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Conserved domains on  [gi|247300942|ref|NP_038668|]
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proteasome subunit beta type-10 [Mus musculus]

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

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_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-226 2.46e-116

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: 331.47  E-value: 2.46e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAIT 199
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*..
gi 247300942 200 AGILSDLGSGGNVDACVITAGGAKLQR 226
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLR 187
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 1.24e-10

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


:

Pssm-ID: 463597  Cd Length: 36  Bit Score: 55.10  E-value: 1.24e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 247300942  231 PTEPVQRAGRYRFAPGTTPVLTREVrPLTLELLEETV 267
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-226 2.46e-116

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: 331.47  E-value: 2.46e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAIT 199
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*..
gi 247300942 200 AGILSDLGSGGNVDACVITAGGAKLQR 226
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLR 187
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-217 4.55e-58

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: 183.54  E-value: 4.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942   37 KTGTTIAGLVFRDGVILGADTRATNDS-VVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRV 115
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSkLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  116 ATVTRI----LRQTLFRYQGHVGASLVVGGVDLNG-PQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAA 190
Cdd:pfam00227  82 ELAARIadllQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 247300942  191 QELLVEAITAGILSDLGSGGNVDACVI 217
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-223 2.61e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 144.52  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  37 KTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVA 116
Cdd:COG0638   33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 117 TVTR----ILRQ-TLFRYQGhVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQ 191
Cdd:COG0638  113 GLAKllsdLLQGyTQYGVRP-FGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|..
gi 247300942 192 ELLVEAITAGILSDLGSGGNVDACVITAGGAK 223
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFR 223
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-221 2.11e-40

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: 138.11  E-value: 2.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942   39 GTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATV 118
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  119 TRILRQTLFRYQGHVGAS-LVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEA 197
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 247300942  198 ITAGILSDLGSGGNVDACVITAGG 221
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
32-223 5.03e-22

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 91.43  E-value: 5.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  32 VPHAR---KTGTTIAGLVFRDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALS 108
Cdd:PRK03996  26 VEYAReavKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 109 TGREPRVATVTRIL---RQTLFRYQGhV---GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQ 182
Cdd:PRK03996 105 YGEPIGVETLTKKIcdhKQQYTQHGG-VrpfGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYK 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 247300942 183 PNMTLEAAQELLVEAItAGILSDLGSGGNVDACVITAGGAK 223
Cdd:PRK03996 184 EDLSLEEAIELALKAL-AKANEGKLDPENVEIAYIDVETKK 223
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 1.24e-10

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 55.10  E-value: 1.24e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 247300942  231 PTEPVQRAGRYRFAPGTTPVLTREVrPLTLELLEETV 267
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
 
Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-226 2.46e-116

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: 331.47  E-value: 2.46e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGHVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAIT 199
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*..
gi 247300942 200 AGILSDLGSGGNVDACVITAGGAKLQR 226
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLR 187
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 40-226 7.54e-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: 218.47  E-value: 7.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQG-HVGASLVVGGVD-LNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEA 197
Cdd:cd01912   81 NLLSNILYSYRGfPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*....
gi 247300942 198 ITAGILSDLGSGGNVDACVITAGGAKLQR 226
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 40-217 2.45e-60

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 189.24  E-value: 2.45e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGHV---GASLVVGGVD-LNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLV 195
Cdd:cd01906   81 KLLANLLYEYTQSLrplGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                        170       180
                 ....*....|....*....|..
gi 247300942 196 EAITAGILSDLGSGGNVDACVI 217
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-217 4.55e-58

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: 183.54  E-value: 4.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942   37 KTGTTIAGLVFRDGVILGADTRATNDS-VVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRV 115
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSkLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  116 ATVTRI----LRQTLFRYQGHVGASLVVGGVDLNG-PQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAA 190
Cdd:pfam00227  82 ELAARIadllQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 247300942  191 QELLVEAITAGILSDLGSGGNVDACVI 217
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-223 3.21e-45

