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Conserved domains on  [gi|1938935480|pdb|3H4P|e]
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Chain e, Proteasome subunit beta

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

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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 ...
 1-187 2.48e-107

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: 306.44  E-value: 2.48e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e          1 MTTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         81 ATLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLAL 160
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVD-EEGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
3H4P_e        161 NALKSAMERDTFSGNGISLAVITKDGV 187
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-187 2.48e-107

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: 306.44  E-value: 2.48e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e          1 MTTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         81 ATLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLAL 160
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVD-EEGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
3H4P_e        161 NALKSAMERDTFSGNGISLAVITKDGV 187
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-191 2.91e-107

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: 306.10  E-value: 2.91e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLALN 161
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                       170       180       190
                ....*....|....*....|....*....|
3H4P_e      162 ALKSAMERDTFSGNGISLAVITKDGVKIFE 191
Cdd:cd03764 159 AIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 2-194 8.52e-94

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 273.56  E-value: 8.52e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSS---RMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKL 158
Cdd:COG0638 116 KLLSDLLQGYtqyGVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|....*.
3H4P_e      159 ALNALKSAMERDTFSGNGISLAVITKDGVKIFEDEE 194
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 2-182 1.03e-68

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: 208.58  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e          2 TTTVGLICDDAVILATDKRASLGNLVADK-EAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         81 ---ATLLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIK 157
Cdd:pfam00227  85 ariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
3H4P_e        158 LALNALKSAMERDTFSGNGISLAVI 182
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
2-200 1.13e-36

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 128.41  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         2 TTTVGLICDDAVILATDKRASlGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        82 TLLSNILHSSRMF----PFLTQIIIGGYDLlEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEEGIK 157
Cdd:PRK03996 116 KKICDHKQQYTQHggvrPFGVALLIAGVDD-GGPRLFETDPSGAYLEYKA-TAIGAGRDTVMEFLEKNYKEDLSLEEAIE 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
3H4P_e       158 LALNALKSAMErDTFSGNGISLAVITKDG--VKIFEDEEIEKILD 200
Cdd:PRK03996 194 LALKALAKANE-GKLDPENVEIAYIDVETkkFRKLSVEEIEKYLE 237
 
Name Accession Description Interval E-value
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 1-187 2.48e-107

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: 306.44  E-value: 2.48e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e          1 MTTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         81 ATLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLAL 160
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVD-EEGPHLYSLDPAGGIIEDD-YTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
3H4P_e        161 NALKSAMERDTFSGNGISLAVITKDGV 187
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-191 2.91e-107

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: 306.10  E-value: 2.91e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLALN 161
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVD-EEGPHLYSLDPLGSIIEDK-YTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                       170       180       190
                ....*....|....*....|....*....|
3H4P_e      162 ALKSAMERDTFSGNGISLAVITKDGVKIFE 191
Cdd:cd03764 159 AIKSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 2-194 8.52e-94

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 273.56  E-value: 8.52e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSS---RMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKL 158
Cdd:COG0638 116 KLLSDLLQGYtqyGVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEK-AVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|....*.
3H4P_e      159 ALNALKSAMERDTFSGNGISLAVITKDGVKIFEDEE 194
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-191 2.03e-78

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: 233.10  E-value: 2.03e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEkTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLALN 161
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEA-PFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKK 159

                       170       180       190
                ....*....|....*....|....*....|
3H4P_e      162 ALKSAMERDTFSGNGISLAVITKDGVKIFE 191
Cdd:cd01912 160 AIDSAIERDLSSGGGVDVAVITKDGVEELR 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 2-182 1.03e-68

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: 208.58  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e          2 TTTVGLICDDAVILATDKRASLGNLVADK-EAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         81 ---ATLLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIK 157
Cdd:pfam00227  85 ariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYK-ATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
3H4P_e        158 LALNALKSAMERDTFSGNGISLAVI 182
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 2-182 6.99e-68

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: 206.19  E-value: 6.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSR--MFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLA 159
Cdd:cd01906  81 KLLANLLYEYTqsLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYK-ATAIGSGSQYALGILEKLYKPDMTLEEAIELA 159

                       170       180
                ....*....|....*....|...
3H4P_e      160 LNALKSAMERDTFSGNGISLAVI 182
Cdd:cd01906 160 LKALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 2-165 5.89e-46

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: 149.85  E-value: 5.89e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSR-MFPFLTQIIIGGYDLLEGaKLFSLDPLGGMNEEKTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLAL 160
Cdd:cd01901  81 KELAKLLQVYTqGRPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....*
3H4P_e      161 NALKS 165
Cdd:cd01901 160 KALKS 164
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-188 1.07e-40

