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Conserved domains on  [gi|1938949811|pdb|5VFP|o]
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Chain o, Proteasome subunit beta type-7

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

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 ...
1-189 2.91e-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: 397.34  E-value: 2.91e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 160
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160
                       170       180
                ....*....|....*....|....*....
5VFP_o      161 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 189
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
192-216 2.40e-08

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: 48.55  E-value: 2.40e-08
                          10        20
                  ....*....|....*....|....*
5VFP_o        192 PNKKGTRLGRYRCEKGTTAVLTEKI 216
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV 25
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-189 2.91e-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: 397.34  E-value: 2.91e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 160
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160
                       170       180
                ....*....|....*....|....*....
5VFP_o      161 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 189
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
1-178 8.41e-62

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: 190.86  E-value: 8.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o          1 TTIAGVVYKDGIVLGADTRATEG-MVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         77 -VTANRMLKQMLFRYQGYIGAALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNL 154
Cdd:pfam00227  85 aRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVEL 164
                         170       180
                  ....*....|....*....|....
5VFP_o        155 VSEAIAAGIFNDLGSGSNIDLCVI 178
Cdd:pfam00227 165 AVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
1-181 7.28e-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: 145.04  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o          1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         81 RMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 158
Cdd:TIGR03634  82 TLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|...
5VFP_o        159 IAAGIFNDLGSGSNIDLCVISKN 181
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
1-186 3.62e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 142.21  E-value: 3.62e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLF-----RYQGYiGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLV 155
Cdd:COG0638 116 KLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194
                       170       180       190
                ....*....|....*....|....*....|.
5VFP_o      156 SEAIAAGIFNDLGSGSNIDLCVISKNKLDFL 186
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
1-175 1.17e-23

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 94.67  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        81 RMLKQMLFRYQGY-IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAI 159
Cdd:PTZ00488 120 KILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
                        170
                 ....*....|....*.
5VFP_o       160 AAGIFNDLGSGSNIDL 175
Cdd:PTZ00488 200 YHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
192-216 2.40e-08

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: 48.55  E-value: 2.40e-08
                          10        20
                  ....*....|....*....|....*
5VFP_o        192 PNKKGTRLGRYRCEKGTTAVLTEKI 216
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV 25
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-189 2.91e-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: 397.34  E-value: 2.91e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIA 160
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160
                       170       180
                ....*....|....*....|....*....
5VFP_o      161 AGIFNDLGSGSNIDLCVISKNKLDFLRPY 189
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-187 2.79e-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: 243.12  E-value: 2.79e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGY-IGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 158
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160
                       170       180
                ....*....|....*....|....*....
5VFP_o      159 IAAGIFNDLGSGSNIDLCVISKNKLDFLR 187
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
1-178 5.96e-66

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: 201.18  E-value: 5.96e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGY---IGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVS 156
Cdd:cd01906  81 KLLANLLYEYTQSlrpLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160
                       170       180
                ....*....|....*....|..
5VFP_o      157 EAIAAGIFNDLGSGSNIDLCVI 178
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
1-178 8.41e-62

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: 190.86  E-value: 8.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o          1 TTIAGVVYKDGIVLGADTRATEG-MVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV--- 76
Cdd:pfam00227   5 TTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVela 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         77 -VTANRMLKQMLFRYQGYIGAALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNL 154
Cdd:pfam00227  85 aRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVEL 164
                         170       180
                  ....*....|....*....|....
5VFP_o        155 VSEAIAAGIFNDLGSGSNIDLCVI 178
Cdd:pfam00227 165 AVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
1-161 2.15e-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: 148.31  E-value: 2.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQ--GYIGAALVLGGVDVTGPHLYSIYPHGSTDKLP-YVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 157
Cdd:cd01901  81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160

                ....
5VFP_o      158 AIAA 161
Cdd:cd01901 161 ALKS 164
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-181 4.39e-44

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: 145.86  E-value: 4.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 158
Cdd:cd03764  81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159
                       170       180
                ....*....|....*....|...
5VFP_o      159 IAAGIFNDLGSGSNIDLCVISKN 181
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKD 182
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
1-181 7.28e-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: 145.04  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o          1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:TIGR03634   2 TTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         81 RMLKQMLF--RYQGYIgAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 158
Cdd:TIGR03634  82 TLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160
                         170       180
                  ....*....|....*....|...
5VFP_o        159 IAAGIFNDLGSGSNIDLCVISKN 181
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKD 183
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-185 1.32e-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: 144.67  E-value: 1.32e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGYIGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAI 159
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160
                       170       180
                ....*....|....*....|....*.
5VFP_o      160 AAGIFNDLGSGSNIDLCVISKNKLDF 185
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVER 186
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
1-186 3.62e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 142.21  E-value: 3.62e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:COG0638  36 TTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLF-----RYQGYiGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLV 155
Cdd:COG0638 116 KLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVELA 194
                       170       180       190
                ....*....|....*....|....*....|.
5VFP_o      156 SEAIAAGIFNDLGSGSNIDLCVISKNKLDFL 186
Cdd:COG0638 195 LRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-181 2.46e-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: 2.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RMLKQMLFRYQGY-IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAI 159
Cdd:cd03761  81 KLLSNMLYQYKGMgLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
                       170       180
                ....*....|....*....|..
5VFP_o      160 AAGIFNDLGSGSNIDLCVISKN 181
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
1-175 1.17e-23

