NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|402549391|ref|XP_003888469|]
View 

20s proteasome beta 7 subunit, (putative) [Leishmania infantum JPCM5]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 3-199 1.87e-90

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: 264.05  E-value: 1.87e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   3 SGGSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNVDELSPS 82
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  83 EVFSYLHRSIYQKRCDFEPCLCQMVFIGFRD-SETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNPsGLSRAQ 161
Cdd:cd03760   81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKP-DLTEEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 402549391 162 AVQILTDCLRVLFYRECRTINKFQMADAASDGVRISEP 199
Cdd:cd03760  160 ARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 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 ...
 3-199 1.87e-90

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: 264.05  E-value: 1.87e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   3 SGGSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNVDELSPS 82
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  83 EVFSYLHRSIYQKRCDFEPCLCQMVFIGFRD-SETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNPsGLSRAQ 161
Cdd:cd03760   81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKP-DLTEEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 402549391 162 AVQILTDCLRVLFYRECRTINKFQMADAASDGVRISEP 199
Cdd:cd03760  160 ARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-187 3.68e-32

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: 115.36  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391    1 MASGGSVIAIKYNGGVLMAADTLLSYGSLAKWPN-IPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDEL 79
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYG-RPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   80 SP---SEVFSYLHRSIYQKRcdFEPCLCQMVFIGF-RDSETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNps 155
Cdd:pfam00227  80 PVelaARIADLLQAYTQYSG--RRPFGVSLLIAGYdEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPD-- 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 402549391  156 gLSRAQAVQILTDCLRVLFYRECRTINKFQMA 187
Cdd:pfam00227 156 -LTLEEAVELAVKALKEAIDRDALSGGNIEVA 186
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 4-163 1.78e-08

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 52.84  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   4 GGSVIAIKYNGGVLMAADTLLSYGSL--AKwpNIPRIKLLGSHSAVCATGSYADFQMMtkqvednierqrmyhnVDELSp 81
Cdd:COG0638   35 GTTTVGIKTKDGVVLAADRRATMGNLiaSK--SIEKIFKIDDHIGVAIAGLVADAREL----------------VRLAR- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  82 seVFSYLHRSIYQKRCDFEPC---LCQMVF----IGFRD--SETFLAGVDD----------VGTRWEDDCVATGYGAYIA 142
Cdd:COG0638   96 --VEAQLYELRYGEPISVEGLaklLSDLLQgytqYGVRPfgVALLIGGVDDggprlfstdpSGGLYEEKAVAIGSGSPFA 173

                        170       180
                 ....*....|....*....|..
gi 402549391 143 lpllRQALEKNPS-GLSRAQAV 163
Cdd:COG0638  174 ----RGVLEKEYReDLSLDEAV 191
 
Name Accession Description Interval E-value
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-199 1.87e-90

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: 264.05  E-value: 1.87e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   3 SGGSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNVDELSPS 82
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSLSPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  83 EVFSYLHRSIYQKRCDFEPCLCQMVFIGFRD-SETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNPsGLSRAQ 161
Cdd:cd03760   81 EIHSYLTRVLYNRRSKMNPLWNTLVVGGVDNeGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKKP-DLTEEE 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 402549391 162 AVQILTDCLRVLFYRECRTINKFQMADAASDGVRISEP 199
Cdd:cd03760  160 ARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-196 9.12e-47

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: 152.60  E-value: 9.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   5 GSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDELSPSEV 84
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNG-RELSVKAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  85 FSYLHRSIYQKRcdFEPCLCQMVFIGF-RDSETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNpsgLSRAQAV 163
Cdd:cd01912   80 ANLLSNILYSYR--GFPYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD---MTLEEAV 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 402549391 164 QILTDCLRVLFYRECRTINKFQMADAASDGVRI 196
Cdd:cd01912  155 ELVKKAIDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 5-187 2.69e-37

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: 128.38  E-value: 2.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   5 GSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDELSPSEV 84
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYG-EPIPVEAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  85 FSYLHRSIYQKRCDFEPCLCQMVFIGF-RDSETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNpsgLSRAQAV 163
Cdd:cd01906   80 AKLLANLLYEYTQSLRPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD---MTLEEAI 156

                        170       180
                 ....*....|....*....|....
gi 402549391 164 QILTDCLRVLFYRECRTINKFQMA 187
Cdd:cd01906  157 ELALKALKSALERDLYSGGNIEVA 180
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-187 3.68e-32

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: 115.36  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391    1 MASGGSVIAIKYNGGVLMAADTLLSYGSLAKWPN-IPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDEL 79
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYG-RPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   80 SP---SEVFSYLHRSIYQKRcdFEPCLCQMVFIGF-RDSETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQALEKNps 155
Cdd:pfam00227  80 PVelaARIADLLQAYTQYSG--RRPFGVSLLIAGYdEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPD-- 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 402549391  156 gLSRAQAVQILTDCLRVLFYRECRTINKFQMA 187
Cdd:pfam00227 156 -LTLEEAVELAVKALKEAIDRDALSGGNIEVA 186
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-171 1.57e-24

