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Conserved domains on  [gi|54019419|ref|NP_476440|]
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proteasome subunit beta type-6 [Rattus norvegicus]

Protein Classification

proteasome subunit beta( domain architecture ID 10132932)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-221 1.08e-131

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: 368.86  E-value: 1.08e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANAL 193
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 54019419 194 ALAMERDGSSGGVIRLAAIQQSGVERQV 221
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 ...
 34-221 1.08e-131

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: 368.86  E-value: 1.08e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANAL 193
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 54019419 194 ALAMERDGSSGGVIRLAAIQQSGVERQV 221
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-212 3.75e-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: 174.68  E-value: 3.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419    30 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   109 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 54019419   185 CLQFTANALALAMERDGSSGGVIRLAAI 212
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-219 2.37e-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: 2.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  15 AFGPEALTPDWEN--REVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAV 92
Cdd:COG0638  15 IFSPDGRLYQVEYarEAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  93 TYQLGFHSIELNEPPLVHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:COG0638  95 RVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPF 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 54019419 168 IYGYVDATYREGMTKDECLQFTANALALAMERDGSSGGVIRLAAIQQSGVER 219
Cdd:COG0638 173 ARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 33-217 6.98e-34

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: 120.01  E-value: 6.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419    33 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   113 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTA 190
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 54019419   191 NALALAMERDGSSGGVIRLAAIQQSGV 217
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-216 4.01e-27

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 104.30  E-value: 4.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   29 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  109 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKDECL 186
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 54019419  187 QFTANALALAMERDGSSGGVIRLAAIQQSG 216
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 ...
 34-221 1.08e-131

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: 368.86  E-value: 1.08e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANAL 193
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 54019419 194 ALAMERDGSSGGVIRLAAIQQSGVERQV 221
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-219 8.32e-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: 235.03  E-value: 8.32e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANA 192
Cdd:cd01912  81 NLLSNILYSYRGfPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*..
gi 54019419 193 LALAMERDGSSGGVIRLAAIQQSGVER 219
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEE 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 34-212 9.15e-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: 188.86  E-value: 9.15e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYRE---DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTA 190
Cdd:cd01906  81 KLLANLLYEYTQslrPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 54019419 191 NALALAMERDGSSGGVIRLAAI 212
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 30-212 3.75e-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: 174.68  E-value: 3.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419    30 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVT-DKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   109 V----HTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDE 184
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 54019419   185 CLQFTANALALAMERDGSSGGVIRLAAI 212
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-218 6.89e-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: 130.78  E-value: 6.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYREDLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANAL 193
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180
                ....*....|....*....|....*
gi 54019419 194 ALAMERDGSSGGVIRLAAIQQSGVE 218
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDGVE 184
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 34-193 9.10e-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: 129.44  E-value: 9.10e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYRE--DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAI-GGSGSSYIYGYVDATYREGMTKDECLQFTA 190
Cdd:cd01901  81 KELAKLLQVYTQgrPFGVNLIVAGVDE-GGGNLYYIDPSGPVIENPGAVaTGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ...
gi 54019419 191 NAL 193
Cdd:cd01901 160 KAL 162
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-219 2.37e-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: 2.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  15 AFGPEALTPDWEN--REVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAV 92
Cdd:COG0638  15 IFSPDGRLYQVEYarEAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  93 TYQLGFHSIELNEPPLVHTAASLFKEMCYRYRED----LMAGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIgGSGSSY 167
Cdd:COG0638  95 RVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVD-DGGPRLFSTdPSGGLYEEKAVAI-GSGSPF 172

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 54019419 168 IYGYVDATYREGMTKDECLQFTANALALAMERDGSSGGVIRLAAIQQSGVER 219
Cdd:COG0638 173 ARGVLEKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-219 4.36e-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: 125.82  E-value: 4.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYR-EDLMAGIIIAGWDpQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANA 192
Cdd:cd03761  81 KLLSNMLYQYKgMGLSMGTMICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*..
gi 54019419 193 LALAMERDGSSGGVIRLAAIQQSGVER 219
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRK 186
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 33-217 6.98e-34

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: 120.01  E-value: 6.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419    33 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   113 ASLFKEMCYRYR-EDLMAGIIIAGWDPqEGGQVYSV-PMGGMMvRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTA 190
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdPAGGII-EDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 54019419   191 NALALAMERDGSSGGVIRLAAIQQSGV 217
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-219 1.48e-33

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: 119.28  E-value: 1.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  34 TTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAA 113
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 114 SLFKEMCYRYRE-DLMAGIIIAGWDPqEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANA 192
Cdd:cd03764  81 TLLSNILNSSKYfPYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*..
gi 54019419 193 LALAMERDGSSGGVIRLAAIQQSGVER 219
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKE 186
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-216 4.01e-27

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 104.30  E-value: 4.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   29 EVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPL 108
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  109 VHTAASLFKEMCYRYRE-DLMAGIIIAGWDpQEGGQVYSVPMGGM-MVRQSFAIgGSGSSYIYGYVDATYREGMTKDECL 186
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWD-KKGPGLFYVDNDGTrLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 54019419  187 QFTANALALAMERDGSSGGVIRLAAIQQSG 216
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-186 6.06e-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: 65.30  E-value: 6.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  35 TIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAAS 114
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54019419 115 lF--KEMCY--RYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECL 186
Cdd:cd03758  83 -FtrRELAEslRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEAL 157
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-204 9.29e-13

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: 9.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  31 STGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVH 110
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 111 TAASLFKEMCYRYRED--LMAgIIIAGWDPQegGQVYSVPM---GGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDEC 185
Cdd:cd03759  81 TFSSLISSLLYEKRFGpyFVE-PVVAGLDPD--GKPFICTMdliGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDEL 157

                       170
                ....*....|....*....
gi 54019419 186 LQFTANALALAMERDGSSG 204
Cdd:cd03759 158 FETISQALLSAVDRDALSG 176
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 28-206 2.38e-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: 61.19  E-value: 2.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  28 RE-VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEP 106
Cdd:cd03756  22 REaVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESI-EKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 107 PLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDPQeGGQVYSV-PMGGMMVRQSFAIGgSGSSYIYGYV 172
Cdd:cd03756 101 IDVEV---LVKKIC-----DLKqqytqhggvrpfgVALLIAGVDDG-GPRLFETdPSGAYNEYKATAIG-SGRQAVTEFL 170

                       170       180       190
                ....*....|....*....|....*....|....
gi 54019419 173 DATYREGMTKDECLQFTANALALAMERDGSSGGV 206
Cdd:cd03756 171 EKEYKEDMSLEEAIELALKALYAALEENETPENV 204
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 33-205 3.42e-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: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419    33 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAdtQAVADAVTYQLGFHSIELNE--PPLVH 110
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAG--LAIELVRLFQVELEHYEKIEgvPLTLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   111 TAASLFKEMCyryREDL---MAGI----IIAGWD-PQEGGQVYSV-PMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMT 181
Cdd:TIGR03690  80 GKANRLAAMV---RGNLpaaMQGLavvpLLAGYDlDAGAGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLD 156

                         170       180
                  ....*....|....*....|....
gi 54019419   182 KDECLQFTANALALAMERDGSSGG 205
Cdd:TIGR03690 157 EDDALRVAVEALYDAADDDSATGG 180
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-222 6.49e-11

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: 59.97  E-value: 6.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  30 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 109
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 110 HTAASLFKEMCYRYRE-DLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDAT---------YREG 179
Cdd:cd03757  85 EAIAQLLSTILYSRRFfPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQvgrknqnnvERTP 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 54019419 180 MTKDECLQFTANALALAMERDGSSGGVIRLAAIQQSGVERQVL 222
Cdd:cd03757 165 LSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
28-206 5.67e-10

