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Conserved domains on  [gi|17380263|sp|Q99436|]
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RecName: Full=Proteasome subunit beta type-7; AltName: Full=Macropain chain Z; AltName: Full=Multicatalytic endopeptidase complex chain Z; AltName: Full=Proteasome subunit Z; Flags: Precursor

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

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_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.39e-143

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: 400.42  E-value: 1.39e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 203
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17380263 204 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 232
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 5.38e-12

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


:

Pssm-ID: 463597  Cd Length: 36  Bit Score: 58.95  E-value: 5.38e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17380263   235 PNKKGTRLGRYRCEKGTTAVLTEKItPLEIEVLEETV 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.39e-143

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: 400.42  E-value: 1.39e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 203
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17380263 204 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 232
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 3.11e-63

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: 197.02  E-value: 3.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263    41 KTGTTIAGVVYKDGIVLGADTRATEG-MVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   120 ----VTANRMLKQMLFRYQGYIGAALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 17380263   195 KNLVSEAIAAGIFNDLGSGSNIDLCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-224 3.43e-44

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: 148.13  E-value: 3.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263    43 GTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   123 NRMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....
gi 17380263   201 AIAAGIFNDLGSGSNIDLCVISKN 224
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 41-229 1.99e-43

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.60  E-value: 1.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVV 120
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 121 TANRMLKQMLF-----RYQGYiGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAK 195
Cdd:COG0638 113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....
gi 17380263 196 NLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFL 229
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 43-218 5.14e-24

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 97.37  E-value: 5.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   43 GTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTA 122
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  123 NRMLKQMLFRYQGY-IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 201
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 17380263  202 IAAGIFNDLGSGSNIDL 218
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 5.38e-12

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 58.95  E-value: 5.38e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17380263   235 PNKKGTRLGRYRCEKGTTAVLTEKItPLEIEVLEETV 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.39e-143

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: 400.42  E-value: 1.39e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 203
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*....
gi 17380263 204 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 232
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 44-230 4.94e-82

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: 244.66  E-value: 4.94e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGY-IGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 201
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*....
gi 17380263 202 IAAGIFNDLGSGSNIDLCVISKNKLDFLR 230
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 44-221 2.23e-65

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 201.95  E-value: 2.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGY---IGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVS 199
Cdd:cd01906  81 KLLANLLYEYTQSlrpLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 17380263 200 EAIAAGIFNDLGSGSNIDLCVI 221
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 3.11e-63

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: 197.02  E-value: 3.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263    41 KTGTTIAGVVYKDGIVLGADTRATEG-MVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   120 ----VTANRMLKQMLFRYQGYIGAALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 17380263   195 KNLVSEAIAAGIFNDLGSGSNIDLCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 44-204 6.01e-45

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: 149.47  E-value: 6.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQ--GYIGAALVLGGVDVTGPHLYSIYPHGSTDKLP-YVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 200
Cdd:cd01901  81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ....
gi 17380263 201 AIAA 204
Cdd:cd01901 161 ALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-224 3.43e-44

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: 148.13  E-value: 3.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263    43 GTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   123 NRMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....
gi 17380263   201 AIAAGIFNDLGSGSNIDLCVISKN 224
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 41-229 1.99e-43

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.60  E-value: 1.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVV 120
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 121 TANRMLKQMLF-----RYQGYiGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAK 195
Cdd:COG0638 113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....
gi 17380263 196 NLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFL 229
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-224 2.18e-43

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: 146.24  E-value: 2.18e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 201
Cdd:cd03764  81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|...
gi 17380263 202 IAAGIFNDLGSGSNIDLCVISKN 224
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKD 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-228 3.49e-43

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: 145.45  E-value: 3.49e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGYIGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAI 202
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*.
gi 17380263 203 AAGIFNDLGSGSNIDLCVISKNKLDF 228
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVER 186
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-224 6.29e-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: 111.18  E-value: 6.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  44 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 123
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 124 RMLKQMLFRYQGY---IGAALVlgGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 200
Cdd:cd03761  81 KLLSNMLYQYKGMglsMGTMIC--GWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                       170       180
                ....*....|....*....|....
gi 17380263 201 AIAAGIFNDLGSGSNIDLCVISKN 224
Cdd:cd03761 159 AIYHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 43-218 5.14e-24

