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Conserved domains on  [gi|334188098|ref|NP_001190443|]
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20S proteasome beta subunit PBB2 [Arabidopsis thaliana]

Protein Classification

proteasome subunit beta( domain architecture ID 10132938)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; such as Arabidopsis thaliana proteasome subunit beta type-7-A

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-222 1.36e-129

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: 364.98  E-value: 1.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  40 TTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTAL 113
Cdd:cd03763    1 TTIvgvvfkDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 114 TLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAIC 193
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 334188098 194 SGIFNDLGSGSNVDICVITKGHKEYLRNY 222
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-222 1.36e-129

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: 364.98  E-value: 1.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  40 TTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTAL 113
Cdd:cd03763    1 TTIvgvvfkDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 114 TLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAIC 193
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 334188098 194 SGIFNDLGSGSNVDICVITKGHKEYLRNY 222
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-211 4.20e-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: 170.83  E-value: 4.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098   37 KTGTTI------DGVILGADTRATEGPIVADKN-CEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRV 109
Cdd:pfam00227   2 KTGTTIvgikgkDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  110 ----VTALTLLKKHLFSYQGHVSAALVLGGVDITG-PHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEG 184
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 334188098  185 IKLVAEAICSGIFNDLGSGSNVDICVI 211
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 32-218 1.10e-39

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 137.58  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  32 APSFLKTGTTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGR 105
Cdd:COG0638   28 AREAVKRGTTTvgiktkDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 106 DSRVVTALTLLKKHLFSYQGH----VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTR 181
Cdd:COG0638  108 PISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSL 187

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334188098 182 DEGIKLVAEAICSGIFNDLGSGSNVDICVITK-GHKEY 218
Cdd:COG0638  188 DEAVELALRALYSAAERDSASGDGIDVAVITEdGFREL 225
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-213 1.21e-39

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: 136.19  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098   39 GTTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTA 112
Cdd:TIGR03634   1 GTTTvgikckDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  113 LTLLKKHLFSYQGHVSAA-LVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEA 191
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|..
gi 334188098  192 ICSGIFNDLGSGSNVDICVITK 213
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITK 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 44-208 9.51e-17

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 77.34  E-value: 9.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  44 GVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFSY 123
Cdd:PTZ00488  50 GIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 124 QGH-VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFNDLGS 202
Cdd:PTZ00488 130 KGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYS 209


                 ....*.
gi 334188098 203 GSNVDI 208
Cdd:PTZ00488 210 GGAINL 215
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-222 1.36e-129

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: 364.98  E-value: 1.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  40 TTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTAL 113
Cdd:cd03763    1 TTIvgvvfkDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 114 TLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAIC 193
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 334188098 194 SGIFNDLGSGSNVDICVITKGHKEYLRNY 222
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-220 1.06e-75

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: 228.10  E-value: 1.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  39 GTTI-----DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTAL 113
Cdd:cd01912    1 TTIVgikgkDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 114 TLLKKHLFSYQG-HVSAALVLGGVD-ITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEA 191
Cdd:cd01912   81 NLLSNILYSYRGfPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*....
gi 334188098 192 ICSGIFNDLGSGSNVDICVITKGHKEYLR 220
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 43-211 9.23e-59

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: 185.01  E-value: 9.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd01906   10 DGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKLLANLLYE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 123 YQGHV---SAALVLGGVD-ITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFN 198
Cdd:cd01906   90 YTQSLrplGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALKALKSALER 169

                        170
                 ....*....|...
gi 334188098 199 DLGSGSNVDICVI 211
Cdd:cd01906  170 DLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-211 4.20e-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: 170.83  E-value: 4.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098   37 KTGTTI------DGVILGADTRATEGPIVADKN-CEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRV 109
Cdd:pfam00227   2 KTGTTIvgikgkDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  110 ----VTALTLLKKHLFSYQGHVSAALVLGGVDITG-PHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEG 184
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 334188098  185 IKLVAEAICSGIFNDLGSGSNVDICVI 211
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-213 1.36e-42

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: 143.90  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  40 TTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTAL 113
Cdd:cd03762    1 TTIiaveydGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 114 TLLKKHLFSYQGHVSAALVLGGVD-ITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAI 192
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|.
gi 334188098 193 CSGIFNDLGSGSNVDICVITK 213
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITK 181
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 32-218 1.10e-39

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 137.58  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  32 APSFLKTGTTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGR 105
Cdd:COG0638   28 AREAVKRGTTTvgiktkDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 106 DSRVVTALTLLKKHLFSYQGH----VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTR 181
Cdd:COG0638  108 PISVEGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSL 187

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334188098 182 DEGIKLVAEAICSGIFNDLGSGSNVDICVITK-GHKEY 218
Cdd:COG0638  188 DEAVELALRALYSAAERDSASGDGIDVAVITEdGFREL 225
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-213 1.21e-39

