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Conserved domains on  [gi|307611968|ref|NP_001182643|]
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proteasome subunit beta type-6 [Macaca mulatta]

Protein Classification

proteasome subunit beta type-6 family protein( domain architecture ID 10132932)

proteasome subunit beta type-6 family protein, similar to proteasome subunit beta type-6 and type-9, is part of the 20S proteasome, a multi-subunit proteolytic complex that is central in nonlysosomal protein degradation in both the cytosol and nucleus.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-222 1.31e-133

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: 373.87  E-value: 1.31e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL 194
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*...
gi 307611968 195 ALAMERDGSSGGVIRLAAIAESGVERQV 222
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-222 1.31e-133

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: 373.87  E-value: 1.31e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL 194
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*...
gi 307611968 195 ALAMERDGSSGGVIRLAAIAESGVERQV 222
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-213 1.66e-55

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: 175.83  E-value: 1.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968   31 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  110 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEE 185
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 307611968  186 CLQFTANALALAMERDGSSGGVIRLAAI 213
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 30-220 2.58e-37

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 130.27  E-value: 2.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  30 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:COG0638   31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 110 VHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSYIYGYVDATYREGMTKE 184
Cdd:COG0638  111 VEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPFARGVLEKEYREDLSLD 188

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 307611968 185 ECLQFTANALALAMERDGSSGGVIRLAAIAESGVER 220
Cdd:COG0638  189 EAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 34-218 9.86e-35

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: 122.32  E-value: 9.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968   34 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 113
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  114 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTA 191
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 307611968  192 NALALAMERDGSSGGVIRLAAIAESGV 218
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 30-217 4.57e-26

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 101.60  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  30 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 110 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKEECL 187
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 307611968 188 QFTANALALAMERDGSSGGVIRLAAIAESG 217
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-222 1.31e-133

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: 373.87  E-value: 1.31e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL 194
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*...
gi 307611968 195 ALAMERDGSSGGVIRLAAIAESGVERQV 222
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-220 1.36e-79

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: 236.96  E-value: 1.36e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANA 193
Cdd:cd01912   81 NLLSNILYSYRGfPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*..
gi 307611968 194 LALAMERDGSSGGVIRLAAIAESGVER 220
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-213 1.95e-61

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: 190.78  E-value: 1.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYRE---DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTA 191
Cdd:cd01906   81 KLLANLLYEYTQslrPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                        170       180
                 ....*....|....*....|..
gi 307611968 192 NALALAMERDGSSGGVIRLAAI 213
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-213 1.66e-55

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: 175.83  E-value: 1.66e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968   31 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  110 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEE 185
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 307611968  186 CLQFTANALALAMERDGSSGGVIRLAAI 213
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-219 1.83e-38

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


Pssm-ID: 239732  Cd Length: 189  Bit Score: 132.32  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYREDLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAL 194
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                        170       180
                 ....*....|....*....|....*
gi 307611968 195 ALAMERDGSSGGVIRLAAIAESGVE 219
Cdd:cd03763  160 EAGIFNDLGSGSNVDLCVITKDGVE 184
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-194 3.55e-38

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: 130.59  E-value: 3.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYRE--DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAI-GGSGSSYIYGYVDATYREGMTKEECLQFTA 191
Cdd:cd01901   81 KELAKLLQVYTQgrPFGVNLIVAGVDE-GGGNLYYIDPSGPVIENPGAVaTGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                 ...
gi 307611968 192 NAL 194
Cdd:cd01901  160 KAL 162
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 30-220 2.58e-37

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 130.27  E-value: 2.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  30 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:COG0638   31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPIS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 110 VHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSYIYGYVDATYREGMTKE 184
Cdd:COG0638  111 VEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPFARGVLEKEYREDLSLD 188

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 307611968 185 ECLQFTANALALAMERDGSSGGVIRLAAIAESGVER 220
Cdd:COG0638  189 EAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-220 3.29e-36

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: 126.21  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYR-EDLMAGIIIAGWDpQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANA 193
Cdd:cd03761   81 KLLSNMLYQYKgMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                        170       180
                 ....*....|....*....|....*..
gi 307611968 194 LALAMERDGSSGGVIRLAAIAESGVER 220
Cdd:cd03761  160 IYHATHRDAYSGGNVNLYHVREDGWRK 186
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 34-218 9.86e-35

