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Conserved domains on  [gi|2043688517|pdb|6ZP8|K]
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Chain K, Proteasome subunit beta type-5

Protein Classification

proteasome subunit beta( domain architecture ID 10132926)

proteasome subunit beta is a subunit of the eukaryotic 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to the catalytic subunit beta type-5 (PSMB5) which has chymotrypsin-like activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 7.94e-133

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: 370.42  E-value: 7.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*....
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDGWIYHG 189
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRKIS 188
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 7.94e-133

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: 370.42  E-value: 7.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*....
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDGWIYHG 189
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-199 1.84e-111

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 318.86  E-value: 1.84e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        81 KILSNLVYQYKGAGLSMGTMICGYTRKeGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:PTZ00488 120 KILANIVWNYKGMGLSMGTMICGWDKK-GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170       180       190
                 ....*....|....*....|....*....|....*....
6ZP8_K       161 ILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWK 199
Cdd:PTZ00488 199 IYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQK 237
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-180 1.14e-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: 182.77  E-value: 1.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K          1 TTTLAFRFQGGIIVAVDSRATAGNWV-ASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         77 -AAASKILSNLVYQYKGaGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALY 155
Cdd:pfam00227  85 aRIADLLQAYTQYSGRR-PFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
6ZP8_K        156 LGKRSILAAAHRDAYSGGSVNLYHV 180
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-184 3.57e-48

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: 155.83  E-value: 3.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K          1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:TIGR03634  82 TLLSNILNSNRFFPFIVQLLVGGVD-EEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
6ZP8_K        161 ILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-184 1.87e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 152.99  E-value: 1.87e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAG---LSMGTMICGYTRkEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLG 157
Cdd:COG0638 116 KLLSDLLQGYTQYGvrpFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                       170       180
                ....*....|....*....|....*..
6ZP8_K      158 KRSILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDG 221
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-189 7.94e-133

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: 370.42  E-value: 7.94e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*....
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDGWIYHG 189
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 1-199 1.84e-111

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 318.86  E-value: 1.84e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        81 KILSNLVYQYKGAGLSMGTMICGYTRKeGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:PTZ00488 120 KILANIVWNYKGMGLSMGTMICGWDKK-GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170       180       190
                 ....*....|....*....|....*....|....*....
6ZP8_K       161 ILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWK 199
Cdd:PTZ00488 199 IYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQK 237
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-188 3.48e-84

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: 247.36  E-value: 3.48e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDGWIYH 188
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 1-180 1.22e-62

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: 192.71  E-value: 1.22e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAG--LSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGK 158
Cdd:cd01906  81 KLLANLLYEYTQSLrpLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
6ZP8_K      159 RSILAAAHRDAYSGGSVNLYHV 180
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 1-180 1.14e-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: 182.77  E-value: 1.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K          1 TTTLAFRFQGGIIVAVDSRATAGNWV-ASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLlSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         77 -AAASKILSNLVYQYKGaGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALY 155
Cdd:pfam00227  85 aRIADLLQAYTQYSGRR-PFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
6ZP8_K        156 LGKRSILAAAHRDAYSGGSVNLYHV 180
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-184 3.57e-48

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: 155.83  E-value: 3.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K          1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:TIGR03634  82 TLLSNILNSNRFFPFIVQLLVGGVD-EEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
6ZP8_K        161 ILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-184 1.87e-46

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 152.99  E-value: 1.87e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAG---LSMGTMICGYTRkEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLG 157
Cdd:COG0638 116 KLLSDLLQGYTQYGvrpFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194

                       170       180
                ....*....|....*....|....*..
6ZP8_K      158 KRSILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDG 221
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-184 2.82e-46

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: 151.25  E-value: 2.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDG 183
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 1-163 3.50e-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: 132.13  E-value: 3.50e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAG-LSMGTMICGYTrKEGPTIYYVDSDGTRLKG-DIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGK 158
Cdd:cd01901  81 KELAKLLQVYTQGRpFGVNLIVAGVD-EGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....*
6ZP8_K      159 RSILA 163
Cdd:cd01901 160 KALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-184 2.43e-34

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: 120.79  E-value: 2.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAgLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS 160
Cdd:cd03762  81 SLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNA 159

                       170       180
                ....*....|....*....|....
6ZP8_K      161 ILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:cd03762 160 LSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-191 2.61e-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: 112.68  E-value: 2.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKG---AGLSMGTMICgytrkEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLG 157
Cdd:cd03763  81 TMLKQHLFRYQGhigAALVLGGVDY-----TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLV 155

                       170       180       190
                ....*....|....*....|....*....|....
6ZP8_K      158 KRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNH 191
Cdd:cd03763 156 CEAIEAGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-161 3.15e-12

