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Conserved domains on  [gi|8567394|ref|NP_038613|]
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proteasome subunit beta type-9 isoform 1 [Mus musculus]

Protein Classification

proteasome subunit beta type-6 family protein( domain architecture ID 10132932)

proteasome subunit beta type-6 family protein, similar to proteasome subunit beta type-6 and type-9, is part of the 20S proteasome, a multi-subunit proteolytic complex that is central in nonlysosomal protein degradation in both the cytosol and nucleus.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-207 8.70e-108

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: 307.61  E-value: 8.70e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYREDLLAHLIVAGWDQCEGGQVY-GTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTDAI 179
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYsIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 8567394  180 TLAMNRDGSSGGVIYLVTITAAGVDHRV 207
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-207 8.70e-108

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: 307.61  E-value: 8.70e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYREDLLAHLIVAGWDQCEGGQVY-GTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTDAI 179
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYsIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 8567394  180 TLAMNRDGSSGGVIYLVTITAAGVDHRV 207
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 17-198 1.05e-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: 150.03  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     17 VHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRV-FDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPL 95
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     96 VLAAANVV----KNISYKYREDLLAHLIVAGWDQCEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEE 170
Cdd:pfam00227  81 VELAARIAdllqAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIdPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 8567394    171 CRRFTTDAITLAMNRDGSSGGVIYLVTI 198
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-204 5.79e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 5.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    5 GAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLE 84
Cdd:COG0638  20 GRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQ 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   85 LHGLELEEPPLVLAAANVVKNI-----SYKYReDLLAHLIVAGWDQcEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYV 158
Cdd:COG0638 100 LYELRYGEPISVEGLAKLLSDLlqgytQYGVR-PFGVALLIGGVDD-GGPRLFSTdPSGGLYEEKAVAIGSGSPFARGVL 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 8567394  159 DAAYKPGMTPEECRRFTTDAITLAMNRDGSSGGVIYLVTITAAGVD 204
Cdd:COG0638 178 EKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 20-203 6.07e-27

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: 101.52  E-value: 6.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     20 GTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAA 99
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    100 ANVVKNISYKYR-EDLLAHLIVAGWDQcEGGQVYGT--MGGMlIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTT 176
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdpAGGI-IEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 8567394    177 DAITLAMNRDGSSGGVIYLVTITAAGV 203
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 16-202 1.64e-21

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 88.89  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    16 EVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPL 95
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    96 VLAAANVVKNISYKYRE-DLLAHLIVAGWDQcEGGQVY--GTMGGMLIRQPFTIgGSGSSYIYGYVDAAYKPGMTPEECR 172
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWDK-KGPGLFyvDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567394   173 RFTTDAITLAMNRDGSSGGVIYLVTITAAG 202
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-207 8.70e-108

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: 307.61  E-value: 8.70e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYREDLLAHLIVAGWDQCEGGQVY-GTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTDAI 179
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYsIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 8567394  180 TLAMNRDGSSGGVIYLVTITAAGVDHRV 207
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 21-206 5.79e-63

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: 193.81  E-value: 5.79e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYRE-DLLAHLIVAGWDQCEGGQVYG-TMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTDA 178
Cdd:cd01912  81 NLLSNILYSYRGfPYYVSLIVGGVDKGGGPFLYYvDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
gi 8567394  179 ITLAMNRDGSSGGVIYLVTITAAGVDHR 206
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 21-198 9.77e-50

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: 159.97  E-value: 9.77e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYRE---DLLAHLIVAGWDQCEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTT 176
Cdd:cd01906  81 KLLANLLYEYTQslrPLGVSLLVAGVDEEGGPQLYSVdPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 8567394  177 DAITLAMNRDGSSGGVIYLVTI 198
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 17-198 1.05e-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: 150.03  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     17 VHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRV-FDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPL 95
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     96 VLAAANVV----KNISYKYREDLLAHLIVAGWDQCEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEE 170
Cdd:pfam00227  81 VELAARIAdllqAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIdPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 8567394    171 CRRFTTDAITLAMNRDGSSGGVIYLVTI 198
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 21-179 3.99e-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: 111.72  E-value: 3.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYRE--DLLAHLIVAGWDQCEGGQVYGTMGGMLIRQP-FTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTD 177
Cdd:cd01901  81 KELAKLLQVYTQgrPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                ..
gi 8567394  178 AI 179
Cdd:cd01901 161 AL 162
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 5-204 5.79e-31