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 94.67  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:PTZ00488  40 TTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAAS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        81 RMLKQMLFRYQGY-IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAI 159
Cdd:PTZ00488 120 KILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
                        170
                 ....*....|....*.
5VFP_o       160 AAGIFNDLGSGSNIDL 175
Cdd:PTZ00488 200 YHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-179 1.40e-19

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: 83.15  E-value: 1.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADkNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTAN 80
Cdd:cd03756  29 TTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPIDVEVLV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       81 RM---LKQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLV 155
Cdd:cd03756 108 KKicdLKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIELA 187
                       170       180
                ....*....|....*....|....
5VFP_o      156 SEAIAAGIfNDLGSGSNIDLCVIS 179
Cdd:cd03756 188 LKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
2-181 4.51e-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: 4.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        2 TIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANR 81
Cdd:cd03757  10 TVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       82 MLKQML-----FRYQGYIgaalVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAV---FEDKFRPDMEE---- 148
Cdd:cd03757  90 LLSTILysrrfFPYYVFN----ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLldnQVGRKNQNNVErtpl 165
                       170       180       190
                ....*....|....*....|....*....|....*
5VFP_o      149 --EEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKN 181
Cdd:cd03757 166 slEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKD 200
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
2-155 4.12e-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: 70.69  E-value: 4.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        2 TIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV-VTAN 80
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPkAAAN 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VFP_o       81 RMLKQML--FRYQGYIGAALVLGGVD-VTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLV 155
Cdd:cd03758  83 FTRRELAesLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-179 8.62e-15

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 70.63  E-value: 8.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         1 TTIAGVVYKDGIVLGADTRATEGMVVADKnCSKIHFISPNIYCCGAGTAADTdmtTQLISS---NLELHSLSTGRLPRVV 77
Cdd:PRK03996  37 TTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADA---RVLIDRarvEAQINRLTYGEPIGVE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        78 T-ANRM--LKQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTdkLPY--VTMGSGSLAAMAVFEDKFRPDMEEEE 150
Cdd:PRK03996 113 TlTKKIcdHKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAY--LEYkaTAIGAGRDTVMEFLEKNYKEDLSLEE 190
                        170       180
                 ....*....|....*....|....*....
5VFP_o       151 AKNLVSEAIAAGIfNDLGSGSNIDLCVIS 179
Cdd:PRK03996 191 AIELALKALAKAN-EGKLDPENVEIAYID 218
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-178 4.37e-14

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: 68.24  E-value: 4.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIaGVVYKDGIVLGADTRATEGMVVADKNcSKIHFISPNIYCCGAGTAADTDMTTQ---LISSNlelHSLSTGRLPRV- 76
Cdd:cd01911  29 TAV-GIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARVLVNrarVEAQN---YRYTYGEPIPVe 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       77 VTANRM--LKQMLFRYQGY--IGAALVLGGVDV-TGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDKFRPDM 146
Cdd:cd01911 104 VLVKRIadLAQVYTQYGGVrpFGVSLLIAGYDEeGGPQLYQTDPSGT-----YFGykataIGKGSQEAKTFLEKRYKKDL 178
                       170       180       190
                ....*....|....*....|....*....|..
5VFP_o      147 EEEEAKNLVSEAIAAGIFNDLgSGSNIDLCVI 178
Cdd:cd01911 179 TLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
1-181 3.03e-12

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: 62.97  E-value: 3.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAAD----TDMTTQLISSNLEL---HSLST--- 70
Cdd:cd03760   3 TSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLddgHSLSPkei 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       71 -GRLPRVVTANRMLKQMLFRyqgyigaALVLGGVDVTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFR--PDM 146
Cdd:cd03760  83 hSYLTRVLYNRRSKMNPLWN-------TLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkPDL 155
                       170       180       190
                ....*....|....*....|....*....|....*
5VFP_o      147 EEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKN 181
Cdd:cd03760 156 TEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
2-183 3.15e-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: 59.95  E-value: 3.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        2 TIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANR 81
Cdd:cd03759   5 AVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       82 MLKQMLF--RYQGYIGAALVlGGVDVTG-PHLYSIYPHGSTDKL-PYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSE 157
Cdd:cd03759  85 LISSLLYekRFGPYFVEPVV-AGLDPDGkPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFETISQ 163
                       170       180
                ....*....|....*....|....*.
5VFP_o      158 AIAAGIFNDLGSGSNIDLCVISKNKL 183
Cdd:cd03759 164 ALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
1-155 2.55e-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: 57.73  E-value: 2.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        1 TTIAGVVYKDGIVLGADTRATEGMVVADkNCSKIHFISPNIYCCGAGTAADT------------------------DMTT 56
Cdd:cd03753  28 STAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADArtlidharveaqnhrftynepmtvESVT 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       57 QLISsNLelhSLSTGRLprvvtanRMLKQMLFRYqgyIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMA 136
Cdd:cd03753 107 QAVS-DL---ALQFGEG-------DDGKKAMSRP---FGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQS 172
                       170
                ....*....|....*....
5VFP_o      137 VFEDKFRPDMEEEEAKNLV 155
Cdd:cd03753 173 SLQEKYHKDMTLEEAEKLA 191
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
192-216 2.40e-08

