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Conserved domains on  [gi|24653999|ref|NP_652031|]
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proteasome beta1 subunit [Drosophila melanogaster]

Protein Classification

proteasome subunit beta( domain architecture ID 10132932)

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_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 16-203 5.54e-118

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: 333.42  E-value: 5.54e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAV 175
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 24653999 176 QHAIYHDGSSGGVVRIGIITKDGIERRI 203
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 ...
 16-203 5.54e-118

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: 333.42  E-value: 5.54e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAV 175
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 24653999 176 QHAIYHDGSSGGVVRIGIITKDGIERRI 203
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 12-194 7.89e-54

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: 170.83  E-value: 7.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVT-DKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDAL 90
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    91 V----FEAASEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALED 166
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 24653999   167 CVTFVKKAVQHAIYHDGSSGGVVRIGII 194
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-201 6.62e-36

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 126.41  E-value: 6.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALV 91
Cdd:COG0638  32 VKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  92 FEAASEFRNYCYSYRES----LLAGIIVAGWDEQrGGQVYSI-PLGGmLTRESCTIGGSGSSFIYGFVREHYRPNMALED 166
Cdd:COG0638 112 EGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDG-GPRLFSTdPSGG-LYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24653999 167 CVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIER 201
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 15-199 3.41e-32

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: 115.38  E-value: 3.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    15 GTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEA 94
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    95 ASEFRNYCYSYR-ESLLAGIIVAGWDEQrGGQVYSI-PLGGMlTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVK 172
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDEE-GPHLYSLdPAGGI-IEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 24653999   173 KAVQHAIYHDGSSGGVVRIGIITKDGI 199
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 5-198 1.74e-24

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 96.98  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    5 FDFTDTPVST----GTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNY 80
Cdd:PTZ00488  25 FDHGDANKAIefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999   81 HENQtNKDALVFEAASE-FRNYCYSYRE-SLLAGIIVAGWDEQRGGQVYSIPLGGMLT--RESCtigGSGSSFIYGFVRE 156
Cdd:PTZ00488 105 YELR-NGELISVAAASKiLANIVWNYKGmGLSMGTMICGWDKKGPGLFYVDNDGTRLHgnMFSC---GSGSTYAYGVLDA 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24653999  157 HYRPNMALEDCVTFVKKAVQHAIYHDGSSGGVVRIGIITKDG 198
Cdd:PTZ00488 181 GFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 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 ...
 16-203 5.54e-118

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: 333.42  E-value: 5.54e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd03762   1 TTIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAV 175
Cdd:cd03762  81 SLFKNLCYNYKEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|....*...
gi 24653999 176 QHAIYHDGSSGGVVRIGIITKDGIERRI 203
Cdd:cd03762 161 SLAMSRDGSSGGVIRLVIITKDGVERKF 188
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 16-202 3.67e-74

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: 222.70  E-value: 3.67e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRES-LLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKA 174
Cdd:cd01912  81 NLLSNILYSYRGFpYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAVELVKKA 160

                       170       180
                ....*....|....*....|....*...
gi 24653999 175 VQHAIYHDGSSGGVVRIGIITKDGIERR 202
Cdd:cd01912 161 IDSAIERDLSSGGGVDVAVITKDGVEEL 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 16-194 1.03e-56

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: 178.07  E-value: 1.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRES---LLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVK 172
Cdd:cd01906  81 KLLANLLYEYTQSlrpLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIELAL 160

                       170       180
                ....*....|....*....|..
gi 24653999 173 KAVQHAIYHDGSSGGVVRIGII 194
Cdd:cd01906 161 KALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 12-194 7.89e-54

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: 170.83  E-value: 7.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVT-DKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDAL 90
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    91 V----FEAASEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALED 166
Cdd:pfam00227  81 VelaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLEE 160

                         170       180
                  ....*....|....*....|....*...
gi 24653999   167 CVTFVKKAVQHAIYHDGSSGGVVRIGII 194
Cdd:pfam00227 161 AVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 16-200 4.42e-37

