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Conserved domains on  [gi|488473106|ref|WP_002516776|]
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MULTISPECIES: proteasome subunit beta [Cutibacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
20S_bact_beta super family cl30780
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 49-267 1.57e-60

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


The actual alignment was detected with superfamily member TIGR03690:

Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 191.07  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106   49 HGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDG 128
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  129 CAVRLSSLVRSHGTMMAQGLAVTPLLAGWDELAHRGRIFSYDGTGGQTEEHSHACVGSGALFASDVLNEDYRTGMDRDES 208
Cdd:TIGR03690  81 KANRLAAMVRGNLPAAMQGLAVVPLLAGYDLDAGAGRIFSYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473106  209 VALAIRALDTAISDDSPSslSGPDLSRGLYPTVACVDSHGVTRMPTEEVAVLTKRLVDQ 267
Cdd:TIGR03690 161 LRVAVEALYDAADDDSAT--GGPDLVRGIYPTVVVITADGARRVPESELEELARAIVES 217
 
Name Accession Description Interval E-value
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 49-267 1.57e-60

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 191.07  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106   49 HGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDG 128
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  129 CAVRLSSLVRSHGTMMAQGLAVTPLLAGWDELAHRGRIFSYDGTGGQTEEHSHACVGSGALFASDVLNEDYRTGMDRDES 208
Cdd:TIGR03690  81 KANRLAAMVRGNLPAAMQGLAVVPLLAGYDLDAGAGRIFSYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473106  209 VALAIRALDTAISDDSPSslSGPDLSRGLYPTVACVDSHGVTRMPTEEVAVLTKRLVDQ 267
Cdd:TIGR03690 161 LRVAVEALYDAADDDSAT--GGPDLVRGIYPTVVVITADGARRVPESELEELARAIVES 217
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 14-256 2.64e-60

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 190.74  E-value: 2.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  14 MSSTTTDSFAVLLRRVAPELLPPTtvDTSVPELLRHGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVI 93
Cdd:COG0638    1 MQPSQQSSYDRAITIFSPDGRLYQ--VEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  94 GVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDGCAVRLSSLVRSHGTMMAQGLAVTPLLAGWDElaHRGRIFSYDGTG 173
Cdd:COG0638   79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGVRPFGVALLIGGVDD--GGPRLFSTDPSG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 174 GQTEEhSHACVGSGALFASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPSslsgpdlsrGLYPTVACVDSHGVTRMP 253
Cdd:COG0638  157 GLYEE-KAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSAS---------GDGIDVAVITEDGFRELS 226


                 ...
gi 488473106 254 TEE 256
Cdd:COG0638  227 EEE 229
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 52-227 6.01e-25

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: 97.95  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDGCAV 131
Cdd:cd01906    2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 132 RLSSLVRSHGTMMaQGLAVTPLLAGWDElAHRGRIFSYDGTGGqTEEHSHACVGSGALFASDVLNEDYRTGMDRDESVAL 211
Cdd:cd01906   82 LLANLLYEYTQSL-RPLGVSLLVAGVDE-EGGPQLYSVDPSGS-YIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                        170
                 ....*....|....*.
gi 488473106 212 AIRALDTAISDDSPSS 227
Cdd:cd01906  159 ALKALKSALERDLYSG 174
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 48-227 1.37e-17

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: 78.38  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106   48 RHGRTVLAIRYNGGVVVAAD----LGSALarrLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQR 123
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADkratRGSKL---LSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  124 ISMDGCAvRLSSLVRSHGTMMAQG-LAVTPLLAGWDElAHRGRIFSYDGTGGQTEEhSHACVGSGALFASDVLNEDYRTG 202
Cdd:pfam00227  79 IPVELAA-RIADLLQAYTQYSGRRpFGVSLLIAGYDE-DGGPHLYQIDPSGSYIEY-KATAIGSGSQYAYGVLEKLYRPD 155

                         170       180
                  ....*....|....*....|....*
gi 488473106  203 MDRDESVALAIRALDTAISDDSPSS 227
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSG 180
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 33-226 1.03e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.61  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  33 LLPPTTVDTSVPELLR--HGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQ 110
Cdd:PTZ00488  20 LAEYTFDHGDANKAIEfaHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 111 AEVDHLEKIQGQRISMDGCAVRLSSLVRSHGTMmaqGLAVTPLLAGWDELAhrGRIFSYDGTGGQTEEHSHACvGSGALF 190
Cdd:PTZ00488 100 MQCRLYELRNGELISVAAASKILANIVWNYKGM---GLSMGTMICGWDKKG--PGLFYVDNDGTRLHGNMFSC-GSGSTY 173

