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Conserved domains on  [gi|1085618496|pdb|5T0H|Q]
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Chain Q, Proteasome subunit beta type-2

Protein Classification

proteasome subunit beta( domain architecture ID 10132911)

proteasome subunit beta is a non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus; belongs to the N-terminal nucleophile (Ntn)-hydrolase superfamily

CATH:  3.60.20.10
Gene Ontology:  GO:0043161|GO:0010498|GO:0005839
MEROPS:  T01
PubMed:  7682410|8882582|1317508|7697118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 4.18e-115

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: 325.31  E-value: 4.18e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       81 ANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|..
5T0H_Q      161 RKCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 4.18e-115

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: 325.31  E-value: 4.18e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       81 ANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|..
5T0H_Q      161 RKCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 2.92e-45

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: 148.10  E-value: 2.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q          5 IGIQGPDYVLVASD-RVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADkRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q         84 TRRNLADCLRS-RTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
5T0H_Q        163 CLEELQKRFILNLPTFSVRII 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 4.43e-19

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 81.34  E-value: 4.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASD-RVAASNIVqMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:COG0638  39 VGIKTKDGVVLAADrRATMGNLI-ASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 trrnLADCLRSRT-----PYHVNLLLAGYDEhEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVE 158
Cdd:COG0638 118 ----LSDLLQGYTqygvrPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|....
5T0H_Q      159 LLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-164 9.33e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 44.98  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        34 KMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADCLRSRTPYHVNL--LLAGYDEhE 111
Cdd:PTZ00488  72 KVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIVWNYKGMGLSMgtMICGWDK-K 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
5T0H_Q       112 GPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCL 164
Cdd:PTZ00488 147 GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
 
Name Accession Description Interval E-value
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 1-192 4.18e-115

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: 325.31  E-value: 4.18e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAA 80
Cdd:cd03758   1 METLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       81 ANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELL 160
Cdd:cd03758  81 ANFTRRELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELM 160

                       170       180       190
                ....*....|....*....|....*....|..
5T0H_Q      161 RKCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:cd03758 161 KKCIKELKKRFIINLPNFTVKVVDKDGIRDLE 192
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-191 3.90e-68

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: 206.53  E-value: 3.90e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        2 EYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAA 81
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       82 NFTRRNLADclRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLR 161
Cdd:cd01912  81 NLLSNILYS--YRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVK 158

                       170       180       190
                ....*....|....*....|....*....|
5T0H_Q      162 KCLEELQKRFILNLPTFSVRIIDKNGIHDL 191
Cdd:cd01912 159 KAIDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 3-183 2.19e-51

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: 163.43  E-value: 2.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        3 YLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAN 82
Cdd:cd01906   2 TIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       83 FTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRK 162
Cdd:cd01906  82 LLANLLYEYTQSLRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELALK 161

                       170       180
                ....*....|....*....|.
5T0H_Q      163 CLEELQKRFILNLPTFSVRII 183
Cdd:cd01906 162 ALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 5-183 2.92e-45

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: 148.10  E-value: 2.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q          5 IGIQGPDYVLVASD-RVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:pfam00227   8 VGIKGKDGVVLAADkRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVELAARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q         84 TRRNLADCLRS-RTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRK 162
Cdd:pfam00227  88 ADLLQAYTQYSgRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEAVELAVK 167

                         170       180
                  ....*....|....*....|.
5T0H_Q        163 CLEELQKRFILNLPTFSVRII 183
Cdd:pfam00227 168 ALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 5-166 4.86e-31

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: 110.95  E-value: 4.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:cd01901   4 VAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKEL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       85 RRNLADCLRSRtPYHVNLLLAGYDEhEGPALYYMDY-LAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKC 163
Cdd:cd01901  84 AKLLQVYTQGR-PFGVNLIVAGVDE-GGGNLYYIDPsGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALKA 161


                ...
5T0H_Q      164 LEE 166
Cdd:cd01901 162 LKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-192 4.43e-19

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 81.34  E-value: 4.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASD-RVAASNIVqMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:COG0638  39 VGIKTKDGVVLAADrRATMGNLI-ASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 trrnLADCLRSRT-----PYHVNLLLAGYDEhEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVE 158
Cdd:COG0638 118 ----LSDLLQGYTqygvrPFGVALLIGGVDD-GGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLSLDEAVE 192

                       170       180       190
                ....*....|....*....|....*....|....
5T0H_Q      159 LLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:COG0638 193 LALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-192 2.14e-18

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: 78.83  E-value: 2.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASD-RVAASNIVQMKDDhDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03764   4 VGIVCKDGVVLAADkRASMGNFIASKNV-KKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 trrnLADCLRSR--TPYHVNLLLAGYDEhEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLR 161
Cdd:cd03764  83 ----LSNILNSSkyFPYIVQLLIGGVDE-EGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAI 157

                       170       180       190
                ....*....|....*....|....*....|.
5T0H_Q      162 KCLEELQKRFILNLPTFSVRIIDKNGIHDLD 192
Cdd:cd03764 158 RAIKSAIERDSASGDGIDVVVITKDGYKELE 188
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 1.26e-15

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: 71.45  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMR-NGYELSPTAAANF 83
Cdd:cd03760   6 IAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLdDGHSLSPKEIHSY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 -TRRNLADclRSR-TPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYY--TPTISRERAVEL 159
Cdd:cd03760  86 lTRVLYNR--RSKmNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWekKPDLTEEEARAL 163

                       170       180       190
                ....*....|....*....|....*....|
5T0H_Q      160 LRKCLEELQKRFILNLPTFSVRIIDKNGIH 189
Cdd:cd03760 164 IEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-189 4.14e-14

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 68.05  E-value: 4.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASD-RVAASNIVQMKDdHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03757  12 LAIAGNDFAVIAGDtRLSEGYSILSRD-SPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 trrnLADCLRSRT--PYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILD--------RYYTPT-IS 152
Cdd:cd03757  91 ----LSTILYSRRffPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqNNVERTpLS 166

                       170       180       190
                ....*....|....*....|....*....|....*..
5T0H_Q      153 RERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIH 189
Cdd:cd03757 167 LEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIE 203
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-120 6.46e-10

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: 56.10  E-value: 6.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        4 LIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANF 83
Cdd:cd03759   6 VVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTFSSL 85

                        90       100       110
                ....*....|....*....|....*....|....*....
5T0H_Q       84 trrnLADCLRSR--TPYHVNLLLAGYDEHEGPALYYMDY 120
Cdd:cd03759  86 ----ISSLLYEKrfGPYFVEPVVAGLDPDGKPFICTMDL 120
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-119 2.71e-07

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: 48.98  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRVAASnivQMKDDH--DKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSptaAAN 82
Cdd:cd01911  31 VGIKGKDGVVLAVEKKVTS---KLLDPSsvEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIP---VEV 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5T0H_Q       83 FTRRnLADCLRSRT------PYHVNLLLAGYDEHEGPALYYMD 119
Cdd:cd01911 105 LVKR-IADLAQVYTqyggvrPFGVSLLIAGYDEEGGPQLYQTD 146
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-119 2.95e-07

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


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 48.77  E-value: 2.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDR-VAASNIVQMKDDHdkMFKMSEKILLLCVGEAGDT---VQFAEYIQKNvqlYKMRNGYELSPTAA 80
Cdd:cd03754  33 VAVRGKDCAVVVTQKkVPDKLIDPSTVTH--LFRITDEIGCVMTGMIADSrsqVQRARYEAAE---FKYKYGYEMPVDVL 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
5T0H_Q       81 AnftrRNLADCLRSRT------PYHVNLLLAGYDEHEGPALYYMD 119
Cdd:cd03754 108 A----KRIADINQVYTqhaymrPLGVSMILIGIDEELGPQLYKCD 148
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 4-165 3.91e-06

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: 45.29  E-value: 3.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        4 LIGIQGPDYVLVASD-RVAASNIVQMKDDhDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAAN 82
Cdd:cd03762   3 IIAVEYDGGVVLGADsRTSTGSYVANRVT-DKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       83 FTRrNLadCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRK 162
Cdd:cd03762  82 LFK-NL--CYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKN 158


                ...
5T0H_Q      163 CLE 165
Cdd:cd03762 159 ALS 161
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-164 9.33e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 44.98  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        34 KMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADCLRSRTPYHVNL--LLAGYDEhE 111
Cdd:PTZ00488  72 KVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKI----LANIVWNYKGMGLSMgtMICGWDK-K 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
5T0H_Q       112 GPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCL 164
Cdd:PTZ00488 147 GPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 48-162 7.20e-05

