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Conserved domains on  [gi|18859271|ref|NP_571227|]
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proteasome subunit beta type-6 [Danio rerio]

Protein Classification

proteasome subunit beta( domain architecture ID 10132932)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-210 1.56e-127

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: 357.69  E-value: 1.56e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAGAL 183
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*..
gi 18859271 184 TLPMERDGSSGGVVRLAVISEQGVERQ 210
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERK 187
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-210 1.56e-127

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: 357.69  E-value: 1.56e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAGAL 183
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*..
gi 18859271 184 TLPMERDGSSGGVVRLAVISEQGVERQ 210
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERK 187
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 20-202 4.49e-48

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: 156.19  E-value: 4.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    20 VSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVT-DKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    99 VQ----TAASLFRDMCYRYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEE 174
Cdd:pfam00227  81 VElaarIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 18859271   175 CLKFTAGALTLPMERDGSSGGVVRLAVI 202
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 19-209 2.64e-35

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 124.49  E-value: 2.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  19 EVSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:COG0638  31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  99 VQTAASLFRDMCYRYREE----LMAGIIVAGWDrRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEE 174
Cdd:COG0638 111 VEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18859271 175 CLKFTAGALTLPMERDGSSGGVVRLAVISEQGVER 209
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 23-207 9.29e-30

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: 109.22  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    23 GTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTA 102
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   103 ASLFRDMCYRYR-EELMAGIIVAGWDrRRGGQVYTV-PVGGMLTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLKFTA 180
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVD-EEGPHLYSLdPAGGIIEDDYTAT-GSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 18859271   181 GALTLPMERDGSSGGVVRLAVISEQGV 207
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 19-206 1.31e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 100.06  E-value: 1.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   19 EVSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   99 VQTAASLFRDMCYRYREE-LMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLK 177
Cdd:PTZ00488 115 VAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQD 193

                        170       180
                 ....*....|....*....|....*....
gi 18859271  178 FTAGALTLPMERDGSSGGVVRLAVISEQG 206
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-210 1.56e-127

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: 357.69  E-value: 1.56e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAGAL 183
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*..
gi 18859271 184 TLPMERDGSSGGVVRLAVISEQGVERQ 210
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERK 187
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 24-209 7.89e-72

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: 216.54  E-value: 7.89e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREE-LMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAGA 182
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*..
gi 18859271 183 LTLPMERDGSSGGVVRLAVISEQGVER 209
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 24-202 1.65e-55

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: 174.99  E-value: 1.65e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREE---LMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTA 180
Cdd:cd01906  81 KLLANLLYEYTQSlrpLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 18859271 181 GALTLPMERDGSSGGVVRLAVI 202
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 20-202 4.49e-48

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: 156.19  E-value: 4.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    20 VSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVT-DKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    99 VQ----TAASLFRDMCYRYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEE 174
Cdd:pfam00227  81 VElaarIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 18859271   175 CLKFTAGALTLPMERDGSSGGVVRLAVI 202
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 19-209 2.64e-35

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 124.49  E-value: 2.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  19 EVSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:COG0638  31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  99 VQTAASLFRDMCYRYREE----LMAGIIVAGWDrRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEE 174
Cdd:COG0638 111 VEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18859271 175 CLKFTAGALTLPMERDGSSGGVVRLAVISEQGVER 209
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-208 5.06e-35

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: 122.69  E-value: 5.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREELMAGIIVAGWDrRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAGAL 183
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVD-YTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180
                ....*....|....*....|....*
gi 18859271 184 TLPMERDGSSGGVVRLAVISEQGVE 208
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDGVE 184
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 24-183 8.70e-35

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: 121.35  E-value: 8.70e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREE--LMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLKFTAG 181
Cdd:cd01901  81 KELAKLLQVYTQGrpFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ..
gi 18859271 182 AL 183
Cdd:cd01901 161 AL 162
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-209 9.29e-32