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: 137.33  E-value: 1.07e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNiPPLACA 81
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRK-PRVVTA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 -TLLSNILhssrmFPFLTQI----IIGGYDlLEGAKLFSLDPLGGMNEEKtFTATGSGSPIAYGVLEAGYDRDMSVEEGI 156
Cdd:cd03763  80 lTMLKQHL-----FRYQGHIgaalVLGGVD-YTGPHLYSIYPHGSTDKLP-FVTMGSGSLAAMSVLEDRYKPDMTEEEAK 152

                       170       180       190
                ....*....|....*....|....*....|..
3H4P_e      157 KLALNALKSAMERDTFSGNGISLAVITKDGVK 188
Cdd:cd03763 153 KLVCEAIEAGIFNDLGSGSNVDLCVITKDGVE 184
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-186 3.19e-40

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: 135.84  E-value: 3.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKTFtATGSGSPIAYGVLEAGYDRDMSVEEGIKLALN 161
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLF-SVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                       170       180
                ....*....|....*....|....*
3H4P_e      162 ALKSAMERDTFSGNGISLAVITKDG 186
Cdd:cd03761 159 AIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-188 6.19e-40

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: 135.04  E-value: 6.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRniPPL--A 79
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGE--PPLvkT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       80 CATLLSNILHSSRMFpFLTQIIIGGYDLLEGAKLFSLdPLGGMNEEKTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLA 159
Cdd:cd03762  79 AASLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSI-PLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFV 156

                       170       180
                ....*....|....*....|....*....
3H4P_e      160 LNALKSAMERDTFSGNGISLAVITKDGVK 188
Cdd:cd03762 157 KNALSLAMSRDGSSGGVIRLVIITKDGVE 185
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
2-200 1.13e-36

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 128.41  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         2 TTTVGLICDDAVILATDKRASlGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        82 TLLSNILHSSRMF----PFLTQIIIGGYDLlEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEEGIK 157
Cdd:PRK03996 116 KKICDHKQQYTQHggvrPFGVALLIAGVDD-GGPRLFETDPSGAYLEYKA-TAIGAGRDTVMEFLEKNYKEDLSLEEAIE 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
3H4P_e       158 LALNALKSAMErDTFSGNGISLAVITKDG--VKIFEDEEIEKILD 200
Cdd:PRK03996 194 LALKALAKANE-GKLDPENVEIAYIDVETkkFRKLSVEEIEKYLE 237
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-182 3.51e-33

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: 118.31  E-value: 3.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASlGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd01911  28 STAVGIKGKDGVVLAVEKKVT-SKLLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILH----SSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEEGIK 157
Cdd:cd01911 107 KRIADLAQvytqYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKA-TAIGKGSQEAKTFLEKRYKKDLTLEEAIK 185

                       170       180
                ....*....|....*....|....*
3H4P_e      158 LALNALKSAMErDTFSGNGISLAVI 182
Cdd:cd01911 186 LALKALKEVLE-EDKKAKNIEIAVV 209
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 3-188 1.95e-32

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: 116.59  E-value: 1.95e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        3 TTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACAT 82
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       83 LLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEkTFTATGSGSPIAYGVLEAGYDR---------DMSVE 153
Cdd:cd03757  90 LLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERE-TYSAGGSASSLIQPLLDNQVGRknqnnvertPLSLE 168

                       170       180       190
                ....*....|....*....|....*....|....*
3H4P_e      154 EGIKLALNALKSAMERDTFSGNGISLAVITKDGVK 188
Cdd:cd03757 169 EAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 2-193 1.56e-31

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 115.47  E-value: 1.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        82 TLLSNILHSSRMFPFLTQIIIGGYDlLEGAKLFSLDPLGGMNEEKTFTAtGSGSPIAYGVLEAGYDRDMSVEEGIKLALN 161
Cdd:PTZ00488 120 KILANIVWNYKGMGLSMGTMICGWD-KKGPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRR 197

                        170       180       190
                 ....*....|....*....|....*....|...
3H4P_e       162 ALKSAMERDTFSGNGISLAVITKDG-VKIFEDE 193
Cdd:PTZ00488 198 AIYHATFRDAYSGGAINLYHMQKDGwKKISADD 230
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-183 3.63e-31

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: 113.19  E-value: 3.63e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASlGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRnipPLACA 81
Cdd:cd03756  29 TTALGIKCKEGVVLAVDKRIT-SKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGE---PIDVE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMF-------PFLTQIIIGGYDLlEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEE 154
Cdd:cd03756 105 VLVKKICDLKQQYtqhggvrPFGVALLIAGVDD-GGPRLFETDPSGAYNEYKA-TAIGSGRQAVTEFLEKEYKEDMSLEE 182