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: 48.55  E-value: 2.40e-08
                          10        20
                  ....*....|....*....|....*
5VFP_o        192 PNKKGTRLGRYRCEKGTTAVLTEKI 216
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV 25
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
5-185 2.69e-08

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 52.55  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o         5 GVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRV---VTANR 81
Cdd:PTZ00246  36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVeqlVVQIC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        82 MLKQMLFRYQGY--IGAALVLGGVDVT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEA 158
Cdd:PTZ00246 116 DLKQSYTQFGGLrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKV 195
                        170       180
                 ....*....|....*....|....*..
5VFP_o       159 IAAGIFNDLGSGSNIDLCVISKNKLDF 185
Cdd:PTZ00246 196 LTKSMDSTSPKADKIEVGILSHGETDG 222
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-182 9.19e-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: 50.78  E-value: 9.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        5 GVVYKDGIVLgADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVvtaNRMLK 84
Cdd:cd03750  32 GIKAANGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPV---SQLVR 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       85 QMLFRYQGY--------IGAALVLGGVDVTGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDKFRPDMEEEEA 151
Cdd:cd03750 108 EIASVMQEYtqsggvrpFGVSLLIAGWDEGGPYLYQVDPSGS-----YFTwkataIGKNYSNAKTFLEKRYNEDLELEDA 182
                       170       180       190
                ....*....|....*....|....*....|.
5VFP_o      152 KNLVSEAIAAGIFNDLgSGSNIDLCVISKNK 182
Cdd:cd03750 183 IHTAILTLKEGFEGQM-TEKNIEIGICGETK 212
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
2-151 5.72e-07

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: 48.43  E-value: 5.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        2 TIAGVVYKDGIVLGADTRATEGMVVADKNcSKIHFISPNIYCCGAGTAADTdmtTQLIS---SNLELHSLSTGR-LPRVV 77
Cdd:cd03751  32 TAIGIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADG---RHLVSrarEEAENYRDNYGTpIPVKV 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VFP_o       78 TANR--MLKQMLFRYQGY--IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEA 151
Cdd:cd03751 108 LADRvaMYMHAYTLYSSVrpFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCREA 185
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
2-155 9.60e-06

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: 45.03  E-value: 9.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        2 TIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGrlpRVVTANR 81
Cdd:cd03752  31 TCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQ---EPIPVEQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       82 MLKQMLFRYQGY--------IGAALVLGGVDVT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAK 152
Cdd:cd03752 108 LVQRLCDIKQGYtqygglrpFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEAL 187

                ...
5VFP_o      153 NLV 155
Cdd:cd03752 188 ALA 190
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
5-161 1.01e-03

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


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 38.81  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        5 GVVYKDGIVLGADTRATEGMVVADKncsKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGR-LPRVVTANRML 83
Cdd:cd03749  32 GLKSKTHAVLVALKRATSELSSYQK---KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSpIPVSRLVSKVA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       84 KQMLFRYQGY----IGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFR--PDMEEEEaknLVSE 157
Cdd:cd03749 109 EKAQINTQRYgrrpYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefEDCSLEE---LIKH 185

                ....
5VFP_o      158 AIAA 161
Cdd:cd03749 186 ALRA 189
proteasome_beta_bacterial cd03765
Bacterial proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is ...
5-187 9.13e-03

Bacterial 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: 239734  Cd Length: 236  Bit Score: 36.02  E-value: 9.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o        5 GVVYKDGIVLGADTRATEGMvvaDK--NCSKIHFIS-PN---IYCCGAGTAADTDMTTQLISSNLELH---SLSTgrLPR 75
Cdd:cd03765   5 GIKLDAGLVFASDSRTNAGV---DNisTYRKMFVFSvPGervIVLLTAGNLATTQAVISLLQRDLEDPeetNLLN--APT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VFP_o       76 VVTANRMLKQMLFRYQGYIGAALVLGGVDVT------------GPHLYSIYPHG----STDKLPYVTMGsgslaamavfE 139
Cdd:cd03765  80 MFDAARYVGETLREVQEQDREALKKAGIDFSasfilggqikgeEPRLFLIYPQGnfieATPDTPFLQIG----------E 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
5VFP_o      140 DK---------FRPDMEEEEAKN--LVSeaIAAGIFNDLGSGSNIDLCVISKNKLDFLR 187
Cdd:cd03765 150 TKygkpildrvITPDTSLEDAAKcaLVS--MDSTMRSNLSVGPPLDLLVYERDSLQVGH 206
 
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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