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Conserved domains on  [gi|389626457|ref|XP_003710882|]
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proteasome component C5 [Pyricularia oryzae 70-15]

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-265 1.20e-124

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: 353.10  E-value: 1.20e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  35 FNPYTDNGGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGGTTadnsdatlVLSVVGFAADGEALKERLDAICK 114
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKC--------VLGSSGFQADILALTKRLKARIK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 115 IYRYRHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQV 194
Cdd:cd03757   73 MYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389626457 195 NFKNQYVpgsgtghdlqeRERKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIEEVIMPLKKD 265
Cdd:cd03757  153 GRKNQNN-----------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-265 1.20e-124

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: 353.10  E-value: 1.20e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  35 FNPYTDNGGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGGTTadnsdatlVLSVVGFAADGEALKERLDAICK 114
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKC--------VLGSSGFQADILALTKRLKARIK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 115 IYRYRHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQV 194
Cdd:cd03757   73 MYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389626457 195 NFKNQYVpgsgtghdlqeRERKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIEEVIMPLKKD 265
Cdd:cd03757  153 GRKNQNN-----------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 39-193 3.00e-33

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: 119.59  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457   39 TDNGGSTLAIAGDDFAIMAGDTRMASGYSINTR-FYPKVFKIGGTtadnsdatLVLSVVGFAADGEALKERLDAICKIYR 117
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDH--------IGMAFAGLAADARTLVDRARAEAQLYR 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389626457  118 YRHGKPMTVKAC---AKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQ 193
Cdd:pfam00227  73 LRYGRPIPVELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKL 151
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 11-258 1.33e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 116.40  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  11 MNGPN-YAFSDTPRVNAPGGARQHGFNPYTDN--GGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggttadns 87
Cdd:COG0638    1 MQPSQqSSYDRAITIFSPDGRLYQVEYAREAVkrGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKI-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  88 DATLVLSVVGFAADGEALKERLDAICKIYRYRHGKPMTVKACAKRLSTILY---QKRFFPYYTHAILAGIDEEGhGAVYS 164
Cdd:COG0638   73 DDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 165 YDPVGSYEREQCRAGGAAASLIMPFLdnqvnfKNQYVPGsgtghdlqererkpLPRETVETLVKDAFDGAVERHIEVGDG 244
Cdd:COG0638  152 TDPSGGLYEEKAVAIGSGSPFARGVL------EKEYRED--------------LSLDEAVELALRALYSAAERDSASGDG 211

                        250
                 ....*....|....
gi 389626457 245 LQMMIITKDGIEEV 258
Cdd:COG0638  212 IDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 18-233 3.49e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.07  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  18 FSDTPRVNAPGGARQHGF-NPYTDNGGS------------TLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggtta 84
Cdd:PTZ00488   2 FCGPEHFEHPPGAHPGDFlAEYTFDHGDankaiefahgttTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEI----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  85 dnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGaVYS 164
Cdd:PTZ00488  77 ---NPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFY 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 165 YDPVGSYEREQCRAGGAAASLIMPFLDnqvnfknqyvpgSGTGHDLQERERKPLPRETV-ETLVKDAFDG 233
Cdd:PTZ00488 153 VDNDGTRLHGNMFSCGSGSTYAYGVLD------------AGFKWDLNDEEAQDLGRRAIyHATFRDAYSG 210
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-265 1.20e-124

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: 353.10  E-value: 1.20e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  35 FNPYTDNGGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGGTTadnsdatlVLSVVGFAADGEALKERLDAICK 114
Cdd:cd03757    1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKC--------VLGSSGFQADILALTKRLKARIK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 115 IYRYRHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQV 194
Cdd:cd03757   73 MYKYSHNKEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389626457 195 NFKNQYVpgsgtghdlqeRERKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIEEVIMPLKKD 265
Cdd:cd03757  153 GRKNQNN-----------VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-258 1.32e-61

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: 192.27  E-value: 1.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  43 GSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGgttaDNsdatLVLSVVGFAADGEALKERLDAICKIYRYRHGK 122
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKIS----DN----ILLGTAGSAADTQALTRLLKRNLRLYELRNGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 123 PMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQVnfknqyvp 202
Cdd:cd01912   73 ELSVKAAANLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY-------- 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389626457 203 gsgtghdlqereRKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIEEV 258
Cdd:cd01912  145 ------------KPDMTLEEAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 43-250 1.55e-45

