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Conserved domains on  [gi|190340004|gb|AAI63781|]
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Proteasome (prosome, macropain) subunit, beta type, 7 [Danio rerio]

Protein Classification

proteasome subunit beta( domain architecture ID 10132940)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-232 1.67e-143

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: 400.42  E-value: 1.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGYIGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDAIA 203
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 190340004 204 AGIFNDLGSGSNIDVCVITKGKVDYLRPH 232
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 1.37e-12

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: 60.49  E-value: 1.37e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 190340004  235 ANKKGVRTGSYRYKHGTTGVLSKAVtPLNLDMVEESV 271
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 ...
 44-232 1.67e-143

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: 400.42  E-value: 1.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGYIGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDAIA 203
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 190340004 204 AGIFNDLGSGSNIDVCVITKGKVDYLRPH 232
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 1.60e-66

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: 205.11  E-value: 1.60e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004   41 KTGTTICGIVYKDGVVLGADTRATEGMIVADKN-CSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  120 ----ATANRMLKQMLFRYQGYIGAALVLGGVDCTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 190340004  195 KSLVRDAIAAGIFNDLGSGSNIDVCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 36-233 2.45e-47

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 157.61  E-value: 2.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  36 SPAARKTGTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGR 115
Cdd:COG0638   28 AREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 116 LPRVATANRMLKQMLF-----RYQGYiGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDME 190
Cdd:COG0638  108 PISVEGLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 190340004 191 EEDAKSLVRDAIAAGIFNDLGSGSNIDVCVITKGKVDYLRPHD 233
Cdd:COG0638  187 LDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-223 2.55e-47

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: 156.22  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004   43 GTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  123 NRMLKQMLF--RYQGYIgAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRD 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|...
gi 190340004  201 AIAAGIFNDLGSGSNIDVCVITK 223
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITK 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-218 7.95e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 99.29  E-value: 7.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  34 FSSPAARKT-----GTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLEL 108
Cdd:PTZ00488  25 FDHGDANKAiefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 109 HSLSTGRLPRVATANRMLKQMLFRYQGY-IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRP 187
Cdd:PTZ00488 105 YELRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|.
gi 190340004 188 DMEEEDAKSLVRDAIAAGIFNDLGSGSNIDV 218
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINL 215
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 1.37e-12

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: 60.49  E-value: 1.37e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 190340004  235 ANKKGVRTGSYRYKHGTTGVLSKAVtPLNLDMVEESV 271
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 ...
 44-232 1.67e-143

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: 400.42  E-value: 1.67e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGYIGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDAIA 203
Cdd:cd03763   81 TMLKQHLFRYQGHIGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKKLVCEAIE 160

                        170       180
                 ....*....|....*....|....*....
gi 190340004 204 AGIFNDLGSGSNIDVCVITKGKVDYLRPH 232
Cdd:cd03763  161 AGIFNDLGSGSNVDLCVITKDGVEYLRNY 189
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 44-230 1.57e-86

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: 256.22  E-value: 1.57e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGY-IGAALVLGGVDC-TGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDA 201
Cdd:cd01912   81 NLLSNILYSYRGFpYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                        170       180
                 ....*....|....*....|....*....
gi 190340004 202 IAAGIFNDLGSGSNIDVCVITKGKVDYLR 230
Cdd:cd01912  161 IDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 44-221 1.60e-68

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: 210.04  E-value: 1.60e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGY---IGAALVLGGVDC-TGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVR 199
Cdd:cd01906   81 KLLANLLYEYTQSlrpLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                        170       180
                 ....*....|....*....|..
gi 190340004 200 DAIAAGIFNDLGSGSNIDVCVI 221
Cdd:cd01906  161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 41-221 1.60e-66

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: 205.11  E-value: 1.60e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004   41 KTGTTICGIVYKDGVVLGADTRATEGMIVADKN-CSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRV 119
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDtVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  120 ----ATANRMLKQMLFRYQGYIGAALVLGGVDCTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDA 194
Cdd:pfam00227  82 elaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEEA 161

                         170       180
                  ....*....|....*....|....*..
gi 190340004  195 KSLVRDAIAAGIFNDLGSGSNIDVCVI 221
Cdd:pfam00227 162 VELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-223 1.14e-47

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: 157.03  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLF--RYQGYIgAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDA 201
Cdd:cd03764   81 TLLSNILNssKYFPYI-VQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIRA 159

                        170       180
                 ....*....|....*....|..
gi 190340004 202 IAAGIFNDLGSGSNIDVCVITK 223
Cdd:cd03764  160 IKSAIERDSASGDGIDVVVITK 181
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 36-233 2.45e-47