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 113.32  E-value: 5.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    5 GAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLE 84
Cdd:COG0638  20 GRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQ 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   85 LHGLELEEPPLVLAAANVVKNI-----SYKYReDLLAHLIVAGWDQcEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYV 158
Cdd:COG0638 100 LYELRYGEPISVEGLAKLLSDLlqgytQYGVR-PFGVALLIGGVDD-GGPRLFSTdPSGGLYEEKAVAIGSGSPFARGVL 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 8567394  159 DAAYKPGMTPEECRRFTTDAITLAMNRDGSSGGVIYLVTITAAGVD 204
Cdd:COG0638 178 EKEYREDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-205 4.56e-27

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: 101.89  E-value: 4.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYREDLLAHLIVAGWDqCEGGQVYGTMG-GMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTDAI 179
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVD-YTGPHLYSIYPhGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAI 159

                       170       180
                ....*....|....*....|....*.
gi 8567394  180 TLAMNRDGSSGGVIYLVTITAAGVDH 205
Cdd:cd03763 160 EAGIFNDLGSGSNVDLCVITKDGVEY 185
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 20-203 6.07e-27

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: 101.52  E-value: 6.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     20 GTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAA 99
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    100 ANVVKNISYKYR-EDLLAHLIVAGWDQcEGGQVYGT--MGGMlIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTT 176
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDE-EGPHLYSLdpAGGI-IEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 8567394    177 DAITLAMNRDGSSGGVIYLVTITAAGV 203
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-202 2.07e-26

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: 100.40  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNI--SYKYREdLLAHLIVAGWDQcEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTD 177
Cdd:cd03764  81 TLLSNIlnSSKYFP-YIVQLLIGGVDE-EGPHLYSLdPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                       170       180
                ....*....|....*....|....*
gi 8567394  178 AITLAMNRDGSSGGVIYLVTITAAG 202
Cdd:cd03764 159 AIKSAIERDSASGDGIDVVVITKDG 183
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 21-206 1.62e-22

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: 90.00  E-value: 1.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAA 100
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  101 NVVKNISYKYR-EDLLAHLIVAGWDQCEGGQVYGTMGGMLIR-QPFTIGgSGSSYIYGYVDAAYKPGMTPEECRRFTTDA 178
Cdd:cd03761  81 KLLSNMLYQYKgMGLSMGTMICGWDKTGPGLYYVDSDGTRLKgDLFSVG-SGSTYAYGVLDSGYRYDLSVEEAYDLARRA 159

                       170       180
                ....*....|....*....|....*...
gi 8567394  179 ITLAMNRDGSSGGVIYLVTITAAGVDHR 206
Cdd:cd03761 160 IYHATHRDAYSGGNVNLYHVREDGWRKI 187
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 16-202 1.64e-21

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 88.89  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    16 EVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPL 95
Cdd:PTZ00488  35 EFAHGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    96 VLAAANVVKNISYKYRE-DLLAHLIVAGWDQcEGGQVY--GTMGGMLIRQPFTIgGSGSSYIYGYVDAAYKPGMTPEECR 172
Cdd:PTZ00488 115 VAAASKILANIVWNYKGmGLSMGTMICGWDK-KGPGLFyvDNDGTRLHGNMFSC-GSGSTYAYGVLDAGFKWDLNDEEAQ 192

                        170       180       190
                 ....*....|....*....|....*....|
gi 8567394   173 RFTTDAITLAMNRDGSSGGVIYLVTITAAG 202
Cdd:PTZ00488 193 DLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 18-199 4.16e-13

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: 65.34  E-value: 4.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   18 HTGTTIMAVEFDGGVVVGSDSR--VSAGTAVVNrvFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPL 95
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRlgVQQQTVSTD--FQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   96 VLAAANVVKNISYKYRED-LLAHLIVAGWDqcEGGQVY-GTM---GGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEE 170
Cdd:cd03759  79 PKTFSSLISSLLYEKRFGpYFVEPVVAGLD--PDGKPFiCTMdliGCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 8567394  171 CRRFTTDAITLAMNRDGSS--GGVIYLVTIT 199
Cdd:cd03759 157 LFETISQALLSAVDRDALSgwGAVVYIITKD 187
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-170 7.18e-09