                       170       180
                ....*....|....*....|....*....
3H4P_e      155 GIKLALNALKSAMErDTFSGNGISLAVIT 183
Cdd:cd03756 183 AIELALKALYAALE-ENETPENVEIAYVT 210
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-190 3.34e-30

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: 110.41  E-value: 3.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        5 VGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACATLL 84
Cdd:cd03759   7 VAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSLI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       85 SNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKLALNALK 164
Cdd:cd03759  87 SSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETISQALL 166

                       170       180
                ....*....|....*....|....*.
3H4P_e      165 SAMERDTFSGNGISLAVITKDGVKIF 190
Cdd:cd03759 167 SAVDRDALSGWGAVVYIITKDKVTTR 192
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 4.30e-29

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: 107.29  E-value: 4.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        1 MTTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLAC 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       81 ATLLSNILHSS--RMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEkTFTATGSGSPIAYGVLEAGYDRDMSVEEGIKL 158
Cdd:cd03758  81 ANFTRRELAESlrSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKV-PYAAHGYGAYFCLSILDRYYKPDMTVEEALEL 159

                       170       180       190
                ....*....|....*....|....*....|....
3H4P_e      159 ALNALKSAMERDTFSGNGISLAVITKDGVKIFED 192
Cdd:cd03758 160 MKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 4-202 6.42e-26

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 100.70  E-value: 6.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e         4 TVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQaivrLLIAEAKLYKMR----TGRNIPPLA 79
Cdd:PTZ00246  34 TVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADAN----ILINQCRLYAQRyrytYGEPQPVEQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        80 CATLLSNILHSSRMF----PFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEEG 155
Cdd:PTZ00246 110 LVVQICDLKQSYTQFgglrPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKA-TAIGQNNQTAQSILKQEWKEDLTLEQG 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
3H4P_e       156 IKLALNALKSAMERDTFSGNGISLAVITKDG------VKIFEDEEIEKILDSM 202
Cdd:PTZ00246 189 LLLAAKVLTKSMDSTSPKADKIEVGILSHGEtdgepiQKMLSEKEIAELLKKV 241
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 2-192 4.67e-25

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: 96.87  E-value: 4.67e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLL---IAEAKLYKmrTGRNIPPL 78
Cdd:cd03760   3 TSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLdqlVIDDECLD--DGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       79 ACATLLSNILHS--SRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTFtATGSGSPIAYGVLEAGY--DRDMSVEE 154
Cdd:cd03760  81 EIHSYLTRVLYNrrSKMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHV-ATGFGAYLALPLLREAWekKPDLTEEE 159

                       170       180       190
                ....*....|....*....|....*....|....*...
3H4P_e      155 GIKLALNALKSAMERDTFSGNGISLAVITKDGVKIFED 192
Cdd:cd03760 160 ARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-182 5.48e-20

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: 84.31  E-value: 5.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASlGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd03753  28 STAIGIKTKEGVVLAVEKRIT-SPLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVT 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNI-LHSSRMF--------PFLTQIIIGGYDLlEGAKLFSLDPLGgmneekTFT-----ATGSGSPIAYGVLEAGYD 147
Cdd:cd03753 107 QAVSDLaLQFGEGDdgkkamsrPFGVALLIAGVDE-NGPQLFHTDPSG------TFTrcdakAIGSGSEGAQSSLQEKYH 179

                       170       180       190
                ....*....|....*....|....*....|....*
3H4P_e      148 RDMSVEEGIKLALNALKSAMErDTFSGNGISLAVI 182
Cdd:cd03753 180 KDMTLEEAEKLALSILKQVME-EKLNSTNVELATV 213
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-182 9.03e-20

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: 83.57  E-value: 9.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRaSLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAqaivRLLIAEAKL----YKMrTGRNIPP 77
Cdd:cd03755  28 TTAVGVRGKDCVVLGVEKK-SVAKLQDPRTVRKICMLDDHVCLAFAGLTADA----RVLINRARLecqsHRL-TVEDPVT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       78 L-----ACATLLSNILHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSV 152
Cdd:cd03755 102 VeyitrYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKA-NAIGRNSKTVREFLEKNYKEEMTR 180

                       170       180       190
                ....*....|....*....|....*....|
3H4P_e      153 EEGIKLALNALKSAMERdtfSGNGISLAVI 182
Cdd:cd03755 181 DDTIKLAIKALLEVVQS---GSKNIELAVM 207
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-182 1.63e-19

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: 82.78  E-value: 1.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        3 TTVGLICDDAVILATDKRASLGNLVADKEAKKLYKIDDYIAMTIAGSVGDAQAivrlLIAEAKLYKMRTGRNI-PPLACA 81
Cdd:cd03752  31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANI----LINYARLIAQRYLYSYqEPIPVE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLSNILHSSRMF-------PFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEE 154
Cdd:cd03752 107 QLVQRLCDIKQGYtqygglrPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKA-TAIGNNNQAAQSLLKQDYKDDMTLEE 185