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: 150.45  E-value: 3.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGHVGASLVVGGVD-LNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEAI 198
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*
gi 247300942 199 TAGILSDLGSGGNVDACVITAGGAK 223
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVE 185
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-223 2.61e-42

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 144.52  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  37 KTGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVA 116
Cdd:COG0638   33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 117 TVTR----ILRQ-TLFRYQGhVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQ 191
Cdd:COG0638  113 GLAKllsdLLQGyTQYGVRP-FGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                        170       180       190
                 ....*....|....*....|....*....|..
gi 247300942 192 ELLVEAITAGILSDLGSGGNVDACVITAGGAK 223
Cdd:COG0638  192 ELALRALYSAAERDSASGDGIDVAVITEDGFR 223
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 40-198 3.71e-41

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: 139.45  E-value: 3.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQ--GHVGASLVVGGVDLNGPQLYEVHPHGSYSRLP-FTALGSGQGAAVALLEDRFQPNMTLEAAQELLVE 196
Cdd:cd01901   81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                 ..
gi 247300942 197 AI 198
Cdd:cd01901  161 AL 162
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-221 2.11e-40

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: 138.11  E-value: 2.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942   39 GTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATV 118
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  119 TRILRQTLFRYQGHVGAS-LVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEA 197
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 247300942  198 ITAGILSDLGSGGNVDACVITAGG 221
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-223 1.46e-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: 136.23  E-value: 1.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLF--RYQGHVgASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEA 197
Cdd:cd03764   81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                        170       180
                 ....*....|....*....|....*.
gi 247300942 198 ITAGILSDLGSGGNVDACVITAGGAK 223
Cdd:cd03764  160 IKSAIERDSASGDGIDVVVITKDGYK 185
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-221 2.21e-27

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: 104.25  E-value: 2.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  40 TTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVT 119
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 120 RILRQTLFRYQGH---VGASLVvgGVDLNGPQLYEVHPHGsySRLP---FtALGSGQGAAVALLEDRFQPNMTLEAAQEL 193
Cdd:cd03761   81 KLLSNMLYQYKGMglsMGTMIC--GWDKTGPGLYYVDSDG--TRLKgdlF-SVGSGSTYAYGVLDSGYRYDLSVEEAYDL 155

                        170       180
                 ....*....|....*....|....*...
gi 247300942 194 LVEAITAGILSDLGSGGNVDACVITAGG 221
Cdd:cd03761  156 ARRAIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-219 2.61e-25

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: 99.71  E-value: 2.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  30 LRVPHAR---KTGTTIAGLVFRDGVILGADTRATNDSVVADkSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHA 106
Cdd:cd03756   16 YQVEYAReavKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 107 LSTGREPRVATVTRI---LRQTLFRYQG--HVGASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRF 181
Cdd:cd03756   95 LTYGEPIDVEVLVKKicdLKQQYTQHGGvrPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEY 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 247300942 182 QPNMTLEAAQELLVEAITAGIlSDLGSGGNVDACVITA 219
Cdd:cd03756  175 KEDMSLEEAIELALKALYAAL-EENETPENVEIAYVTV 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
32-223 5.03e-22

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 91.43  E-value: 5.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  32 VPHAR---KTGTTIAGLVFRDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALS 108
Cdd:PRK03996  26 VEYAReavKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVLIDRARVEAQINRLT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 109 TGREPRVATVTRIL---RQTLFRYQGhV---GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQ 182
Cdd:PRK03996 105 YGEPIGVETLTKKIcdhKQQYTQHGG-VrpfGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEKNYK 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 247300942 183 PNMTLEAAQELLVEAItAGILSDLGSGGNVDACVITAGGAK 223
Cdd:PRK03996 184 EDLSLEEAIELALKAL-AKANEGKLDPENVEIAYIDVETKK 223
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-213 3.57e-21

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 89.66  E-value: 3.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  39 GTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATV 118
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 119 TRILRQTLFRYQGHvGASL--VVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVE 196
Cdd:PTZ00488 119 SKILANIVWNYKGM-GLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRR 197

                        170
                 ....*....|....*..
gi 247300942 197 AITAGILSDLGSGGNVD 213
Cdd:PTZ00488 198 AIYHATFRDAYSGGAIN 214
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-217 2.27e-19

