NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2030424403|ref|NP_001381580|]
View 

proteasome subunit beta type-11 [Rattus norvegicus]

Protein Classification

proteasome subunit beta( domain architecture ID 10132926)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-237 5.96e-104

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: 301.09  E-value: 5.96e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCAV 209
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 2030424403 210 AHATHRDAYSGGSVDLFHVRESGWEYIS 237
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-237 5.96e-104

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: 301.09  E-value: 5.96e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCAV 209
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 2030424403 210 AHATHRDAYSGGSVDLFHVRESGWEYIS 237
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
30-245 7.71e-75

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 229.49  E-value: 7.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  30 PRGCDPQTFLQIY------GPR---LAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSAD 100
Cdd:PTZ00488   11 PPGAHPGDFLAEYtfdhgdANKaieFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAAD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 101 CATWYRVLRRELRLRELREGQLPSVAGTAKLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSG 180
Cdd:PTZ00488   91 CSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSG 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030424403 181 SPYAYGVLDRSYHYDMTVQEAYTLARCAVAHATHRDAYSGGSVDLFHVRESGWEYISRSDACVLY 245
Cdd:PTZ00488  171 STYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLH 235
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
48-228 7.59e-42

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: 142.71  E-value: 7.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPAS-RKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVA 126
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 127 GT---AKLLSAMMSRYRGLDLCVATALCGWDHSG-PALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAY 202
Cdd:pfam00227  83 LAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162
                         170       180
                  ....*....|....*....|....*.
gi 2030424403 203 TLARCAVAHATHRDAYSGGSVDLFHV 228
Cdd:pfam00227 163 ELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
49-232 6.41e-36

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: 127.33  E-value: 6.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 129 AKLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCA 208
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 2030424403 209 VAHATHRDAYSGGSVDLFHVRESG 232
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
48-240 5.72e-33

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 121.02  E-value: 5.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAG 127
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 128 TAKLLSAMM-----SRYRGLdlCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAY 202
Cdd:COG0638   114 LAKLLSDLLqgytqYGVRPF--GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2030424403 203 TLARCAVAHATHRDAYSGGSVDLFHVRESGWEYISRSD 240
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-237 5.96e-104

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: 301.09  E-value: 5.96e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCAV 209
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 2030424403 210 AHATHRDAYSGGSVDLFHVRESGWEYIS 237
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
30-245 7.71e-75

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 229.49  E-value: 7.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  30 PRGCDPQTFLQIY------GPR---LAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSAD 100
Cdd:PTZ00488   11 PPGAHPGDFLAEYtfdhgdANKaieFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAAD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 101 CATWYRVLRRELRLRELREGQLPSVAGTAKLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSG 180
Cdd:PTZ00488   91 CSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSG 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030424403 181 SPYAYGVLDRSYHYDMTVQEAYTLARCAVAHATHRDAYSGGSVDLFHVRESGWEYISRSDACVLY 245
Cdd:PTZ00488  171 STYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLH 235
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
50-236 2.76e-67

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: 208.07  E-value: 2.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGLDLCVATALCGWD-HSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCA 208
Cdd:cd01912    81 NLLSNILYSYRGFPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160
                         170       180
                  ....*....|....*....|....*...
gi 2030424403 209 VAHATHRDAYSGGSVDLFHVRESGWEYI 236
Cdd:cd01912   161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
50-228 1.25e-48

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: 159.97  E-value: 1.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGL--DLCVATALCGWD-HSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLAR 206
Cdd:cd01906    81 KLLANLLYEYTQSlrPLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160
                         170       180
                  ....*....|....*....|..
gi 2030424403 207 CAVAHATHRDAYSGGSVDLFHV 228
Cdd:cd01906   161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
48-228 7.59e-42

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: 142.71  E-value: 7.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPAS-RKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVA 126
Cdd:pfam00227   3 TGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 127 GT---AKLLSAMMSRYRGLDLCVATALCGWDHSG-PALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAY 202
Cdd:pfam00227  83 LAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAV 162
                         170       180
                  ....*....|....*....|....*.
gi 2030424403 203 TLARCAVAHATHRDAYSGGSVDLFHV 228
Cdd:pfam00227 163 ELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
49-232 6.41e-36

