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Conserved domains on  [gi|24584895|ref|NP_724081|]
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proteasome beta5 subunit-related 2, isoform A [Drosophila melanogaster]

Protein Classification

proteasome subunit beta( domain architecture ID 10132926)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-259 6.74e-118

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: 335.75  E-value: 6.74e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLAV 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 24584895 232 YHATMTDIFSGGVVRLYHMDQGNWRNVA 259
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 ...
 72-259 6.74e-118

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: 335.75  E-value: 6.74e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLAV 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 24584895 232 YHATMTDIFSGGVVRLYHMDQGNWRNVA 259
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 46-279 7.53e-97

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 284.57  E-value: 7.53e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   46 PPYENPRESVKKL---NALSEVQIDFDHGTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAAD 122
Cdd:PTZ00488  11 PPGAHPGDFLAEYtfdHGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAAD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  123 CTYWDRALTRECRLHELRYKERLPVQSAAKYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSG 202
Cdd:PTZ00488  91 CSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSG 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584895  203 APNALGILDSDYRLDLSDNEAYDLAFLAVYHATMTDIFSGGVVRLYHMDQGNWRNVANKDCQELHEQYSGVGNQQTP 279
Cdd:PTZ00488 171 STYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKEINKA 247
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-250 9.22e-46

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: 152.34  E-value: 9.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895    69 DHGTTTVGFVYQGGIILCVDSRATSG-KLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPV 147
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   148 QSAAKYISNVAAE--YKGMGLC-MGMMLAGWSPEG-PSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEA 223
Cdd:pfam00227  82 ELAARIADLLQAYtqYSGRRPFgVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 24584895   224 YDLAFLAVYHATMTDIFSGGVVRLYHM 250
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 70-242 1.94e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 144.90  E-value: 1.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  70 HGTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdRALTR----ECRLHELRYKERL 145
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADA----RELVRlarvEAQLYELRYGEPI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 146 PVQSAAKYISNVAAEYKGMGLcMG----MMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDN 221
Cdd:COG0638 110 SVEGLAKLLSDLLQGYTQYGV-RPfgvaLLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLD 188

                       170       180
                ....*....|....*....|.
gi 24584895 222 EAYDLAFLAVYHATMTDIFSG 242
Cdd:COG0638 189 EAVELALRALYSAAERDSASG 209
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 71-251 9.51e-37

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: 128.87  E-value: 9.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895    71 GTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSA 150
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   151 AKYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLA 230
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|.
gi 24584895   231 VYHATMTDIFSGGVVRLYHMD 251
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVIT 181
 
Name Accession Description Interval E-value
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-259 6.74e-118

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: 335.75  E-value: 6.74e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLAV 231
Cdd:cd03761  81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|....*...
gi 24584895 232 YHATMTDIFSGGVVRLYHMDQGNWRNVA 259
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDGWRKIS 188
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 46-279 7.53e-97

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 284.57  E-value: 7.53e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   46 PPYENPRESVKKL---NALSEVQIDFDHGTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAAD 122
Cdd:PTZ00488  11 PPGAHPGDFLAEYtfdHGDANKAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAAD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  123 CTYWDRALTRECRLHELRYKERLPVQSAAKYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSG 202
Cdd:PTZ00488  91 CSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSG 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584895  203 APNALGILDSDYRLDLSDNEAYDLAFLAVYHATMTDIFSGGVVRLYHMDQGNWRNVANKDCQELHEQYSGVGNQQTP 279
Cdd:PTZ00488 171 STYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKKISADDCFDLHQKYAAEKEINKA 247
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 72-256 9.38e-65

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: 200.75  E-value: 9.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCMGMMLAGW-SPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLA 230
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVdKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*.
gi 24584895 231 VYHATMTDIFSGGVVRLYHMDQGNWR 256
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVE 186
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 72-250 2.16e-53