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 97.37  E-value: 5.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   43 GTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTA 122
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  123 NRMLKQMLFRYQGY-IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 201
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 17380263  202 IAAGIFNDLGSGSNIDL 218
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 41-222 1.60e-20

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: 87.00  E-value: 1.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADkNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVV 120
Cdd:cd03756  26 KRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 121 TANRM---LKQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAK 195
Cdd:cd03756 105 VLVKKicdLKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAI 184

                       170       180
                ....*....|....*....|....*..
gi 17380263 196 NLVSEAIAAGIfNDLGSGSNIDLCVIS 222
Cdd:cd03756 185 ELALKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-224 3.42e-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: 75.37  E-value: 3.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  43 GTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTA 122
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 123 NRMLKQML-----FRYQGYIgaalVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAV---FEDKFRPDMEE-- 191
Cdd:cd03757  88 AQLLSTILysrrfFPYYVFN----ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLldnQVGRKNQNNVErt 163

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17380263 192 ----EEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKN 224
Cdd:cd03757 164 plslEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKD 200
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
41-222 1.16e-15

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 74.10  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADKnCSKIHFISPNIYCCGAGTAADTdmtTQLISS---NLELHSLSTGRLP 117
Cdd:PRK03996  34 KRGTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADA---RVLIDRarvEAQINRLTYGEPI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  118 RVVTANRML---KQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTdkLPY--VTMGSGSLAAMAVFEDKFRPDME 190
Cdd:PRK03996 110 GVETLTKKIcdhKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAY--LEYkaTAIGAGRDTVMEFLEKNYKEDLS 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 17380263  191 EEEAKNLVSEAIAAGIfNDLGSGSNIDLCVIS 222
Cdd:PRK03996 188 LEEAIELALKALAKAN-EGKLDPENVEIAYID 218
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-221 4.36e-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: 72.09  E-value: 4.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  39 VRKTGTTIaGVVYKDGIVLGADTRATEGMVVADKNcSKIHFISPNIYCCGAGTAADTDMTTQ---LISSNlelHSLSTGR 115
Cdd:cd01911  24 VKNGSTAV-GIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARVLVNrarVEAQN---YRYTYGE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 116 LPRV-VTANRM--LKQMLFRYQGY--IGAALVLGGVDV-TGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDK 184
Cdd:cd01911  99 PIPVeVLVKRIadLAQVYTQYGGVrpFGVSLLIAGYDEeGGPQLYQTDPSGT-----YFGykataIGKGSQEAKTFLEKR 173

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17380263 185 FRPDMEEEEAKNLVSEAIAAGIFNDLgSGSNIDLCVI 221
Cdd:cd01911 174 YKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-198 8.85e-15

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: 71.08  E-value: 8.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  45 TIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV-VTAN 123
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPkAAAN 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17380263 124 RMLKQML--FRYQGYIGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLV 198
Cdd:cd03758  83 FTRRELAesLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-224 6.23e-14

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: 68.75  E-value: 6.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  42 TGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAAD----TDMTTQLISSNLEL---HSLST- 113
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLddgHSLSPk 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 114 ---GRLPRVVTANRMLKQMLFRyqgyigaALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFR--P 187
Cdd:cd03760  81 eihSYLTRVLYNRRSKMNPLWN-------TLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkP 153

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17380263 188 DMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKN 224
Cdd:cd03760 154 DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 5.38e-12

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 58.95  E-value: 5.38e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17380263   235 PNKKGTRLGRYRCEKGTTAVLTEKItPLEIEVLEETV 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-226 1.38e-11

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: 61.87  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  42 TGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVT 121
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 122 ANRMLKQMLF--RYQGYIGAALVlGGVDVTG-PHLYSIYPHGSTDKL-PYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNL 197
Cdd:cd03759  82 FSSLISSLLYekRFGPYFVEPVV-AGLDPDGkPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                       170       180
                ....*....|....*....|....*....
gi 17380263 198 VSEAIAAGIFNDLGSGSNIDLCVISKNKL 226
Cdd:cd03759 161 ISQALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 41-198 2.31e-11