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: 128.08  E-value: 4.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd03763   1 TTIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRESLLAGIIVAGWDeQRGGQVYSI-PLGGMLTRESCTIgGSGSSFIYGFVREHYRPNMALEDCVTFVKKA 174
Cdd:cd03763  81 TMLKQHLFRYQGHIGAALVLGGVD-YTGPHLYSIyPHGSTDKLPFVTM-GSGSLAAMSVLEDRYKPDMTEEEAKKLVCEA 158

                       170       180
                ....*....|....*....|....*.
gi 24653999 175 VQHAIYHDGSSGGVVRIGIITKDGIE 200
Cdd:cd03763 159 IEAGIFNDLGSGSNVDLCVITKDGVE 184
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 12-201 6.62e-36

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 126.41  E-value: 6.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALV 91
Cdd:COG0638  32 VKRGTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  92 FEAASEFRNYCYSYRES----LLAGIIVAGWDEQrGGQVYSI-PLGGmLTRESCTIGGSGSSFIYGFVREHYRPNMALED 166
Cdd:COG0638 112 EGLAKLLSDLLQGYTQYgvrpFGVALLIGGVDDG-GPRLFSTdPSGG-LYEEKAVAIGSGSPFARGVLEKEYREDLSLDE 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24653999 167 CVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIER 201
Cdd:COG0638 190 AVELALRALYSAAERDSASGDGIDVAVITEDGFRE 224
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 16-177 1.64e-34

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: 120.58  E-value: 1.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRES--LLAGIIVAGWDEqRGGQVYSI-PLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVK 172
Cdd:cd01901  81 KELAKLLQVYTQGrpFGVNLIVAGVDE-GGGNLYYIdPSGPVIENPGAVATGSRSQRAKSLLEKLYKPDMTLEEAVELAL 159


                ....*
gi 24653999 173 KAVQH 177
Cdd:cd01901 160 KALKS 164
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
 15-199 3.41e-32

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: 115.38  E-value: 3.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    15 GTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEA 94
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGNFVASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    95 ASEFRNYCYSYR-ESLLAGIIVAGWDEQrGGQVYSI-PLGGMlTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVK 172
Cdd:TIGR03634  81 ATLLSNILNSNRfFPFIVQLLVGGVDEE-GPHLYSLdPAGGI-IEDDYTATGSGSPVAYGVLEDEYREDMSVEEAKKLAV 158

                         170       180
                  ....*....|....*....|....*..
gi 24653999   173 KAVQHAIYHDGSSGGVVRIGIITKDGI 199
Cdd:TIGR03634 159 RAIKSAIERDVASGNGIDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 16-202 5.46e-31

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: 112.35  E-value: 5.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAA 95
Cdd:cd03764   1 TTTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SEFRNYCYSYRE-SLLAGIIVAGWDEQrGGQVYSI-PLGGMlTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKK 173
Cdd:cd03764  81 TLLSNILNSSKYfPYIVQLLIGGVDEE-GPHLYSLdPLGSI-IEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKLAIR 158

                       170       180
                ....*....|....*....|....*....
gi 24653999 174 AVQHAIYHDGSSGGVVRIGIITKDGIERR 202
Cdd:cd03764 159 AIKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 16-202 1.76e-25

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: 98.09  E-value: 1.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHEnQTNKDALVFEAA 95
Cdd:cd03761   1 TTTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYE-LRNKERISVAAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  96 SE-FRNYCYSYR-ESLLAGIIVAGWDEqRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKK 173
Cdd:cd03761  80 SKlLSNMLYQYKgMGLSMGTMICGWDK-TGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLARR 158

                       170       180
                ....*....|....*....|....*....
gi 24653999 174 AVQHAIYHDGSSGGVVRIGIITKDGIERR 202
Cdd:cd03761 159 AIYHATHRDAYSGGNVNLYHVREDGWRKI 187
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 5-198 1.74e-24