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: 122.32  E-value: 9.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968   34 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 113
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  114 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTA 191
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 307611968  192 NALALAMERDGSSGGVIRLAAIAESGV 218
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-220 2.53e-34

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: 121.59  E-value: 2.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  35 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 114
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 115 SLFKEMCYRYRE-DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANA 193
Cdd:cd03764   81 TLLSNILNSSKYfPYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                        170       180
                 ....*....|....*....|....*..
gi 307611968 194 LALAMERDGSSGGVIRLAAIAESGVER 220
Cdd:cd03764  160 IKSAIERDSASGDGIDVVVITKDGYKE 186
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 30-217 4.57e-26

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 101.60  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  30 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 109
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 110 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKEECL 187
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 307611968 188 QFTANALALAMERDGSSGGVIRLAAIAESG 217
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-187 6.41e-13

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: 64.91  E-value: 6.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  36 TIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAAS 115
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307611968 116 lF--KEMCY--RYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECL 187
Cdd:cd03758   83 -FtrRELAEslRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-205 1.11e-12

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: 64.57  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  32 STGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVH 111
Cdd:cd03759    1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 112 TAASLFKEMCYRYRED--LMAgIIIAGWDPQegGQVYSVPM---GGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEEC 186
Cdd:cd03759   81 TFSSLISSLLYEKRFGpyFVE-PVVAGLDPD--GKPFICTMdliGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDEL 157

                        170
                 ....*....|....*....
gi 307611968 187 LQFTANALALAMERDGSSG 205
Cdd:cd03759  158 FETISQALLSAVDRDALSG 176
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-223 4.55e-12

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: 63.05  E-value: 4.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  31 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 110
Cdd:cd03757    5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 111 HTAASLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDAT---------YREG 180
Cdd:cd03757   85 EAIAQLLSTILYSRRFfPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQvgrknqnnvERTP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 307611968 181 MTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVL 223
Cdd:cd03757  165 LSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 22-207 1.19e-11

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: 61.96  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  22 FTPDWE------SRE-VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVADAVT 94
Cdd:cd03756    9 FSPDGRlyqveyAREaVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESI-EKIYKIDDHVGAATSGLVADARVLIDRAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  95 YQLGFHSIELNEPPLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDPQeGGQVYSV-PMGGMMVRQSFA 160
Cdd:cd03756   88 VEAQIHRLTYGEPIDVEV---LVKKIC-----DLKqqytqhggvrpfgVALLIAGVDDG-GPRLFETdPSGAYNEYKATA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 307611968 161 IGgSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGV 207
Cdd:cd03756  159 IG-SGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENV 204
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 34-220 3.23e-11

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


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 60.88  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968   34 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAdtQAVADAVTYQLGFHSIELNE--PPLVH 111
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG--LAIELVRLFQVELEHYEKIEgvPLTLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  112 TAASLFKEMCyryREDL---MAGI----IIAGWD-PQEGGQVYSV-PMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMT 182
Cdd:TIGR03690  80 GKANRLAAMV---RGNLpaaMQGLavvpLLAGYDlDAGAGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLD 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 307611968  183 KEECLQFTANALALAMERDGSSGG--VIR-----LAAIAESGVER 220
Cdd:TIGR03690 157 EDDALRVAVEALYDAADDDSATGGpdLVRgiyptVVVITADGARR 201
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-204 3.60e-10

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: 57.84  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  31 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTdKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsielN 105
Cdd:cd01911   24 VKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVE-KIFKIDDHIGCAVAGLTADARVLVNrarveAQNYRYTY-----G 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 106 EPPLVhtaASLFKEMCyryreDLM-------------AGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIgGSGSSYIYG 171
Cdd:cd01911   98 EPIPV---EVLVKRIA-----DLAqvytqyggvrpfgVSLLIAGYDEEGGPQLYQTdPSGTYFGYKATAI-GKGSQEAKT 168

                        170       180       190
                 ....*....|....*....|....*....|...
gi 307611968 172 YVDATYREGMTKEECLQFTANALALAMERDGSS 204
Cdd:cd01911  169 FLEKRYKKDLTLEEAIKLALKALKEVLEEDKKA 201
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
29-207 6.46e-10