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: 171.52  E-value: 2.16e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYK--GMGLCMGMMLAGW-SPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAF 228
Cdd:cd01906  81 KLLANLLYEYTqsLRPLGVSLLVAGVdEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 24584895 229 LAVYHATMTDIFSGGVVRLYHM 250
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 69-250 9.22e-46

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: 152.34  E-value: 9.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895    69 DHGTTTVGFVYQGGIILCVDSRATSG-KLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPV 147
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   148 QSAAKYISNVAAE--YKGMGLC-MGMMLAGWSPEG-PSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEA 223
Cdd:pfam00227  82 ELAARIADLLQAYtqYSGRRPFgVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 24584895   224 YDLAFLAVYHATMTDIFSGGVVRLYHM 250
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 70-242 1.94e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 144.90  E-value: 1.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  70 HGTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdRALTR----ECRLHELRYKERL 145
Cdd:COG0638  34 RGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADA----RELVRlarvEAQLYELRYGEPI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 146 PVQSAAKYISNVAAEYKGMGLcMG----MMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDN 221
Cdd:COG0638 110 SVEGLAKLLSDLLQGYTQYGV-RPfgvaLLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLD 188

                       170       180
                ....*....|....*....|.
gi 24584895 222 EAYDLAFLAVYHATMTDIFSG 242
Cdd:COG0638 189 EAVELALRALYSAAERDSASG 209
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 72-233 2.42e-38

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 132.52  E-value: 2.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMG-LCMGMMLAGWSPEGPSLVYVDSNGLRIHG-KLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFL 229
Cdd:cd01901  81 KELAKLLQVYTQGRpFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
gi 24584895 230 AVYH 233
Cdd:cd01901 161 ALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 71-251 9.51e-37

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: 128.87  E-value: 9.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895    71 GTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSA 150
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   151 AKYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLA 230
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|.
gi 24584895   231 VYHATMTDIFSGGVVRLYHMD 251
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVIT 181
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-247 1.72e-36

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: 128.14  E-value: 1.72e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLAV 231
Cdd:cd03764  81 TLLSNILNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAI 160

                       170
                ....*....|....*.
gi 24584895 232 YHATMTDIFSGGVVRL 247
Cdd:cd03764 161 KSAIERDSASGDGIDV 176
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-247 1.43e-23

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: 94.60  E-value: 1.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCmGMMLAGWSP-EGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLA 230
Cdd:cd03762  81 SLFKNLCYNYKEMLSA-GIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNA 159

                       170
                ....*....|....*..
gi 24584895 231 VYHATMTDIFSGGVVRL 247
Cdd:cd03762 160 LSLAMSRDGSSGGVIRL 176
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 72-248 6.70e-22

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: 89.95  E-value: 6.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  72 TTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAA 151
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 152 KYISNVAAEYKGMGLCmGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAYDLAFLAV 231
Cdd:cd03763  81 TMLKQHLFRYQGHIGA-ALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170
                ....*....|....*..
gi 24584895 232 YHATMTDIFSGGVVRLY 248
Cdd:cd03763 160 EAGIFNDLGSGSNVDLC 176
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 49-235 1.98e-21

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: 89.31  E-value: 1.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  49 ENPRESVKKlnalsevqidfdhGTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdR 128
Cdd:cd03756  19 EYAREAVKR-------------GTTALGIKCKEGVVLAVDKRITS-KLVEPESIEKIYKIDDHVGAATSGLVADA----R 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 129 ALTRECRL----HELRYKERLPVQSAAKYISNVAAEYKGMG----LCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVG 200
Cdd:cd03756  81 VLIDRARVeaqiHRLTYGEPIDVEVLVKKICDLKQQYTQHGgvrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIG 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24584895 201 SGAPNALGILDSDYRLDLSDNEAYDLAFLAVYHAT 235
Cdd:cd03756 161 SGRQAVTEFLEKEYKEDMSLEEAIELALKALYAAL 195
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
52-235 1.36e-20

