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Conserved domains on  [gi|15235889|ref|NP_194858|]
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N-terminal nucleophile aminohydrolases (Ntn hydrolases) superfamily protein [Arabidopsis thaliana]

Protein Classification

proteasome subunit beta( domain architecture ID 10132932)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-200 6.42e-121

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: 341.51  E-value: 6.42e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAV 172
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 15235889 173 SLAIARDGASGGVVRTVIINSEGVTRNF 200
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-200 6.42e-121

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: 341.51  E-value: 6.42e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAV 172
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 15235889 173 SLAIARDGASGGVVRTVIINSEGVTRNF 200
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 12-191 4.74e-60

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: 187.00  E-value: 4.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRAS-DKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKV 90
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    91 SANLIRM----LAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQ 166
Cdd:pfam00227  84 AARIADLlqayTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
gi 15235889   167 LVVKAVSLAIARDGASGGVVRTVII 191
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-198 5.17e-45

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.91  E-value: 5.17e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 ANLIRMLAYNNknmLQTG-------LIVGGWDKyEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEA 164
Cdd:COG0638 115 AKLLSDLLQGY---TQYGvrpfgvaLLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEA 190

                       170       180       190
                ....*....|....*....|....*....|....
gi 15235889 165 EQLVVKAVSLAIARDGASGGVVRTVIINSEGVTR 198
Cdd:COG0638 191 VELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 12-196 2.32e-39

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: 134.26  E-value: 2.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    92 ANLIRMLAYNNK---NMLQtgLIVGGWDKyEGGKIYGI-PLGGtVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQL 167
Cdd:TIGR03634  81 ATLLSNILNSNRffpFIVQ--LLVGGVDE-EGPHLYSLdPAGG-IIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKL 156

                         170       180
                  ....*....|....*....|....*....
gi 15235889   168 VVKAVSLAIARDGASGGVVRTVIINSEGV 196
Cdd:TIGR03634 157 AVRAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-195 8.04e-28

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 106.23  E-value: 8.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    4 NLDAPHSM----GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHT 79
Cdd:PTZ00488  27 HGDANKAIefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   80 IQHGQPATVKVSANLIRMLAYNNKNM-LQTGLIVGGWDKyEGGKIYGIPLGGT-VVEQPFAIgGSGSSYLYGFFDQAWKD 157
Cdd:PTZ00488 107 LRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDK-KGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15235889  158 NMTKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEG 195
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-200 6.42e-121

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: 341.51  E-value: 6.42e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAV 172
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 15235889 173 SLAIARDGASGGVVRTVIINSEGVTRNF 200
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-198 1.84e-75

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: 226.17  E-value: 1.84e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNM-LQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKA 171
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*..
gi 15235889 172 VSLAIARDGASGGVVRTVIINSEGVTR 198
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 13-191 4.83e-62

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: 191.94  E-value: 4.83e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNK---NMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVV 169
Cdd:cd01906  81 KLLANLLYEYTqslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 15235889 170 KAVSLAIARDGASGGVVRTVII 191
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 12-191 4.74e-60

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: 187.00  E-value: 4.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRAS-DKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKV 90
Cdd:pfam00227   4 GTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    91 SANLIRM----LAYNNKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQ 166
Cdd:pfam00227  84 AARIADLlqayTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVE 163

                         170       180
                  ....*....|....*....|....*
gi 15235889   167 LVVKAVSLAIARDGASGGVVRTVII 191
Cdd:pfam00227 164 LAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-198 5.17e-45

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.91  E-value: 5.17e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 ANLIRMLAYNNknmLQTG-------LIVGGWDKyEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEA 164
Cdd:COG0638 115 AKLLSDLLQGY---TQYGvrpfgvaLLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEA 190

                       170       180       190
                ....*....|....*....|....*....|....
gi 15235889 165 EQLVVKAVSLAIARDGASGGVVRTVIINSEGVTR 198
Cdd:COG0638 191 VELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 13-173 5.03e-41