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 57.54  E-value: 5.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   28 RE-VSTGTTIMAVQFDGGVVLGADSRTTTgSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsi 101
Cdd:PRK03996  30 REaVKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDrarveAQINRLTY--- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  102 elNEPPLVHTaasLFKEMCyryreDLM-------------AGIIIAGWDpQEGGQVYSV-PMGGMMVRQSFAIGgSGSSY 167
Cdd:PRK03996 106 --GEPIGVET---LTKKIC-----DHKqqytqhggvrpfgVALLIAGVD-DGGPRLFETdPSGAYLEYKATAIG-AGRDT 173

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 54019419  168 IYGYVDATYREGMTKDECLQFTANALALAMERDGSSGGV 206
Cdd:PRK03996 174 VMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENV 212
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-203 7.00e-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: 57.07  E-value: 7.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  30 VSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTdKLTPIHDHIFCCRSGSAADTQAVAD-----AVTYQLGFhsielN 104
Cdd:cd01911  24 VKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVE-KIFKIDDHIGCAVAGLTADARVLVNrarveAQNYRYTY-----G 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 105 EPPLVhtaASLFKEMCyryreDLM-------------AGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIgGSGSSYIYG 170
Cdd:cd01911  98 EPIPV---EVLVKRIA-----DLAqvytqyggvrpfgVSLLIAGYDEEGGPQLYQTdPSGTYFGYKATAI-GKGSQEAKT 168

                       170       180       190
                ....*....|....*....|....*....|...
gi 54019419 171 YVDATYREGMTKDECLQFTANALALAMERDGSS 203
Cdd:cd01911 169 FLEKRYKKDLTLEEAIKLALKALKEVLEEDKKA 201
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 33-198 1.00e-08

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: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  33 GTTIMAVQFDGGVVLGADSRTTTGSYIANRVtDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTA 112
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 113 ASLFKEMCYRYRED-----LMA-----GIIIAGWDpQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTK 182
Cdd:cd03753 106 TQAVSDLALQFGEGddgkkAMSrpfgvALLIAGVD-ENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTL 184

                       170
                ....*....|....*.
gi 54019419 183 DECLQFTANALALAME 198
Cdd:cd03753 185 EEAEKLALSILKQVME 200
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-86 9.34e-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: 47.95  E-value: 9.34e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 54019419  32 TGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQ 86
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQ 55
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 42-198 2.14e-06

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 47.15  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419   42 DGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAAD-----TQAVADAVTYQLGFhsielNEPPLVhtaASLF 116
Cdd:PTZ00246  40 KEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADaniliNQCRLYAQRYRYTY-----GEPQPV---EQLV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  117 KEMCYRYREDLMAG--------IIIAGWDPQEGGQVY-SVPMGGMMVRQSFAIgGSGSSYIYGYVDATYREGMTKDECLQ 187
Cdd:PTZ00246 112 VQICDLKQSYTQFGglrpfgvsFLFAGYDENLGYQLYhTDPSGNYSGWKATAI-GQNNQTAQSILKQEWKEDLTLEQGLL 190

                        170
                 ....*....|.
gi 54019419  188 FTANALALAME 198
Cdd:PTZ00246 191 LAAKVLTKSMD 201
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-210 6.58e-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: 45.43  E-value: 6.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419  30 VSTGTTIMAVQFDGGVVLGADsRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLV 109
Cdd:cd03755  24 VRKGTTAVGVRGKDCVVLGVE-KKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54019419 110 HTAASLFKEMCYRY-----REDLMAGIIIAGWDPQEGGQVYSV-PMGGMMVRQSFAIGgSGSSYIYGYVDATYREGMTKD 183
Cdd:cd03755 103 EYITRYIAGLQQRYtqsggVRPFGISTLIVGFDPDGTPRLYQTdPSGTYSAWKANAIG-RNSKTVREFLEKNYKEEMTRD 181

                       170       180
                ....*....|....*....|....*..
gi 54019419 184 ECLQFTANALALAMErdgSSGGVIRLA 210
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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