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: 136.19  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098   39 GTTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTA 112
Cdd:TIGR03634   1 GTTTvgikckDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  113 LTLLKKHLFSYQGHVSAA-LVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEA 191
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|..
gi 334188098  192 ICSGIFNDLGSGSNVDICVITK 213
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITK 182
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-218 1.95e-39

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: 135.46  E-value: 1.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd03764   10 DGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 123 YQGH-VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFNDLG 201
Cdd:cd03764   90 SKYFpYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRAIKSAIERDSA 169

                        170
                 ....*....|....*...
gi 334188098 202 SGSNVDICVITK-GHKEY 218
Cdd:cd03764  170 SGDGIDVVVITKdGYKEL 187
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 43-192 7.07e-39

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: 133.29  E-value: 7.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd01901   10 GGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKELAKLLQV 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188098 123 YQ--GHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATM-GSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAI 192
Cdd:cd01901   90 YTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPGAVAtGSRSQRAKSLLEKLYKPDMTLEEAVELALKAL 162
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-214 2.29e-20

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: 85.76  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd03761   10 GGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 123 YQGH-VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFNDLG 201
Cdd:cd03761   90 YKGMgLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAIYHATHRDAY 169

                        170
                 ....*....|...
gi 334188098 202 SGSNVDICVITKG 214
Cdd:cd03761  170 SGGNVNLYHVRED 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 37-212 9.07e-17

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: 76.60  E-value: 9.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  37 KTGTTI------DGVILGADTRATEgPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGR--DSR 108
Cdd:cd03756   26 KRGTTAlgikckEGVVLAVDKRITS-KLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEpiDVE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 109 VVTALTLLKKHLFSYQGHV---SAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGI 185
Cdd:cd03756  105 VLVKKICDLKQQYTQHGGVrpfGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEEAI 184

                        170       180
                 ....*....|....*....|....*..
gi 334188098 186 KLVAEAICSGIfNDLGSGSNVDICVIT 212
Cdd:cd03756  185 ELALKALYAAL-EENETPENVEIAYVT 210
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 44-208 9.51e-17

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 77.34  E-value: 9.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  44 GVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFSY 123
Cdd:PTZ00488  50 GIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 124 QGH-VSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFNDLGS 202
Cdd:PTZ00488 130 KGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAIYHATFRDAYS 209


                 ....*.
gi 334188098 203 GSNVDI 208
Cdd:PTZ00488 210 GGAINL 215
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-188 1.71e-14

proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis.Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239727  Cd Length: 193  Bit Score: 69.92  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd03758   11 DFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAANFTRRELAE 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 123 Y---QGHVSAALVLGGVD-ITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLV 188
Cdd:cd03758   91 SlrsRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-213 9.55e-14

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: 68.44  E-value: 9.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  39 GTTI-----DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRD--SRVVT 111
Cdd:cd03757    9 GTVLaiagnDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEmsTEAIA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 112 AL---TLLKKHLFSYQghvsAALVLGGVDITG-PHLHTIYPHGSTDTLPFATMGSGSLAAMSVFE---------AKYKEG 178
Cdd:cd03757   89 QLlstILYSRRFFPYY----VFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERTP 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 334188098 179 LTRDEGIKLVAEAICSGIFNDLGSGSNVDICVITK 213
Cdd:cd03757  165 LSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK 199
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
37-218 1.98e-13

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 67.94  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  37 KTGTTI------DGVILGADTRATEgPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDsrvV 110
Cdd:PRK03996  34 KRGTTAvgvktkDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLTYGEP---I 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 111 TALTLLK-----KHLFSYQGHV---SAALVLGGVDITGPHLHTIYPHGsTDTLPFAT-MGSGSLAAMSVFEAKYKEGLTR 181
Cdd:PRK03996 110 GVETLTKkicdhKQQYTQHGGVrpfGVALLIAGVDDGGPRLFETDPSG-AYLEYKATaIGAGRDTVMEFLEKNYKEDLSL 188

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334188098 182 DEGIKLVAEAICSGIfNDLGSGSNVDICVITKGHKEY 218
Cdd:PRK03996 189 EEAIELALKALAKAN-EGKLDPENVEIAYIDVETKKF 224
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-211 3.68e-11

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: 60.92  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  30 LKAPSflKTGTTI-----DGVILGADTRATEgPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDmvssQLRL----HR 100
Cdd:cd01911   21 LEAVK--NGSTAVgikgkDGVVLAVEKKVTS-KLLDPSSVEKIFKIDDHIGCAVAGLTADARVLVN----RARVeaqnYR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 101 YQTGRD---SRVVTALTLlKKHLFSYQGHV---SAALVLGGVD-ITGPHLHTIYPHGSTDTLpFAT-MGSGSLAAMSVFE 172
Cdd:cd01911   94 YTYGEPipvEVLVKRIAD-LAQVYTQYGGVrpfGVSLLIAGYDeEGGPQLYQTDPSGTYFGY-KATaIGKGSQEAKTFLE 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 334188098 173 AKYKEGLTRDEGIKLVAEAICSGIFNDLgSGSNVDICVI 211
Cdd:cd01911  172 KRYKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-213 1.05e-09