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: 94.77  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   5 GSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDELSPSEV 84
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYG-EPISVVAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  85 FSYLHRSIYQKRCDFEPClCQMVFIGFRDSETFLAGVDDVGTRWED-DCVATGYGAYIALPLLRQALEKNpsgLSRAQAV 163
Cdd:cd01901   80 AKELAKLLQVYTQGRPFG-VNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD---MTLEEAV 155


                 ....*...
gi 402549391 164 QILTDCLR 171
Cdd:cd01901  156 ELALKALK 163
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-168 1.65e-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: 58.42  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   4 GGSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEdniERQRMYHNVDELSPS- 82
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLK---ARIKMYKYSHNKEMSt 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  83 EVFSYLHRSI-YQKRcdFEPCLCQMVFIGFrDSETflAGV----DDVGTRWEDDCVATGYGAYIALPLL-RQALEKNPSG 156
Cdd:cd03757   85 EAIAQLLSTIlYSRR--FFPYYVFNILAGI-DEEG--KGVvysyDPVGSYERETYSAGGSASSLIQPLLdNQVGRKNQNN 159

                        170
                 ....*....|....*..
gi 402549391 157 -----LSRAQAVQILTD 168
Cdd:cd03757  160 vertpLSLEEAVSLVKD 176
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 10-171 4.26e-09

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: 54.18  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  10 IKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNVDeLSPSEVFSYLH 89
Cdd:cd03764    6 IVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRP-MSIKALATLLS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  90 RSIYQKRcdFEPCLCQMVFIGFRDSETFLAGVDDVGTRWEDDCVATGYGAYIALPLLRQalEKNPsGLSRAQAVQILTDC 169
Cdd:cd03764   85 NILNSSK--YFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLED--EYKE-DMTVEEAKKLAIRA 159


                 ..
gi 402549391 170 LR 171
Cdd:cd03764  160 IK 161
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 4-163 1.78e-08

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 52.84  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   4 GGSVIAIKYNGGVLMAADTLLSYGSL--AKwpNIPRIKLLGSHSAVCATGSYADFQMMtkqvednierqrmyhnVDELSp 81
Cdd:COG0638   35 GTTTVGIKTKDGVVLAADRRATMGNLiaSK--SIEKIFKIDDHIGVAIAGLVADAREL----------------VRLAR- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  82 seVFSYLHRSIYQKRCDFEPC---LCQMVF----IGFRD--SETFLAGVDD----------VGTRWEDDCVATGYGAYIA 142
Cdd:COG0638   96 --VEAQLYELRYGEPISVEGLaklLSDLLQgytqYGVRPfgVALLIGGVDDggprlfstdpSGGLYEEKAVAIGSGSPFA 173

                        170       180
                 ....*....|....*....|..
gi 402549391 143 lpllRQALEKNPS-GLSRAQAV 163
Cdd:COG0638  174 ----RGVLEKEYReDLSLDEAV 191
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-170 3.23e-05

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: 42.96  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   6 SVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNVdELSPSEVF 85
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGY-ELSPKAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391  86 SY----LHRSIyQKRCDFEpclCQMVFIGFRDSE-TFLAGVDDVGTRWEDDCVATGYGAYIALPLlrqaLEKN-PSGLSR 159
Cdd:cd03758   82 NFtrreLAESL-RSRTPYQ---VNLLLAGYDKVEgPSLYYIDYLGTLVKVPYAAHGYGAYFCLSI----LDRYyKPDMTV 153

                        170
                 ....*....|.
gi 402549391 160 AQAVQILTDCL 170
Cdd:cd03758  154 EEALELMKKCI 164
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-125 3.31e-04

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: 40.30  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402549391   3 SGGSVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMYHNvDELSPS 82
Cdd:cd03759    2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREE-REIKPK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 402549391  83 EVFSYLHRSIYQKRcdFEPCLCQMVFIGF-RDSETFLAGVDDVG 125
Cdd:cd03759   81 TFSSLISSLLYEKR--FGPYFVEPVVAGLdPDGKPFICTMDLIG 122
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-63 2.12e-03

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: 37.59  E-value: 2.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 402549391   6 SVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQV 63
Cdd:cd03762    2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYV 59
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-73 9.49e-03

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: 35.64  E-value: 9.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402549391   6 SVIAIKYNGGVLMAADTLLSYGSLAKWPNIPRIKLLGSHSAVCATGSYADFQMMTKQVEDNIERQRMY 73
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLN 69
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH