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Conserved domains on  [gi|927157203|ref|XP_013918181|]
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PREDICTED: proteasome subunit beta type-7, partial [Thamnophis sirtalis]

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 ...
 61-249 2.84e-145

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: 405.43  E-value: 2.84e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGYIGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDAIA 220
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 927157203 221 AGIFNDLGSGSNIDICVISKNKLDFLRPF 249
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 252-288 4.37e-13

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: 62.03  E-value: 4.37e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 927157203  252 PNKKGERQGKYRCEKGTTGVLSEKVIrLELEVAEETV 288
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVP-LKLEVVEEVV 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 ...
 61-249 2.84e-145

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: 405.43  E-value: 2.84e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGYIGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDAIA 220
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 927157203 221 AGIFNDLGSGSNIDICVISKNKLDFLRPF 249
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 58-238 7.20e-65

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: 201.64  E-value: 7.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203   58 KTGTTIAGIVYKDGIVLGADTRATEG-MVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRV 136
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  137 ----VTANRMLKQMLFRYQGYIGAALVLGGVDITG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEA 211
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 927157203  212 KQLVRDAIAAGIFNDLGSGSNIDICVI 238
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 60-241 5.37e-45

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: 150.82  E-value: 5.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203   60 GTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTA 139
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  140 NRMLKQMLF--RYQGYIgAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRD 217
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....
gi 927157203  218 AIAAGIFNDLGSGSNIDICVISKN 241
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKD 183
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 58-246 2.02e-43

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.98  E-value: 2.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  58 KTGTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVV 137
Cdd:COG0638   33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 138 TANRMLKQMLF-----RYQGYiGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAK 212
Cdd:COG0638  113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|....
gi 927157203 213 QLVRDAIAAGIFNDLGSGSNIDICVISKNKLDFL 246
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 60-235 6.00e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 100.06  E-value: 6.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  60 GTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTA 139
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 140 NRMLKQMLFRYQGY-IGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDA 218
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 927157203 219 IAAGIFNDLGSGSNIDI 235
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 252-288 4.37e-13

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: 62.03  E-value: 4.37e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 927157203  252 PNKKGERQGKYRCEKGTTGVLSEKVIrLELEVAEETV 288
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVP-LKLEVVEEVV 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 ...
 61-249 2.84e-145

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: 405.43  E-value: 2.84e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGYIGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDAIA 220
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 927157203 221 AGIFNDLGSGSNIDICVISKNKLDFLRPF 249
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 61-247 1.87e-85

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: 253.91  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGY-IGAALVLGGVD-ITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDA 218
Cdd:cd01912   81 NLLSNILYSYRGFpYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*....
gi 927157203 219 IAAGIFNDLGSGSNIDICVISKNKLDFLR 247
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 61-238 2.80e-68

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: 210.04  E-value: 2.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGY---IGAALVLGGVD-ITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVR 216
Cdd:cd01906   81 KLLANLLYEYTQSlrpLGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                        170       180
                 ....*....|....*....|..
gi 927157203 217 DAIAAGIFNDLGSGSNIDICVI 238
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 58-238 7.20e-65

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: 201.64  E-value: 7.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203   58 KTGTTIAGIVYKDGIVLGADTRATEG-MVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRV 136
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  137 ----VTANRMLKQMLFRYQGYIGAALVLGGVDITG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEA 211
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 927157203  212 KQLVRDAIAAGIFNDLGSGSNIDICVI 238
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 61-221 7.60e-47

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: 154.86  E-value: 7.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQ--GYIGAALVLGGVDITGPHLYSIYPHGSTDKLP-YVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRD 217
Cdd:cd01901   81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                 ....
gi 927157203 218 AIAA 221
Cdd:cd01901  161 ALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 60-241 5.37e-45

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: 150.82  E-value: 5.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203   60 GTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTA 139
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  140 NRMLKQMLF--RYQGYIgAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRD 217
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|....
gi 927157203  218 AIAAGIFNDLGSGSNIDICVISKN 241
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-241 7.78e-45

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: 150.48  E-value: 7.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLF--RYQGYIgAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDA 218
Cdd:cd03764   81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                        170       180
                 ....*....|....*....|...
gi 927157203 219 IAAGIFNDLGSGSNIDICVISKN 241
Cdd:cd03764  160 IKSAIERDSASGDGIDVVVITKD 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-245 9.02e-44

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: 147.76  E-value: 9.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGYIGAALVLGGVD-ITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDAI 219
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*.
gi 927157203 220 AAGIFNDLGSGSNIDICVISKNKLDF 245
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVER 186
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 58-246 2.02e-43

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.98  E-value: 2.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  58 KTGTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVV 137
Cdd:COG0638   33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 138 TANRMLKQMLF-----RYQGYiGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAK 212
Cdd:COG0638  113 GLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|....
gi 927157203 213 QLVRDAIAAGIFNDLGSGSNIDICVISKNKLDFL 246
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-241 4.43e-29

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: 109.26  E-value: 4.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  61 TTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTAN 140
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQMLFRYQGY---IGAALVlgGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRD 217
Cdd:cd03761   81 KLLSNMLYQYKGMglsMGTMIC--GWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                        170       180
                 ....*....|....*....|....
gi 927157203 218 AIAAGIFNDLGSGSNIDICVISKN 241
Cdd:cd03761  159 AIYHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 60-235 6.00e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 100.06  E-value: 6.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  60 GTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTA 139
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 140 NRMLKQMLFRYQGY-IGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDA 218
Cdd:PTZ00488 119 SKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRA 198

                        170
                 ....*....|....*..
gi 927157203 219 IAAGIFNDLGSGSNIDI 235
Cdd:PTZ00488 199 IYHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 55-239 7.07e-22

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: 90.85  E-value: 7.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  55 TARKTGTTIAGIVYKDGIVLGADTRATEGMVVADkNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLP 134
Cdd:cd03756   23 EAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 135 RVVTANRM---LKQMLFRYQGY--IGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEE 209
Cdd:cd03756  102 DVEVLVKKicdLKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLE 181

                        170       180       190
                 ....*....|....*....|....*....|
gi 927157203 210 EAKQLVRDAIAAGIfNDLGSGSNIDICVIS 239
Cdd:cd03756  182 EAIELALKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 60-241 1.92e-19

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 84.23  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  60 GTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVTA 139
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 140 NRMLKQML-----FRYQGYIgaalVLGGVDITG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAV---FEDKFKPDMEE-- 208
Cdd:cd03757   88 AQLLSTILysrrfFPYYVFN----ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLldnQVGRKNQNNVErt 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 927157203 209 ----EEAKQLVRDAIAAGIFNDLGSGSNIDICVISKN 241
Cdd:cd03757  164 plslEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKD 200
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 56-238 1.24e-16

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: 76.71  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  56 ARKTGTTIAGIVYKDGIVLGADTRATEGMVVADKNcSKIHFIAPNIYCCGAGTAAD------------------------ 111
Cdd:cd01911   23 AVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADarvlvnrarveaqnyrytygepip 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 112 TEMTTQMISSNMELHSLSTGRLPrvvtanrmlkqmlFryqgyiGAALVLGGVD-ITGPHLYSIYPHGStdklpYVT---- 186
Cdd:cd01911  102 VEVLVKRIADLAQVYTQYGGVRP-------------F------GVSLLIAGYDeEGGPQLYQTDPSGT-----YFGykat 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927157203 187 -MGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDAIAAGIFNDLgSGSNIDICVI 238
Cdd:cd01911  158 aIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 59-241 2.55e-16

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 75.68  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  59 TGTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAAD----TEMTTQMISSNMEL---HSLST- 130
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLddgHSLSPk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 131 ---GRLPRVVTANRMLKQMLFRyqgyigaALVLGGVDITG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFED--KFKP 204
Cdd:cd03760   81 eihSYLTRVLYNRRSKMNPLWN-------TLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREawEKKP 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 927157203 205 DMEEEEAKQLVRDAIAAGIFNDLGSGSNIDICVISKN 241
Cdd:cd03760  154 DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKE 190
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 62-220 3.64e-16

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 74.93  E-value: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  62 TIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRV-VTAN 140
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPkAAAN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 141 RMLKQML--FRYQGYIGAALVLGGVD-ITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRD 217
Cdd:cd03758   83 FTRRELAesLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162


                 ...
gi 927157203 218 AIA 220
Cdd:cd03758  163 CIK 165
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
56-239 2.17e-15

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 73.71  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  56 ARKTGTTIAGIVYKDGIVLGADTRATEGMVVADKnCSKIHFIAPNIYCCGAGTAADTEmttQMISS---NMELHSLSTGR 132
Cdd:PRK03996  32 AVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADAR---VLIDRarvEAQINRLTYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 133 LPRVVT-ANRM--LKQMLFRYQGY--IGAALVLGGVDITGPHLYSIYPHGSTdkLPY--VTMGSGSLAAMAVFEDKFKPD 205
Cdd:PRK03996 108 PIGVETlTKKIcdHKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAY--LEYkaTAIGAGRDTVMEFLEKNYKED 185

                        170       180       190
                 ....*....|....*....|....*....|....
gi 927157203 206 MEEEEAKQLVRDAIAAGIfNDLGSGSNIDICVIS 239
Cdd:PRK03996 186 LSLEEAIELALKALAKAN-EGKLDPENVEIAYID 218
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 252-288 4.37e-13

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: 62.03  E-value: 4.37e-13
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 927157203  252 PNKKGERQGKYRCEKGTTGVLSEKVIrLELEVAEETV 288
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETVP-LKLEVVEEVV 36
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 56-215 6.77e-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: 60.81  E-value: 6.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  56 ARKTGTTIAGIVYKDGIVLGADTRATEGMVVADkNCSKIHFIAPNIYCCGAGTAADT----------------------- 112
Cdd:cd03753   23 AIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADArtlidharveaqnhrftynepmt 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 113 -EMTTQMISsnmELhSLSTGRLprvvtanRMLKQMLFRYqgyIGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGS 191
Cdd:cd03753  102 vESVTQAVS---DL-ALQFGEG-------DDGKKAMSRP---FGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGS 167