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: 56.81  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  38 TGTTI------DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAAD----TEAVTDMVSSQLRLHryqtgrDS 107
Cdd:cd03760    1 TGTSViaikykDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLD------DG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 108 RVVTAltllkKHLFSYQGHVS-----------AALVLGGVDITG-PHLHTIYPHGSTDTLPFATMGSGSLAAMSVF--EA 173
Cdd:cd03760   75 HSLSP-----KEIHSYLTRVLynrrskmnplwNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLreAW 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334188098 174 KYKEGLTRDEGIKLVAEAICSGIFNDLGSGSNVDICVITK 213
Cdd:cd03760  150 EKKPDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTK 189
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 41-211 1.27e-09

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


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 56.58  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  41 TIDGVILGADTRATEgPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVvTALTLLKKHL 120
Cdd:cd03753   35 TKEGVVLAVEKRITS-PLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTV-ESVTQAVSDL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 121 FSYQGHVSA-----------ALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVA 189
Cdd:cd03753  113 ALQFGEGDDgkkamsrpfgvALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLAL 192

                        170       180
                 ....*....|....*....|..
gi 334188098 190 EaICSGIFNDLGSGSNVDICVI 211
Cdd:cd03753  193 S-ILKQVMEEKLNSTNVELATV 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 43-217 6.03e-09

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 55.24  E-value: 6.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRD---SRVVTALTLLKKH 119
Cdd:PTZ00246  41 EGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPqpvEQLVVQICDLKQS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 120 LFSYQG--HVSAALVLGGVDIT-GPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGI 196
Cdd:PTZ00246 121 YTQFGGlrPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSM 200

                        170       180
                 ....*....|....*....|.
gi 334188098 197 FNDLGSGSNVDICVITKGHKE 217
Cdd:PTZ00246 201 DSTSPKADKIEVGILSHGETD 221
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-192 1.80e-07

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


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 50.42  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  39 GTTI-----DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDmvssQLRL----HRYQTGRD--- 106
Cdd:cd03752   30 GTCLgilakDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILIN----YARLiaqrYLYSYQEPipv 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 107 SRVVTALTLLKKHLFSYQG----HVSaaLVLGGVD-ITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTR 181
Cdd:cd03752  106 EQLVQRLCDIKQGYTQYGGlrpfGVS--FLYAGWDkHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTL 183

                        170
                 ....*....|.
gi 334188098 182 DEGIKLVAEAI 192
Cdd:cd03752  184 EEALALAVKVL 194
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-213 4.98e-07

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: 48.78  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVVTALTLLKKHLFS 122
Cdd:cd03759   13 DCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSLISSLLYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 123 YQ-GHVSAALVLGGVDITG-PHLHTIYPHGSTDTL-PFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIFND 199
Cdd:cd03759   93 KRfGPYFVEPVVAGLDPDGkPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDMEPDELFETISQALLSAVDRD 172

                        170
                 ....*....|....
gi 334188098 200 LGSGSNVDICVITK 213
Cdd:cd03759  173 ALSGWGAVVYIITK 186
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-192 4.26e-05

proteasome_alpha_type_3. 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: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 43.42  E-value: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  39 GTTI-----DGVILGADTRATEGPIVADKNcEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRD--SRVVT 111
Cdd:cd03751   31 GTAIgirckDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPipVKVLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 112 ALTLLKKHLFSYQGHV---SAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLV 188
Cdd:cd03751  110 DRVAMYMHAYTLYSSVrpfGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCREAVKEA 189


                 ....
gi 334188098 189 AEAI 192
Cdd:cd03751  190 AKII 193
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-211 5.02e-04

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: 40.04  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILGADTRATEgPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYqTGRDSRVVTALT-----LLK 117
Cdd:cd03755   37 DCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRL-TVEDPVTVEYITryiagLQQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 118 KHlfSYQGHV---SAALVLGGVDITG-PHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAIC 193
Cdd:cd03755  115 RY--TQSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALL 192

                        170
                 ....*....|....*...
gi 334188098 194 SGIfnDLGSGsNVDICVI 211
Cdd:cd03755  193 EVV--QSGSK-NIELAVM 207
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 43-213 8.43e-04

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: 39.61  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098  43 DGVILgADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMV--SSQLRLHRYQTGRDSRVVTALTLLKKHL 120
Cdd:cd03750   37 NGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKArkIAQQYYLVYGEPIPVSQLVREIASVMQE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188098 121 FSYQGHV---SAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAEAICSGIF 197
Cdd:cd03750  116 YTQSGGVrpfGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFE 195

                        170
                 ....*....|....*.
gi 334188098 198 NDLgSGSNVDICVITK 213
Cdd:cd03750  196 GQM-TEKNIEIGICGE 210
 
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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