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: 127.33  E-value: 6.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 129 AKLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCA 208
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 2030424403 209 VAHATHRDAYSGGSVDLFHVRESG 232
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-234 2.45e-33

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: 120.82  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCAV 209
Cdd:cd03764    81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160
                         170       180
                  ....*....|....*....|....*
gi 2030424403 210 AHATHRDAYSGGSVDLFHVRESGWE 234
Cdd:cd03764   161 KSAIERDSASGDGIDVVVITKDGYK 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
48-240 5.72e-33

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 121.02  E-value: 5.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  48 HGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAG 127
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 128 TAKLLSAMM-----SRYRGLdlCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAY 202
Cdd:COG0638   114 LAKLLSDLLqgytqYGVRPF--GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2030424403 203 TLARCAVAHATHRDAYSGGSVDLFHVRESGWEYISRSD 240
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
50-211 5.44e-32

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: 116.34  E-value: 5.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGL-DLCVATALCGWDHSGPALFYVYSDGTCLQGDVF-SVGSGSPYAYGVLDRSYHYDMTVQEAYTLARC 207
Cdd:cd01901    81 KELAKLLQVYTQGrPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160

                  ....
gi 2030424403 208 AVAH 211
Cdd:cd01901   161 ALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-232 1.64e-27

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: 105.38  E-value: 1.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRglDLCVATALC-GWD-HSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARC 207
Cdd:cd03762    81 SLFKNLCYNYK--EMLSAGIIVaGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
                         170       180
                  ....*....|....*....|....*
gi 2030424403 208 AVAHATHRDAYSGGSVDLFHVRESG 232
Cdd:cd03762   159 ALSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
50-236 5.19e-20

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: 85.33  E-value: 5.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  50 TTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTA 129
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 130 KLLSAMMSRYRGlDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQEAYTLARCAV 209
Cdd:cd03763    81 TMLKQHLFRYQG-HIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159
                         170       180
                  ....*....|....*....|....*..
gi 2030424403 210 AHATHRDAYSGGSVDLFHVRESGWEYI 236
Cdd:cd03763   160 EAGIFNDLGSGSNVDLCVITKDGVEYL 186
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
49-205 4.49e-12

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: 64.28  E-value: 4.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSScgSYVACPAS-RKVIPVHRHLLGTTSGTSADCATWY---RVLRRELRLRELREGQLPS 124
Cdd:cd03753    27 GSTAIGIKTKEGVVLAVEKRIT--SPLMEPSSvEKIMEIDDHIGCAMSGLIADARTLIdhaRVEAQNHRFTYNEPMTVES 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 125 VA----------GTAKLLSAMMSRYRGLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHY 194
Cdd:cd03753   105 VTqavsdlalqfGEGDDGKKAMSRPFGVALLIA----GVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180
                         170
                  ....*....|.
gi 2030424403 195 DMTVQEAYTLA 205
Cdd:cd03753   181 DMTLEEAEKLA 191
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
51-204 2.00e-08

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: 53.36  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  51 TTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATW----------YRVLRrelrlrelreG 120
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFaeyiqkniqlYKMRN----------G 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 121 QLPSVAGTAKLLSAMMSRY--RGLDLCVATALCGWD-HSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMT 197
Cdd:cd03758    73 YELSPKAAANFTRRELAESlrSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMT 152

                  ....*..
gi 2030424403 198 VQEAYTL 204
Cdd:cd03758   153 VEEALEL 159
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
49-240 3.16e-08

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: 53.03  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGT 128
Cdd:cd03757     8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 129 AKLLSAMMSRYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDVFS-VGSGSPYAYGVLD---------RSYHYDMTV 198
Cdd:cd03757    88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSaGGSASSLIQPLLDnqvgrknqnNVERTPLSL 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2030424403 199 QEAYTLARCAVAHATHRDAYSGGSVDLFHVRESG--WEYIS-RSD 240
Cdd:cd03757   168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGieEETFPlRKD 212
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
49-225 1.14e-05

