NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499286200|ref|WP_010978284|]
View 

MULTISPECIES: archaeal proteasome endopeptidase complex subunit beta [Sulfurisphaera]

Protein Classification

archaeal proteasome endopeptidase complex subunit beta( domain architecture ID 10022721)

archaeal proteasome endopeptidase complex subunit beta is component of the proteasome core, a large protease complex with broad specificity involved in protein degradation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 5-187 8.74e-98

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


:

Pssm-ID: 274690  Cd Length: 185  Bit Score: 281.02  E-value: 8.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200    5 PATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAA 83
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDdYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   84 AKLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKA 163
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 499286200  164 LKAAIERDVTSGDGIDILTIKRDN 187
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 5-187 8.74e-98

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 281.02  E-value: 8.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200    5 PATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAA 83
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDdYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   84 AKLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKA 163
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 499286200  164 LKAAIERDVTSGDGIDILTIKRDN 187
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-186 2.58e-88

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: 257.18  E-value: 2.58e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDdKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd03764   81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                        170       180
                 ....*....|....*....|..
gi 499286200 165 KAAIERDVTSGDGIDILTIKRD 186
Cdd:cd03764  161 KSAIERDSASGDGIDVVVITKD 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-186 2.10e-72

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 218.48  E-value: 2.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRF-GIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:COG0638   36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHiGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQY---KWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVL 161
Cdd:COG0638  116 KLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELAL 195

                        170       180
                 ....*....|....*....|....*
gi 499286200 162 KALKAAIERDVTSGDGIDILTIKRD 186
Cdd:COG0638  196 RALYSAAERDSASGDGIDVAVITED 220
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-183 2.58e-58

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: 181.23  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200    7 TALGIKLNDGIILAAERRLSYGGFVLSR-SAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAA- 83
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDdHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAa 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   84 --AKLLSVILYQYKWTPFISELLFGGVDDEG-PKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIV 160
Cdd:pfam00227  86 riADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 499286200  161 LKALKAAIERDVTSGDGIDILTI 183
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-187 5.95e-31

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 113.01  E-value: 5.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDdHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYkwT------PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKE 158
Cdd:PRK03996 116 KKICDHKQQY--TqhggvrPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIE 193

                        170       180
                 ....*....|....*....|....*....
gi 499286200 159 IVLKALKAAIERDVTSgDGIDILTIKRDN 187
Cdd:PRK03996 194 LALKALAKANEGKLDP-ENVEIAYIDVET 221
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 5-187 8.74e-98

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274690  Cd Length: 185  Bit Score: 281.02  E-value: 8.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200    5 PATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAA 83
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDdYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   84 AKLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKA 163
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 499286200  164 LKAAIERDVTSGDGIDILTIKRDN 187
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-186 2.58e-88

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: 257.18  E-value: 2.58e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDdKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd03764   81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                        170       180
                 ....*....|....*....|..
gi 499286200 165 KAAIERDVTSGDGIDILTIKRD 186
Cdd:cd03764  161 KSAIERDSASGDGIDVVVITKD 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-186 2.10e-72

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 218.48  E-value: 2.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRF-GIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:COG0638   36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHiGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQY---KWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVL 161
Cdd:COG0638  116 KLLSDLLQGYtqyGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELAL 195

                        170       180
                 ....*....|....*....|....*
gi 499286200 162 KALKAAIERDVTSGDGIDILTIKRD 186
Cdd:COG0638  196 RALYSAAERDSASGDGIDVAVITED 220
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-186 9.17e-68

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: 205.37  E-value: 9.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd01912    2 TIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISdNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKWTPFISELLFGGVD-DEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd01912   82 LLSNILYSYRGFPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKAI 161

                        170       180
                 ....*....|....*....|..
gi 499286200 165 KAAIERDVTSGDGIDILTIKRD 186
Cdd:cd01912  162 DSAIERDLSSGGGVDVAVITKD 183
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 7-183 3.87e-59

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: 183.08  E-value: 3.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd01906    2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDdHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKWT--PFISELLFGGVD-DEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLK 162
Cdd:cd01906   82 LLANLLYEYTQSlrPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                        170       180
                 ....*....|....*....|.
gi 499286200 163 ALKAAIERDVTSGDGIDILTI 183
Cdd:cd01906  162 ALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 7-183 2.58e-58