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 157.61  E-value: 2.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  36 SPAARKTGTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGR 115
Cdd:COG0638   28 AREAVKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 116 LPRVATANRMLKQMLF-----RYQGYiGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDME 190
Cdd:COG0638  108 PISVEGLAKLLSDLLQgytqyGVRPF-GVALLIGGVDDGGPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYREDLS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 190340004 191 EEDAKSLVRDAIAAGIFNDLGSGSNIDVCVITKGKVDYLRPHD 233
Cdd:COG0638  187 LDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELSEEE 229
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 43-223 2.55e-47

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: 156.22  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004   43 GTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATA 122
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  123 NRMLKQMLF--RYQGYIgAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRD 200
Cdd:TIGR03634  81 ATLLSNILNsnRFFPFI-VQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAVR 159

                         170       180
                  ....*....|....*....|...
gi 190340004  201 AIAAGIFNDLGSGSNIDVCVITK 223
Cdd:TIGR03634 160 AIKSAIERDVASGNGIDVAVITK 182
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-227 1.17e-45

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 151.99  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03762    1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGYIGAALVLGGVDCT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDAI 202
Cdd:cd03762   81 SLFKNLCYNYKEMLSAGIIVAGWDEQnGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                        170       180
                 ....*....|....*....|....*
gi 190340004 203 AAGIFNDLGSGSNIDVCVITKGKVD 227
Cdd:cd03762  161 SLAMSRDGSSGGVIRLVIITKDGVE 185
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 44-204 1.24e-45

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: 151.01  E-value: 1.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQ--GYIGAALVLGGVDCTGPHLYSIYPHGSTDKLP-YVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRD 200
Cdd:cd01901   81 KELAKLLQVYTqgRPFGVNLIVAGVDEGGGNLYYIDPSGPVIENPgAVATGSRSQRAKSLLEKLYKPDMTLEEAVELALK 160


                 ....
gi 190340004 201 AIAA 204
Cdd:cd01901  161 ALKS 164
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-224 3.15e-31

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: 114.65  E-value: 3.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  44 TTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATAN 123
Cdd:cd03761    1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQMLFRYQGY-IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRDAI 202
Cdd:cd03761   81 KLLSNMLYQYKGMgLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARRAI 160

                        170       180
                 ....*....|....*....|..
gi 190340004 203 AAGIFNDLGSGSNIDVCVITKG 224
Cdd:cd03761  161 YHATHRDAYSGGNVNLYHVRED 182
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 34-218 7.95e-25

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 99.29  E-value: 7.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  34 FSSPAARKT-----GTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLEL 108
Cdd:PTZ00488  25 FDHGDANKAiefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 109 HSLSTGRLPRVATANRMLKQMLFRYQGY-IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRP 187
Cdd:PTZ00488 105 YELRNGELISVAAASKILANIVWNYKGMgLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKW 184

                        170       180       190
                 ....*....|....*....|....*....|.
gi 190340004 188 DMEEEDAKSLVRDAIAAGIFNDLGSGSNIDV 218
Cdd:PTZ00488 185 DLNDEEAQDLGRRAIYHATFRDAYSGGAINL 215
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-222 1.84e-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: 94.70  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  39 ARKTGTTICGIVYKDGVVLGADTRATEGMIVADkNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPR 118
Cdd:cd03756   24 AVKRGTTALGIKCKEGVVLAVDKRITSKLVEPE-SIEKIYKIDDHVGAATSGLVADARVLIDRARVEAQIHRLTYGEPID 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 119 VATANRM---LKQMLFRYQGY--IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEED 193
Cdd:cd03756  103 VEVLVKKicdLKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLEE 182

                        170       180
                 ....*....|....*....|....*....
gi 190340004 194 AKSLVRDAIAAGIfNDLGSGSNIDVCVIT 222
Cdd:cd03756  183 AIELALKALYAAL-EENETPENVEIAYVT 210
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 43-223 4.67e-18

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: 80.38  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  43 GTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVATA 122
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 123 NRMLKQML-----FRYQGYIgaalVLGGVDCTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFE---------DRYRP 187
Cdd:cd03757   88 AQLLSTILysrrfFPYYVFN----ILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrknqnNVERT 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 190340004 188 DMEEEDAKSLVRDAIAAGIFNDLGSGSNIDVCVITK 223
Cdd:cd03757  164 PLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK 199
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
39-222 1.36e-17