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: 137.91  E-value: 5.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNM--LQTGLIVGGWDKyEGGKIYGIPLGGTVVEQPFAI-GGSGSSYLYGFFDQAWKDNMTKEEAEQLVV 169
Cdd:cd01901  81 KELAKLLQVYTQGrpFGVNLIVAGVDE-GGGNLYYIDPSGPVIENPGAVaTGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....
gi 15235889 170 KAVS 173
Cdd:cd01901 160 KALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-200 2.93e-40

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: 136.61  E-value: 2.93e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNM-LQTGLIVGGWDKyEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKA 171
Cdd:cd03764  81 TLLSNILNSSKYFpYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*....
gi 15235889 172 VSLAIARDGASGGVVRTVIINSEGVTRNF 200
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKELE 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 12-196 2.32e-39

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: 134.26  E-value: 2.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    92 ANLIRMLAYNNK---NMLQtgLIVGGWDKyEGGKIYGI-PLGGtVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQL 167
Cdd:TIGR03634  81 ATLLSNILNSNRffpFIVQ--LLVGGVDE-EGPHLYSLdPAGG-IIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKL 156

                         170       180
                  ....*....|....*....|....*....
gi 15235889   168 VVKAVSLAIARDGASGGVVRTVIINSEGV 196
Cdd:TIGR03634 157 AVRAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-200 1.02e-38

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: 132.71  E-value: 1.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSA 92
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  93 NLIRMLAYNNKNMLQTGLIVGGWDkYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAV 172
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVD-YTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180       190
                ....*....|....*....|....*....|
gi 15235889 173 SLAIARDGASGGVVRTVIINSEGVT--RNF 200
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDGVEylRNY 189
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-198 3.52e-30

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: 110.41  E-value: 3.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  13 TTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQ----VVSDYVRyfLHQhtIQHGQPATV 88
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQywerVLGRECR--LYE--LRNKERISV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  89 KVSANLIRMLAYNNKNM-LQTGLIVGGWDKyEGGKIYGIPLGGTVVE-QPFAIGgSGSSYLYGFFDQAWKDNMTKEEAEQ 166
Cdd:cd03761  77 AAASKLLSNMLYQYKGMgLSMGTMICGWDK-TGPGLYYVDSDGTRLKgDLFSVG-SGSTYAYGVLDSGYRYDLSVEEAYD 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 15235889 167 LVVKAVSLAIARDGASGGVVRTVIINSEGVTR 198
Cdd:cd03761 155 LARRAIYHATHRDAYSGGNVNLYHVREDGWRK 186
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 4-195 8.04e-28

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 106.23  E-value: 8.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    4 NLDAPHSM----GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHT 79
Cdd:PTZ00488  27 HGDANKAIefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   80 IQHGQPATVKVSANLIRMLAYNNKNM-LQTGLIVGGWDKyEGGKIYGIPLGGT-VVEQPFAIgGSGSSYLYGFFDQAWKD 157
Cdd:PTZ00488 107 LRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDK-KGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15235889  158 NMTKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEG 195
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 14-172 1.49e-24

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: 96.12  E-value: 1.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  14 TIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSAN 93
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  94 LIR-MLAYN--NKNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVK 170
Cdd:cd03758  83 FTRrELAESlrSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162


                ..
gi 15235889 171 AV 172
Cdd:cd03758 163 CI 164
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-197 7.25e-19

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: 81.08  E-value: 7.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQvvsdYVRYFLHQHTIQ---HGQPATV 88
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQ----YLKRLLDQLVIDdecLDDGHSL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  89 KVSA--NLIRMLAYN--NK-NMLQTGLIVGGWDKyeGGKIY--GIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKD--NM 159
Cdd:cd03760  78 SPKEihSYLTRVLYNrrSKmNPLWNTLVVGGVDN--EGEPFlgYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDL 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15235889 160 TKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEGVT 197
Cdd:cd03760 156 TEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-176 5.19e-17