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: 151.11  E-value: 1.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  43 GSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGgttaDNsdatLVLSVVGFAADGEALKERLDAICKIYRYRHGK 122
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKID----DH----IGCAFAGLAADAQTLVERLRKEAQLYRLRYGE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 123 PMTVKACAKRLSTILYQKRF--FPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQVnfknqy 200
Cdd:cd01906   73 PIPVEALAKLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY------ 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 389626457 201 vpgsgtghdlqereRKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMII 250
Cdd:cd01906  147 --------------KPDMTLEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 39-193 3.00e-33

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: 119.59  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457   39 TDNGGSTLAIAGDDFAIMAGDTRMASGYSINTR-FYPKVFKIGGTtadnsdatLVLSVVGFAADGEALKERLDAICKIYR 117
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDH--------IGMAFAGLAADARTLVDRARAEAQLYR 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389626457  118 YRHGKPMTVKAC---AKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQ 193
Cdd:pfam00227  73 LRYGRPIPVELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKL 151
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 11-258 1.33e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 116.40  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  11 MNGPN-YAFSDTPRVNAPGGARQHGFNPYTDN--GGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggttadns 87
Cdd:COG0638    1 MQPSQqSSYDRAITIFSPDGRLYQVEYAREAVkrGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKI-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  88 DATLVLSVVGFAADGEALKERLDAICKIYRYRHGKPMTVKACAKRLSTILY---QKRFFPYYTHAILAGIDEEGhGAVYS 164
Cdd:COG0638   73 DDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 165 YDPVGSYEREQCRAGGAAASLIMPFLdnqvnfKNQYVPGsgtghdlqererkpLPRETVETLVKDAFDGAVERHIEVGDG 244
Cdd:COG0638  152 TDPSGGLYEEKAVAIGSGSPFARGVL------EKEYRED--------------LSLDEAVELALRALYSAAERDSASGDG 211

                        250
                 ....*....|....
gi 389626457 245 LQMMIITKDGIEEV 258
Cdd:COG0638  212 IDVAVITEDGFREL 225
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-258 2.74e-29

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: 109.26  E-value: 2.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  45 TLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHGKPM 124
Cdd:cd03764    3 TVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQI--------DDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 125 TVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGhGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDnqvnfkNQYVPGS 204
Cdd:cd03764   75 SIKALATLLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE------DEYKEDM 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 389626457 205 GTghdlqererkplpRETVETLVKdAFDGAVERHIEVGDGLQMMIITKDGIEEV 258
Cdd:cd03764  148 TV-------------EEAKKLAIR-AIKSAIERDSASGDGIDVVVITKDGYKEL 187
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 43-197 2.06e-27

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: 103.63  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  43 GSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHGK 122
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKN--------EDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGE 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389626457 123 PMTVKACAKRLSTILYQKRF-FPYYTHAILAGIDEEGhGAVYSYDPVGSY-EREQCRAGGAAASLIMPFLDNQVNFK 197
Cdd:cd01901   73 PISVVALAKELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPViENPGAVATGSRSQRAKSLLEKLYKPD 148
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 41-255 4.93e-23

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: 93.08  E-value: 4.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  41 NGGSTLAIAGDD-FAIMAgDTRM-ASGYSINTRFyPKVFKIGgttaDNsdatLVLSVVGFAADGEALKERLDAICKIYRY 118
Cdd:cd03759    2 NGGAVVAMAGKDcVAIAS-DLRLgVQQQTVSTDF-QKVFRIG----DR----LYIGLAGLATDVQTLAQKLRFRVNLYRL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 119 RHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYDPVG--SYEREQCRAGGAAASLiMPFLDnqvnf 196
Cdd:cd03759   72 REEREIKPKTFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcpSIPSDFVVSGTASEQL-YGMCE----- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 389626457 197 kNQYVPGSGtghdlqererkplPRETVETLVKdAFDGAVERHIEVGDGLQMMIITKDGI 255
Cdd:cd03759  146 -SLWRPDME-------------PDELFETISQ-ALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 40-171 4.44e-13

