NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622934609|ref|XP_014991573|]
View 

proteasome subunit beta type-8 isoform X2 [Macaca mulatta]

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 ...
118-305 4.08e-138

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: 388.53  E-value: 4.08e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 1622934609 278 AHATHRDSYSGGVVNMYHMKEDGWVKVE 305
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 ...
118-305 4.08e-138

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: 388.53  E-value: 4.08e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 1622934609 278 AHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
82-316 7.94e-129

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 367.39  E-value: 7.94e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609  82 LPTPVSSRCPSLEPTEFFQSLGGD-GEGNVQIEMAHGTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLG 160
Cdd:PTZ00488    3 CGPEHFEHPPGAHPGDFLAEYTFDhGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 161 TMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSG 240
Cdd:PTZ00488   83 TMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934609 241 NMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQY 316
Cdd:PTZ00488  163 NMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
114-296 6.67e-61

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: 192.40  E-value: 6.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 114 MAHGTTTLAFKFQHGVIVAVDSRASAGSYIATLR-VNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRIS 192
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 193 VS----AASKLLSNMmcQYRGMG-LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSP 266
Cdd:pfam00227  81 VElaarIADLLQAYT--QYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 1622934609 267 EEAYDLGRRAIAHATHRDSYSGGVVNMYHM 296
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
117-300 1.07e-53

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: 173.93  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 117 GTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAA 196
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 197 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 276
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 1622934609 277 IAHATHRDSYSGGVVNMYHMKEDG 300
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
116-305 3.14e-48

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 161.08  E-value: 3.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 116 HGTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSA 195
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 196 ASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAY 270
Cdd:COG0638   114 LAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622934609 271 DLGRRAIAHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
118-305 4.08e-138

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: 388.53  E-value: 4.08e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 1622934609 278 AHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:cd03761   161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
82-316 7.94e-129

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 367.39  E-value: 7.94e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609  82 LPTPVSSRCPSLEPTEFFQSLGGD-GEGNVQIEMAHGTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLG 160
Cdd:PTZ00488    3 CGPEHFEHPPGAHPGDFLAEYTFDhGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 161 TMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSG 240
Cdd:PTZ00488   83 TMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622934609 241 NMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQY 316
Cdd:PTZ00488  163 NMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKY 238
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
118-305 2.52e-87

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: 259.68  E-value: 2.52e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 276
Cdd:cd01912    81 NLLSNILYSYRGFPYYVSLIVGGVDKGgGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160
                         170       180
                  ....*....|....*....|....*....
gi 1622934609 277 IAHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:cd01912   161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
118-296 1.42e-64

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: 201.57  E-value: 1.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYR--GMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGR 274
Cdd:cd01906    81 KLLANLLYEYTqsLRPLGVSLLVAGVDEEgGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160
                         170       180
                  ....*....|....*....|..
gi 1622934609 275 RAIAHATHRDSYSGGVVNMYHM 296
Cdd:cd01906   161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
114-296 6.67e-61

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: 192.40  E-value: 6.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 114 MAHGTTTLAFKFQHGVIVAVDSRASAGSYIATLR-VNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRIS 192
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 193 VS----AASKLLSNMmcQYRGMG-LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSP 266
Cdd:pfam00227  81 VElaarIADLLQAYT--QYSGRRpFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTL 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 1622934609 267 EEAYDLGRRAIAHATHRDSYSGGVVNMYHM 296
Cdd:pfam00227 159 EEAVELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
117-300 1.07e-53

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: 173.93  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 117 GTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAA 196
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 197 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 276
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|....
gi 1622934609 277 IAHATHRDSYSGGVVNMYHMKEDG 300
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
118-305 5.60e-52

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: 169.74  E-value: 5.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd03764    81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160
                         170       180
                  ....*....|....*....|....*...
gi 1622934609 278 AHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:cd03764   161 KSAIERDSASGDGIDVVVITKDGYKELE 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
116-305 3.14e-48

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 161.08  E-value: 3.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 116 HGTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSA 195
Cdd:COG0638    34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 196 ASKLLSNMMCQY-----RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAY 270
Cdd:COG0638   114 LAKLLSDLLQGYtqygvRPFGVAL--LIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622934609 271 DLGRRAIAHATHRDSYSGGVVNMYHMKEDGWVKVE 305
Cdd:COG0638   192 ELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
118-279 4.58e-44

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: 148.31  E-value: 4.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMG-LSMGSMICGWDKKGPGLYYVDEHGTRLSG-NMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRR 275
Cdd:cd01901    81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160