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 57.54  E-value: 6.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  29 RE-VSTGTTIMAVQFDGGVVLGADSRTTTgSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsi 102
Cdd:PRK03996  30 REaVKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDrarveAQINRLTY--- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 103 elNEPPLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIGgSGSSY 168
Cdd:PRK03996 106 --GEPIGVET---LTKKIC-----DHKqqytqhggvrpfgVALLIAGVD-DGGPRLFETdPSGAYLEYKATAIG-AGRDT 173

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 307611968 169 IYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGV 207
Cdd:PRK03996 174 VMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENV 212
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-199 7.60e-09

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: 53.88  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  34 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 113
Cdd:cd03753   27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 114 ASLFKEMCYRYRED-----LMA-----GIIIAGWDpQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTK 183
Cdd:cd03753  106 TQAVSDLALQFGEGddgkkAMSrpfgvALLIAGVD-ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184

                        170
                 ....*....|....*.
gi 307611968 184 EECLQFTANALALAME 199
Cdd:cd03753  185 EEAEKLALSILKQVME 200
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 33-219 1.13e-07

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: 50.65  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  33 TGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQavadAVTYQLGFHSIE--LNEPPLV 110
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQ----YLKRLLDQLVIDdeCLDDGHS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 111 HTAASLFKEMC---YRYRED---LMAGIIIAGWDPQeggqvysvpmggmmvrqsfaiggsGSSYIyGYVD---------- 174
Cdd:cd03760   77 LSPKEIHSYLTrvlYNRRSKmnpLWNTLVVGGVDNE------------------------GEPFL-GYVDllgtayedph 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307611968 175 -AT----------------YREGMTKEEclqftANALAL-AME----RDGSSGGVIRLAAIAESGVE 219
Cdd:cd03760  132 vATgfgaylalpllreaweKKPDLTEEE-----ARALIEeCMKvlyyRDARSINKYQIAVVTKEGVE 193
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-200 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: 50.42  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  31 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADT-----QAVADAVTYQLGFhsielN 105
Cdd:cd03752   26 ISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDAnilinYARLIAQRYLYSY-----Q 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 106 EPPLVhtaaslfkEMCYRYREDLMAG-------------IIIAGWDPQEGGQVY-SVPMGGMMVRQSFAIGGSGSSyIYG 171
Cdd:cd03752  101 EPIPV--------EQLVQRLCDIKQGytqygglrpfgvsFLYAGWDKHYGFQLYqSDPSGNYSGWKATAIGNNNQA-AQS 171

                        170       180
                 ....*....|....*....|....*....
gi 307611968 172 YVDATYREGMTKEECLQFTANALALAMER 200
Cdd:cd03752  172 LLKQDYKDDMTLEEALALAVKVLSKTMDS 200
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 43-199 2.02e-06

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 47.54  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  43 DGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAD-----TQAVADAVTYQLGFhsielNEPPLVhtaASLF 117
Cdd:PTZ00246  40 KEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADaniliNQCRLYAQRYRYTY-----GEPQPV---EQLV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 118 KEMCYRYREDLMAG--------IIIAGWDPQEGGQVY-SVPMGGMMVRQSFAIgGSGSSYIYGYVDATYREGMTKEECLQ 188
Cdd:PTZ00246 112 VQICDLKQSYTQFGglrpfgvsFLFAGYDENLGYQLYhTDPSGNYSGWKATAI-GQNNQTAQSILKQEWKEDLTLEQGLL 190

                        170
                 ....*....|.
gi 307611968 189 FTANALALAME 199
Cdd:PTZ00246 191 LAAKVLTKSMD 201
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-211 8.49e-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: 45.05  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968  31 VSTGTTIMAVQFDGGVVLGADsRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 110
Cdd:cd03755   24 VRKGTTAVGVRGKDCVVLGVE-KKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307611968 111 HTAASLFKEMCYRY-----REDLMAGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIGgSGSSYIYGYVDATYREGMTKE 184
Cdd:cd03755  103 EYITRYIAGLQQRYtqsggVRPFGISTLIVGFDPDGTPRLYQTdPSGTYSAWKANAIG-RNSKTVREFLEKNYKEEMTRD 181

                        170       180
                 ....*....|....*....|....*..
gi 307611968 185 ECLQFTANALALAMErdgSSGGVIRLA 211
Cdd:cd03755  182 DTIKLAIKALLEVVQ---SGSKNIELA 205
 
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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