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 96.98  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    5 FDFTDTPVST----GTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNY 80
Cdd:PTZ00488  25 FDHGDANKAIefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999   81 HENQtNKDALVFEAASE-FRNYCYSYRE-SLLAGIIVAGWDEQRGGQVYSIPLGGMLT--RESCtigGSGSSFIYGFVRE 156
Cdd:PTZ00488 105 YELR-NGELISVAAASKiLANIVWNYKGmGLSMGTMICGWDKKGPGLFYVDNDGTRLHgnMFSC---GSGSTYAYGVLDA 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24653999  157 HYRPNMALEDCVTFVKKAVQHAIYHDGSSGGVVRIGIITKDG 198
Cdd:PTZ00488 181 GFKWDLNDEEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDG 222
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 12-204 3.42e-19

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: 81.92  E-value: 3.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALV 91
Cdd:cd03757   5 TDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMST 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  92 FEAASEFRNYCYS------YRESLLAGIivagwDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHY-RPNM-- 162
Cdd:cd03757  85 EAIAQLLSTILYSrrffpyYVFNILAGI-----DEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVgRKNQnn 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24653999 163 ------ALEDCVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIERRIF 204
Cdd:cd03757 160 vertplSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETF 207
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 14-200 2.04e-13

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: 66.05  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  14 TGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALvfe 93
Cdd:cd03760   1 TGTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDDECLDDGHSL--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  94 AASEFRNYC----YSYR---ESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYR--PNMAL 164
Cdd:cd03760  78 SPKEIHSYLtrvlYNRRskmNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLREAWEkkPDLTE 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24653999 165 EDCVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIE 200
Cdd:cd03760 158 EEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 13-203 3.53e-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: 65.73  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  13 STGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVF 92
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  93 EAASEFRNYCYSYRES-LLAGIIVAGWDEQrgGQVY-----SIplGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALED 166
Cdd:cd03759  81 TFSSLISSLLYEKRFGpYFVEPVVAGLDPD--GKPFictmdLI--GCPSIPSDFVVSGTASEQLYGMCESLWRPDMEPDE 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24653999 167 CVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIERRI 203
Cdd:cd03759 157 LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRT 193
20S_bact_beta TIGR03690
proteasome, beta subunit, bacterial type; Members of this family are the beta subunit of the ...
 15-201 1.47e-11

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: 61.65  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    15 GTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHEnQTNKDALVFEA 94
Cdd:TIGR03690   2 GTTIVALTYPGGVLMAGDRRATQGNMIASRDVEKVYPTDEYSAVGIAGTAGLAIELVRLFQVELEHYE-KIEGVPLTLDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999    95 -----ASEFRNYCYSYRESLLAGIIVAGWDEQRG-GQVYSI-PLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDC 167
Cdd:TIGR03690  81 kanrlAAMVRGNLPAAMQGLAVVPLLAGYDLDAGaGRIFSYdVTGGRYEERGYHAVGSGSVFAKGALKKLYSPDLDEDDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 24653999   168 VTFVKKAVQHAIYHDGSSGG--VVR-----IGIITKDGIER 201
Cdd:TIGR03690 161 LRVAVEALYDAADDDSATGGpdLVRgiyptVVVITADGARR 201
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-203 5.23e-11

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: 59.52  E-value: 5.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  27 VVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDaLVFEAASEF--RNYCYS 104
Cdd:cd03758  13 VILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYE-LSPKAAANFtrRELAES 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999 105 YRESLL--AGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAVqHAIYHD 182
Cdd:cd03758  92 LRSRTPyqVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMTVEEALELMKKCI-KELKKR 170

                       170       180
                ....*....|....*....|....
gi 24653999 183 ---GSSGGVVRigIITKDGIERRI 203
Cdd:cd03758 171 fiiNLPNFTVK--VVDKDGIRDLE 192
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-195 1.82e-08