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: 114.26  E-value: 9.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYR-EELMAGIIVAGWDrRRGGQVYTVPVGGM-LTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLKFTAG 181
Cdd:cd03761  81 KLLSNMLYQYKgMGLSMGTMICGWD-KTGPGLYYVDSDGTrLKGDLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                       170       180
                ....*....|....*....|....*...
gi 18859271 182 ALTLPMERDGSSGGVVRLAVISEQGVER 209
Cdd:cd03761 159 AIYHATHRDAYSGGNVNLYHVREDGWRK 186
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 23-207 9.29e-30

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: 109.22  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    23 GTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTA 102
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   103 ASLFRDMCYRYR-EELMAGIIVAGWDrRRGGQVYTV-PVGGMLTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLKFTA 180
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVD-EEGPHLYSLdPAGGIIEDDYTAT-GSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 18859271   181 GALTLPMERDGSSGGVVRLAVISEQGV 207
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 24-209 8.92e-29

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: 106.57  E-value: 8.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAA 103
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 104 SLFRDMCYRYREE-LMAGIIVAGWDrRRGGQVYTV-PVGGMLTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLKFTAG 181
Cdd:cd03764  81 TLLSNILNSSKYFpYIVQLLIGGVD-EEGPHLYSLdPLGSIIEDKYTAT-GSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                       170       180
                ....*....|....*....|....*...
gi 18859271 182 ALTLPMERDGSSGGVVRLAVISEQGVER 209
Cdd:cd03764 159 AIKSAIERDSASGDGIDVVVITKDGYKE 186
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 19-206 1.31e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 100.06  E-value: 1.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   19 EVSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPL 98
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   99 VQTAASLFRDMCYRYREE-LMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVgGSGSSYIYGYVDSNYRSGMSKEECLK 177
Cdd:PTZ00488 115 VAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQD 193

                        170       180
                 ....*....|....*....|....*....
gi 18859271  178 FTAGALTLPMERDGSSGGVVRLAVISEQG 206
Cdd:PTZ00488 194 LGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-212 7.02e-11

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: 59.58  E-value: 7.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  20 VSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLV 99
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 100 QTAASLFRDMCYRYRE-ELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDS---------NYRSG 169
Cdd:cd03757  85 EAIAQLLSTILYSRRFfPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvgrknqnnVERTP 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18859271 170 MSKEECLKFTAGALTLPMERDGSSGGVVRLAVISEQGVERQAI 212
Cdd:cd03757 165 LSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 23-209 5.98e-10

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


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 57.02  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    23 GTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAAdtQAIADAVTYQLGF-HSIELDEAPL--- 98
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG--LAIELVRLFQVELeHYEKIEGVPLtld 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271    99 --VQTAASLFRDMCYRYREELMAGIIVAGWDRRRG-GQVYTV-PVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEE 174
Cdd:TIGR03690  80 gkANRLAAMVRGNLPAAMQGLAVVPLLAGYDLDAGaGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 18859271   175 CLKFTAGALTLPMERDGSSGG--VVR-----LAVISEQGVER 209
Cdd:TIGR03690 160 ALRVAVEALYDAADDDSATGGpdLVRgiyptVVVITADGARR 201
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 18-204 7.98e-09

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: 53.87  E-value: 7.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  18 RE-VSTGTTIMAVEFDGGVVMGADSRTTTGAYIANRVtDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEA 96
Cdd:cd03756  22 REaVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESI-EKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  97 PLVQTAASLFRDMCYRYRE-----ELMAGIIVAGWDRRrGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMS 171
Cdd:cd03756 101 IDVEVLVKKICDLKQQYTQhggvrPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMS 179

                       170       180       190
                ....*....|....*....|....*....|...
gi 18859271 172 KEECLKFTAGALTLPMErDGSSGGVVRLAVISE 204
Cdd:cd03756 180 LEEAIELALKALYAALE-ENETPENVEIAYVTV 211
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-194 4.34e-08