                  ....
gi 1622934609 276 AIAH 279
Cdd:cd01901   161 ALKS 164
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
118-300 3.01e-36

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: 128.88  E-value: 3.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMgLSMGSMICGWDK-KGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRA 276
Cdd:cd03762    81 SLFKNLCYNYKEM-LSAGIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNA 159
                         170       180
                  ....*....|....*....|....
gi 1622934609 277 IAHATHRDSYSGGVVNMYHMKEDG 300
Cdd:cd03762   160 LSLAMSRDGSSGGVIRLVIITKDG 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
118-300 7.17e-26

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: 101.50  E-value: 7.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 118 TTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAAS 197
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 198 KLLSNMMCQYRGMgLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd03763    81 TMLKQHLFRYQGH-IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159
                         170       180
                  ....*....|....*....|...
gi 1622934609 278 AHATHRDSYSGGVVNMYHMKEDG 300
Cdd:cd03763   160 EAGIFNDLGSGSNVDLCVITKDG 182
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
117-308 4.66e-19

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: 83.85  E-value: 4.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 117 GTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAA 196
Cdd:cd03757     8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 197 SKLLSNMMCQYRGMGLSMGSMICGWDKKGPG-LYYVDEHGTRLSGNMFSTGSGNTYAYGVMDS---------GYRPNLSP 266
Cdd:cd03757    88 AQLLSTILYSRRFFPYYVFNILAGIDEEGKGvVYSYDPVGSYERETYSAGGSASSLIQPLLDNqvgrknqnnVERTPLSL 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622934609 267 EEAYDLGRRAIAHATHRDSYSGGVVNMYHMKEDGwVKVESTD 308
Cdd:cd03757   168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG-IEEETFP 208
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
119-278 1.40e-16

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: 76.47  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 119 TTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAASK 198
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 199 LLSNMMCQY--RGMGLSMGSMICGWDKK-GPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRR 275
Cdd:cd03758    83 FTRRELAESlrSRTPYQVNLLLAGYDKVeGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162

                  ...
gi 1622934609 276 AIA 278
Cdd:cd03758   163 CIK 165
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
117-305 2.71e-16

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: 75.68  E-value: 2.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 117 GTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRL-YYLRNGDRISVSA 195
Cdd:cd03760     2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDdECLDDGHSLSPKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 196 ASKLLSNMMCQYRGMG--LSMGSMICGWDKKG-PGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYR--PNLSPEEAY 270
Cdd:cd03760    82 IHSYLTRVLYNRRSKMnpLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkPDLTEEEAR 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622934609 271 DLGRRAIAHATHRDSYSGGVVNMYHMKEDGwVKVE 305
Cdd:cd03760   162 ALIEECMKVLYYRDARSINKYQIAVVTKEG-VEIE 195
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
111-272 1.02e-13

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: 68.90  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 111 QIEMA-----HGTTTLAFKFQHGVIVAVDSRASAGSYIATlRVNKVIEINPYLLGTMSGCAADCqyweRLLAK----ECR 181
Cdd:cd03753    16 QVEYAieaikLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADA----RTLIDharvEAQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 182 LYYLRNGDRISVSAASKLLSNMMCQYRGMGLSMGSM---------ICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYA 252
Cdd:cd03753    91 NHRFTYNEPMTVESVTQAVSDLALQFGEGDDGKKAMsrpfgvallIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGA 170
                         170       180
                  ....*....|....*....|
gi 1622934609 253 YGVMDSGYRPNLSPEEAYDL 272
Cdd:cd03753   171 QSSLQEKYHKDMTLEEAEKL 190
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
107-277 5.49e-13

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: 66.70  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 107 EGNV-QIEMA-----HGTTTLAFKFQHGVIVAVDSRASAgSYIATLRVNKVIEINPYLLGTMSGCAADCqyweRLLAKEC 180
Cdd:cd01911    11 EGRLfQVEYAleavkNGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 181 RL----YYLRNGDRISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKK-GPGLYYVDEhgtrlSGNMF-----S 244
Cdd:cd01911    86 RVeaqnYRYTYGEPIPVEVLVKRIADLAQVYtqyggvRPFGVSL--LIAGYDEEgGPQLYQTDP-----SGTYFgykatA 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622934609 245 TGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAI 277
Cdd:cd01911   159 IGKGSQEAKTFLEKRYKKDLTLEEAIKLALKAL 191
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
117-288 1.06e-12

