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Conserved domains on  [gi|4506191|ref|NP_002792|]
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proteasome subunit beta type-10 [Homo sapiens]

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins

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 ...
 40-227 3.33e-119

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: 338.79  E-value: 3.33e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVT 199
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*...
gi 4506191  200 AGILGDLGSGGNVDACVITKTGAKLLRT 227
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRN 188
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 3.92e-11

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: 56.64  E-value: 3.92e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4506191    231 PTEPVKRSGRYHFVPGTTAVLTQTVkPLTLELVEETV 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 ...
 40-227 3.33e-119

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: 338.79  E-value: 3.33e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVT 199
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*...
gi 4506191  200 AGILGDLGSGGNVDACVITKTGAKLLRT 227
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRN 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-217 6.65e-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: 183.15  E-value: 6.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191     37 KTGTTIAGLVFQDGVILGADTRATNDS-VVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRV 115
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSkLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    116 ATVTRI----LRQTLFRYQGHVGASLIVGGVDLTG-PQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAA 190
Cdd:pfam00227  82 ELAARIadllQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 4506191    191 QGLLVEAVTAGILGDLGSGGNVDACVI 217
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-225 2.47e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.53  E-value: 2.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   37 KTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVA 116
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  117 TVTR----ILRQ-TLFRYQGhVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQ 191
Cdd:COG0638 113 GLAKllsdLLQGyTQYGVRP-FGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....
gi 4506191  192 GLLVEAVTAGILGDLGSGGNVDACVITKTGAKLL 225
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-221 2.37e-43

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: 145.82  E-value: 2.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191     39 GTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATV 118
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    119 TRILRQTLFRYQGHVGAS-LIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEA 197
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 4506191    198 VTAGILGDLGSGGNVDACVITKTG 221
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-223 1.77e-23

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 95.83  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    39 GTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATV 118
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   119 TRILRQTLFRYQGHvGASL--IVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVE 196
Cdd:PTZ00488 119 SKILANIVWNYKGM-GLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRR 197

                        170       180
                 ....*....|....*....|....*..
gi 4506191   197 AVTAGILGDLGSGGNVDACVITKTGAK 223
Cdd:PTZ00488 198 AIYHATFRDAYSGGAINLYHMQKDGWK 224
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 3.92e-11

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: 56.64  E-value: 3.92e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4506191    231 PTEPVKRSGRYHFVPGTTAVLTQTVkPLTLELVEETV 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 ...
 40-227 3.33e-119

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: 338.79  E-value: 3.33e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVT 199
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                       170       180
                ....*....|....*....|....*...
gi 4506191  200 AGILGDLGSGGNVDACVITKTGAKLLRT 227
Cdd:cd03763 161 AGIFNDLGSGSNVDLCVITKDGVEYLRN 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 40-226 1.73e-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: 220.39  E-value: 1.73e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQG-HVGASLIVGGVD-LTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEA 197
Cdd:cd01912  81 NLLSNILYSYRGfPYYVSLIVGGVDkGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*....
gi 4506191  198 VTAGILGDLGSGGNVDACVITKTGAKLLR 226
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 40-217 1.08e-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: 187.32  E-value: 1.08e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGHV---GASLIVGGVD-LTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLV 195
Cdd:cd01906  81 KLLANLLYEYTQSLrplGVSLLVAGVDeEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 4506191  196 EAVTAGILGDLGSGGNVDACVI 217
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 37-217 6.65e-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: 183.15  E-value: 6.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191     37 KTGTTIAGLVFQDGVILGADTRATNDS-VVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRV 115
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSkLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    116 ATVTRI----LRQTLFRYQGHVGASLIVGGVDLTG-PQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAA 190
Cdd:pfam00227  82 ELAARIadllQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 4506191    191 QGLLVEAVTAGILGDLGSGGNVDACVI 217
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 37-225 2.47e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 149.53  E-value: 2.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   37 KTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVA 116
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  117 TVTR----ILRQ-TLFRYQGhVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQ 191
Cdd:COG0638 113 GLAKllsdLLQGyTQYGVRP-FGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAV 191