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


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 45.40  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSscGSYVACPAS-RKVIPVHRHLLGTTSGTSADC----------ATWYRVLRrelrlrel 117
Cdd:cd03756    28 GTTALGIKCKEGVVLAVDKRI--TSKLVEPESiEKIYKIDDHVGAATSGLVADArvlidrarveAQIHRLTY-------- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 118 reGQLPSVAGTAKLLSAMMSRYR--------GLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLD 189
Cdd:cd03756    98 --GEPIDVEVLVKKICDLKQQYTqhggvrpfGVALLIA----GVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLE 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2030424403 190 RSYHYDMTVQEAYTLARCAVAHAThRDAYSGGSVDL 225
Cdd:cd03756   172 KEYKEDMSLEEAIELALKALYAAL-EENETPENVEI 206
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
49-220 1.06e-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: 42.17  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHRHLLGTTSGTSADCATWYRV-LRRELRLRELREGQLPSVAG 127
Cdd:cd03760     2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLlDQLVIDDECLDDGHSLSPKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 128 TAKLLSAMM--SRYRGLDLCVATALCGWDHSG-PALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHY--DMTVQEAY 202
Cdd:cd03760    82 IHSYLTRVLynRRSKMNPLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEEEAR 161
                         170
                  ....*....|....*...
gi 2030424403 203 TLARCAVAHATHRDAYSG 220
Cdd:cd03760   162 ALIEECMKVLYYRDARSI 179
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
48-205 7.82e-04

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: 39.73  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  48 HGTTTLAFRFRHGVIAAADTRSScgSYVACPAS-RKVIPVHRHLLGTTSGTSAD-----------CATWYRVLrrelrlr 115
Cdd:cd01911    26 NGSTAVGIKGKDGVVLAVEKKVT--SKLLDPSSvEKIFKIDDHIGCAVAGLTADarvlvnrarveAQNYRYTY------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 116 elreGQLPSVAGTAKLLSAMMSRY------RglDLCVATALCGWD-HSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVL 188
Cdd:cd01911    97 ----GEPIPVEVLVKRIADLAQVYtqyggvR--PFGVSLLIAGYDeEGGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFL 170
                         170
                  ....*....|....*..
gi 2030424403 189 DRSYHYDMTVQEAYTLA 205
Cdd:cd01911   171 EKRYKKDLTLEEAIKLA 187
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
49-213 9.76e-04

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 39.82  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRsscgsyvacPASRKVIP-----VHR---HLLGTTSGTSADC----------ATWYRVLRr 110
Cdd:PRK03996   36 GTTAVGVKTKDGVVLAVDKR---------ITSPLIEPssiekIFKiddHIGAASAGLVADArvlidrarveAQINRLTY- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 111 elrlrelreGQLPSVAGTAKLLSAMMSRY------R--GLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDVFSVGSGSP 182
Cdd:PRK03996  106 ---------GEPIGVETLTKKICDHKQQYtqhggvRpfGVALLIA----GVDDGGPRLFETDPSGAYLEYKATAIGAGRD 172
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2030424403 183 YAYGVLDRSYHYDMTVQEAYTLARCAVAHAT 213
Cdd:PRK03996  173 TVMEFLEKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
49-201 5.88e-03

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 37.30  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403  49 GTTTLAFRFRHGVIAAADTRSScgSYVACPAS-RKVIPVHRHLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAG 127
Cdd:cd03750    27 GAPSVGIKAANGVVLATEKKVP--SPLIDESSvHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030424403 128 TAKLLSAMMSRYR--------GLDLCVAtalcGWDHSGPALFYVYSDGTCLQGDVFSVGSGSPYAYGVLDRSYHYDMTVQ 199
Cdd:cd03750   105 LVREIASVMQEYTqsggvrpfGVSLLIA----GWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELE 180

                  ..
gi 2030424403 200 EA 201
Cdd:cd03750   181 DA 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH