34e-40

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: 139.24  E-value: 1.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  50 MVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRN-ISRIMRVNDSTMLGASGDYADFQYLKQVLgQMVIDEELLGDGHSY 128
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRA-RAEAQLYRLRYGRPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 129 SPR--AIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLS 206
Cdd:pfam00227  80 PVElaARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK--LYRPDLT 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2567451157 207 QSEARELVERCMRVLYYRDARSYNRFQIATV 237
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 54-219 1.25e-31

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: 115.18  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMVIDEELLgDGHSYSPRAI 133
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLR-YGEPISVVAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 134 HSWLTRAMYSRRSkMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPS-LATGYGAYLAQPLLREVLEKQpvLSQSEARE 212
Cdd:cd01901    80 AKELAKLLQVYTQ-GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGaVATGSRSQRAKSLLEKLYKPD--MTLEEAVE 156


                  ....*..
gi 2567451157 213 LVERCMR 219
Cdd:cd01901   157 LALKALK 163
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 53-242 4.99e-16

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 74.17  E-value: 4.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  53 GTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVL-GQMVIDEelLGDGHSYSPR 131
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILkAEAKLYE--LRRGRPMSVK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRskMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLSQSEAR 211
Cdd:TIGR03634  79 ALATLLSNILNSNR--FFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLED--EYREDMSVEEAK 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2567451157 212 ELVERCMRVLYYRDARSYNRFQIATVTEKGV 242
Cdd:TIGR03634 155 KLAVRAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 54-245 1.23e-15

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: 73.44  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVL-GQMVIDEelLGDGHSYSPRA 132
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILkAEARLYE--LRRGRPMSIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 133 IHSWLTRAMYSrrSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAylaqPLLREVLEKQ--PVLSQSEA 210
Cdd:cd03764    79 LATLLSNILNS--SKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGS----PYAYGVLEDEykEDMTVEEA 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2567451157 211 RELVERCMRVLYYRDARSYNRFQIATVTEKGVEIE 245
Cdd:cd03764   153 KKLAIRAIKSAIERDSASGDGIDVVVITKDGYKEL 187
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 52-245 4.19e-15

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 72.87  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADfqylkqvlGQMVID--------EELLG 123
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVAD--------ARELVRlarveaqlYELRY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 124 dGHSYSPRAIHSWLTRAMYSR-RSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAqpllREVLEKQ 202
Cdd:COG0638   106 -GEPISVEGLAKLLSDLLQGYtQYGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFA----RGVLEKE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2567451157 203 --PVLSQSEARELVERCMRVLYYRDARSYNRFQIATVTEKGVEIE 245
Cdd:COG0638   181 yrEDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 55-243 4.83e-13

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: 66.07  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  55 SVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYAD-FQYLKQVlgQMVIDEELLGDGHSYSPRAI 133
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDrLQFAEYI--QKNIQLYKMRNGYELSPKAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 134 HSWlTR---AMYSRRSKmnPLWNTMVIGGY-ADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLSQSE 209
Cdd:cd03758    81 ANF-TRrelAESLRSRT--PYQVNLLLAGYdKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR--YYKPDMTVEE 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2567451157 210 ARELVERCMRVLYYRDARSYNRFQIATVTEKGVE 243
Cdd:cd03758   156 ALELMKKCIKELKKRFIINLPNFTVKVVDKDGIR 189
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 37-245 1.50e-10

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: 59.58  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  37 SPYggpitrTQNpmvtGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQYLKQVLGQMv 116
Cdd:cd03757     2 SPY------TDN----GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKAR- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 117 IDEELLGDGHSYSPRAIHSWLTRAMYSRRSkmNPLWNTMVIGGY-ADGESFLGYVDMLGvAYEAPSL-ATGYGAYLAQPL 194
Cdd:cd03757    71 IKMYKYSHNKEMSTEAIAQLLSTILYSRRF--FPYYVFNILAGIdEEGKGVVYSYDPVG-SYERETYsAGGSASSLIQPL 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2567451157 195 LREVLEKQP-------VLSQSEARELVERCMRVLYYRDARSYNRFQIATVTEKGVEIE 245
Cdd:cd03757   148 LDNQVGRKNqnnvertPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEE 205
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-228 2.18e-08