                       170       180       190
                ....*....|....*....|....*....|....
gi 4506191  192 GLLVEAVTAGILGDLGSGGNVDACVITKTGAKLL 225
Cdd:COG0638 192 ELALRALYSAAERDSASGDGIDVAVITEDGFREL 225
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-223 3.72e-44

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: 147.76  E-value: 3.72e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGHVGASLIVGGVD-LTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAV 198
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDeQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*
gi 4506191  199 TAGILGDLGSGGNVDACVITKTGAK 223
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVE 185
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 39-221 2.37e-43

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: 145.82  E-value: 2.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191     39 GTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATV 118
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    119 TRILRQTLFRYQGHVGAS-LIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEA 197
Cdd:TIGR03634  81 ATLLSNILNSNRFFPFIVqLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVRA 160

                         170       180
                  ....*....|....*....|....
gi 4506191    198 VTAGILGDLGSGGNVDACVITKTG 221
Cdd:TIGR03634 161 IKSAIERDVASGNGIDVAVITKDG 184
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-225 3.25e-43

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: 145.47  E-value: 3.25e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLF--RYQGHVgASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEA 197
Cdd:cd03764  81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                       170       180
                ....*....|....*....|....*...
gi 4506191  198 VTAGILGDLGSGGNVDACVITKTGAKLL 225
Cdd:cd03764 160 IKSAIERDSASGDGIDVVVITKDGYKEL 187
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 40-198 1.01e-40

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: 138.30  E-value: 1.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQ--GHVGASLIVGGVDLTGPQLYGVHPHGSYSRLP-FTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVE 196
Cdd:cd01901  81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ..
gi 4506191  197 AV 198
Cdd:cd01901 161 AL 162
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 40-221 2.59e-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: 2.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   40 TTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVT 119
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  120 RILRQTLFRYQGH---VGAslIVGGVDLTGPQLYGVHPHGsySRLP---FtALGSGQDAALAVLEDRFQPNMTLEAAQGL 193
Cdd:cd03761  81 KLLSNMLYQYKGMglsMGT--MICGWDKTGPGLYYVDSDG--TRLKgdlF-SVGSGSTYAYGVLDSGYRYDLSVEEAYDL 155

                       170       180
                ....*....|....*....|....*...
gi 4506191  194 LVEAVTAGILGDLGSGGNVDACVITKTG 221
Cdd:cd03761 156 ARRAIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-218 1.37e-23

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: 95.09  E-value: 1.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   30 LKVPHAR---KTGTTIAGLVFQDGVILGADTRATNDSVVADkSCEKIHFIAPKIYCCGAGVAADAEMT---TRMVAskmE 103
Cdd:cd03756  16 YQVEYAReavKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLidrARVEA---Q 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  104 LHALSTGREPRVATVTRI---LRQTLFRYQG--HVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLE 178
Cdd:cd03756  92 IHRLTYGEPIDVEVLVKKicdLKQQYTQHGGvrPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLE 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4506191  179 DRFQPNMTLEAAQGLLVEAVTAGILGDLgSGGNVDACVIT 218
Cdd:cd03756 172 KEYKEDMSLEEAIELALKALYAALEENE-TPENVEIAYVT 210
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 39-223 1.77e-23

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 95.83  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    39 GTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATV 118
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   119 TRILRQTLFRYQGHvGASL--IVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVE 196
Cdd:PTZ00488 119 SKILANIVWNYKGM-GLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRR 197

                        170       180
                 ....*....|....*....|....*..
gi 4506191   197 AVTAGILGDLGSGGNVDACVITKTGAK 223
Cdd:PTZ00488 198 AIYHATFRDAYSGGAINLYHMQKDGWK 224
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
32-229 2.04e-21