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 79.49  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  39 ARKTGTTICGIVYKDGVVLGADTRATEGMIVADKnCSKIHYISPNIYCCGAGTAAD-------TEMTTQIissnlelHSL 111
Cdd:PRK03996  32 AVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSS-IEKIFKIDDHIGAASAGLVADarvlidrARVEAQI-------NRL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 112 STGRLPRVAT-ANRM--LKQMLFRYQGY--IGAALVLGGVDCTGPHLYSIYPHGSTdkLPY--VTMGSGSLAAMAVFEDR 184
Cdd:PRK03996 104 TYGEPIGVETlTKKIcdHKQQYTQHGGVrpFGVALLIAGVDDGGPRLFETDPSGAY--LEYkaTAIGAGRDTVMEFLEKN 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 190340004 185 YRPDMEEEDAKSLVRDAIAAGIfNDLGSGSNIDVCVIT 222
Cdd:PRK03996 182 YKEDLSLEEAIELALKALAKAN-EGKLDPENVEIAYID 218
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 45-203 1.85e-17

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: 78.40  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  45 TICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRV-ATAN 123
Cdd:cd03758    3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPkAAAN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 124 RMLKQML--FRYQGYIGAALVLGGVD-CTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLVRD 200
Cdd:cd03758   83 FTRRELAesLRSRTPYQVNLLLAGYDkVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKK 162


                 ...
gi 190340004 201 AIA 203
Cdd:cd03758  163 CIK 165
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-231 1.35e-16

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: 76.07  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  42 TGTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAAD----TEMTTQIISSNLEL---HSLST- 113
Cdd:cd03760    1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADfqylKRLLDQLVIDDECLddgHSLSPk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 114 ---GRLPRVATANRMLKQMLFRyqgyigaALVLGGVDCTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYR--P 187
Cdd:cd03760   81 eihSYLTRVLYNRRSKMNPLWN-------TLVVGGVDNEGePFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkP 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 190340004 188 DMEEEDAKSLVRDAIAAGIFNDLGSGSNIDVCVITKGKVDYLRP 231
Cdd:cd03760  154 DLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEIEGP 197
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-221 2.05e-15

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: 72.86  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  38 AARKTGTTIcGIVYKDGVVLGADTRATEGMIVADKNcSKIHYISPNIYCCGAGTAADTEMTTQI---ISSNlelHSLSTG 114
Cdd:cd01911   23 AVKNGSTAV-GIKGKDGVVLAVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADARVLVNRarvEAQN---YRYTYG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 115 RLPRVAT-ANRM--LKQMLFRYQGY--IGAALVLGGVD-CTGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFED 183
Cdd:cd01911   98 EPIPVEVlVKRIadLAQVYTQYGGVrpFGVSLLIAGYDeEGGPQLYQTDPSGT-----YFGykataIGKGSQEAKTFLEK 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 190340004 184 RYRPDMEEEDAKSLVRDAIAAGIFNDLgSGSNIDVCVI 221
Cdd:cd01911  173 RYKKDLTLEEAIKLALKALKEVLEEDK-KAKNIEIAVV 209
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-226 9.06e-14

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: 68.04  E-value: 9.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  42 TGTTICGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVAT 121
Cdd:cd03759    2 NGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 122 ANRMLKQMLF--RYQGYIGAALV----------LGGVDCTGPhlysiyPHGSTDklpYVTMGSGSLAAMAVFEDRYRPDM 189
Cdd:cd03759   82 FSSLISSLLYekRFGPYFVEPVVagldpdgkpfICTMDLIGC------PSIPSD---FVVSGTASEQLYGMCESLWRPDM 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 190340004 190 EEEDAKSLVRDAIAAGIFNDLGSGSNIDVCVITKGKV 226
Cdd:cd03759  153 EPDELFETISQALLSAVDRDALSGWGAVVYIITKDKV 189
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-198 4.69e-13

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: 66.59  E-value: 4.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  39 ARKTGTTICGIVYKDGVVLGADTRATEGMIVADkNCSKIHYISPNIYCCGAGTAADTEmtTQIISSNLEL--HSLSTGRL 116
Cdd:cd03753   23 AIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPS-SVEKIMEIDDHIGCAMSGLIADAR--TLIDHARVEAqnHRFTYNEP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 117 PRV-----ATANRML--------KQMLFRYqgyIGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFED 183
Cdd:cd03753  100 MTVesvtqAVSDLALqfgegddgKKAMSRP---FGVALLIAGVDENGPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQE 176

                        170
                 ....*....|....*
gi 190340004 184 RYRPDMEEEDAKSLV 198
Cdd:cd03753  177 KYHKDMTLEEAEKLA 191
Pr_beta_C pfam12465
Proteasome beta subunits C terminal; This domain family is found in eukaryotes, and is ...
 235-271 1.37e-12