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: 76.60  E-value: 5.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTsTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKvs 91
Cdd:cd03756  28 GTTALGIKCKEGVVLAVDKRI-TSKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVE-- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 aNLIRMLAYNNKNMLQTG--------LIVGGWDKyEGGKIYGIPLGGTVVE-QPFAIgGSGSSYLYGFFDQAWKDNMTKE 162
Cdd:cd03756 105 -VLVKKICDLKQQYTQHGgvrpfgvaLLIAGVDD-GGPRLFETDPSGAYNEyKATAI-GSGRQAVTEFLEKEYKEDMSLE 181

                       170
                ....*....|....
gi 15235889 163 EAEQLVVKAVSLAI 176
Cdd:cd03756 182 EAIELALKALYAAL 195
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-202 5.53e-16

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: 73.83  E-value: 5.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 ANLIRMLAYNNKNM-LQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFD-QAWKDNM--------TK 161
Cdd:cd03757  88 AQLLSTILYSRRFFpYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnQVGRKNQnnvertplSL 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15235889 162 EEAEQLVVKAVSLAIARDGASGGVVRTVIINSEGVTRNFYP 202
Cdd:cd03757 168 EEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFP 208
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 12-198 1.65e-15

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


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 72.43  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    12 GTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAAdsqVVSDYVRYFlhQHTIQH-----GQPA 86
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG---LAIELVRLF--QVELEHyekieGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889    87 TVKVSANLIRMLAYNNKNMLQTGLIV----GGWDKYEG-GKIYGI-PLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMT 160
Cdd:TIGR03690  77 TLDGKANRLAAMVRGNLPAAMQGLAVvpllAGYDLDAGaGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLD 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15235889   161 KEEAEQLVVKAVSLAIARDGASGG--VVR-----TVIINSEGVTR 198
Cdd:TIGR03690 157 EDDALRVAVEALYDAADDDSATGGpdLVRgiyptVVVITADGARR 201
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-171 3.04e-15

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: 71.71  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADSRTSTGMYVAnRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:cd01911  27 GSTAVGIKGKDGVVLAVEKKVTSKLLDP-SSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 ANLI--RMLAYNNKNMLQ---TGLIVGGWDKYEGGKIYGIPLGGTVVE-QPFAIGgSGSSYLYGFFDQAWKDNMTKEEAE 165
Cdd:cd01911 106 VKRIadLAQVYTQYGGVRpfgVSLLIAGYDEEGGPQLYQTDPSGTYFGyKATAIG-KGSQEAKTFLEKRYKKDLTLEEAI 184


                ....*.
gi 15235889 166 QLVVKA 171
Cdd:cd01911 185 KLALKA 190
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 14-173 4.22e-14

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: 68.53  E-value: 4.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  14 TIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVsan 93
Cdd:cd03752  31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVEQ--- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  94 LIRMLAYNNKNMLQTG--------LIVGGWDKYEGGKIYGI-PLGGTVVEQPFAIGG---SGSSYLygffDQAWKDNMTK 161
Cdd:cd03752 108 LVQRLCDIKQGYTQYGglrpfgvsFLYAGWDKHYGFQLYQSdPSGNYSGWKATAIGNnnqAAQSLL----KQDYKDDMTL 183

                       170
                ....*....|..
gi 15235889 162 EEAEQLVVKAVS 173
Cdd:cd03752 184 EEALALAVKVLS 195
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
12-175 5.44e-14

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 68.71  E-value: 5.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   12 GTTIIGVTYNGGVVLGADSRTSTGMYVANrASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVS 91
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITSPLIEPS-SIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEPIGVETL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   92 ANLI--RMLAYNnknmlQTG--------LIVGGWDKyEGGKIYGIPLGGTVVE-QPFAIgGSGSSYLYGFFDQAWKDNMT 160
Cdd:PRK03996 115 TKKIcdHKQQYT-----QHGgvrpfgvaLLIAGVDD-GGPRLFETDPSGAYLEyKATAI-GAGRDTVMEFLEKNYKEDLS 187