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 89.89  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    32 VPHAR---KTGTTIAGLVFQDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADAEM---TTRMVAskmELH 105
Cdd:PRK03996  26 VEYAReavKRGTTAVGVKTKDGVVLAVDKRITS-PLIEPSSIEKIFKIDDHIGAASAGLVADARVlidRARVEA---QIN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   106 ALSTGREPRVATVTRIL---RQTLFRYQGhV---GASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLED 179
Cdd:PRK03996 102 RLTYGEPIGVETLTKKIcdhKQQYTQHGG-VrpfGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIGAGRDTVMEFLEK 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 4506191   180 RFQPNMTLEAAQGLLVEAVTAGILGDLGSgGNVDACVITkTGAKLLRTLS 229
Cdd:PRK03996 181 NYKEDLSLEEAIELALKALAKANEGKLDP-ENVEIAYID-VETKKFRKLS 228
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-196 5.33e-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: 82.77  E-value: 5.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   35 ARKTGTTIAGLVFQDGVILGADTRATNDSVVADkSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPR 114
Cdd:cd03753  23 AIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  115 VATVTRILRQTLFRYqGHV-----------GASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQP 183
Cdd:cd03753 102 VESVTQAVSDLALQF-GEGddgkkamsrpfGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK 180

                       170
                ....*....|...
gi 4506191  184 NMTLEAAQGLLVE 196
Cdd:cd03753 181 DMTLEEAEKLALS 193
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-200 8.04e-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: 79.41  E-value: 8.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   35 ARKTGTTIAGLVFQDGVILGADTRATnDSVVADKSCEKIHFIAPKIYCCGAGVAADA----------------------- 91
Cdd:cd01911  23 AVKNGSTAVGIKGKDGVVLAVEKKVT-SKLLDPSSVEKIFKIDDHIGCAVAGLTADArvlvnrarveaqnyrytygepip 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   92 -EMTTRMVASKMELHALSTGREPrvatvtrilrqtlFryqghvGASLIVGGVDL-TGPQLYGVHPHGSYSRLPFTALGSG 169
Cdd:cd01911 102 vEVLVKRIADLAQVYTQYGGVRP-------------F------GVSLLIAGYDEeGGPQLYQTDPSGTYFGYKATAIGKG 162

                       170       180       190
                ....*....|....*....|....*....|.
gi 4506191  170 QDAALAVLEDRFQPNMTLEAAqglLVEAVTA 200
Cdd:cd01911 163 SQEAKTFLEKRYKKDLTLEEA---IKLALKA 190
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 39-221 3.20e-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: 72.29  E-value: 3.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   39 GTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATV 118
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  119 TRILRQTL-----FRYQghvgASLIVGGVDLTG-PQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRF-QPNM------ 185
Cdd:cd03757  88 AQLLSTILysrrfFPYY----VFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVgRKNQnnvert 163

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4506191  186 --TLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTG 221
Cdd:cd03757 164 plSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDG 201
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-199 5.17e-14

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: 69.30  E-value: 5.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   34 HArktGTTIaGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEM---TTRMVASKmelHALSTG 110
Cdd:cd03752  28 HA---GTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANIlinYARLIAQR---YLYSYQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  111 RE-PRVATVTRI--LRQTLFRYQG--HVGASLIVGGVD-LTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPN 184
Cdd:cd03752 101 EPiPVEQLVQRLcdIKQGYTQYGGlrPFGVSFLYAGWDkHYGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDD 180

                       170
                ....*....|....*
gi 4506191  185 MTLEAAQGLLVEAVT 199
Cdd:cd03752 181 MTLEEALALAVKVLS 195
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-222 5.30e-14

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: 69.27  E-value: 5.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   35 ARKTGTTIAGLVFQDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPR 114
Cdd:cd03750  23 AVSSGAPSVGIKAANGVVLATEKKVPS-PLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  115 VATVTRILRQTLFRY--QGHV---GASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEA 189
Cdd:cd03750 102 VSQLVREIASVMQEYtqSGGVrpfGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNEDLELED 181

                       170       180       190
                ....*....|....*....|....*....|...
gi 4506191  190 AQGLLVEAVTAGILGDLgSGGNVDACVITKTGA 222
Cdd:cd03750 182 AIHTAILTLKEGFEGQM-TEKNIEIGICGETKG 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 44-199 1.05e-13

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 69.11  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191    44 GLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTG-REPRVATVTRI- 121
Cdd:PTZ00246  36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGePQPVEQLVVQIc 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   122 -LRQTLFRYQG--HVGASLIVGGVDLT-GPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEA 197
Cdd:PTZ00246 116 dLKQSYTQFGGlrPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKV 195


                 ..
gi 4506191   198 VT 199
Cdd:PTZ00246 196 LT 197
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 41-194 3.47e-13