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: 83.93  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  35 ARKTGTTIAGLVFRDGVILGADTRATNDSVVADkSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPR 114
Cdd:cd03753   23 AIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 115 VATVTRILRQTLFRYqGHV-----------GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQP 183
Cdd:cd03753  102 VESVTQAVSDLALQF-GEGddgkkamsrpfGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180

                        170       180       190
                 ....*....|....*....|....*....|....
gi 247300942 184 NMTLEAAqELLVEAITAGILSDLGSGGNVDACVI 217
Cdd:cd03753  181 DMTLEEA-EKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-200 5.18e-18

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: 79.79  E-value: 5.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  35 ARKTGTTIAGLVFRDGVILGADTRATnDSVVADKSCEKIHFIAPKIYCCGAGVAADTemttRMAASKMEL----HALSTG 110
Cdd:cd01911   23 AVKNGSTAVGIKGKDGVVLAVEKKVT-SKLLDPSSVEKIFKIDDHIGCAVAGLTADA----RVLVNRARVeaqnYRYTYG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 111 REPRVATVTRILRQTLFRY--QGHV---GASLVVGGVDLN-GPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPN 184
Cdd:cd01911   98 EPIPVEVLVKRIADLAQVYtqYGGVrpfGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKATAIGKGSQEAKTFLEKRYKKD 177

                        170
                 ....*....|....*.
gi 247300942 185 MTLEaaqELLVEAITA 200
Cdd:cd01911  178 LTLE---EAIKLALKA 190
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-199 1.76e-15

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: 73.15  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  34 HArktGTTIaGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEM---TTRMAASKmelHALSTG 110
Cdd:cd03752   28 HA---GTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANIlinYARLIAQR---YLYSYQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 111 RE-PRVATVTRI--LRQTLFRYQG--HVGASLVVGGVDLN-GPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPN 184
Cdd:cd03752  101 EPiPVEQLVQRLcdIKQGYTQYGGlrPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDD 180

                        170
                 ....*....|....*
gi 247300942 185 MTLEAAQELLVEAIT 199
Cdd:cd03752  181 MTLEEALALAVKVLS 195
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-204 3.77e-15

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: 72.74  E-value: 3.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  35 ARKTGTTIAGLVFRDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPR 114
Cdd:cd03750   23 AVSSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 115 VATVTRILRQTLFRY--QGHV---GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEa 189
Cdd:cd03750  102 VSQLVREIASVMQEYtqSGGVrpfGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELE- 180

                        170
                 ....*....|....*
gi 247300942 190 aqellvEAITAGILS 204
Cdd:cd03750  181 ------DAIHTAILT 189
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 44-199 8.14e-15

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 72.19  E-value: 8.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  44 GLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTG-REPRVATVTRI- 121
Cdd:PTZ00246  36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGePQPVEQLVVQIc 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 122 -LRQTLFRYQG--HVGASLVVGGVDLN-GPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELLVEA 197
Cdd:PTZ00246 116 dLKQSYTQFGGlrPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKV 195


                 ..
gi 247300942 198 IT 199
Cdd:PTZ00246 196 LT 197
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-221 8.57e-15

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: 71.14  E-value: 8.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  39 GTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATV 118
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 119 TRILRQTL-----FRYQghvgASLVVGGVDLNG-PQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRF-QPNM------ 185
Cdd:cd03757   88 AQLLSTILysrrfFPYY----VFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVgRKNQnnvert 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 247300942 186 --TLEAAQELLVEAITAGILSDLGSGGNVDACVITAGG 221
Cdd:cd03757  164 plSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 41-194 1.04e-12

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: 64.91  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  41 TIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVATVTR 120
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 247300942 121 ILRQTLFRY---QGHVGASLVVGGVDL-NGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPNMTLEAAQELL 194
Cdd:cd03758   83 FTRRELAESlrsRTPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-225 1.14e-10