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488473106 191 ASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPS 226
Cdd:PTZ00488 174 AYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYS 209
 
Name Accession Description Interval E-value
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 49-267 1.57e-60

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 191.07  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106   49 HGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDG 128
Cdd:TIGR03690   1 HGTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  129 CAVRLSSLVRSHGTMMAQGLAVTPLLAGWDELAHRGRIFSYDGTGGQTEEHSHACVGSGALFASDVLNEDYRTGMDRDES 208
Cdd:TIGR03690  81 KANRLAAMVRGNLPAAMQGLAVVPLLAGYDLDAGAGRIFSYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473106  209 VALAIRALDTAISDDSPSslSGPDLSRGLYPTVACVDSHGVTRMPTEEVAVLTKRLVDQ 267
Cdd:TIGR03690 161 LRVAVEALYDAADDDSAT--GGPDLVRGIYPTVVVITADGARRVPESELEELARAIVES 217
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 14-256 2.64e-60

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 190.74  E-value: 2.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  14 MSSTTTDSFAVLLRRVAPELLPPTtvDTSVPELLRHGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVI 93
Cdd:COG0638    1 MQPSQQSSYDRAITIFSPDGRLYQ--VEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  94 GVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDGCAVRLSSLVRSHGTMMAQGLAVTPLLAGWDElaHRGRIFSYDGTG 173
Cdd:COG0638   79 AIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGVRPFGVALLIGGVDD--GGPRLFSTDPSG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 174 GQTEEhSHACVGSGALFASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPSslsgpdlsrGLYPTVACVDSHGVTRMP 253
Cdd:COG0638  157 GLYEE-KAVAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERDSAS---------GDGIDVAVITEDGFRELS 226


                 ...
gi 488473106 254 TEE 256
Cdd:COG0638  227 EEE 229
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 52-227 6.01e-25

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: 97.95  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDGCAV 131
Cdd:cd01906    2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 132 RLSSLVRSHGTMMaQGLAVTPLLAGWDElAHRGRIFSYDGTGGqTEEHSHACVGSGALFASDVLNEDYRTGMDRDESVAL 211
Cdd:cd01906   82 LLANLLYEYTQSL-RPLGVSLLVAGVDE-EGGPQLYSVDPSGS-YIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                        170
                 ....*....|....*.
gi 488473106 212 AIRALDTAISDDSPSS 227
Cdd:cd01906  159 ALKALKSALERDLYSG 174
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 52-218 1.08e-19

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: 83.60  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMDGCAV 131
Cdd:cd01901    2 TSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 132 RLSSLVRSHGTMMaqGLAVTPLLAGWDElaHRGRIFSYDGTGGQTEEHSHACVGSGALFASDVLNEDYRTGMDRDESVAL 211
Cdd:cd01901   82 ELAKLLQVYTQGR--PFGVNLIVAGVDE--GGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVEL 157


                 ....*..
gi 488473106 212 AIRALDT 218
Cdd:cd01901  158 ALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 52-220 4.08e-19

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: 82.49  E-value: 4.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADlgsalaRRLGQ------TDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVdHLEKIQ-GQRI 124
Cdd:cd01912    2 TIVGIKGKDGVVLAAD------TRASAgslvasRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNL-RLYELRnGREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 125 SMDGCAVRLSSLVRSHGTMMAQglaVTPLLAGWDELaHRGRIFSYDgTGGQTEEHSHACVGSGALFASDVLNEDYRTGMD 204
Cdd:cd01912   75 SVKAAANLLSNILYSYRGFPYY---VSLIVGGVDKG-GGPFLYYVD-PLGSLIEAPFVATGSGSKYAYGILDRGYKPDMT 149

                        170
                 ....*....|....*.
gi 488473106 205 RDESVALAIRALDTAI 220
Cdd:cd01912  150 LEEAVELVKKAIDSAI 165
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-226 5.48e-18

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: 79.60  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVdHLEKIQ-GQRISMDGCA 130
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEA-RLYELRrGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 131 VRLSSLVRSHGTM--MAQglavtPLLAGWDELAhrGRIFSYDGTGGQTEEhSHACVGSGALFASDVLNEDYRTGMDRDES 208
Cdd:cd03764   81 TLLSNILNSSKYFpyIVQ-----LLIGGVDEEG--PHLYSLDPLGSIIED-KYTATGSGSPYAYGVLEDEYKEDMTVEEA 152