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: 53.02  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  52 TGTSVLGVKFEGGVVIAADM-LGSYGSLARFrNISRIMRVNDSTMLGASGDYADFQYLKQVLgQMVIDEELLGDGHSYSP 130
Cdd:cd03759     2 NGGAVVAMAGKDCVAIASDLrLGVQQQTVST-DFQKVFRIGDRLYIGLAGLATDVQTLAQKL-RFRVNLYRLREEREIKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 131 RAIHSWLTRAMYSRRskMNPLWNTMVIGGY-ADGESFLGYVDMLGvayeAPSLATGYG-AYLAQPLLREVLEK--QPVLS 206
Cdd:cd03759    80 KTFSSLISSLLYEKR--FGPYFVEPVVAGLdPDGKPFICTMDLIG----CPSIPSDFVvSGTASEQLYGMCESlwRPDME 153

                         170       180
                  ....*....|....*....|..
gi 2567451157 207 QSEARELVERCMRVLYYRDARS 228
Cdd:cd03759   154 PDELFETISQALLSAVDRDALS 175
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 18-228 3.16e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.45  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  18 PGQFYHIP-PTPGASLEPASSPYG-GPITRTqnpMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNdSTM 95
Cdd:PTZ00488    5 PEHFEHPPgAHPGDFLAEYTFDHGdANKAIE---FAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEIN-PTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  96 LGA-SGDYADFQYLKQVLGQMVIDEELLgDGHSYSPRAIHSWLTRAMYSRRSkMNPLWNTMVIGGYADGESfLGYVDMLG 174
Cdd:PTZ00488   81 LGTmAGGAADCSFWERELAMQCRLYELR-NGELISVAAASKILANIVWNYKG-MGLSMGTMICGWDKKGPG-LFYVDNDG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2567451157 175 VAYEAPSLATGYGAYLAQPLLREVLEKQpvLSQSEARELVERCMRVLYYRDARS 228
Cdd:PTZ00488  158 TRLHGNMFSCGSGSTYAYGVLDAGFKWD--LNDEEAQDLGRRAIYHATFRDAYS 209
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 54-243 1.35e-05

proteasome beta type-6 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: 239731  Cd Length: 188  Bit Score: 44.91  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNDSTMLGASGDYADFQ----YLKQVLGQMVIDEEllgdghsyS 129
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQaiadYVRYYLDMHSIELG--------E 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 130 PRAIHSW--LTRAM-YSRRskmNPLWNTMVIGGYADGESFLGY-VDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVL 205
Cdd:cd03762    73 PPLVKTAasLFKNLcYNYK---EMLSAGIIVAGWDEQNGGQVYsIPLGGMLIRQPFAIGGSGSTYIYGYVDA--NYKPGM 147

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2567451157 206 SQSEARELVERCMRVLYYRDARSYNRFQIATVTEKGVE 243
Cdd:cd03762   148 TLEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVE 185
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 54-243 1.58e-04

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: 41.85  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157  54 TSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNdSTMLGA-SGDYADFQYLKQVLG-QMVIDEelLGDGHSYSPR 131
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEIN-PYLLGTmAGGAADCQYWERVLGrECRLYE--LRNKERISVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2567451157 132 AIHSWLTRAMYSRRSkMNPLWNTMVIGGYADGESfLGYVDMLGVAYEAPSLATGYGAYLAQPLLREvlEKQPVLSQSEAR 211
Cdd:cd03761    78 AASKLLSNMLYQYKG-MGLSMGTMICGWDKTGPG-LYYVDSDGTRLKGDLFSVGSGSTYAYGVLDS--GYRYDLSVEEAY 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2567451157 212 ELVERCMRVLYYRDARSYNRFQIATVTEKGVE 243
Cdd:cd03761   154 DLARRAIYHATHRDAYSGGNVNLYHVREDGWR 185
 
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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