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: 59.51  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  38 TGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKM-ELHALSTGREPRVA 116
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLViDDECLDDGHSLSPK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 117 TV----TRIL--RQTLFRyqgHVGASLVVGGVDLNG-PQLYEVHPHGSYSRLPFTALGSGQGAAVALLED--RFQPNMTL 187
Cdd:cd03760   81 EIhsylTRVLynRRSKMN---PLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREawEKKPDLTE 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 247300942 188 EAAQELLVEAITAGILSDLGSGGNVDACVITAGGAKLQ 225
Cdd:cd03760  158 EEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIE 195
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 1.24e-10

Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00227. There is a conserved GTT sequence motif. There is a single completely conserved residue Y that may be functionally important. This family includes the C terminal of the beta-type subunits of the proteasome, a multimeric complex that degrades proteins into peptides as part of the MHC class I-mediated Ag-presenting pathway.


Pssm-ID: 463597  Cd Length: 36  Bit Score: 55.10  E-value: 1.24e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 247300942  231 PTEPVQRAGRYRFAPGTTPVLTREVrPLTLELLEETV 267
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-198 2.43e-10

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: 58.53  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  30 LRVPHAR---KTGTTIAGLVFRDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHA 106
Cdd:cd03755   15 FQVEYAQeavRKGTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 107 LSTGREPRVATVTRILRQTLFRY--QGHV---GASLVVGGVDLNG-PQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDR 180
Cdd:cd03755   94 LTVEDPVTVEYITRYIAGLQQRYtqSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKN 173

                        170
                 ....*....|....*...
gi 247300942 181 FQPNMTLEAAQELLVEAI 198
Cdd:cd03755  174 YKEEMTRDDTIKLAIKAL 191
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-197 1.02e-08

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: 54.21  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  39 GTTIaGLVFRDGVILGADtratndSVVADK-----SCEKIHFIAPKIYCCGAGVAADTemttRMAASKMELHALSTGREP 113
Cdd:cd03751   31 GTAI-GIRCKDGVVLAVE------KLVTSKlyepgSNKRIFNVDRHIGIAVAGLLADG----RHLVSRAREEAENYRDNY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 114 RVATVTRILRQTLFRY-QGHV--------GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQPN 184
Cdd:cd03751  100 GTPIPVKVLADRVAMYmHAYTlyssvrpfGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSE 179

                        170
                 ....*....|...
gi 247300942 185 MTLEaaqELLVEA 197
Cdd:cd03751  180 LTCR---EAVKEA 189
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-200 2.64e-08

proteasome_alpha_type_1. 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: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 53.06  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  35 ARKTGTTIAGLVFRDGVILGADTRATNDsvVADKScEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPR 114
Cdd:cd03749   23 AVKQGSATVGLKSKTHAVLVALKRATSE--LSSYQ-KKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 115 VATVTRILRQtlfRYQGHV--------GASLVVGGVDLNGPQLYEVHPHGSYSRLPFTALGSGQGAAVALLEDRFQ--PN 184
Cdd:cd03749  100 VSRLVSKVAE---KAQINTqrygrrpyGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefED 176

                        170
                 ....*....|....*.
gi 247300942 185 MTLEaaqELLVEAITA 200
Cdd:cd03749  177 CSLE---ELIKHALRA 189
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-218 2.49e-04

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: 41.07  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942  38 TGTTIAGLVFRDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADTEMTTRMAASKMELHALSTGREPRVAT 117
Cdd:cd03759    2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247300942 118 VTRILRQTLfrYQGHVG---ASLVVGGVDLNG-PQLYEVHPHGSYSrLP--FTALGSGQGAAVALLEDRFQPNMTLEAAQ 191
Cdd:cd03759   82 FSSLISSLL--YEKRFGpyfVEPVVAGLDPDGkPFICTMDLIGCPS-IPsdFVVSGTASEQLYGMCESLWRPDMEPDELF 158

                        170       180
                 ....*....|....*....|....*..
gi 247300942 192 ELLVEAITAGILSDLGSGGNVDACVIT 218
Cdd:cd03759  159 ETISQALLSAVDRDALSGWGAVVYIIT 185
 
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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