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Conserved domains on  [gi|6322459|ref|NP_012533|]
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proteasome core particle subunit beta 1 [Saccharomyces cerevisiae S288C]

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 ...
 20-204 6.77e-112

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


:

Pssm-ID: 239731  Cd Length: 188  Bit Score: 317.63  E-value: 6.77e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPST-ETAA 98
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLvKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSL 178
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*.
gi 6322459  179 SQAIKWDGSSGGVIRMVVLTAAGVER 204
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVER 186
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-204 6.77e-112

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 317.63  E-value: 6.77e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPST-ETAA 98
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLvKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSL 178
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*.
gi 6322459  179 SQAIKWDGSSGGVIRMVVLTAAGVER 204
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVER 186
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 16-197 4.82e-59

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: 183.92  E-value: 4.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459     16 VSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVT-DKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPST 94
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459     95 -----ETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE 169
Cdd:pfam00227  81 velaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 6322459    170 TVDFIKHSLSQAIKWDGSSGGVIRMVVL 197
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-205 5.58e-36

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 126.03  E-value: 5.58e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   15 EVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-S 93
Cdd:COG0638  31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPiS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   94 TETAAsvfKELCYENKDNLTAG-------IIVAGYDDkNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMS 166
Cdd:COG0638 111 VEGLA---KLLSDLLQGYTQYGvrpfgvaLLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLS 186

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322459  167 KEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:COG0638 187 LDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 12-194 1.44e-20

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 86.20  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    12 KKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGT 91
Cdd:PTZ00488  32 KAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    92 PSTETAAS-VFKELCYENKD-NLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIaGSGSTFIYGYCDKNFRENMSKEE 169
Cdd:PTZ00488 112 LISVAAASkILANIVWNYKGmGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEE 190

                        170       180
                 ....*....|....*....|....*
gi 6322459   170 TVDFIKHSLSQAIKWDGSSGGVIRM 194
Cdd:PTZ00488 191 AQDLGRRAIYHATFRDAYSGGAINL 215
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-204 6.77e-112

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 317.63  E-value: 6.77e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPST-ETAA 98
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLvKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSL 178
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*.
gi 6322459  179 SQAIKWDGSSGGVIRMVVLTAAGVER 204
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVER 186
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 20-205 3.22e-72

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: 217.31  E-value: 3.22e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGT-PSTETAA 98
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGReLSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDN-LTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHS 177
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
gi 6322459  178 LSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 16-197 4.82e-59

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: 183.92  E-value: 4.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459     16 VSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVT-DKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPST 94
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459     95 -----ETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE 169
Cdd:pfam00227  81 velaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 6322459    170 TVDFIKHSLSQAIKWDGSSGGVIRMVVL 197
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 20-197 1.88e-55

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: 174.61  E-value: 1.88e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-STETAA 98
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPiPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENK---DNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIK 175
Cdd:cd01906  81 KLLANLLYEYTqslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 6322459  176 HSLSQAIKWDGSSGGVIRMVVL 197
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 20-179 7.54e-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: 129.05  E-value: 7.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-STETAA 98
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPiSVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDN--LTAGIIVAGYdDKNKGEVYTIPLGGSVHKLPYAIA-GSGSTFIYGYCDKNFRENMSKEETVDFIK 175
Cdd:cd01901  81 KELAKLLQVYTQGrpFGVNLIVAGV-DEGGGNLYYIDPSGPVIENPGAVAtGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....
gi 6322459  176 HSLS 179
Cdd:cd01901 160 KALK 163
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 15-205 5.58e-36

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 126.03  E-value: 5.58e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   15 EVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-S 93
Cdd:COG0638  31 AVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPiS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   94 TETAAsvfKELCYENKDNLTAG-------IIVAGYDDkNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMS 166
Cdd:COG0638 111 VEGLA---KLLSDLLQGYTQYGvrpfgvaLLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLS 186

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6322459  167 KEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:COG0638 187 LDEAVELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-205 2.70e-34

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: 120.76  E-value: 2.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGT-PSTETAA 98
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRkPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDNLTAGIIVAGYDdkNKG-EVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHS 177
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVD--YTGpHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEA 158

                       170       180
                ....*....|....*....|....*...
gi 6322459  178 LSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:cd03763 159 IEAGIFNDLGSGSNVDLCVITKDGVEYL 186
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-205 5.55e-31

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: 111.96  E-value: 5.55e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-STETAA 98
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPmSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKDN-LTAGIIVAGYDDkNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHS 177
Cdd:cd03764  81 TLLSNILNSSKYFpYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*...
gi 6322459  178 LSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-205 6.36e-26

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: 98.86  E-value: 6.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   20 TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-STETAA 98
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERiSVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELCYENKD-NLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIaGSGSTFIYGYCDKNFRENMSKEETVDFIKHS 177
Cdd:cd03761  81 KLLSNMLYQYKGmGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSV-GSGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*...
gi 6322459  178 LSQAIKWDGSSGGVIRMVVLTAAGVERL 205
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRKI 187
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-176 8.51e-22

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: 88.41  E-value: 8.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   21 SIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASV 100
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459  101 F--KELCY--ENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKH 176
Cdd:cd03758  83 FtrRELAEslRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 12-194 1.44e-20

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 86.20  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    12 KKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGT 91
Cdd:PTZ00488  32 KAIEFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    92 PSTETAAS-VFKELCYENKD-NLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIaGSGSTFIYGYCDKNFRENMSKEE 169
Cdd:PTZ00488 112 LISVAAASkILANIVWNYKGmGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEE 190