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: 41.85  E-value: 7.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       48 GEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFtrrnLADCLRSRTPYH--VNLLLAGYDeHEGPALYYMDYLAALA 125
Cdd:cd03761  47 GGAADCQYWERVLGRECRLYELRNKERISVAAASKL----LSNMLYQYKGMGlsMGTMICGWD-KTGPGLYYVDSDGTRL 121

                        90       100       110
                ....*....|....*....|....*....|....*..
5T0H_Q      126 KAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRK 162
Cdd:cd03761 122 KGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-119 1.44e-04

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: 41.16  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRVAASNIVQmKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGyelSPTAAANFT 84
Cdd:cd03756  32 LGIKCKEGVVLAVDKRITSKLVE-PESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYG---EPIDVEVLV 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
5T0H_Q       85 RRnLADCLRSRT------PYHVNLLLAGYDEHeGPALYYMD 119
Cdd:cd03756 108 KK-ICDLKQQYTqhggvrPFGVALLIAGVDDG-GPRLFETD 146
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-119 2.86e-04

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: 40.41  E-value: 2.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYkmRNGYElSPTAAANFT 84
Cdd:cd03752  33 LGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRY--LYSYQ-EPIPVEQLV 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
5T0H_Q       85 RRnLADCLRSRT------PYHVNLLLAGYDEHEGPALYYMD 119
Cdd:cd03752 110 QR-LCDIKQGYTqygglrPFGVSFLYAGWDKHYGFQLYQSD 149
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 5-119 8.18e-04

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 39.07  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q         5 IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDtvqfAEYIQKNVQLYKMRNGYELSPTAAANFT 84
Cdd:PTZ00246  35 VGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTAD----ANILINQCRLYAQRYRYTYGEPQPVEQL 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
5T0H_Q        85 RRNLADCLRSRT------PYHVNLLLAGYDEHEGPALYYMD 119
Cdd:PTZ00246 111 VVQICDLKQSYTqfgglrPFGVSFLFAGYDENLGYQLYHTD 151
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 5-165 1.43e-03

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: 37.95  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASD-RVAASNIVQMKDdHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYElSPTAAANf 83
Cdd:cd03763   4 VGVVFKDGVVLGADtRATEGPIVADKN-CEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRK-PRVVTAL- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       84 trRNLADCLrsrTPYH----VNLLLAGYDeHEGPALY------YMDYLAALAKapfaahGYGAFLTLSILDRYYTPTISR 153
Cdd:cd03763  81 --TMLKQHL---FRYQghigAALVLGGVD-YTGPHLYsiyphgSTDKLPFVTM------GSGSLAAMSVLEDRYKPDMTE 148

                       170
                ....*....|..
5T0H_Q      154 ERAVELLRKCLE 165
Cdd:cd03763 149 EEAKKLVCEAIE 160
PH_BCR-related cd01228
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 155-187 7.04e-03

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. ABR, a related smaller protein, is structurally similar to BCR, but lacks the N-terminal kinase domain and has GAP activity for both Rac and Cdc42. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269935  Cd Length: 166  Bit Score: 35.79  E-value: 7.04e-03
                        10        20        30
                ....*....|....*....|....*....|...
5T0H_Q      155 RAVELLRKCLEELQKRFILNLPTFSVRIIDKNG 187
Cdd:cd01228 108 KAIEKLRKKLAEQEAALLLASPSLPLRLYHRNG 140
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-167 8.86e-03

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: 35.80  E-value: 8.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q        5 IGIQGPDYVLVASDRvaaSNIVQMKDDHD--KMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRngYELSPT---- 78
Cdd:cd03755  31 VGVRGKDCVVLGVEK---KSVAKLQDPRTvrKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLT--VEDPVTveyi 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5T0H_Q       79 --AAAN----FTRRNladclrSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTIS 152
Cdd:cd03755 106 trYIAGlqqrYTQSG------GVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMT 179

                       170
                ....*....|....*
5T0H_Q      153 RERAVELLRKCLEEL 167
Cdd:cd03755 180 RDDTIKLAIKALLEV 194
 
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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