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


Pssm-ID: 239727  Cd Length: 193  Bit Score: 66.45  E-value: 3.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   41 TIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTR 120
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506191  121 ILRQTLFRY---QGHVGASLIVGGVDL-TGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLL 194
Cdd:cd03758  83 FTRRELAESlrsRTPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 231-267 3.92e-11

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: 56.64  E-value: 3.92e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4506191    231 PTEPVKRSGRYHFVPGTTAVLTQTVkPLTLELVEETV 267
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-190 2.31e-10

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: 58.83  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   39 GTTIaGLVFQDGVILGADtratndSVVADK-----SCEKIHFIAPKIYCCGAGVAADAemttRMVASKMELHALSTGREP 113
Cdd:cd03751  31 GTAI-GIRCKDGVVLAVE------KLVTSKlyepgSNKRIFNVDRHIGIAVAGLLADG----RHLVSRAREEAENYRDNY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  114 RVATVTRILRQTLFRY-QGHV--------GASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPN 184
Cdd:cd03751 100 GTPIPVKVLADRVAMYmHAYTlyssvrpfGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSE 179


                ....*.
gi 4506191  185 MTLEAA 190
Cdd:cd03751 180 LTCREA 185
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-224 3.40e-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: 57.97  E-value: 3.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   38 TGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKM-ELHALSTGREPRVA 116
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLViDDECLDDGHSLSPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  117 TV----TRIL--RQTLFRyqgHVGASLIVGGVDLTG-PQLYGVHPHGSYSRLPFTALGSGQDAALAVLED--RFQPNMTL 187
Cdd:cd03760  81 EIhsylTRVLynRRSKMN---PLWNTLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREawEKKPDLTE 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4506191  188 EAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKL 224
Cdd:cd03760 158 EEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEI 194
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-197 4.62e-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: 57.76  E-value: 4.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   30 LKVPHAR---KTGTTIAGLVFQDGVILGADTRATNdSVVADKSCEKIHFIAPKIYCCGAGVAADAemttRMVASKMEL-- 104
Cdd:cd03755  15 FQVEYAQeavRKGTTAVGVRGKDCVVLGVEKKSVA-KLQDPRTVRKICMLDDHVCLAFAGLTADA----RVLINRARLec 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  105 --HALSTGREPRVATVTRILRQTLFRY--QGHV---GASLIVGGVDLTG-PQLYGVHPHGSYSRLPFTALGSGQDAALAV 176
Cdd:cd03755  90 qsHRLTVEDPVTVEYITRYIAGLQQRYtqSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREF 169

                       170       180
                ....*....|....*....|.
gi 4506191  177 LEDRFQPNMTLEAAQGLLVEA 197
Cdd:cd03755 170 LEKNYKEEMTRDDTIKLAIKA 190
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-204 2.18e-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: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   35 ARKTGTTIAGLVFQDGVILGADTRATNDsvVADKScEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPR 114
Cdd:cd03749  23 AVKQGSATVGLKSKTHAVLVALKRATSE--LSSYQ-KKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  115 VATVTRILRQtlfRYQGHV--------GASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQ--PN 184
Cdd:cd03749 100 VSRLVSKVAE---KAQINTqrygrrpyGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFEefED 176

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4506191  185 MTLE---------------AAQGLLVEAVTAGILG 204
Cdd:cd03749 177 CSLEelikhalralretlpGEQELTIKNVSIAIVG 211
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 38-221 1.08e-05

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: 44.93  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191   38 TGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVAT 117
Cdd:cd03759   2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506191  118 VTRILRQTLfrYQGHVG---ASLIVGGVDLTG-PQLYGVHPHGSYSrLP--FTALGSGQDAALAVLEDRFQPNMTLEAAQ 191
Cdd:cd03759  82 FSSLISSLL--YEKRFGpyfVEPVVAGLDPDGkPFICTMDLIGCPS-IPsdFVVSGTASEQLYGMCESLWRPDMEPDELF 158

                       170       180       190
                ....*....|....*....|....*....|
gi 4506191  192 GLLVEAVTAGILGDLGSGGNVDACVITKTG 221
Cdd:cd03759 159 ETISQALLSAVDRDALSGWGAVVYIITKDK 188
 
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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