                       170       180
                ....*....|....*....|....*...
3H4P_e      155 GIKLALNALKSAMERDTFSGNGISLAVI 182
Cdd:cd03752 186 ALALAVKVLSKTMDSTKLTSEKLEFATL 213
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-182 5.23e-19

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: 81.57  E-value: 5.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASlGNLVADKeaKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLACA 81
Cdd:cd03749  28 SATVGLKSKTHAVLVALKRAT-SELSSYQ--KKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVSRLV 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       82 TLLS-----NILHSSRMfPFLTQIIIGGYDLLeGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYD--RDMSVEE 154
Cdd:cd03749 105 SKVAekaqiNTQRYGRR-PYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKA-TSIGARSQSARTYLERHFEefEDCSLEE 181

                       170       180
                ....*....|....*....|....*....
3H4P_e      155 GIKLALNALKSAMERDT-FSGNGISLAVI 182
Cdd:cd03749 182 LIKHALRALRETLPGEQeLTIKNVSIAIV 210
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-200 1.05e-17

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: 78.52  E-value: 1.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        2 TTTVGLICDDAVILATDKRASlgNLVADK-EAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPPLA- 79
Cdd:cd03750  28 APSVGIKAANGVVLATEKKVP--SPLIDEsSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQl 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       80 ---CATLLSNILHSSRMFPFLTQIIIGGYDLlEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRDMSVEEGI 156
Cdd:cd03750 106 vreIASVMQEYTQSGGVRPFGVSLLIAGWDE-GGPYLYQVDPSGSYFTWKA-TAIGKNYSNAKTFLEKRYNEDLELEDAI 183

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3H4P_e      157 KLALNALKSAMERDtFSGNGISLAVITKDGV-KIFEDEEIEKILD 200
Cdd:cd03750 184 HTAILTLKEGFEGQ-MTEKNIEIGICGETKGfRLLTPAEIKDYLA 227
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-182 1.42e-14

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: 69.57  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        3 TTVGLICDDAVILATDKRaslgnlVADK-----EAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPP 77
Cdd:cd03754  31 TSVAVRGKDCAVVVTQKK------VPDKlidpsTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPV 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       78 LACATLLSNI----LHSSRMFPFLTQIIIGGYDLLEGAKLFSLDPLGGMNEEKTfTATGSGSPIAYGVLEAGYDRD---- 149
Cdd:cd03754 105 DVLAKRIADInqvyTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKA-TAAGVKEQEATNFLEKKLKKKpdli 183

                       170       180       190
                ....*....|....*....|....*....|...
3H4P_e      150 MSVEEGIKLALNALKSAMERDtFSGNGISLAVI 182
Cdd:cd03754 184 ESYEETVELAISCLQTVLSTD-FKATEIEVGVV 215
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-157 6.54e-14

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: 67.69  E-value: 6.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e        3 TTVGLICDDAVILATDKraslgnLVADK-----EAKKLYKIDDYIAMTIAGSVGDAQAIVRLLIAEAKLYKMRTGRNIPP 77
Cdd:cd03751  32 TAIGIRCKDGVVLAVEK------LVTSKlyepgSNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H4P_e       78 LACATLLSNILH------SSRmfPFLTQIIIGGYDlLEGAKLFSLDPlGGMNEEKTFTATGSGSPIAYGVLEAGYDRDMS 151
Cdd:cd03751 106 KVLADRVAMYMHaytlysSVR--PFGCSVLLGGYD-SDGPQLYMIEP-SGVSYGYFGCAIGKGKQAAKTELEKLKFSELT 181


                ....*.
3H4P_e      152 VEEGIK 157
Cdd:cd03751 182 CREAVK 187
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 2-66 7.50e-03

Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system that is the prokaryotic homolog of the proteasome. HslV is a dimer of hexamers (a dodecamer) that forms a central proteolytic chamber with active sites on the interior walls of the cavity. HslV shares significant sequence and structural similarity with the proteasomal beta-subunit and both are members of the Ntn-family of hydrolases. HslV has a nucleophilic threonine residue at its N-terminus that is exposed after processing of the propeptide and is directly involved in active site catalysis.


Pssm-ID: 238894  Cd Length: 171  Bit Score: 36.02  E-value: 7.50e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3H4P_e        2 TTTVGLICDDAVILATDKRASLGNLVADKEAKKLYKI-DDYIAMTIAGSVGDAQAIVRLLiaEAKL 66
Cdd:cd01913   1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLyNGKVIAGFAGSTADAFTLFERF--EAKL 64
 
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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