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: 181.23  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200    7 TALGIKLNDGIILAAERRLSYGGFVLSR-SAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAA- 83
Cdd:pfam00227   6 TIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDdHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAa 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   84 --AKLLSVILYQYKWTPFISELLFGGVDDEG-PKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIV 160
Cdd:pfam00227  86 riADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELA 165

                         170       180
                  ....*....|....*....|...
gi 499286200  161 LKALKAAIERDVTSGDGIDILTI 183
Cdd:pfam00227 166 VKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 7-166 1.26e-39

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: 132.90  E-value: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd01901    2 TSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEdGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKW-TPFISELLFGGVDDEGPKLFVLDPIGSLIED-NYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKA 163
Cdd:cd01901   82 ELAKLLQVYTQgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALKA 161


                 ...
gi 499286200 164 LKA 166
Cdd:cd01901  162 LKS 164
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-194 2.50e-37

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: 128.53  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd03757   10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTdKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKWTPFISELLFGGVDDEG-PKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYD-PSMNLDKGK------ 157
Cdd:cd03757   90 LLSTILYSRRFFPYYVFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGrKNQNNVERTplslee 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499286200 158 --EIVLKALKAAIERDVTSGDGIDILTIKRDNTSSEDFI 194
Cdd:cd03757  170 avSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFP 208
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-187 9.35e-34

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: 118.50  E-value: 9.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRFgIAG--AGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:cd03761    2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPY-LLGtmAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd03761   81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                        170       180
                 ....*....|....*....|...
gi 499286200 165 KAAIERDVTSGDGIDILTIKRDN 187
Cdd:cd03761  161 YHATHRDAYSGGNVNLYHVREDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-188 1.35e-31

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: 113.06  E-value: 1.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd03763    2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIApNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKwtPFIS-ELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd03763   82 MLKQHLFRYQ--GHIGaALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                        170       180
                 ....*....|....*....|....
gi 499286200 165 KAAIERDVTSGDGIDILTIKRDNT 188
Cdd:cd03763  160 EAGIFNDLGSGSNVDLCVITKDGV 183
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-187 5.95e-31

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 113.01  E-value: 5.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDdHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYkwT------PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKE 158
Cdd:PRK03996 116 KKICDHKQQY--TqhggvrPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAIE 193

                        170       180
                 ....*....|....*....|....*....
gi 499286200 159 IVLKALKAAIERDVTSgDGIDILTIKRDN 187
Cdd:PRK03996 194 LALKALAKANEGKLDP-ENVEIAYIDVET 221
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-184 1.91e-30

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: 110.88  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:cd03756   29 TTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDdHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYKWT----PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIV 160
Cdd:cd03756  108 KKICDLKQQYTQHggvrPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELA 187

                        170       180
                 ....*....|....*....|....
gi 499286200 161 LKALKAAIErDVTSGDGIDILTIK 184
Cdd:cd03756  188 LKALYAALE-ENETPENVEIAYVT 210
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 9-190 1.47e-29

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: 108.10  E-value: 1.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   9 LGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAKLL 87
Cdd:cd03759    7 VAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGdRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSLI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  88 SVILYQYKWTPFISELLFGGVDDEG-PKLFVLDPIGSL-IEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKALK 165
Cdd:cd03759   87 SSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGCPsIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETISQALL 166

                        170       180
                 ....*....|....*....|....*
gi 499286200 166 AAIERDVTSGDGIDILTIKRDNTSS 190
Cdd:cd03759  167 SAVDRDALSGWGAVVYIITKDKVTT 191
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-183 7.85e-29

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: 106.65  E-value: 7.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   4 LPATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIGR-FGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKA 82
Cdd:cd03753   26 LGSTAIGIKTKEGVVLAVEKRIT-SPLMEPSSVEKIMEIDDhIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVES 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  83 AAKLLSVILYQYKWT---------PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNL 153
Cdd:cd03753  105 VTQAVSDLALQFGEGddgkkamsrPFGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184

                        170       180       190
                 ....*....|....*....|....*....|
gi 499286200 154 DKGKEIVLKALKAAIERDVTSgDGIDILTI 183
Cdd:cd03753  185 EEAEKLALSILKQVMEEKLNS-TNVELATV 213
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-191 5.14e-28