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: 65.73  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 117 GTTTLAFKFQHGVIVAVDSRASAGSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGDRISVSAA 196
Cdd:cd03759     3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 197 SKLLSNMMCQYRGMGLSMGSMICGWDKKG-PGLYYVDEHG-TRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGR 274
Cdd:cd03759    83 SSLISSLLYEKRFGPYFVEPVVAGLDPDGkPFICTMDLIGcPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFETIS 162
                         170
                  ....*....|....
gi 1622934609 275 RAIAHATHRDSYSG 288
Cdd:cd03759   163 QALLSAVDRDALSG 176
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
110-269 2.69e-11

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: 62.34  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 110 VQIEMA-----HGTTTLAFKFQHGVIVAVDSRASAgSYIATLRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYY 184
Cdd:cd03750    15 VQIEYAlaavsSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 185 LRNGDRISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDS 258
Cdd:cd03750    94 LVYGEPIPVSQLVREIASVMQEYtqsggvRPFGVSL--LIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEK 171
                         170
                  ....*....|.
gi 1622934609 259 GYRPNLSPEEA 269
Cdd:cd03750   172 RYNEDLELEDA 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
111-281 4.95e-11

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: 61.19  E-value: 4.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 111 QIEMA-----HGTTTLAFKFQHGVIVAVDSRAsAGSYIATLRVNKVIEINPYLLGTMSGCAADCQY---WERLLAKECRL 182
Cdd:cd03756    17 QVEYAreavkRGTTALGIKCKEGVVLAVDKRI-TSKLVEPESIEKIYKIDDHVGAATSGLVADARVlidRARVEAQIHRL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 183 YYlrnGDRISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVM 256
Cdd:cd03756    96 TY---GEPIDVEVLVKKICDLKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFL 170
                         170       180
                  ....*....|....*....|....*
gi 1622934609 257 DSGYRPNLSPEEAYDLGRRAIAHAT 281
Cdd:cd03756   171 EKEYKEDMSLEEAIELALKALYAAL 195
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
111-281 2.53e-09

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 56.77  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 111 QIEMA-----HGTTTLAFKFQHGVIVAVDSRASaGSYIATLRVNKVIEINPYLLGTMSGCAADCQY---WERLLAKECRL 182
Cdd:PRK03996   25 QVEYAreavkRGTTAVGVKTKDGVVLAVDKRIT-SPLIEPSSIEKIFKIDDHIGAASAGLVADARVlidRARVEAQINRL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 183 YYlrnGDRISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVM 256
Cdd:PRK03996  104 TY---GEPIGVETLTKKICDHKQQYtqhggvRPFGVAL--LIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFL 178
                         170       180
                  ....*....|....*....|....*
gi 1622934609 257 DSGYRPNLSPEEAYDLGRRAIAHAT 281
Cdd:PRK03996  179 EKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
111-277 2.99e-03

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 38.43  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 111 QIEMA-----HGTTTLAFKFQ-HGVIVAVDSRASA-GSYiatlrVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLY 183
Cdd:cd03749    16 QVEYAmeavkQGSATVGLKSKtHAVLVALKRATSElSSY-----QKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 184 -YLRNGD----RISVSAASKLLSNMmcQ---YRGMGLsmGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSG----NTY 251
Cdd:cd03749    91 rFVYDSPipvsRLVSKVAEKAQINT--QrygRRPYGV--GLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARsqsaRTY 166
                         170       180
                  ....*....|....*....|....*.
gi 1622934609 252 AYGVMDSgyRPNLSPEEAYDLGRRAI 277
Cdd:cd03749   167 LERHFEE--FEDCSLEELIKHALRAL 190
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
108-282 7.66e-03

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 37.26  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 108 GNV-QIEMA-----HGTTTLAFKFQHGVIVAVDSRASAGSYIAtlRVNKVI-EINPYLLGTMSGCAADcqywERLLAK-- 178
Cdd:cd03751    15 GRVfQVEYAnkaveNSGTAIGIRCKDGVVLAVEKLVTSKLYEP--GSNKRIfNVDRHIGIAVAGLLAD----GRHLVSra 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934609 179 --ECRLYYLRNGDRISVSAASKLLSNMMCQY------RGMGLSMgsMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNT 250
Cdd:cd03751    89 reEAENYRDNYGTPIPVKVLADRVAMYMHAYtlyssvRPFGCSV--LLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQ 166
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622934609 251 YAYGVMDSGYRPNLSPEEA-YDLGRraIAHATH 282
Cdd:cd03751   167 AAKTELEKLKFSELTCREAvKEAAK--IIYIVH 197
 
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