                        170
                 ....*....|....*
gi 15235889  161 KEEAEQLVVKAVSLA 175
Cdd:PRK03996 188 LEEAIELALKALAKA 202
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-197 6.12e-14

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: 67.65  E-value: 6.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  20 YNGGVVLG----------ADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVK 89
Cdd:cd03759   1 YNGGAVVAmagkdcvaiaSDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  90 VSANLIRMLAYNNK-NMLQTGLIVGGWDKYEGGKIYGIPL-GGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQL 167
Cdd:cd03759  81 TFSSLISSLLYEKRfGPYFVEPVVAGLDPDGKPFICTMDLiGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180       190
                ....*....|....*....|....*....|
gi 15235889 168 VVKAVSLAIARDGASGGVVRTVIINSEGVT 197
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKVT 190
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 11-170 6.06e-10

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: 56.96  E-value: 6.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  11 MGTTIIGVTYNGGVVLGADSRTSTGMYVANRAsDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKV 90
Cdd:cd03753  26 LGSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVES 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  91 SANLIRMLAYN-------NKNM---LQTGLIVGGWDKyEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMT 160
Cdd:cd03753 105 VTQAVSDLALQfgegddgKKAMsrpFGVALLIAGVDE-NGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMT 183

                       170
                ....*....|
gi 15235889 161 KEEAEQLVVK 170
Cdd:cd03753 184 LEEAEKLALS 193
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-173 4.61e-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: 54.68  E-value: 4.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  12 GTTIIGVTYNGGVVLGADsRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVs 91
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVE-KKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEY- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  92 anLIRMLAYNNKNMLQTG--------LIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEE 163
Cdd:cd03755 105 --ITRYIAGLQQRYTQSGgvrpfgisTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDD 182

                       170
                ....*....|
gi 15235889 164 AEQLVVKAVS 173
Cdd:cd03755 183 TIKLAIKALL 192
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 16-173 5.72e-08

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 51.78  E-value: 5.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   16 IGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKvsaNLI 95
Cdd:PTZ00246  35 VGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVE---QLV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889   96 RMLAYNNKNMLQTG--------LIVGGWDKYEGGKIYGI-PLGGTVVEQPFAIGG---SGSSYLygffDQAWKDNMTKEE 163
Cdd:PTZ00246 112 VQICDLKQSYTQFGglrpfgvsFLFAGYDENLGYQLYHTdPSGNYSGWKATAIGQnnqTAQSIL----KQEWKEDLTLEQ 187

                        170
                 ....*....|
gi 15235889  164 AEQLVVKAVS 173
Cdd:PTZ00246 188 GLLLAAKVLT 197
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 14-148 2.94e-06

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: 46.50  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  14 TIIGVTYNGGVVLGADSRTSTGMYVANrASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSAN 93
Cdd:cd03751  32 TAIGIRCKDGVVLAVEKLVTSKLYEPG-SNKRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPVKVLAD 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  94 LIRMLA-----YNNKNMLQTGLIVGGWDKyEGGKIYGIplggtvveQPfaiggSGSSYLY 148
Cdd:cd03751 111 RVAMYMhaytlYSSVRPFGCSVLLGGYDS-DGPQLYMI--------EP-----SGVSYGY 156
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 21-140 4.07e-04

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: 40.35  E-value: 4.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235889  21 NGGVVLGADSRTSTGMYVANRAS-------DKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKvsaN 93
Cdd:cd03749  26 QGSATVGLKSKTHAVLVALKRATselssyqKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVS---R 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15235889  94 LIRMLAYNNKNMLQT--------GLIVGGWDKyEGGKIYGIPLGGTVVE-QPFAIG 140
Cdd:cd03749 103 LVSKVAEKAQINTQRygrrpygvGLLIAGYDE-SGPHLFQTCPSGNYFEyKATSIG 157
 
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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