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: 103.84  E-value: 5.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd03762    2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHdRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKWTpFISELLFGGVDD-EGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKAL 164
Cdd:cd03762   82 LFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*..
gi 499286200 165 KAAIERDVTSGDGIDILTIKRDNTSSE 191
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVERK 187
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-197 1.57e-27

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 104.30  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRFGIAG-AGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:PTZ00488  41 TTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTmAGGAADCSFWERELAMQCRLYELRNGELISVAAASK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLKALK 165
Cdd:PTZ00488 121 ILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIY 200

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499286200 166 AAIERDVTSGDGIDILTIKRD---NTSSEDFIKIF 197
Cdd:PTZ00488 201 HATFRDAYSGGAINLYHMQKDgwkKISADDCFDLH 235
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-183 6.40e-26

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: 99.05  E-value: 6.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIGR-FGIAGAGIMGDIQTLTRLMNVE-IKYYEMYNNkPISVKAA 83
Cdd:cd01911   28 STAVGIKGKDGVVLAVEKKVT-SKLLDPSSVEKIFKIDDhIGCAVAGLTADARVLVNRARVEaQNYRYTYGE-PIPVEVL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  84 AKLLS--VILY-QYKWT-PFISELLFGGVDDE-GPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKE 158
Cdd:cd01911  106 VKRIAdlAQVYtQYGGVrPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDLTLEEAIK 185

                        170       180
                 ....*....|....*....|....*
gi 499286200 159 IVLKALKAAIERDVTSgDGIDILTI 183
Cdd:cd01911  186 LALKALKEVLEEDKKA-KNIEIAVV 209
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-186 1.09e-21

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: 87.63  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRFGIAGA-GIMGDIQTLTRLMNVEIKYYEMYNNK-PISVKAA 83
Cdd:cd03760    3 TSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGAsGDYADFQYLKRLLDQLVIDDECLDDGhSLSPKEI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  84 AKLLSVILYQY--KWTPFISELLFGGVDDEG-PKLFVLDPIGSLIEDNYAAVGSGARVAIGVL--ESEYDPSMNLDKGKE 158
Cdd:cd03760   83 HSYLTRVLYNRrsKMNPLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLreAWEKKPDLTEEEARA 162

                        170       180
                 ....*....|....*....|....*...
gi 499286200 159 IVLKALKAAIERDVTSGDGIDILTIKRD 186
Cdd:cd03760  163 LIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 7-170 1.16e-19

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: 82.25  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSdHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 LLSVILYQY--KWTPFISELLFGGVDD-EGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEIVLK 162
Cdd:cd03758   83 FTRRELAESlrSRTPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162


                 ....*...
gi 499286200 163 ALKAAIER 170
Cdd:cd03758  163 CIKELKKR 170
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-183 2.03e-16

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: 73.92  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRFGIAG-AGIMGDIQTLT-RLMNVEIKYYEMYnNKPISVKAA 83
Cdd:cd03752   30 GTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAvAGITSDANILInYARLIAQRYLYSY-QEPIPVEQL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  84 AKLLSVILYQYK----WTPFISELLFGGVDD-EGPKLFVLDPIGsliedNYA-----AVGSGARVAIGVLESEYDPSMNL 153
Cdd:cd03752  109 VQRLCDIKQGYTqyggLRPFGVSFLYAGWDKhYGFQLYQSDPSG-----NYSgwkatAIGNNNQAAQSLLKQDYKDDMTL 183

                        170       180       190
                 ....*....|....*....|....*....|
gi 499286200 154 DKGKEIVLKALKAAIERDVTSGDGIDILTI 183
Cdd:cd03752  184 EEALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-180 7.22e-16

proteasome_alpha_type_2. 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: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 72.74  E-value: 7.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRL-MNVEIKYYEMYNnKPISVKAA 83
Cdd:cd03750   28 APSVGIKAANGVVLATEKKVP-SPLIDESSVHKVEQITpHIGMVYSGMGPDFRVLVKKaRKIAQQYYLVYG-EPIPVSQL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  84 AKLLSVILYQYKWT----PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKEI 159
Cdd:cd03750  106 VREIASVMQEYTQSggvrPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDAIHT 185

