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Conserved domains on  [gi|47125243|gb|AAH70836|]
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MGC84496 protein [Xenopus laevis]

Protein Classification

proteasome subunit beta( domain architecture ID 10132911)

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_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 2.15e-127

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: 356.51  E-value: 2.15e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   1 MEYLIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 47125243 161 KKCISELQKRFILNLPSFTVRVIDKDGIHDLDS 193
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 2.15e-127

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: 356.51  E-value: 2.15e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   1 MEYLIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 47125243 161 KKCISELQKRFILNLPSFTVRVIDKDGIHDLDS 193
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 5.06e-53

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: 167.74  E-value: 5.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243     5 IGIQGNDFVLVAADT-VCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADKrATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243    84 TRRNLADYLRS-RTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLKK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
gi 47125243   163 CISELQKRFILNLPSFTVRVI 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 2.49e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 103.30  E-value: 2.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFt 84
Cdd:COG0638  39 VGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL- 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 rrnLADYLRSRT-----PYHVNLLLAGYDEHaGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVEL 159
Cdd:COG0638 118 ---LSDLLQGYTqygvrPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|...
gi 47125243 160 LKKCISELQKRFILNLPSFTVRVIDKDGIHDLD 192
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-164 5.21e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.22  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   13 VLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADYL 92
Cdd:PTZ00488  51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIV 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47125243   93 RSRTPYHVNL--LLAGYDEhAGPSLYYMDYL-SALAKTRFAAhGYGAYLTLSILDRYYKPDLTREDAVELLKKCI 164
Cdd:PTZ00488 127 WNYKGMGLSMgtMICGWDK-KGPGLFYVDNDgTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-193 2.15e-127

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: 356.51  E-value: 2.15e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   1 MEYLIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  81 ANFTRRNLADYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 47125243 161 KKCISELQKRFILNLPSFTVRVIDKDGIHDLDS 193
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-191 6.11e-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: 233.87  E-value: 6.11e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   2 EYLIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAA 81
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  82 NFTRRNLADYLRsrTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLK 161
Cdd:cd01912  81 NLLSNILYSYRG--FPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                       170       180       190
                ....*....|....*....|....*....|
gi 47125243 162 KCISELQKRFILNLPSFTVRVIDKDGIHDL 191
Cdd:cd01912 159 KAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 3-183 1.54e-60

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: 186.93  E-value: 1.54e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   3 YLIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAN 82
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  83 FTRRNLADYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLKK 162
Cdd:cd01906  82 LLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                       170       180
                ....*....|....*....|.
gi 47125243 163 CISELQKRFILNLPSFTVRVI 183
Cdd:cd01906 162 ALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 5.06e-53

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: 167.74  E-value: 5.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243     5 IGIQGNDFVLVAADT-VCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADKrATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243    84 TRRNLADYLRS-RTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLKK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
gi 47125243   163 CISELQKRFILNLPSFTVRVI 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-166 2.49e-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: 129.82  E-value: 2.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:cd01901   4 VAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKEL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 RRNLADYLRSRtPYHVNLLLAGYDEHaGPSLYYMDY-LSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLKKC 163
Cdd:cd01901  84 AKLLQVYTQGR-PFGVNLIVAGVDEG-GGNLYYIDPsGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALKA 161


                ...
gi 47125243 164 ISE 166
Cdd:cd01901 162 LKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 2.49e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 103.30  E-value: 2.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFt 84
Cdd:COG0638  39 VGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL- 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 rrnLADYLRSRT-----PYHVNLLLAGYDEHaGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVEL 159
Cdd:COG0638 118 ---LSDLLQGYTqygvrPFGVALLIGGVDDG-GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVEL 193

                       170       180       190
                ....*....|....*....|....*....|...
gi 47125243 160 LKKCISELQKRFILNLPSFTVRVIDKDGIHDLD 192
Cdd:COG0638 194 ALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-192 9.90e-25

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: 95.40  E-value: 9.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADT-VCANSIIQMKhDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03764   4 VGIVCKDGVVLAADKrASMGNFIASK-NVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  84 trrnLADYLRSR--TPYHVNLLLAGYDEHaGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLK 161
Cdd:cd03764  83 ----LSNILNSSkyFPYIVQLLIGGVDEE-GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 47125243 162 KCISELQKRFILNLPSFTVRVIDKDGIHDLD 192
Cdd:cd03764 158 RAIKSAIERDSASGDGIDVVVITKDGYKELE 188
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 6.57e-23