                        170       180
                 ....*....|....*....|....
gi 927157203 192 LAAMAVFEDKFKPDMEEEEAKQLV 215
Cdd:cd03753  168 EGAQSSLQEKYHKDMTLEEAEKLA 191
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 59-243 2.74e-10

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: 58.41  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  59 TGTTIAGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRVVT 138
Cdd:cd03759    2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 139 ANRMLKQMLF--RYQGYIGAALVlGGVDITG-PHLYSIYPHGSTDKL-PYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQL 214
Cdd:cd03759   82 FSSLISSLLYekRFGPYFVEPVV-AGLDPDGkPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFET 160

                        170       180
                 ....*....|....*....|....*....
gi 927157203 215 VRDAIAAGIFNDLGSGSNIDICVISKNKL 243
Cdd:cd03759  161 ISQALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 55-242 3.49e-10

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: 58.87  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  55 TARKTGTTIAGIVYKDGIVLgADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAAD----------------------- 111
Cdd:cd03750   22 AAVSSGAPSVGIKAANGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDfrvlvkkarkiaqqyylvygepi 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 112 -TEMTTQMISSNMELHSLSTGRLPrvvtanrmlkqmlfryqgyIGAALVLGGVDITGPHLYSIYPHGStdklpYVT---- 186
Cdd:cd03750  101 pVSQLVREIASVMQEYTQSGGVRP-------------------FGVSLLIAGWDEGGPYLYQVDPSGS-----YFTwkat 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927157203 187 -MGSGSLAAMAVFEDKFKPDMEEEeakqlvrDAIAAGI------FNDLGSGSNIDICVISKNK 242
Cdd:cd03750  157 aIGKNYSNAKTFLEKRYNEDLELE-------DAIHTAIltlkegFEGQMTEKNIEIGICGETK 212
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 60-211 1.99e-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: 53.44  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  60 GTTIaGIVYKDGIVLGADTRATEGMVVADKNcSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGR-LPRVVT 138
Cdd:cd03751   31 GTAI-GIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTpIPVKVL 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927157203 139 ANR--MLKQMLFRYQGY--IGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEA 211
Cdd:cd03751  109 ADRvaMYMHAYTLYSSVrpFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCREA 185
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 65-245 3.02e-08

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 53.32  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  65 GIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPRV---VTANR 141
Cdd:PTZ00246  36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVeqlVVQIC 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 142 MLKQMLFRYQGY--IGAALVLGGVDIT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEEAKQLVRDA 218
Cdd:PTZ00246 116 DLKQSYTQFGGLrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKV 195

                        170       180
                 ....*....|....*....|....*..
gi 927157203 219 IAAGIFNDLGSGSNIDICVISKNKLDF 245
Cdd:PTZ00246 196 LTKSMDSTSPKADKIEVGILSHGETDG 222
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 60-215 1.33e-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: 51.19  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  60 GTTIaGIVYKDGIVLGADTRATEGMVVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGrlpRVVTA 139
Cdd:cd03752   30 GTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQ---EPIPV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 140 NRMLKQMLFRYQGY--------IGAALVLGGVD-ITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEEE 210
Cdd:cd03752  106 EQLVQRLCDIKQGYtqygglrpFGVSFLYAGWDkHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEE 185


                 ....*
gi 927157203 211 AKQLV 215
Cdd:cd03752  186 ALALA 190
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 56-221 4.63e-06

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: 46.51  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  56 ARKTGTTIAGIVYKDGIVLGADTRATEGMVVADKncsKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGR-LP 134
Cdd:cd03749   23 AVKQGSATVGLKSKTHAVLVALKRATSELSSYQK---KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSpIP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 135 RVVTANRMLKQMLFRYQGY----IGAALVLGGVDITGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFK--PDMEE 208
Cdd:cd03749  100 VSRLVSKVAEKAQINTQRYgrrpYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefEDCSL 179

                        170
                 ....*....|...
gi 927157203 209 EEakqLVRDAIAA 221
Cdd:cd03749  180 EE---LIKHALRA 189
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 56-238 5.52e-06

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


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 46.20  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203  56 ARKTGTTIAGIVYKDGIVLGADTRATEGMvVADKNCSKIHFIAPNIYCCGAGTAADTEMTTQMISSNMELHSLSTGRLPR 135
Cdd:cd03755   23 AVRKGTTAVGVRGKDCVVLGVEKKSVAKL-QDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927157203 136 VVTANRMLKQMLFRY--QGYI---GAALVLGGVDITG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFKPDMEEE 209
Cdd:cd03755  102 VEYITRYIAGLQQRYtqSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRD 181

                        170       180
                 ....*....|....*....|....*....
gi 927157203 210 EAKQLVRDAIAAGIfnDLGSGsNIDICVI 238
Cdd:cd03755  182 DTIKLAIKALLEVV--QSGSK-NIELAVM 207
 
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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