                        170       180
                 ....*....|....*....|....*
gi 6322459   170 TVDFIKHSLSQAIKWDGSSGGVIRM 194
Cdd:PTZ00488 191 AQDLGRRAIYHATFRDAYSGGAINL 215
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 19-207 3.66e-18

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: 79.23  E-value: 3.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   19 GTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYG-TPSTETA 97
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNkEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   98 ASVFKELCYENK------DNltagiIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCD-----KNF----R 162
Cdd:cd03757  88 AQLLSTILYSRRffpyyvFN-----ILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrKNQnnveR 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6322459  163 ENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIF 207
Cdd:cd03757 163 TPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 19-196 7.96e-16

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: 72.66  E-value: 7.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   19 GTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-STETA 97
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREiKPKTF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   98 ASVFKELCYENKDN--LTAgIIVAGYDDKNKGEVYTIPLGGSVHKL-PYAIAGSGSTFIYGYCDKNFRENMSKEETVDFI 174
Cdd:cd03759  83 SSLISSLLYEKRFGpyFVE-PVVAGLDPDGKPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFETI 161

                       170       180
                ....*....|....*....|...
gi 6322459  175 KHSLSQAIKWDGSSG-GVIRMVV 196
Cdd:cd03759 162 SQALLSAVDRDALSGwGAVVYII 184
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-183 2.69e-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: 51.95  E-value: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    5 QVDINR--LKKGEVSLGtsimaVTFKDGVILGADSRTTTGAYIANRVtDKLTRVHDKIWCCRSGSAADTQAIADIVQYHL 82
Cdd:cd03756  17 QVEYAReaVKRGTTALG-----IKCKEGVVLAVDKRITSKLVEPESI-EKIYKIDDHVGAATSGLVADARVLIDRARVEA 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   83 ELYTSQYGTP-STETAAsvfKELCyENKDNLT---------AGIIVAGYDDkNKGEVY-TIPLGGSVHKLPYAIaGSGST 151
Cdd:cd03756  91 QIHRLTYGEPiDVEVLV---KKIC-DLKQQYTqhggvrpfgVALLIAGVDD-GGPRLFeTDPSGAYNEYKATAI-GSGRQ 164

                       170       180       190
                ....*....|....*....|....*....|..
gi 6322459  152 FIYGYCDKNFRENMSKEETVDFIKHSLSQAIK 183
Cdd:cd03756 165 AVTEFLEKEYKEDMSLEEAIELALKALYAALE 196
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 19-203 3.08e-07

proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239729  Cd Length: 197  Bit Score: 48.72  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   19 GTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQyHLELYTSQYGTPSTETAA 98
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLD-QLVIDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   99 SVFKELC---Y--ENK-DNLTAGIIVAGYDdkNKGEVY--TIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRE--NMSKE 168
Cdd:cd03760  81 EIHSYLTrvlYnrRSKmNPLWNTLVVGGVD--NEGEPFlgYVDLLGTAYEDPHVATGFGAYLALPLLREAWEKkpDLTEE 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6322459  169 ETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVE 203
Cdd:cd03760 159 EARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 16-179 2.00e-06

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: 46.67  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   16 VSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTdKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTP-ST 94
Cdd:cd01911  24 VKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVE-KIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPiPV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   95 ETAAsvfKELCyENKDNLT---------AGIIVAGYDDKNKGEVYTIPLGGSV--HKlpyAIA-GSGSTFIYGYCDKNFR 162
Cdd:cd01911 103 EVLV---KRIA-DLAQVYTqyggvrpfgVSLLIAGYDEEGGPQLYQTDPSGTYfgYK---ATAiGKGSQEAKTFLEKRYK 175

                       170
                ....*....|....*..
gi 6322459  163 ENMSKEETvdfIKHSLS 179
Cdd:cd01911 176 KDLTLEEA---IKLALK 189
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-172 1.03e-04

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 41.74  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459     5 QVDINR--LKKGEVSLGtsimaVTFKDGVILGADSRTTTgAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHL 82
Cdd:PRK03996  25 QVEYAReaVKRGTTAVG-----VKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459    83 ELYTSQYGTP-STETAAsvfKELCyENKDNLT---------AGIIVAGYDDKnKGEVY-TIPLGGSvhkLPY-AIA-GSG 149
Cdd:PRK03996  99 QINRLTYGEPiGVETLT---KKIC-DHKQQYTqhggvrpfgVALLIAGVDDG-GPRLFeTDPSGAY---LEYkATAiGAG 170

                        170       180
                 ....*....|....*....|...
gi 6322459   150 STFIYGYCDKNFRENMSKEETVD 172
Cdd:PRK03996 171 RDTVMEFLEKNYKEDLSLEEAIE 193
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 16-169 1.44e-04

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: 41.17  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   16 VSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVtDKLTRVHDKIWCCRSGSAADTQAIADIV----QYHLELYTSQYGT 91
Cdd:cd03753  24 IKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHArveaQNHRFTYNEPMTV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322459   92 PSTETAASVFKELCYENKDNLTA-------GIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIaGSGSTFIYGYCDKNFREN 164
Cdd:cd03753 103 ESVTQAVSDLALQFGEGDDGKKAmsrpfgvALLIAGVDENGPQLFHTDPSGTFTRCDAKAI-GSGSEGAQSSLQEKYHKD 181


                ....*
gi 6322459  165 MSKEE 169
Cdd:cd03753 182 MTLEE 186
 
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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