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: 91.17  E-value: 6.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:cd03757  12 LAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQLL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 RRNLadYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILD---------RYYKPDLTRED 155
Cdd:cd03757  92 STIL--YSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTPLSLEE 169

                       170       180       190
                ....*....|....*....|....*....|....
gi 47125243 156 AVELLKKCISELQKRFILNLPSFTVRVIDKDGIH 189
Cdd:cd03757 170 AVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 4.76e-21

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: 86.08  E-value: 4.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMR-NGYELSPTAAANF 83
Cdd:cd03760   6 IAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLdDGHSLSPKEIHSY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  84 TRRNLadY-LRSR-TPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYY--KPDLTREDAVEL 159
Cdd:cd03760  86 LTRVL--YnRRSKmNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWekKPDLTEEEARAL 163

                       170       180       190
                ....*....|....*....|....*....|
gi 47125243 160 LKKCISELQKRFILNLPSFTVRVIDKDGIH 189
Cdd:cd03760 164 IEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-188 2.50e-17

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: 76.13  E-value: 2.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   4 LIGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03759   6 VVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  84 TRRNLadYLRSRTPYHVNLLLAGYDEHAGPSLYYMDYLSALAKTR-FAAHGYGAYLTLSILDRYYKPDLTREDAVELLKK 162
Cdd:cd03759  86 ISSLL--YEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYGMCESLWRPDMEPDELFETISQ 163

                       170       180
                ....*....|....*....|....*.
gi 47125243 163 CISELQKRFILNLPSFTVRVIDKDGI 188
Cdd:cd03759 164 ALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-165 9.87e-14

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: 66.48  E-value: 9.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   4 LIGIQGNDFVLVAADT-VCANSIIQMKhDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAN 82
Cdd:cd03762   3 IIAVEYDGGVVLGADSrTSTGSYVANR-VTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  83 FTRrNLADYLRSRTPYHVnlLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELLKK 162
Cdd:cd03762  82 LFK-NLCYNYKEMLSAGI--IVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158


                ...
gi 47125243 163 CIS 165
Cdd:cd03762 159 ALS 161
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-166 1.34e-13

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 66.31  E-value: 1.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHdMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAnft 84
Cdd:cd01911  31 VGIKGKDGVVLAVEKKVTSKLLDPSS-VEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVEVLV--- 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 rRNLADYLRSRT------PYHVNLLLAGYDEHAGPSLYYMD----YLSALAktrfAAHGYGAYLTLSILDRYYKPDLTRE 154
Cdd:cd01911 107 -KRIADLAQVYTqyggvrPFGVSLLIAGYDEEGGPQLYQTDpsgtYFGYKA----TAIGKGSQEAKTFLEKRYKKDLTLE 181

                       170
                ....*....|..
gi 47125243 155 DAVELLKKCISE 166
Cdd:cd01911 182 EAIKLALKALKE 193
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-165 8.50e-12

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: 61.06  E-value: 8.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYElSPTAAANft 84
Cdd:cd03763   4 VGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRK-PRVVTAL-- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 rRNLADYLrsrTPYH----VNLLLAGYDeHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVELL 160
Cdd:cd03763  81 -TMLKQHL---FRYQghigAALVLGGVD-YTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLV 155


                ....*
gi 47125243 161 KKCIS 165
Cdd:cd03763 156 CEAIE 160
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 13-164 5.21e-09

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 54.22  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   13 VLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADYL 92
Cdd:PTZ00488  51 IIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIV 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47125243   93 RSRTPYHVNL--LLAGYDEhAGPSLYYMDYL-SALAKTRFAAhGYGAYLTLSILDRYYKPDLTREDAVELLKKCI 164
Cdd:PTZ00488 127 WNYKGMGLSMgtMICGWDK-KGPGLFYVDNDgTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-159 1.10e-08

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: 52.72  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQmKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGyelSPTAAANFT 84
Cdd:cd03756  32 LGIKCKEGVVLAVDKRITSKLVE-PESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYG---EPIDVEVLV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 RRnLADYLRSRT------PYHVNLLLAGYDEHaGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVE 158
Cdd:cd03756 108 KK-ICDLKQQYTqhggvrPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAIE 185


                .
gi 47125243 159 L 159
Cdd:cd03756 186 L 186
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-165 1.55e-08

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 52.35  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYkmRNGYElSPTAAANFT 84
Cdd:cd03752  33 LGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRY--LYSYQ-EPIPVEQLV 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  85 RRnLADYLRSRT------PYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVE 158
Cdd:cd03752 110 QR-LCDIKQGYTqygglrPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTLEEALA 188