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 87.97  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   52 RESVKKlnalsevqidfdhGTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdRALT 131
Cdd:PRK03996  30 REAVKR-------------GTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADA----RVLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  132 ----RECRLHELRYKERLPVQSAAKYISNVAAEYKGMGlcmG-------MMLAGWSPEGPSLVYVDSNGLRIHGKLFAVG 200
Cdd:PRK03996  92 drarVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHG---GvrpfgvaLLIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24584895  201 SGAPNALGILDSDYRLDLSDNEAYDLAFLAVYHAT 235
Cdd:PRK03996 169 AGRDTVMEFLEKNYKEDLSLEEAIELALKALAKAN 203
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-227 1.65e-19

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 84.31  E-value: 1.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  71 GTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADC-TYWDRALTrECRLHELRYKERLPVQS 149
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITS-PLMEPSSVEKIMEIDDHIGCAMSGLIADArTLIDHARV-EAQNHRFTYNEPMTVES 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 150 AAKYISNVAAEY-------KGMGLCMG--MMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSD 220
Cdd:cd03753 105 VTQAVSDLALQFgegddgkKAMSRPFGvaLLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184


                ....*..
gi 24584895 221 NEAYDLA 227
Cdd:cd03753 185 EEAEKLA 191
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 69-234 3.52e-19

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: 83.26  E-value: 3.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  69 DHGTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdRALTRECRL----HELRYKER 144
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRARVeaqnYRYTYGEP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 145 LPVQSAAKYISNVAAEY--KGMGLCMG--MMLAGWSPE-GPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLS 219
Cdd:cd01911 100 IPVEVLVKRIADLAQVYtqYGGVRPFGvsLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKDLT 179

                       170
                ....*....|....*
gi 24584895 220 DNEAYDLAFLAVYHA 234
Cdd:cd01911 180 LEEAIKLALKALKEV 194
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 64-230 2.08e-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: 2.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  64 VQIDF-----DHGTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHE 138
Cdd:cd03750  15 VQIEYalaavSSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYY 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 139 LRYKERLPVQSAAKYISNVAAEYKGMG----LCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDY 214
Cdd:cd03750  94 LVYGEPIPVSQLVREIASVMQEYTQSGgvrpFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRY 173

                       170
                ....*....|....*.
gi 24584895 215 RLDLSDNEAYDLAFLA 230
Cdd:cd03750 174 NEDLELEDAIHTAILT 189
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 73-226 7.55e-10

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: 57.21  E-value: 7.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  73 TTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSAAK 152
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 153 YISNVAAEY--KGMGLCMGMMLAGW-SPEGPSLVYVD--SNGLRIHgklFAV-GSGAPNALGILDSDYRLDLSDNEAYDL 226
Cdd:cd03758  83 FTRRELAESlrSRTPYQVNLLLAGYdKVEGPSLYYIDylGTLVKVP---YAAhGYGAYFCLSILDRYYKPDMTVEEALEL 159
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-227 1.08e-09

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 56.99  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  71 GTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADC-TYWDRALTrECRLHELRYKERLPVQS 149
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADArVLINRARL-ECQSHRLTVEDPVTVEY 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 150 AAKYISNVAAEYKGMG----LCMGMMLAGWSPEG-PSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEAY 224
Cdd:cd03755 105 ITRYIAGLQQRYTQSGgvrpFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTI 184


                ...
gi 24584895 225 DLA 227
Cdd:cd03755 185 KLA 187
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 70-236 1.43e-08

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 53.89  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  70 HGTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTywdrALTRECRLHELR----YKERL 145
Cdd:cd03752  28 HAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDAN----ILINYARLIAQRylysYQEPI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 146 PVQSAAKYISNVAAEYKGMG----LCMGMMLAGWSP-EGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSD 220
Cdd:cd03752 104 PVEQLVQRLCDIKQGYTQYGglrpFGVSFLYAGWDKhYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTL 183