                        170       180
                 ....*....|....*....|.
gi 499286200 160 VLKALKAAIERDVTsGDGIDI 180
Cdd:cd03750  186 AILTLKEGFEGQMT-EKNIEI 205
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 8-189 3.10e-14

proteasome_alpha_type_1. 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: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 68.09  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   8 ALGIKLNDGIILAAERRLSYGgfvLSRSAKKVFKIG-RFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAKL 86
Cdd:cd03749   30 TVGLKSKTHAVLVALKRATSE---LSSYQKKIFKVDdHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVSRLVSK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  87 LS----VILYQYKWTPFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKgKEIVLK 162
Cdd:cd03749  107 VAekaqINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEEFEDCSL-EELIKH 185

                        170       180
                 ....*....|....*....|....*..
gi 499286200 163 ALKAAieRDVTSGDgiDILTIKrdNTS 189
Cdd:cd03749  186 ALRAL--RETLPGE--QELTIK--NVS 206
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-165 2.22e-13

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 65.76  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERrlsyggFVLSR-----SAKKVFKIGR-FGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPIS 79
Cdd:cd03751   31 GTAIGIRCKDGVVLAVEK------LVTSKlyepgSNKRIFNVDRhIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  80 VKAAAKLLS--VILYQ-YKWT-PFISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLdk 155
Cdd:cd03751  105 VKVLADRVAmyMHAYTlYSSVrPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTC-- 182

                        170
                 ....*....|
gi 499286200 156 gKEIVLKALK 165
Cdd:cd03751  183 -REAVKEAAK 191
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-180 3.85e-12

proteasome_alpha_type_7. 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: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 62.38  E-value: 3.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRlSYGGFVLSRSAKKVFKI-GRFGIAGAGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAAK 85
Cdd:cd03755   29 TAVGVRGKDCVVLGVEKK-SVAKLQDPRTVRKICMLdDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYITR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  86 llSVILYQYKWT------PF-ISELLFGGVDDEGPKLFVLDPIGSLIEDNYAAVGSGARVAIGVLESEYDPSMNLDKGKE 158
Cdd:cd03755  108 --YIAGLQQRYTqsggvrPFgISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTIK 185

                        170       180
                 ....*....|....*....|..
gi 499286200 159 IVLKALKAAIErdvTSGDGIDI 180
Cdd:cd03755  186 LAIKALLEVVQ---SGSKNIEL 204
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 6-196 4.24e-11

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 60.25  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   6 ATALGIKLNDGIILAAERRLSYGGFVLSRSAKKVFKIGRFGIAG-AGIMGDIQTLTRLMNVEIKYYEMYNNKPISVKAAA 84
Cdd:PTZ00246  32 SLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAvAGLTADANILINQCRLYAQRYRYTYGEPQPVEQLV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  85 KLLSVILYQYK----WTPFISELLFGGVD-DEGPKLFVLDPIGsliedNYA-----AVGSGARVAIGVLESEYDPSMNLD 154
Cdd:PTZ00246 112 VQICDLKQSYTqfggLRPFGVSFLFAGYDeNLGYQLYHTDPSG-----NYSgwkatAIGQNNQTAQSILKQEWKEDLTLE 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 499286200 155 KGKEIVLKALKAAIERDVTSGDGIDILTIKRDNTSSEDFIKI 196
Cdd:PTZ00246 187 QGLLLAAKVLTKSMDSTSPKADKIEVGILSHGETDGEPIQKM 228
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 7-176 3.44e-04

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 39.91  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200   7 TALGIKLNDGIILAAERRLSyGGFVLSRSAKKVFKIG-RFGIAGAGIMGD---IQTLTRLMNVEIKY---YEMynnkPIS 79
Cdd:cd03754   31 TSVAVRGKDCAVVVTQKKVP-DKLIDPSTVTHLFRITdEIGCVMTGMIADsrsQVQRARYEAAEFKYkygYEM----PVD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499286200  80 V--KAAAKLLSVILYQYKWTPFISELLFGGVDDE-GPKLFVLDPIGSLIedNYAAVGSGARV--AIGVLESEY----DPS 150
Cdd:cd03754  106 VlaKRIADINQVYTQHAYMRPLGVSMILIGIDEElGPQLYKCDPAGYFA--GYKATAAGVKEqeATNFLEKKLkkkpDLI 183

                        170       180
                 ....*....|....*....|....*.
gi 499286200 151 MNLDKGKEIVLKALKAAIERDVTSGD 176
Cdd:cd03754  184 ESYEETVELAISCLQTVLSTDFKATE 209
 
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