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: 66.31  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  40 DNGGSTLAIAGDDFAIMAGDTRMASGYsINTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYR 119
Cdd:cd01911   25 KNGSTAVGIKGKDGVVLAVEKKVTSKL-LDPSSVEKIFKI--------DDHIGCAVAGLTADARVLVNRARVEAQNYRYT 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389626457 120 HGKPMTVKACAKRLSTIL------YQKRffPYYTHAILAGIDEEGHGAVYSYDPVGSY 171
Cdd:cd01911   96 YGEPIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTY 151
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 46-259 3.74e-12

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: 63.40  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  46 LAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggttADNsdatLVLSVVGFAADGEALKERLDAICKIYRYRHGKPMT 125
Cdd:cd03762    4 IAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQL----HDR----IYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 126 VKACAKRLSTILYQKRFFpYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNqvNFKnqyvPGSG 205
Cdd:cd03762   76 VKTAASLFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDA--NYK----PGMT 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 389626457 206 tghdlqererkplpRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIEEVI 259
Cdd:cd03762  149 --------------LEECIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-191 1.95e-09

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: 55.67  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  44 STLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGGTtadnsdatLVLSVVGFAADGEALKERLDAICKIYRYRHGKP 123
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDH--------KLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 389626457 124 MTVKACA----KRLSTILyqKRFFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLD 191
Cdd:cd03758   75 LSPKAAAnftrRELAESL--RSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILD 144
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-256 1.35e-08

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: 53.34  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  42 GGSTLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIGGTTadnsdatlVLSVVGFAADGEALKERLD-AICKIYRYRH 120
Cdd:cd03760    2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNT--------LLGASGDYADFQYLKRLLDqLVIDDECLDD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 121 GKPMTVKACAKRLSTILYQKR--FFPYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLDNQVnfkn 198
Cdd:cd03760   74 GHSLSPKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAW---- 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389626457 199 qyvpgsgtghdlqeRERKPLPRETVETLVKDAFDGAVERHIEVGDGLQMMIITKDGIE 256
Cdd:cd03760  150 --------------EKKPDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 18-233 3.49e-08

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 53.07  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  18 FSDTPRVNAPGGARQHGF-NPYTDNGGS------------TLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIggtta 84
Cdd:PTZ00488   2 FCGPEHFEHPPGAHPGDFlAEYTFDHGDankaiefahgttTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEI----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  85 dnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHGKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGaVYS 164
Cdd:PTZ00488  77 ---NPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFY 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 165 YDPVGSYEREQCRAGGAAASLIMPFLDnqvnfknqyvpgSGTGHDLQERERKPLPRETV-ETLVKDAFDG 233
Cdd:PTZ00488 153 VDNDGTRLHGNMFSCGSGSTYAYGVLD------------AGFKWDLNDEEAQDLGRRAIyHATFRDAYSG 210
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-166 7.50e-08

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: 51.09  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  45 TLAIAGDDFAIMAGDTRMASGYSINTRFYPKVFKIG----GTTAdnsdatlvlsvvGFAADGEALKERLDAICKIYRYRH 120
Cdd:cd03761    3 TLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINpyllGTMA------------GGAADCQYWERVLGRECRLYELRN 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 389626457 121 GKPMTVKACAKRLSTILYQKRFFPYYTHAILAGIDEEGHGAVYSYD 166
Cdd:cd03761   71 KERISVAAASKLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDS 116
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 42-171 7.51e-07

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


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 48.77  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  42 GGSTLAIAGDDFAIMAGDTRMASGYsINTRFYPKVFKIGGTTAdnsdatlvLSVVGFAADGEALKERLDAICKIYRYRHG 121
Cdd:cd03754   29 GLTSVAVRGKDCAVVVTQKKVPDKL-IDPSTVTHLFRITDEIG--------CVMTGMIADSRSQVQRARYEAAEFKYKYG 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 389626457 122 KPMTVKACAKRLSTI--LYQKRFF--PYYTHAILAGIDEEGHGAVYSYDPVGSY 171
Cdd:cd03754  100 YEMPVDVLAKRIADInqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYF 153
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 40-198 4.47e-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: 46.13  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  40 DNGGSTLAIAGDDFAIMAGDTRMASGYSintRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYR 119
Cdd:cd03749   25 KQGSATVGLKSKTHAVLVALKRATSELS---SYQKKIFKV--------DDHIGIAIAGLTADARVLSRYMRQECLNYRFV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457 120 HGKPMTVKACAKRLS------TILYQKRffPYYTHAILAGIDEEG-HgaVYSYDPVGSYEREQCRAGGAAASLIMPFLDN 192
Cdd:cd03749   94 YDSPIPVSRLVSKVAekaqinTQRYGRR--PYGVGLLIAGYDESGpH--LFQTCPSGNYFEYKATSIGARSQSARTYLER 169