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: 52.72  E-value: 1.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  12 VSTGTTIMAVEFDGGVVIGADSRTSSgAYVANRVTDKLTRITDKVYCCRSGSAADTQAIAD---IVA--YSLNYHEnQTN 86
Cdd:cd03756  25 VKRGTTALGIKCKEGVVLAVDKRITS-KLVEPESIEKIYKIDDHVGAATSGLVADARVLIDrarVEAqiHRLTYGE-PID 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  87 KDALVFEAASEFRNYC-YSYRESLLAGIIVAGWDEqRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALE 165
Cdd:cd03756 103 VEVLVKKICDLKQQYTqHGGVRPFGVALLIAGVDD-GGPRLFETDPSGAYNEYKATAIGSGRQAVTEFLEKEYKEDMSLE 181

                       170       180       190
                ....*....|....*....|....*....|
gi 24653999 166 DCVTFVKKAVqHAIYHDGSSGGVVRIGIIT 195
Cdd:cd03756 182 EAIELALKAL-YAALEENETPENVEIAYVT 210
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-194 3.54e-08

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: 51.67  E-value: 3.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  12 VSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTdKLTRITDKVYCCRSGSAADTQAIADI-----VAYSLNYHENQTn 86
Cdd:cd01911  24 VKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVE-KIFKIDDHIGCAVAGLTADARVLVNRarveaQNYRYTYGEPIP- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  87 KDALVFEAASEFRNY-CYSYRESLLAGIIVAGWDEQRGGQVYSI-PLGGMLTRESCTIgGSGSSFIYGFVREHYRPNMAL 164
Cdd:cd01911 102 VEVLVKRIADLAQVYtQYGGVRPFGVSLLIAGYDEEGGPQLYQTdPSGTYFGYKATAI-GKGSQEAKTFLEKRYKKDLTL 180

                       170       180       190
                ....*....|....*....|....*....|.
gi 24653999 165 EDCVTFVKKAVQHAiyHDGSSGGV-VRIGII 194
Cdd:cd01911 181 EEAIKLALKALKEV--LEEDKKAKnIEIAVV 209
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 24-197 3.48e-03

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 37.52  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999   24 DGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAAD-----TQAIADIVAYSLNYHENQTnKDALVFEAASEF 98
Cdd:PTZ00246  40 KEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADaniliNQCRLYAQRYRYTYGEPQP-VEQLVVQICDLK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999   99 RNYC-YSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAVQH 177
Cdd:PTZ00246 119 QSYTqFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTK 198

                        170       180
                 ....*....|....*....|
gi 24653999  178 AIYHDGSSGGVVRIGIITKD 197
Cdd:PTZ00246 199 SMDSTSPKADKIEVGILSHG 218
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 15-166 4.61e-03

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: 36.94  E-value: 4.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  15 GTTIMAVEFDGgVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAI---ADIVA--YSLNYHENQTNKDa 89
Cdd:cd03752  30 GTCLGILAKDG-IVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILinyARLIAqrYLYSYQEPIPVEQ- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653999  90 LVFEAASEFRNYCY-----SYRESLLagiiVAGWDEQRGGQVY-SIPLGGMLTRESCTIGGSGSSfIYGFVREHYRPNMA 163
Cdd:cd03752 108 LVQRLCDIKQGYTQygglrPFGVSFL----YAGWDKHYGFQLYqSDPSGNYSGWKATAIGNNNQA-AQSLLKQDYKDDMT 182


                ...
gi 24653999 164 LED 166
Cdd:cd03752 183 LEE 185
protease_HslV cd01913
Protease HslV and the ATPase/chaperone HslU are part of an ATP-dependent proteolytic system ...
 16-66 6.96e-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: 36.02  E-value: 6.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24653999  16 TTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRI-TDKVYCCRSGSAAD 66
Cdd:cd01913   1 TTILAVRKNGKVVIAGDGQVTLGNTVMKGNARKVRRLyNGKVIAGFAGSTAD 52
 
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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