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Conserved domains on  [gi|1720364642|ref|XP_030101534|]
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proteasome subunit beta type-6 isoform X1 [Mus musculus]

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 ...
 34-191 4.83e-112

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: 318.01  E-value: 4.83e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTAN 191
Cdd:cd03762    81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-191 4.83e-112

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: 318.01  E-value: 4.83e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTAN 191
Cdd:cd03762    81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-188 9.59e-48

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: 155.03  E-value: 9.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  30 VSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 109 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160


                  ....
gi 1720364642 185 CLQF 188
Cdd:pfam00227 161 AVEL 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-186 2.41e-30

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 111.39  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  15 AFGPEALTPDWEN--REVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAV 92
Cdd:COG0638    15 IFSPDGRLYQVEYarEAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  93 TYQLGFHSIELNEPPLVHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:COG0638    95 RVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPF 172

                         170
                  ....*....|....*....
gi 1720364642 168 IYGYVDATYREGMTKDECL 186
Cdd:COG0638   173 ARGVLEKEYREDLSLDEAV 191
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 33-184 5.44e-27

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: 101.52  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  33 GTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364642 113 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEE 152
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-184 3.07e-20

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 85.43  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  29 EVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:PTZ00488   35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 109 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKDE 184
Cdd:PTZ00488  115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEE 190
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-191 4.83e-112

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: 318.01  E-value: 4.83e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTAN 191
Cdd:cd03762    81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-188 2.14e-67

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: 204.98  E-value: 2.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364642 114 SLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQF 188
Cdd:cd01912    81 NLLSNILYSYRGfPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVEL 156
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 34-188 2.11e-53

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: 169.21  E-value: 2.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 114 SLFKEMCYRYRE---DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQF 188
Cdd:cd01906    81 KLLANLLYEYTQslrPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-188 9.59e-48

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: 155.03  E-value: 9.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  30 VSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 109 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160


                  ....
gi 1720364642 185 CLQF 188
Cdd:pfam00227 161 AVEL 164
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 34-187 2.21e-37

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: 127.51  E-value: 2.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364642 114 SLFKEMCYRYRE--DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAI-GGSGSSYIYGYVDATYREGMTKDECLQ 187
Cdd:cd01901    81 KELAKLLQVYTQgrPFGVNLIVAGVDE-GGGNLYYIDPSGPVIENPGAVaTGSRSQRAKSLLEKLYKPDMTLEEAVE 156
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-187 1.12e-33

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: 118.84  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364642 114 SLFKEMCYRYREDLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQ 187
Cdd:cd03763    81 TMLKQHLFRYQGHIGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKK 153
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-186 2.41e-30

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 111.39  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  15 AFGPEALTPDWEN--REVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAV 92
Cdd:COG0638    15 IFSPDGRLYQVEYarEAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  93 TYQLGFHSIELNEPPLVHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:COG0638    95 RVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPF 172

                         170
                  ....*....|....*....
gi 1720364642 168 IYGYVDATYREGMTKDECL 186
Cdd:COG0638   173 ARGVLEKEYREDLSLDEAV 191
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-184 6.61e-28

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: 103.86  E-value: 6.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03761     1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364642 114 SLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:cd03761    81 KLLSNMLYQYKgMGLSMGTMICGWDK-TGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEE 151
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 33-184 5.44e-27

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: 101.52  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  33 GTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364642 113 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEE 152
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-184 3.60e-26

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: 99.63  E-value: 3.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  34 TTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364642 114 SLFKEMCYRYRE-DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:cd03764    81 TLLSNILNSSKYfPYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEE 151
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-184 3.07e-20

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 85.43  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  29 EVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:PTZ00488   35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720364642 109 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKDE 184
Cdd:PTZ00488  115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEE 190
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-186 6.77e-14

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: 67.23  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  35 TIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAAS 114
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364642 115 lF--KEMCY--RYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECL 186
Cdd:cd03758    83 -FtrRELAEslRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 28-186 1.84e-10

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: 58.11  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  28 RE-VSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsi 101
Cdd:cd03756    22 REaVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESI-EKIYKIDDHVGAATSGLVADARVLIDrarveAQIHRLTY--- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 102 elNEPPLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDPQeGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:cd03756    98 --GEPIDVEV---LVKKIC-----DLKqqytqhggvrpfgVALLIAGVDDG-GPRLFETdPSGAYNEYKATAI-GSGRQA 165

                         170
                  ....*....|....*....
gi 1720364642 168 IYGYVDATYREGMTKDECL 186
Cdd:cd03756   166 VTEFLEKEYKEDMSLEEAI 184
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-184 1.38e-09

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: 55.33  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  31 STGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVH 110
Cdd:cd03759     1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364642 111 TAASLFKEMCYRYRED--LMAgIIIAGWDPQegGQVYSVPM---GGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:cd03759    81 TFSSLISSLLYEKRFGpyFVE-PVVAGLDPD--GKPFICTMdliGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 33-187 1.73e-09

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: 55.48  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  33 GTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAdtQAVADAVTYQLGFHSIELNE--PPLVH 110
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG--LAIELVRLFQVELEHYEKIEgvPLTLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 111 TAASLFKEMCyryREDL---MAGI----IIAGWD-PQEGGQVYSV-PMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMT 181
Cdd:TIGR03690  80 GKANRLAAMV---RGNLpaaMQGLavvpLLAGYDlDAGAGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLD 156


                  ....*.
gi 1720364642 182 KDECLQ 187
Cdd:TIGR03690 157 EDDALR 162
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 33-184 4.58e-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: 54.27  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  33 GTTIMAVQFNGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:cd03753    27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 113 ASLFKEMCYRYRED-----LMA-----GIIIAGWDpQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTK 182
Cdd:cd03753   106 TQAVSDLALQFGEGddgkkAMSrpfgvALLIAGVD-ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184


                  ..
gi 1720364642 183 DE 184
Cdd:cd03753   185 EE 186
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-187 2.07e-08

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: 52.45  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  30 VSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTdKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsielN 104
Cdd:cd01911    24 VKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVE-KIFKIDDHIGCAVAGLTADARVLVNrarveAQNYRYTY-----G 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 105 EPPLVhtaASLFKEMCyryreDLM-------------AGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIgGSGSSYIYG 170
Cdd:cd01911    98 EPIPV---EVLVKRIA-----DLAqvytqyggvrpfgVSLLIAGYDEEGGPQLYQTdPSGTYFGYKATAI-GKGSQEAKT 168

                         170
                  ....*....|....*..
gi 1720364642 171 YVDATYREGMTKDECLQ 187
Cdd:cd01911   169 FLEKRYKKDLTLEEAIK 185
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
28-186 5.42e-08

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 51.37  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  28 RE-VSTGTTIMAVQFNGGVVLGADSRTTTgSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsi 101
Cdd:PRK03996   30 REaVKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDrarveAQINRLTY--- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 102 elNEPPLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:PRK03996  106 --GEPIGVET---LTKKIC-----DHKqqytqhggvrpfgVALLIAGVD-DGGPRLFETdPSGAYLEYKATAI-GAGRDT 173

                         170
                  ....*....|....*....
gi 1720364642 168 IYGYVDATYREGMTKDECL 186
Cdd:PRK03996  174 VMEFLEKNYKEDLSLEEAI 192
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-192 1.34e-07

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: 49.95  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  30 VSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 109
Cdd:cd03757     5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 110 HTAASLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDAT---------YREG 179
Cdd:cd03757    85 EAIAQLLSTILYSRRFfPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQvgrknqnnvERTP 164

                         170
                  ....*....|...
gi 1720364642 180 MTKDECLQFTANV 192
Cdd:cd03757   165 LSLEEAVSLVKDA 177
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-86 4.20e-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: 48.34  E-value: 4.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364642  32 TGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQ 86
Cdd:cd03760     1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQ 55
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 42-192 2.50e-05

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 43.69  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  42 NGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAD-----TQAVADAVTYQLGFhsielNEPPLVhtaASLF 116
Cdd:PTZ00246   40 KEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADaniliNQCRLYAQRYRYTY-----GEPQPV---EQLV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 117 KEMCYRYREDLMAG--------IIIAGWDPQEGGQVY-SVPMGGMMVRQSFAIgGSGSSYIYGYVDATYREGMTKDECLQ 187
Cdd:PTZ00246  112 VQICDLKQSYTQFGglrpfgvsFLFAGYDENLGYQLYhTDPSGNYSGWKATAI-GQNNQTAQSILKQEWKEDLTLEQGLL 190


                  ....*
gi 1720364642 188 FTANV 192
Cdd:PTZ00246  191 LAAKV 195
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-189 7.40e-05

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: 41.97  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642  30 VSTGTTIMAVQFNGGVVLGADsRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 109
Cdd:cd03755    24 VRKGTTAVGVRGKDCVVLGVE-KKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364642 110 HTAASLFKEMCYRY-----REDLMAGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIGgSGSSYIYGYVDATYREGMTKD 183
Cdd:cd03755   103 EYITRYIAGLQQRYtqsggVRPFGISTLIVGFDPDGTPRLYQTdPSGTYSAWKANAIG-RNSKTVREFLEKNYKEEMTRD 181


                  ....*.
gi 1720364642 184 ECLQFT 189
Cdd:cd03755   182 DTIKLA 187
 
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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