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Conserved domains on  [gi|116806246|emb|CAL26546|]
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CG11981 [Drosophila melanogaster]

Protein Classification

proteasome subunit beta type-3( domain architecture ID 10132915)

proteasome subunit beta type-3 is a non-catalytic component of the 20S proteasome which degrades ubiquitin-tagged proteins in both the cytosol and nucleus

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-201 1.41e-132

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: 370.03  E-value: 1.41e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   6 YNGGCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPK 85
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  86 PFSAMMSSFLYEHRFGPYFIEPVVAGLDPKtMEPFICNMDLIGCPNAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFE 165
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116806246 166 VIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTLK 201
Cdd:cd03759  160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-201 1.41e-132

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: 370.03  E-value: 1.41e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   6 YNGGCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPK 85
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  86 PFSAMMSSFLYEHRFGPYFIEPVVAGLDPKtMEPFICNMDLIGCPNAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFE 165
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116806246 166 VIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTLK 201
Cdd:cd03759  160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-190 1.21e-51

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: 164.66  E-value: 1.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246    6 YNGGCVVAMRGKDCVAIATDHRFGIQAQTISTD-FKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   85 KP---FSAMMSSFLYEHRFGPYFIEPVVAGLDpKTMEPFICNMDLIGCPNAPDdFVVAGTCAEQLYGMCETLWKPDLEPD 161
Cdd:pfam00227  82 ELaarIADLLQAYTQYSGRRPFGVSLLIAGYD-EDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 116806246  162 QLFEVIAQSIVNAFDRDAMSGWGATVYII 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 11-199 5.82e-17

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 75.95  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  11 VVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFSAM 90
Cdd:COG0638   38 TVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  91 MSSFLYE---HRFGPYFIEPVVAGLDPKtmEPFICNMDLIGCPNaPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVI 167
Cdd:COG0638  118 LSDLLQGytqYGVRPFGVALLIGGVDDG--GPRLFSTDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                        170       180       190
                 ....*....|....*....|....*....|..
gi 116806246 168 AQSIVNAFDRDAMSGWGATVYIIEKDKITERT 199
Cdd:COG0638  195 LRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 6-193 9.22e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.06  E-value: 9.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   6 YNGGCVVAMRGKdcvaiATDHRFgIQAQTIstdfKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPK 85
Cdd:PTZ00488  47 YGGGIIIAVDSK-----ATAGPY-IASQSV----KKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  86 PFSAMMSSFLYEHRFGPYFIEPVVAGLDPKTMEPFICNMDliGCPNAPDDFVVaGTCAEQLYGMCETLWKPDLEPDQLFE 165
Cdd:PTZ00488 117 AASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDND--GTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQD 193

                        170       180
                 ....*....|....*....|....*...
gi 116806246 166 VIAQSIVNAFDRDAMSGWGATVYIIEKD 193
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKD 221
 
Name Accession Description Interval E-value
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-201 1.41e-132

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: 370.03  E-value: 1.41e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   6 YNGGCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPK 85
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  86 PFSAMMSSFLYEHRFGPYFIEPVVAGLDPKtMEPFICNMDLIGCPNAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFE 165
Cdd:cd03759   81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPD-GKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFE 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116806246 166 VIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTLK 201
Cdd:cd03759  160 TISQALLSAVDRDALSGWGAVVYIITKDKVTTRTLK 195
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 9-199 2.14e-70

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: 212.30  E-value: 2.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   9 GCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFS 88
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  89 AMMSSFLYEHRFGPYFIEPVVAGLDPKTmEPFICNMDLIGCPnAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVIA 168
Cdd:cd01912   81 NLLSNILYSYRGFPYYVSLIVGGVDKGG-GPFLYYVDPLGSL-IEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 116806246 169 QSIVNAFDRDAMSGWGATVYIIEKDKITERT 199
Cdd:cd01912  159 KAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-190 1.21e-51

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: 164.66  E-value: 1.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246    6 YNGGCVVAMRGKDCVAIATDHRFGIQAQTISTD-FKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCP 84
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   85 KP---FSAMMSSFLYEHRFGPYFIEPVVAGLDpKTMEPFICNMDLIGCPNAPDdFVVAGTCAEQLYGMCETLWKPDLEPD 161
Cdd:pfam00227  82 ELaarIADLLQAYTQYSGRRPFGVSLLIAGYD-EDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 116806246  162 QLFEVIAQSIVNAFDRDAMSGWGATVYII 190
Cdd:pfam00227 160 EAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 9-190 3.03e-48

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: 155.73  E-value: 3.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   9 GCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFS 88
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  89 AMMSSFLYEHRF--GPYFIEPVVAGLDPKTmEPFICNMDLIGCPNAPdDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEV 166
Cdd:cd01906   81 KLLANLLYEYTQslRPLGVSLLVAGVDEEG-GPQLYSVDPSGSYIEY-KATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                        170       180
                 ....*....|....*....|....
gi 116806246 167 IAQSIVNAFDRDAMSGWGATVYII 190
Cdd:cd01906  159 ALKALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 9-171 1.51e-32

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: 1.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   9 GCVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFS 88
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  89 AMMSSFLYEHRFG-PYFIEPVVAGLDPKtmEPFICNMDLIGCPNAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVI 167
Cdd:cd01901   81 KELAKLLQVYTQGrPFGVNLIVAGVDEG--GGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELA 158


                 ....
gi 116806246 168 AQSI 171
Cdd:cd01901  159 LKAL 162
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-198 5.30e-27