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: 51.47  E-value: 4.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  21 STGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQ 100
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 101 TAASLFRDMCYRYRE-ELMAGIIVAGWDRRrgGQVYTVP---VGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECL 176
Cdd:cd03759  81 TFSSLISSLLYEKRFgPYFVEPVVAGLDPD--GKPFICTmdlIGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELF 158

                       170
                ....*....|....*...
gi 18859271 177 KFTAGALTLPMERDGSSG 194
Cdd:cd03759 159 ETISQALLSAVDRDALSG 176
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-177 3.13e-07

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: 49.12  E-value: 3.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  35 VVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTAASLFRDM---CY 111
Cdd:cd03758  13 VILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAANFTRRElaeSL 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859271 112 RYREELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSKEECLK 177
Cdd:cd03758  93 RSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALE 158
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
18-203 9.30e-06

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 45.21  E-value: 9.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   18 RE-VSTGTTIMAVEFDGGVVMGADSRTTTgAYIANRVTDKLTPIHDRIFCCRSGSAADTQAIAD-----AVTYQLGFhsi 91
Cdd:PRK03996  30 REaVKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDrarveAQINRLTY--- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271   92 elDEAPLVQTAASLFRDMCYRYREelMAG-------IIVAGWDrRRGGQVY-TVPVGGMLTRQPVSVgGSGSSYIYGYVD 163
Cdd:PRK03996 106 --GEPIGVETLTKKICDHKQQYTQ--HGGvrpfgvaLLIAGVD-DGGPRLFeTDPSGAYLEYKATAI-GAGRDTVMEFLE 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18859271  164 SNYRSGMSKEECLKFTAGALTLPMERDGSSGGvVRLAVIS 203
Cdd:PRK03996 180 KNYKEDLSLEEAIELALKALAKANEGKLDPEN-VEIAYID 218
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 23-202 4.45e-05

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: 43.09  E-value: 4.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  23 GTTIMAVEFDGGVVMGADSRTTTGAYIANRVtDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDEAPLVQTA 102
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271 103 ASLFRDMCYRY-----REELMA-----GIIVAGWDrRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGMSK 172
Cdd:cd03753 106 TQAVSDLALQFgegddGKKAMSrpfgvALLIAGVD-ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184

                       170       180       190
                ....*....|....*....|....*....|
gi 18859271 173 EECLKFTAGALTLPMERDGSSGGvVRLAVI 202
Cdd:cd03753 185 EEAEKLALSILKQVMEEKLNSTN-VELATV 213
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 22-78 1.19e-04

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 41.40  E-value: 1.19e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859271  22 TGTTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPIHDRIFCCRSGSAADTQAI 78
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYL 57
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 17-202 1.99e-03

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: 38.11  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  17 QREVSTGTTIMAVEFDGGVVMGADSRTTtgAYIAN-RVTDKLTPIHDRIFCCRSGSAADTQAIADAVTYQLGFHSIELDE 95
Cdd:cd03755  21 QEAVRKGTTAVGVRGKDCVVLGVEKKSV--AKLQDpRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVED 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859271  96 APLVQTAASLFRDMCYRY-----REELMAGIIVAGWDRRRGGQVYTVPVGGMLTRQPVSVGGSGSSYIYGYVDSNYRSGM 170
Cdd:cd03755  99 PVTVEYITRYIAGLQQRYtqsggVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEM 178

                       170       180       190
                ....*....|....*....|....*....|..
gi 18859271 171 SKEECLKFTAGALtlpMERDGSSGGVVRLAVI 202
Cdd:cd03755 179 TRDDTIKLAIKAL---LEVVQSGSKNIELAVM 207
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 24-74 6.97e-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: 6.97e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859271  24 TTIMAVEFDGGVVMGADSRTTTGAYIANRVTDKLTPI-HDRIFCCRSGSAAD 74
Cdd:cd01913   1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLyNGKVIAGFAGSTAD 52
 
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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