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: 62.60  E-value: 3.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        2 TTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADC-QFWEtWLGSQCRLHELREKERISV-AAA 79
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRlQFAE-YIQKNIQLYKMRNGYELSPkAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       80 SKILSNLV-YQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGK 158
Cdd:cd03758  82 NFTRRELAeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMK 161


                ...
6ZP8_K      159 RSI 161
Cdd:cd03758 162 KCI 164
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-184 3.51e-12

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: 63.05  E-value: 3.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        2 TTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEI-NPFLLGTmAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLtDKCVLGS-SGFQADILALTKRLKARIKMYKYSHNKEMSTEAIA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDS-----NYKW----DLSVE 151
Cdd:cd03757  89 QLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvgrkNQNNvertPLSLE 168

                       170       180       190
                ....*....|....*....|....*....|...
6ZP8_K      152 DALYLGKRSILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:cd03757 169 EAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-184 1.36e-11

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: 61.10  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        4 LAFRFQGGIIVAVDSRatagNWVASQTV----KKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAA 79
Cdd:cd03759   7 VAMAGKDCVAIASDLR----LGVQQQTVstdfQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       80 SKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDG-TRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGK 158
Cdd:cd03759  83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162

                       170       180
                ....*....|....*....|....*.
6ZP8_K      159 RSILAAAHRDAYSGGSVNLYHVTEDG 184
Cdd:cd03759 163 QALLSAVDRDALSGWGAVVYIITKDK 188
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-156 5.78e-11

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: 59.66  E-value: 5.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNWVASqTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03753  28 STAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAGLSMGTM---------ICGYTrKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVE 151
Cdd:cd03753 107 QAVSDLALQFGEGDDGKKAMsrpfgvallIAGVD-ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLE 185


                ....*
6ZP8_K      152 DALYL 156
Cdd:cd03753 186 EAEKL 190
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-182 4.01e-08

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: 51.56  E-value: 4.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATaGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03756  29 TTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYK--GAGLSMGT-MICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLG 157
Cdd:cd03756 108 KKICDLKQQYTqhGGVRPFGVaLLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELA 187

                       170       180
                ....*....|....*....|....*
6ZP8_K      158 KRsILAAAHRDAYSGGSVNLYHVTE 182
Cdd:cd03756 188 LK-ALYAALEENETPENVEIAYVTV 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-164 4.75e-08

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: 51.29  E-value: 4.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAGNwVASQTVKKVIEINPFLLGTMAGGAADCQFwetwLGSQCRL----HELREKERISV 76
Cdd:cd01911  28 STAVGIKGKDGVVLAVEKKVTSKL-LDPSSVEKIFKIDDHIGCAVAGLTADARV----LVNRARVeaqnYRYTYGEPIPV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       77 AAASKILSNL--VY-QYKGA---GLSMgtMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV 150
Cdd:cd01911 103 EVLVKRIADLaqVYtQYGGVrpfGVSL--LIAGYDEEGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDLTL 180

                       170
                ....*....|....
6ZP8_K      151 EDALYLGKRSILAA 164
Cdd:cd01911 181 EEAIKLALKALKEV 194
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-204 9.15e-06

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 44.82  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K         1 TTTLAFRFQGGIIVAVDSRATaGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        81 KILSNL--VY-QYKGA---GLSMgtMICGYTRKeGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDAL 154
Cdd:PRK03996 116 KKICDHkqQYtQHGGVrpfGVAL--LIAGVDDG-GPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYKEDLSLEEAI 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
6ZP8_K       155 YLGKRSiLAAAHRDAYSGGSVNLYHVTEDgwiyhgnhdvGELFWKVKEEE 204
Cdd:PRK03996 193 ELALKA-LAKANEGKLDPENVEIAYIDVE----------TKKFRKLSVEE 231
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-162 4.12e-04

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: 40.04  E-value: 4.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAgNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03755  28 TTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYIT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQYKGAG----LSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYL 156
Cdd:cd03755 107 RYIAGLQQRYTQSGgvrpFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTIKL 186


                ....*.
6ZP8_K      157 GKRSIL 162
Cdd:cd03755 187 AIKALL 192
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 1-154 2.81e-03

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: 37.69  E-value: 2.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K        1 TTTLAFRFQGGIIVAVDSRATAgNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAAS 80
Cdd:cd03750  28 APSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQLV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6ZP8_K       81 KILSNLVYQY--KGA----GLSMgtMICGYTRKeGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDAL 154
Cdd:cd03750 107 REIASVMQEYtqSGGvrpfGVSL--LIAGWDEG-GPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDAI 183
 
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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