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: 101.56  E-value: 5.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  12 VAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFSAMM 91
Cdd:cd03764    4 VGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  92 SSFLYEHRFGPYFIEPVVAGLDPKtmEPFICNMDLIGCPNaPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVIAQSI 171
Cdd:cd03764   84 SNILNSSKYFPYIVQLLIGGVDEE--GPHLYSLDPLGSII-EDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                        170       180
                 ....*....|....*....|....*..
gi 116806246 172 VNAFDRDAMSGWGATVYIIEKDKITER 198
Cdd:cd03764  161 KSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-205 3.57e-24

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: 94.63  E-value: 3.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   7 NGGCVVAMRGKDCVAIATDHR----FGIQaqtiSTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREM 82
Cdd:cd03757    7 NGGTVLAIAGNDFAVIAGDTRlsegYSIL----SRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  83 CPKPFSAMMSSFLYEHRFGPYFIEPVVAGLDPKTmEPFICNMDLIGCPNaPDDFVVAGTCAE--------QLYGMCETLW 154
Cdd:cd03757   83 STEAIAQLLSTILYSRRFFPYYVFNILAGIDEEG-KGVVYSYDPVGSYE-RETYSAGGSASSliqplldnQVGRKNQNNV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116806246 155 KP-DLEPDQLFEVIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTLKTRMD 205
Cdd:cd03757  161 ERtPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 11-199 5.82e-17

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 75.95  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  11 VVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFSAM 90
Cdd:COG0638   38 TVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  91 MSSFLYE---HRFGPYFIEPVVAGLDPKtmEPFICNMDLIGCPNaPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVI 167
Cdd:COG0638  118 LSDLLQGytqYGVRPFGVALLIGGVDDG--GPRLFSTDPSGGLY-EEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                        170       180       190
                 ....*....|....*....|....*....|..
gi 116806246 168 AQSIVNAFDRDAMSGWGATVYIIEKDKITERT 199
Cdd:COG0638  195 LRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 10-200 7.52e-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: 56.05  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  10 CVVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDiltvrdRLMF----RKN--LYETRENREMC 83
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGD------RLQFaeyiQKNiqLYKMRNGYELS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  84 PKPFSAMMSSFLYEH--RFGPYFIEPVVAGLDPKTmEPFICNMDLIGCpNAPDDFVVAGTCAEQLYGMCETLWKPDLEPD 161
Cdd:cd03758   77 PKAAANFTRRELAESlrSRTPYQVNLLLAGYDKVE-GPSLYYIDYLGT-LVKVPYAAHGYGAYFCLSILDRYYKPDMTVE 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 116806246 162 QLFEVIAQSIVNAFDRDAMSGWGATVYIIEKDKITERTL 200
Cdd:cd03758  155 EALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 8-182 1.11e-08

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: 52.96  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   8 GGCVVAMRGKDCVAIATDHR--FGIQAQTisTDFKKVFHIGPRMFLGLTGLQTD---ILTVRDRLMFRKNLYETRENreM 82
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLgsYGSLARF--KNVERIFKVGDNTLLGASGDYADfqyLKRLLDQLVIDDECLDDGHS--L 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  83 CPKPFSAMMSSFLYEHR--FGPYFIEPVVAGLDPKTmEPFICNMDLIGCpNAPDDFVVAGTCAEQLYGMCETLW--KPDL 158
Cdd:cd03760   78 SPKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEG-EPFLGYVDLLGT-AYEDPHVATGFGAYLALPLLREAWekKPDL 155

                        170       180
                 ....*....|....*....|....
gi 116806246 159 EPDQLFEVIAQSIVNAFDRDAMSG 182
Cdd:cd03760  156 TEEEARALIEECMKVLYYRDARSI 179
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 6-193 9.22e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.06  E-value: 9.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246   6 YNGGCVVAMRGKdcvaiATDHRFgIQAQTIstdfKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPK 85
Cdd:PTZ00488  47 YGGGIIIAVDSK-----ATAGPY-IASQSV----KKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  86 PFSAMMSSFLYEHRFGPYFIEPVVAGLDPKTMEPFICNMDliGCPNAPDDFVVaGTCAEQLYGMCETLWKPDLEPDQLFE 165
Cdd:PTZ00488 117 AASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDND--GTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQD 193

                        170       180
                 ....*....|....*....|....*...
gi 116806246 166 VIAQSIVNAFDRDAMSGWGATVYIIEKD 193
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKD 221
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-59 1.19e-04

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: 41.27  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116806246   7 NGGCVVAMRGKDCVAIATDHRfgIQAQTISTD-FKKVFHIGPRMFLGLTGLQTD 59
Cdd:cd01911   26 NGSTAVGIKGKDGVVLAVEKK--VTSKLLDPSsVEKIFKIDDHIGCAVAGLTAD 77
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 11-198 1.95e-04

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: 40.67  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  11 VVAMRGKDCVAIATDHRFGIQAQTISTDFKKVFHIGPRMFLGLTGLQTDILTVRDRLMFRKNLYETRENREMCPKPFSAM 90
Cdd:cd03762    3 IIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116806246  91 MSSFLYEHRfgpYFIEP--VVAGLDPKTmEPFICNMDLIGCPnAPDDFVVAGTCAEQLYGMCETLWKPDLEPDQLFEVIA 168
Cdd:cd03762   83 FKNLCYNYK---EMLSAgiIVAGWDEQN-GGQVYSIPLGGML-IRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVK 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 116806246 169 QSIVNAFDRDAMSGWGATVYIIEKDKITER 198
Cdd:cd03762  158 NALSLAMSRDGSSGGVIRLVIITKDGVERK 187
 
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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