                        170
                 ....*....|....*...
gi 488473106 209 VALAIRALDTAISDDSPS 226
Cdd:cd03764  153 KKLAIRAIKSAIERDSAS 170
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 48-227 1.37e-17

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: 78.38  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106   48 RHGRTVLAIRYNGGVVVAAD----LGSALarrLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQR 123
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADkratRGSKL---LSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  124 ISMDGCAvRLSSLVRSHGTMMAQG-LAVTPLLAGWDElAHRGRIFSYDGTGGQTEEhSHACVGSGALFASDVLNEDYRTG 202
Cdd:pfam00227  79 IPVELAA-RIADLLQAYTQYSGRRpFGVSLLIAGYDE-DGGPHLYQIDPSGSYIEY-KATAIGSGSQYAYGVLEKLYRPD 155

                         170       180
                  ....*....|....*....|....*
gi 488473106  203 MDRDESVALAIRALDTAISDDSPSS 227
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSG 180
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-226 2.80e-10

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: 58.41  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAADLGSALARRLGQTDVDRI-------LGTDDRCVIGVAGAAGLAGEMIRLFQAEvdhlekiQGQRI 124
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVieinpylLGTMAGGAADCQYWERVLGRECRLYELR-------NKERI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 125 SMDGCAVRLSSLVRSHGTMmaqGLAVTPLLAGWDelaHRG-RIFSYDGTGGQTEeHSHACVGSGALFASDVLNEDYRTGM 203
Cdd:cd03761   75 SVAAASKLLSNMLYQYKGM---GLSMGTMICGWD---KTGpGLYYVDSDGTRLK-GDLFSVGSGSTYAYGVLDSGYRYDL 147

                        170       180
                 ....*....|....*....|...
gi 488473106 204 DRDESVALAIRALDTAISDDSPS 226
Cdd:cd03761  148 SVEEAYDLARRAIYHATHRDAYS 170
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 33-226 1.03e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.61  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  33 LLPPTTVDTSVPELLR--HGRTVLAIRYNGGVVVAADLGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQ 110
Cdd:PTZ00488  20 LAEYTFDHGDANKAIEfaHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 111 AEVDHLEKIQGQRISMDGCAVRLSSLVRSHGTMmaqGLAVTPLLAGWDELAhrGRIFSYDGTGGQTEEHSHACvGSGALF 190
Cdd:PTZ00488 100 MQCRLYELRNGELISVAAASKILANIVWNYKGM---GLSMGTMICGWDKKG--PGLFYVDNDGTRLHGNMFSC-GSGSTY 173

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488473106 191 ASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPS 226
Cdd:PTZ00488 174 AYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYS 209
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 52-226 1.55e-06

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: 47.60  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  52 TVLAIRYNGGVVVAAD----LGSALARRLgqtdVDRILGTDDR---CVIGVAGAAGLAGEMIRlFQAEVDHLEkiQGQRI 124
Cdd:cd03762    2 TIIAVEYDGGVVLGADsrtsTGSYVANRV----TDKLTQLHDRiycCRSGSAADTQAIADYVR-YYLDMHSIE--LGEPP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 125 SMDGCAVRLSSLVRSHGTMMAQGLAVtpllAGWDELAHrGRIFSYDgTGGQTEEHSHACVGSGALFASDVLNEDYRTGMD 204
Cdd:cd03762   75 LVKTAASLFKNLCYNYKEMLSAGIIV----AGWDEQNG-GQVYSIP-LGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMT 148

                        170       180
                 ....*....|....*....|..
gi 488473106 205 RDESVALAIRALDTAISDDSPS 226
Cdd:cd03762  149 LEECIKFVKNALSLAMSRDGSS 170
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-195 6.39e-06

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: 46.10  E-value: 6.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  50 GRTVLAIRYNGGVVVAAD----LGSALARRlgqtDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRIS 125
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDtrlsEGYSILSR----DSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 126 MDGCAVRLSSLVRSHGTMMAQglaVTPLLAGWDELAhRGRIFSYDGTgGQTEEHSHACVGSGALFASDVL 195
Cdd:cd03757   84 TEAIAQLLSTILYSRRFFPYY---VFNILAGIDEEG-KGVVYSYDPV-GSYERETYSAGGSASSLIQPLL 148
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 45-222 6.94e-06

