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Conserved domains on  [gi|2062817455|ref|XP_006975993|]
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proteasome subunit beta type-1 isoform X4 [Peromyscus maniculatus bairdii]

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 112-323 6.88e-148

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: 414.35  E-value: 6.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 112 FSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 191
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 192 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 271
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062817455 272 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 323
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 112-323 6.88e-148

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: 414.35  E-value: 6.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 112 FSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 191
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 192 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 271
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062817455 272 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 323
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 117-308 6.91e-49

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: 161.58  E-value: 6.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 117 FNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDS-PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMT- 194
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 195 --TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgFKNMqnve 272
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL---- 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2062817455 273 hvplSLDRAMRLVKDVFISAAERDVYTGDALRICIV 308
Cdd:pfam00227 157 ----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 99-317 5.56e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 116.40  E-value: 5.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455  99 MGPHGSAGPVQL--RFSP--------YAFN----GGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGC 164
Cdd:COG0638     1 MQPSQQSSYDRAitIFSPdgrlyqveYAREavkrGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 165 SGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYS---RRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQ 241
Cdd:COG0638    81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062817455 242 RDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP-LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 317
Cdd:COG0638   160 EEKAVAIGSGSPFARGVLEK----------EYREdLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 102-312 6.66e-10

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 58.46  E-value: 6.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 102 HGSaGPVQLRFSpyafNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEAR 181
Cdd:PTZ00488   27 HGD-ANKAIEFA----HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 182 LKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGaVYSFDPVGSYQRDSFKAGGSASAMLQPLLDn 261
Cdd:PTZ00488  102 CRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLD- 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2062817455 262 qVGFKnmqnvehVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 312
Cdd:PTZ00488  180 -AGFK-------WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 112-323 6.88e-148

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: 414.35  E-value: 6.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 112 FSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNK 191
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 192 AMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNV 271
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062817455 272 EHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD 323
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 120-317 2.34e-75

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: 229.64  E-value: 2.34e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 120 GTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 199
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 200 AMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLSLD 279
Cdd:cd01912    81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD---------MTLE 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2062817455 280 RAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 317
Cdd:cd01912   152 EAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 120-308 2.44e-53

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: 173.06  E-value: 2.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 120 GTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 199
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 200 AMLSTILYSRRF--FPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLS 277
Cdd:cd01906    81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD---------MT 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2062817455 278 LDRAMRLVKDVFISAAERDVYTGDALRICIV 308
Cdd:cd01906   152 LEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 117-308 6.91e-49

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: 161.58  E-value: 6.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 117 FNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDS-PKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMT- 194
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 195 --TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgFKNMqnve 272
Cdd:pfam00227  82 elAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL---- 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2062817455 273 hvplSLDRAMRLVKDVFISAAERDVYTGDALRICIV 308
Cdd:pfam00227 157 ----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 121-316 2.71e-41

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: 142.01  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 121 TVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 200
Cdd:cd03764     2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 201 MLSTILYSRRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDnqVGFKNmqnvehvPLSLDR 280
Cdd:cd03764    82 LLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE--DEYKE-------DMTVEE 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2062817455 281 AMRLVKDVFISAAERDVYTGDALRICIVTKEGIREE 316
Cdd:cd03764   152 AKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 117-313 1.88e-31

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: 116.57  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 117 FNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTG 196
Cdd:cd03759     1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 197 AIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVG--SYQRDsFKAGGSASAMLQPLLDNQVGfKNMqnvehv 274
Cdd:cd03759    81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcpSIPSD-FVVSGTASEQLYGMCESLWR-PDM------ 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2062817455 275 plSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGI 313
Cdd:cd03759   153 --EPDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 99-317 5.56e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 116.40  E-value: 5.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455  99 MGPHGSAGPVQL--RFSP--------YAFN----GGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGC 164
Cdd:COG0638     1 MQPSQQSSYDRAitIFSPdgrlyqveYAREavkrGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 165 SGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYS---RRFFPYYVYNIIGGLDEEGkGAVYSFDPVGSYQ 241
Cdd:COG0638    81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062817455 242 RDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP-LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREET 317
Cdd:COG0638   160 EEKAVAIGSGSPFARGVLEK----------EYREdLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 120-291 1.37e-30

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: 113.26  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 120 GTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIA 199
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 200 AMLSTILYSRRF-FPYYVYNIIGGLDEEGkGAVYSFDPVGSYQRDS-FKAGGSASAMLQPLLDNQVGFKnmqnvehvpLS 277
Cdd:cd01901    81 KELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPD---------MT 150