                       170
                ....*....|....*.
gi 24584895 221 NEAYDLAfLAVYHATM 236
Cdd:cd03752 184 EEALALA-VKVLSKTM 198
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 71-226 7.04e-06

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: 45.64  E-value: 7.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  71 GTTTVGFVYQGGIILCVDSRATSGKLIGSQSIHKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLhELRYKERLPVQSA 150
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVID-DECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 151 A--KYISNV--AAEYKGMGLCMGMMLAGWSPEG-PSLVYVDSNGLRIHGKLFAVGSGAPNALGIL--DSDYRLDLSDNEA 223
Cdd:cd03760  81 EihSYLTRVlyNRRSKMNPLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLreAWEKKPDLTEEEA 160


                ...
gi 24584895 224 YDL 226
Cdd:cd03760 161 RAL 163
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 74-271 1.05e-05

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 45.61  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895   74 TVGFVYQGGIILCVDsRATSGKLIG-SQSIHKVVQVNQYIMGTTAGGAADCTywdrALTRECRLHELRYK----ERLPVQ 148
Cdd:PTZ00246  34 TVGILCKEGVILGAD-KPISSKLLDpGKINEKIYKIDSHIFCAVAGLTADAN----ILINQCRLYAQRYRytygEPQPVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  149 SAAKYISNVAAEYKGMG----LCMGMMLAGW-SPEGPSLVYVDSNGLRIHGKLFAVGSGAPNALGILDSDYRLDLSDNEA 223
Cdd:PTZ00246 109 QLVVQICDLKQSYTQFGglrpFGVSFLFAGYdENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQG 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24584895  224 YDLAFLAVYHATMTDIFSGGVVRLYHMDQGNWRN------VANKDCQELHEQYS 271
Cdd:PTZ00246 189 LLLAAKVLTKSMDSTSPKADKIEVGILSHGETDGepiqkmLSEKEIAELLKKVT 242
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 65-206 7.62e-04

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: 39.96  E-value: 7.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  65 QIDF-----DHGTTTVGFVYQGGIILCVDSRATSgKLIGSQSIHKVVQVNQYIMGTTAGGAADctywDRALTR----ECR 135
Cdd:cd03751  19 QVEYankavENSGTAIGIRCKDGVVLAVEKLVTS-KLYEPGSNKRIFNVDRHIGIAVAGLLAD----GRHLVSrareEAE 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 136 LHELRYKERLPVqsaaKYISNVAAEYkgMGLC----------MGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPN 205
Cdd:cd03751  94 NYRDNYGTPIPV----KVLADRVAMY--MHAYtlyssvrpfgCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQA 167


                .
gi 24584895 206 A 206
Cdd:cd03751 168 A 168
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 71-206 3.61e-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: 37.66  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  71 GTTTVGFVYQGGIILCVDSRATSgKLIGSQSihKVVQVNQYIMGTTAGGAADCTYWDRALTRECRLHELRYKERLPVQSA 150
Cdd:cd03749  27 GSATVGLKSKTHAVLVALKRATS-ELSSYQK--KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVSRL 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895 151 AKYISNVA----AEYKGMGLCMGMMLAGWSPEGPSLVYVDSNGLRIHGKLFAVGSGAPNA 206
Cdd:cd03749 104 VSKVAEKAqintQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSA 163
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 95-189 4.57e-03

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 37.60  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584895  95 KLIGSQSIHKVVQVNQYIMGTTAGGAADCtywdRALTRECRLH--ELRYKE--RLPVQSAAKYISNVA------AEYKGM 164
Cdd:cd03754  52 KLIDPSTVTHLFRITDEIGCVMTGMIADS----RSQVQRARYEaaEFKYKYgyEMPVDVLAKRIADINqvytqhAYMRPL 127

                        90       100
                ....*....|....*....|....*.
gi 24584895 165 GLCMgmMLAGWSPE-GPSLVYVDSNG 189
Cdd:cd03754 128 GVSM--ILIGIDEElGPQLYKCDPAG 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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