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: 53.36  E-value: 7.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   32 VVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIAD-----MAAYQlelhgLELEEPPLVLAAANVV-KN 105
Cdd:cd03758  13 VILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEyiqknIQLYK-----MRNGYELSPKAAANFTrRE 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8567394  106 ISYKYREDLLAH--LIVAGWDQCEGGQVY-----GTMggmlIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEE 170
Cdd:cd03758  88 LAESLRSRTPYQvnLLLAGYDKVEGPSLYyidylGTL----VKVPYAAHGYGAYFCLSILDRYYKPDMTVEE 155
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 20-208 5.32e-08

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: 51.49  E-value: 5.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   20 GTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAA 99
Cdd:cd03757   8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394  100 ANVVKNISYKYRE-DLLAHLIVAGWDQCEGGQVYG-TMGGMLIRQPFTIGGSGSSYIYGYVD----------AAYKPgMT 167
Cdd:cd03757  88 AQLLSTILYSRRFfPYYVFNILAGIDEEGKGVVYSyDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnnVERTP-LS 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 8567394  168 PEECRRFTTDAITLAMNRDGSSGGVIYLVTITAAGVDHRVI 208
Cdd:cd03757 167 LEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 20-202 9.11e-08

proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the 20S proteasome as found in Actinobacteria such as Mycobacterium, Rhodococcus, and Streptomyces. In Streptomyces, maturation during proteasome assembly was shown to remove a 53-amino acid propeptide. Most of the length of the propeptide is not included in this model. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163402 [Multi-domain]  Cd Length: 219  Bit Score: 50.86  E-value: 9.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394     20 GTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAA 99
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYEKIEGVPLTLDGK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394    100 ANvvkNISYKYREDLLAHL-------IVAGWDQCEG-GQV--YGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPE 169
Cdd:TIGR03690  82 AN---RLAAMVRGNLPAAMqglavvpLLAGYDLDAGaGRIfsYDVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDED 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 8567394    170 ECRRFTTDAITLAMNRDGSSGGV-----IY--LVTITAAG 202
Cdd:TIGR03690 159 DALRVAVEALYDAADDDSATGGPdlvrgIYptVVVITADG 198
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 15-198 2.18e-05

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: 43.86  E-value: 2.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   15 EEVHTGTTIMAVEFDGGVVVGSDSRVsAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMAAYQLELHGLELEEPP 94
Cdd:cd03756  23 EAVKRGTTALGIKCKEGVVLAVDKRI-TSKLVEPESIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPI 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567394   95 LVLAAANVVKNISYKYRE-----DLLAHLIVAGWDQcEGGQVYGT-MGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTP 168
Cdd:cd03756 102 DVEVLVKKICDLKQQYTQhggvrPFGVALLIAGVDD-GGPRLFETdPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSL 180

                       170       180       190
                ....*....|....*....|....*....|.
gi 8567394  169 EECRRFTTDAITLAMNRDGSSGGV-IYLVTI 198
Cdd:cd03756 181 EEAIELALKALYAALEENETPENVeIAYVTV 211
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 14-79 3.71e-05

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: 43.09  E-value: 3.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8567394   14 TEEVHTGTTIMAVEFDGGVVVGSDSRVSAgTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMA 79
Cdd:cd03753  21 IEAIKLGSTAIGIKTKEGVVLAVEKRITS-PLMEPSSVEKIMEIDDHIGCAMSGLIADARTLIDHA 85
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 19-75 1.57e-04

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: 41.02  E-value: 1.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8567394   19 TGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAI 75
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYL 57
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 21-72 1.34e-03

Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system that is the prokaryotic homolog of the proteasome. HslV is a dimer of hexamers (a dodecamer) that forms a central proteolytic chamber with active sites on the interior walls of the cavity. HslV shares significant sequence and structural similarity with the proteasomal beta-subunit and both are members of the Ntn-family of hydrolases. HslV has a nucleophilic threonine residue at its N-terminus that is exposed after processing of the propeptide and is directly involved in active site catalysis.


Pssm-ID: 238894  Cd Length: 171  Bit Score: 37.94  E-value: 1.34e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 8567394   21 TTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPL-HQHIFCALSGSAADA 72
Cdd:cd01913   1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLyNGKVIAGFAGSTADA 53
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 29-79 1.40e-03

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 38.68  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 8567394    29 DGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQHIFCALSGSAADAQAIADMA 79
Cdd:PTZ00246  40 KEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQC 90
 
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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