                         170
                  ....*....|....
gi 2062817455 278 LDRAMRLVKDVFIS 291
Cdd:cd01901   151 LEEAVELALKALKS 164
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 119-314 1.48e-22

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: 93.02  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 119 GGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIE-ARLKMYKHSNNKAMTTGA 197
Cdd:cd03760     2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDqLVIDDECLDDGHSLSPKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 198 IAAMLSTILYSRR--FFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVgfKNMQNvehvp 275
Cdd:cd03760    82 IHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAW--EKKPD----- 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2062817455 276 LSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIR 314
Cdd:cd03760   155 LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 121-318 3.47e-22

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: 91.88  E-value: 3.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 121 TVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 200
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 201 MLSTIL--YSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNqvgfknmqnvEHVP-LS 277
Cdd:cd03758    83 FTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR----------YYKPdMT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2062817455 278 LDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETV 318
Cdd:cd03758   153 VEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 121-316 1.14e-15

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: 73.80  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 121 TVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 200
Cdd:cd03762     2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 201 MLSTILYSRRFFpYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQvgFK-NMqnvehvplSLD 279
Cdd:cd03762    82 LFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDAN--YKpGM--------TLE 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2062817455 280 RAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREE 316
Cdd:cd03762   151 ECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERK 187
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 112-247 2.66e-10

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: 58.99  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 112 FSP--------YAF----NGGTVLAIAGEDFSIVASD----TRLSEGFSIHtrdspKCYKLTDKTVIGCSGFHGDCLTLT 175
Cdd:cd01911     8 FSPegrlfqveYALeavkNGSTAVGIKGKDGVVLAVEkkvtSKLLDPSSVE-----KIFKIDDHIGCAVAGLTADARVLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 176 KIieARLKM--YKHSNNKAMTTGAIAAMLSTIL------YSRRffPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRdsFKA 247
Cdd:cd01911    83 NR--ARVEAqnYRYTYGEPIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTYFG--YKA 156
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 102-312 6.66e-10

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 58.46  E-value: 6.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 102 HGSaGPVQLRFSpyafNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEAR 181
Cdd:PTZ00488   27 HGD-ANKAIEFA----HGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 182 LKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGaVYSFDPVGSYQRDSFKAGGSASAMLQPLLDn 261
Cdd:PTZ00488  102 CRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGTRLHGNMFSCGSGSTYAYGVLD- 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2062817455 262 qVGFKnmqnvehVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 312
Cdd:PTZ00488  180 -AGFK-------WDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 121-312 3.21e-07

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: 49.89  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 121 TVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKtvIGC--SGFHGDCLTLTKIIEARLKMykHSNNKAMTTGAI 198
Cdd:cd03763     2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPN--IYCcgAGTAADTEAVTNMISSNLEL--HRLNTGRKPRVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 199 AAMlsTILySRRFFPY--YV--YNIIGGLDEEGKgAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQvgFKNmqnvehv 274
Cdd:cd03763    78 TAL--TML-KQHLFRYqgHIgaALVLGGVDYTGP-HLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDR--YKP------- 144

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2062817455 275 PLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEG 312
Cdd:cd03763   145 DMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 121-314 9.55e-07

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: 48.39  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 121 TVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAA 200
Cdd:cd03761     2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 201 MLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYsFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKnmqnvehvpLSLDR 280
Cdd:cd03761    82 LLSNMLYQYKGMGLSMGTMICGWDKTGPGLYY-VDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYD---------LSVEE 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2062817455 281 AMRLVKDVFISAAERDVYTGDALRICIVTKEGIR 314
Cdd:cd03761   152 AYDLARRAIYHATHRDAYSGGNVNLYHVREDGWR 185
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 112-240 9.92e-05

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: 42.61  E-value: 9.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 112 FSP--------YAF----NGG-TVLAIAGEDFSIVASDTRLSEGFsIHTRDSPKCYKLTDKtvIGC--SGFHGDCLTLtk 176
Cdd:cd03754     9 FSPegrlyqveYAFkavkNAGlTSVAVRGKDCAVVVTQKKVPDKL-IDPSTVTHLFRITDE--IGCvmTGMIADSRSQ-- 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062817455 177 IIEARLKM--YKHSNNKAMTTGAIAAMLSTI--LYSRRFF--PYYVYNIIGGLDEEGKGAVYSFDPVGSY 240
Cdd:cd03754    84 VQRARYEAaeFKYKYGYEMPVDVLAKRIADInqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYF 153
 
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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