                 ....*..
gi 389626457 193 QV-NFKN 198
Cdd:cd03749  170 HFeEFED 176
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 40-171 1.10e-05

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: 45.35  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  40 DNGGSTLAIAGDDFAIMAGDTRMASGYSI---NTRFYpkvfkiggttadNSDATLVLSVVGFAADGEALKERLDAICKIY 116
Cdd:cd03751   28 ENSGTAIGIRCKDGVVLAVEKLVTSKLYEpgsNKRIF------------NVDRHIGIAVAGLLADGRHLVSRAREEAENY 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389626457 117 RYRHGKPMTVKACAKRLS------TILYQKRffPYYTHAILAGIDEEGhGAVYSYDPVGSY 171
Cdd:cd03751   96 RDNYGTPIPVKVLADRVAmymhayTLYSSVR--PFGCSVLLGGYDSDG-PQLYMIEPSGVS 153
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-183 1.42e-05

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: 45.02  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  43 GST-LAIAGDDFAIMAGDTRMASGYSINTRFyPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHG 121
Cdd:cd03753   27 GSTaIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEI--------DDHIGCAMSGLIADARTLIDHARVEAQNHRFTYN 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389626457 122 KPMTVKACAKRLSTILYQkrfF------------PYYTHAILAGIDEEGhGAVYSYDPVGSYEREQCRAGGAAA 183
Cdd:cd03753   98 EPMTVESVTQAVSDLALQ---FgegddgkkamsrPFGVALLIAGVDENG-PQLFHTDPSGTFTRCDAKAIGSGS 167
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 42-191 1.71e-05

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: 44.63  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  42 GGSTLAIAGDDFAIMAGDTRMASGYsINTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHG 121
Cdd:cd03756   28 GTTALGIKCKEGVVLAVDKRITSKL-VEPESIEKIYKI--------DDHVGAATSGLVADARVLIDRARVEAQIHRLTYG 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389626457 122 KPMTVKACAKRLSTILYQKRFF----PYYTHAILAGIDEEGhGAVYSYDPVGSYEREQCRAGGAAASLIMPFLD 191
Cdd:cd03756   99 EPIDVEVLVKKICDLKQQYTQHggvrPFGVALLIAGVDDGG-PRLFETDPSGAYNEYKATAIGSGRQAVTEFLE 171
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
42-190 3.82e-05

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 43.67  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  42 GGSTLAIAGDDFAIMAGDTRMASGYsINTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHG 121
Cdd:PRK03996  36 GTTAVGVKTKDGVVLAVDKRITSPL-IEPSSIEKIFKI--------DDHIGAASAGLVADARVLIDRARVEAQINRLTYG 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389626457 122 KPMTVKACAKRLSTILYQKRFF----PYYTHAILAGIDEEGhGAVYSYDPVGSYEREQCRAGGAAASLIMPFL 190
Cdd:PRK03996 107 EPIGVETLTKKICDHKQQYTQHggvrPFGVALLIAGVDDGG-PRLFETDPSGAYLEYKATAIGAGRDTVMEFL 178
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 42-191 2.81e-03

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: 38.11  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389626457  42 GGSTLAIAGDDFAIMAGDTRMASGYSiNTRFYPKVFKIggttadnsDATLVLSVVGFAADGEALKERLDAICKIYRYRHG 121
Cdd:cd03755   27 GTTAVGVRGKDCVVLGVEKKSVAKLQ-DPRTVRKICML--------DDHVCLAFAGLTADARVLINRARLECQSHRLTVE 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 389626457 122 KPMTVKACAKRLSTIlyQKRFF------PYYTHAILAGIDEEGHGAVYSYDPVGSYEREQCRAGGAAASLIMPFLD 191
Cdd:cd03755   98 DPVTVEYITRYIAGL--QQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLE 171
 
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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