                ....*..
gi 47125243 159 LLKKCIS 165
Cdd:cd03752 189 LAVKVLS 195
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 48-164 2.11e-07

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: 48.78  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  48 GEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADYlrSRTPYHVNLLLAGYDEHaGPSLYYMDYL-SALAK 126
Cdd:cd03761  47 GGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQY--KGMGLSMGTMICGWDKT-GPGLYYVDSDgTRLKG 123

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 47125243 127 TRFAAhGYGAYLTLSILDRYYKPDLTREDAVELLKKCI 164
Cdd:cd03761 124 DLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-166 6.72e-07

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 48.31  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243    5 IGIQGNDFVLVAADTVCANSIIQMKHDMDKMFKMSEKILLLCVGEAGDtvqfAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:PTZ00246  35 VGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTAD----ANILINQCRLYAQRYRYTYGEPQPVEQL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   85 RRNLADYLRSRT------PYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDAVE 158
Cdd:PTZ00246 111 VVQICDLKQSYTqfgglrPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLL 190


                 ....*...
gi 47125243  159 LLKKCISE 166
Cdd:PTZ00246 191 LAAKVLTK 198
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-167 7.42e-07

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: 47.74  E-value: 7.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAadtVCANSIIQMKHD--MDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRngYELSPTAAan 82
Cdd:cd03755  31 VGVRGKDCVVLG---VEKKSVAKLQDPrtVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLT--VEDPVTVE-- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  83 FTRRNLADYLRSRT------PYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPDLTREDA 156
Cdd:cd03755 104 YITRYIAGLQQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDT 183

                       170
                ....*....|.
gi 47125243 157 VELLKKCISEL 167
Cdd:cd03755 184 IKLAIKALLEV 194
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-165 6.48e-06

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


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 44.92  E-value: 6.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   5 IGIQGNDFVLVAADTVCANSIIQMKhDMDKMFKMSEKILLLCVGEAGDT---VQFAEYIQKNvqlYKMRNGYELSPTAAA 81
Cdd:cd03754  33 VAVRGKDCAVVVTQKKVPDKLIDPS-TVTHLFRITDEIGCVMTGMIADSrsqVQRARYEAAE---FKYKYGYEMPVDVLA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  82 nftrRNLADYLRSRT------PYHVNLLLAGYDEHAGPSLYYMDYLSALAKTRFAAHGYGAYLTLSILDRYYKPD----L 151
Cdd:cd03754 109 ----KRIADINQVYTqhaymrPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATAAGVKEQEATNFLEKKLKKKpdliE 184

                       170
                ....*....|....
gi 47125243 152 TREDAVELLKKCIS 165
Cdd:cd03754 185 SYEETVELAISCLQ 198
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 94-166 1.67e-05

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 43.86  E-value: 1.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243  94 SRtPYHVNLLLAGYDEHaGPSLYYMD----YLSALAKtrfaAHGYGAYLTLSILDRYYKPDLTREDA----VELLKKCIS 165
Cdd:cd03753 127 SR-PFGVALLIAGVDEN-GPQLFHTDpsgtFTRCDAK----AIGSGSEGAQSSLQEKYHKDMTLEEAeklaLSILKQVME 200


                .
gi 47125243 166 E 166
Cdd:cd03753 201 E 201
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-159 2.67e-04

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 40.59  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243    5 IGIQGNDFVLVAADT------VCANSIiqmkhdmDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGyelSPT 78
Cdd:PRK03996  40 VGVKTKDGVVLAVDKritsplIEPSSI-------EKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYG---EPI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47125243   79 AAANFTRRnLADYLRSRT------PYHVNLLLAGYDEHaGPSLY-------YMDYlSALAKtrfaahGYGAYLTLSILDR 145
Cdd:PRK03996 110 GVETLTKK-ICDHKQQYTqhggvrPFGVALLIAGVDDG-GPRLFetdpsgaYLEY-KATAI------GAGRDTVMEFLEK 180

                        170
                 ....*....|....
gi 47125243  146 YYKPDLTREDAVEL 159
Cdd:PRK03996 181 NYKEDLSLEEAIEL 194
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 97-157 6.72e-03

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 36.15  E-value: 6.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47125243  97 PYHVNLLLAGYDEhAGPSLYYMD----YLSALAktrfAAHGYGAYLTLSILDRYYKPDLTREDAV 157
Cdd:cd03750 124 PFGVSLLIAGWDE-GGPYLYQVDpsgsYFTWKA----TAIGKNYSNAKTFLEKRYNEDLELEDAI 183
 
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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