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


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 45.78  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  45 ELLRHGRTVLAIRYNGGVVVAADlGSALARRLGQTDVDRILGTDDRCVIGVAGAAGLAGEMI---RLFqAEVDHLekIQG 121
Cdd:cd03756   23 EAVKRGTTALGIKCKEGVVLAVD-KRITSKLVEPESIEKIYKIDDHVGAATSGLVADARVLIdraRVE-AQIHRL--TYG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 122 QRISMDGcavrLSSLVRSHGTMMAQGLAVTP-----LLAGWDElaHRGRIFSYDgTGGQTEEHSHACVGSGALFASDVLN 196
Cdd:cd03756   99 EPIDVEV----LVKKICDLKQQYTQHGGVRPfgvalLIAGVDD--GGPRLFETD-PSGAYNEYKATAIGSGRQAVTEFLE 171

                        170       180
                 ....*....|....*....|....*.
gi 488473106 197 EDYRTGMDRDESVALAIRALDTAISD 222
Cdd:cd03756  172 KEYKEDMSLEEAIELALKALYAALEE 197
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
45-258 5.04e-05

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 43.67  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  45 ELLRHGRTVLAIRYNGGVVVAAD--LGSALARRlgqTDVDRILGTDDRCVIGVAGAAGLAGEMIRL--FQAEVDHLekIQ 120
Cdd:PRK03996  31 EAVKRGTTAVGVKTKDGVVLAVDkrITSPLIEP---SSIEKIFKIDDHIGAASAGLVADARVLIDRarVEAQINRL--TY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 121 GQRISMDGCAVRLSSL---------VRSHGTMMaqglavtpLLAGWDElaHRGRIFSYDgTGGQTEEHSHACVGSGALFA 191
Cdd:PRK03996 106 GEPIGVETLTKKICDHkqqytqhggVRPFGVAL--------LIAGVDD--GGPRLFETD-PSGAYLEYKATAIGAGRDTV 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473106 192 SDVLNEDYRTGMDRDESVALAIRALdtAISDDSPSSLSGPDLSrglyptVACVDSHGVTRMPTEEVA 258
Cdd:PRK03996 175 MEFLEKNYKEDLSLEEAIELALKAL--AKANEGKLDPENVEIA------YIDVETKKFRKLSVEEIE 233
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 50-93 7.41e-04

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: 39.86  E-value: 7.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488473106  50 GRTVLAIRYNGGVVVAAD-LGS--ALARrlgQTDVDRILGTDDRCVI 93
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADtLGSygSLAR---FKNVERIFKVGDNTLL 45
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 48-227 2.20e-03

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: 38.19  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  48 RHGRTVLAIRYNGGVVVAADLGSAlARRLGQTDVDRILGTDDR--CVIGVagaaglageMIRLFQAEVDHLEKI-Q---- 120
Cdd:cd01911   25 KNGSTAVGIKGKDGVVLAVEKKVT-SKLLDPSSVEKIFKIDDHigCAVAG---------LTADARVLVNRARVEaQnyry 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 121 --GQRISMDGCAVRLSSL---------VRSHGTMMaqglavtpLLAGWDElaHRG-RIFsydgtggQTE------EHSHA 182
Cdd:cd01911   95 tyGEPIPVEVLVKRIADLaqvytqyggVRPFGVSL--------LIAGYDE--EGGpQLY-------QTDpsgtyfGYKAT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488473106 183 CVGSGALFASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPSS 227
Cdd:cd01911  158 AIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAK 202
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 150-227 2.37e-03

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 38.48  E-value: 2.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473106 150 VTPLLAGWDelAHRG-RIFSYDGTGGQTEEHShACVGSGALFASDVLNEDYRTGMDRDESVALAIRALDTAISDDSPSS 227
Cdd:cd03752  130 VSFLYAGWD--KHYGfQLYQSDPSGNYSGWKA-TAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDSTKLTS 205
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 50-216 4.00e-03

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


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 37.70  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106  50 GRTVLAIRYNGGVVVAAD--LGSALarrLGQTDVDRILGTDDRCVIGVAGAAGLAGEMIRLFQAEVDHLEKIQGQRISMD 127
Cdd:cd03753   27 GSTAIGIKTKEGVVLAVEkrITSPL---MEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473106 128 GCAVRLSSLVRSHG------TMMAQGLAVTPLLAGWDElaHRGRIFSYDGTGGQTEEHSHAcVGSGALFASDVLNEDYRT 201
Cdd:cd03753  104 SVTQAVSDLALQFGegddgkKAMSRPFGVALLIAGVDE--NGPQLFHTDPSGTFTRCDAKA-IGSGSEGAQSSLQEKYHK 180

                        170
                 ....*....|....*
gi 488473106 202 GMDRDESVALAIRAL 216
Cdd:cd03753  181 DMTLEEAEKLALSIL 195
 
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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