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: 60.49  E-value: 1.37e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 190340004  235 ANKKGVRTGSYRYKHGTTGVLSKAVtPLNLDMVEESV 271
Cdd:pfam12465   1 PNERGERQGSYKFKRGTTAVLSETV-PLKLEVVEEVV 36
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-230 1.20e-11

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: 62.72  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  38 AARKTGTTICGIVYKDGVVLgADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLP 117
Cdd:cd03750   22 AAVSSGAPSVGIKAANGVVL-ATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 118 RVataNRMLKQMLFRYQGY--------IGAALVLGGVDCTGPHLYSIYPHGStdklpYVT-----MGSGSLAAMAVFEDR 184
Cdd:cd03750  101 PV---SQLVREIASVMQEYtqsggvrpFGVSLLIAGWDEGGPYLYQVDPSGS-----YFTwkataIGKNYSNAKTFLEKR 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 190340004 185 YRPDMEEEDAKSLVRDAIAAGIFNDLgSGSNIDVCVITKGKV----------DYLR 230
Cdd:cd03750  173 YNEDLELEDAIHTAILTLKEGFEGQM-TEKNIEIGICGETKGfrlltpaeikDYLA 227
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-194 1.92e-08

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 53.44  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  38 AARKTGTTIcGIVYKDGVVLGADTRATEGMIVADKNcSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGR-L 116
Cdd:cd03751   26 AVENSGTAI-GIRCKDGVVLAVEKLVTSKLYEPGSN-KRIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTpI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 117 PRVATANR--MLKQMLFRYQGY--IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEE 192
Cdd:cd03751  104 PVKVLADRvaMYMHAYTLYSSVrpFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIGKGKQAAKTELEKLKFSELTCR 183


                 ..
gi 190340004 193 DA 194
Cdd:cd03751  184 EA 185
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 48-227 2.64e-07

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 50.62  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  48 GIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLPRVataNRMLK 127
Cdd:PTZ00246  36 GILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPV---EQLVV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 128 QMLFRYQGY--------IGAALVLGGVDCT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEEEDAKSLV 198
Cdd:PTZ00246 113 QICDLKQSYtqfgglrpFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLA 192

                        170       180
                 ....*....|....*....|....*....
gi 190340004 199 RDAIAAGIFNDLGSGSNIDVCVITKGKVD 227
Cdd:PTZ00246 193 AKVLTKSMDSTSPKADKIEVGILSHGETD 221
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-198 3.55e-07

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


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 49.65  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  38 AARKTGTTIcGIVYKDGVVLGADTRATEGMIVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLP 117
Cdd:cd03752   25 AISHAGTCL-GILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 118 RVATANRML---KQMLFRYQGY--IGAALVLGGVDCT-GPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEE 191
Cdd:cd03752  104 PVEQLVQRLcdiKQGYTQYGGLrpFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATAIGNNNQAAQSLLKQDYKDDMTL 183


                 ....*..
gi 190340004 192 EDAKSLV 198
Cdd:cd03752  184 EEALALA 190
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-221 1.88e-06

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: 47.36  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  38 AARKtGTTICGIVYKDGVVLGADTRATEGMiVADKNCSKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGRLP 117
Cdd:cd03755   23 AVRK-GTTAVGVRGKDCVVLGVEKKSVAKL-QDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 118 RVATANRMLKQMLFRY--QGYI---GAALVLGGVDCTG-PHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRPDMEE 191
Cdd:cd03755  101 TVEYITRYIAGLQQRYtqSGGVrpfGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIGRNSKTVREFLEKNYKEEMTR 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 190340004 192 EDAKSLVRDAIAAGIfnDLGSGsNIDVCVI 221
Cdd:cd03755  181 DDTIKLAIKALLEVV--QSGSK-NIELAVM 207
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 39-204 7.15e-06

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: 45.74  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004  39 ARKTGTTICGIVYKDGVVLGADTRATEGMIVADKncsKIHYISPNIYCCGAGTAADTEMTTQIISSNLELHSLSTGR-LP 117
Cdd:cd03749   23 AVKQGSATVGLKSKTHAVLVALKRATSELSSYQK---KIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSpIP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190340004 118 RVATANRMLKQMLFRYQGY----IGAALVLGGVDCTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDRYRpDMEEED 193
Cdd:cd03749  100 VSRLVSKVAEKAQINTQRYgrrpYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARSQSARTYLERHFE-EFEDCS 178

                        170
                 ....*....|.
gi 190340004 194 AKSLVRDAIAA 204
Cdd:cd03749  179 LEELIKHALRA 189
 
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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