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: 61.58  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADkNCSKIHFISPNIYCCGAGTAADT------------------------D 96
Cdd:cd03753  25 KLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADArtlidharveaqnhrftynepmtvE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  97 MTTQLISsNLelhSLSTGRLprvvtanRMLKQMLFRYqgyIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLA 176
Cdd:cd03753 104 SVTQAVS-DL---ALQFGEG-------DDGKKAMSRP---FGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEG 169

                       170       180
                ....*....|....*....|..
gi 17380263 177 AMAVFEDKFRPDMEEEEAKNLV 198
Cdd:cd03753 170 AQSSLQEKYHKDMTLEEAEKLA 191
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 34-228 5.40e-09

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 55.63  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263   34 YKLPKVRKTGTTIaGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLST 113
Cdd:PTZ00246  23 YALEAINNASLTV-GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  114 GRLPRV---VTANRMLKQMLFRYQGY--IGAALVLGGVDVT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRP 187
Cdd:PTZ00246 102 GEPQPVeqlVVQICDLKQSYTQFGGLrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKE 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 17380263  188 DMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDF 228
Cdd:PTZ00246 182 DLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGETDG 222
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-225 3.00e-08

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: 53.09  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  43 GTTIAGVVYKDGIVLgADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVvta 122
Cdd:cd03750  27 GAPSVGIKAANGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPV--- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 123 NRMLKQMLFRYQGY--------IGAALVLGGVDVTGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDKFRPDM 189
Cdd:cd03750 103 SQLVREIASVMQEYtqsggvrpFGVSLLIAGWDEGGPYLYQVDPSGS-----YFTwkataIGKNYSNAKTFLEKRYNEDL 177

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17380263 190 EEEEAKNLVSEAIAAGIFNDLgSGSNIDLCVISKNK 225
Cdd:cd03750 178 ELEDAIHTAILTLKEGFEGQM-TEKNIEIGICGETK 212
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-194 4.79e-08

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: 52.28  E-value: 4.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  34 YKLPKVRKTGTTIaGVVYKDGIVLGADTRATEGMVVADKNcSKIHFISPNIYCCGAGTAADtdmTTQLIS---SNLELHS 110
Cdd:cd03751  22 YANKAVENSGTAI-GIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLAD---GRHLVSrarEEAENYR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 111 LSTGR-LPRVVTANR--MLKQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKF 185
Cdd:cd03751  97 DNYGTpIPVKVLADRvaMYMHAYTLYSSVrpFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLK 176


                ....*....
gi 17380263 186 RPDMEEEEA 194
Cdd:cd03751 177 FSELTCREA 185
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-198 8.94e-07

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: 48.50  E-value: 8.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  34 YKLPKVRKTGTTIaGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLST 113
Cdd:cd03752  21 YAMEAISHAGTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 114 GrlpRVVTANRMLKQMLFRYQGY--------IGAALVLGGVDVT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDK 184
Cdd:cd03752 100 Q---EPIPVEQLVQRLCDIKQGYtqygglrpFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQD 176

                       170
                ....*....|....
gi 17380263 185 FRPDMEEEEAKNLV 198
Cdd:cd03752 177 YKDDMTLEEALALA 190
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 41-204 1.04e-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: 42.28  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263  41 KTGTTIAGVVYKDGIVLGADTRATEGMVVADKncsKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGR-LPRV 119
Cdd:cd03749  25 KQGSATVGLKSKTHAVLVALKRATSELSSYQK---KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSpIPVS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380263 120 VTANRMLKQMLFRYQGY----IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFR--PDMEEEE 193
Cdd:cd03749 102 RLVSKVAEKAQINTQRYgrrpYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefEDCSLEE 181

                       170
                ....*....|.
gi 17380263 194 aknLVSEAIAA 204
Cdd:cd03749 182 ---LIKHALRA 189
 
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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