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Conserved domains on  [gi|17737605|ref|NP_524115|]
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proteasome beta6 subunit [Drosophila melanogaster]

Protein Classification

proteasome subunit beta( domain architecture ID 10132910)

proteasome subunit beta is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit beta type-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 22-235 9.40e-128

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: 359.65  E-value: 9.40e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  22 FSPYESNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLR 101
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 102 TMTTEAVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIGHKNMNLe 181
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17737605 182 dADKIKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIEVRTLTLRQD 235
Cdd:cd03757 160 -VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 22-235 9.40e-128

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: 359.65  E-value: 9.40e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  22 FSPYESNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLR 101
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 102 TMTTEAVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIGHKNMNLe 181
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17737605 182 dADKIKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIEVRTLTLRQD 235
Cdd:cd03757 160 -VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-220 2.04e-37

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: 129.22  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605    27 SNGGSIVAIAGDDFAVIAADTRLSSGYNIHSR-TQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTT 105
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605   106 E---AVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLED 182
Cdd:pfam00227  82 ElaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDLTLEE 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 17737605   183 AdkIKLTKeRAVSvasdtfiSAAERDIYTGDSVLINII 220
Cdd:pfam00227 161 A--VELAV-KALK-------EAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 29-226 2.16e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 104.46  E-value: 2.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  29 GGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAV 108
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 109 AQMLSIAMYN---RRFFPYYVSNILAGIDNEGkGVVYSYDPIGHCEKATYRAGGTAGTLLQPVldnqighknmnLEDADK 185
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGV-----------LEKEYR 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17737605 186 IKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIE 226
Cdd:COG0638 183 EDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 42-224 4.20e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 49.22  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605   42 VIAADTRLSSGYNIHSRTQSKLFKLSPqTVLGS-AGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQMLSIAMYNRR 120
Cdd:PTZ00488  52 IIAVDSKATAGPYIASQSVKKVIEINP-TLLGTmAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  121 FFPYYVSNILAGIDNEGKGVVYsYDPIGHCEKATYRAGGTAGTLLQPVLDNqiGHK-NMNLEDADKIkltKERAVsvasd 199
Cdd:PTZ00488 131 GMGLSMGTMICGWDKKGPGLFY-VDNDGTRLHGNMFSCGSGSTYAYGVLDA--GFKwDLNDEEAQDL---GRRAI----- 199

                        170       180
                 ....*....|....*....|....*
gi 17737605  200 tfISAAERDIYTGDSVLINIITKDG 224
Cdd:PTZ00488 200 --YHATFRDAYSGGAINLYHMQKDG 222
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 22-235 9.40e-128

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: 359.65  E-value: 9.40e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  22 FSPYESNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLR 101
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 102 TMTTEAVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIGHKNMNLe 181
Cdd:cd03757  81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNN- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17737605 182 dADKIKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIEVRTLTLRQD 235
Cdd:cd03757 160 -VERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 30-229 8.60e-70

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: 211.92  E-value: 8.60e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  30 GSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVA 109
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 110 QMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLEDadkiklt 189
Cdd:cd01912  81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY-KPDMTLEE------- 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17737605 190 kerAVSVASDTFISAAERDIYTGDSVLINIITKDGIEVRT 229
Cdd:cd01912 153 ---AVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 30-220 4.25e-50

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 161.51  E-value: 4.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  30 GSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVA 109
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 110 QMLSIAMYNRRF--FPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLEDadkik 187
Cdd:cd01906  81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY-KPDMTLEE----- 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 17737605 188 ltkerAVSVASDTFISAAERDIYTGDSVLINII 220
Cdd:cd01906 155 -----AIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-220 2.04e-37

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: 129.22  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605    27 SNGGSIVAIAGDDFAVIAADTRLSSGYNIHSR-TQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTT 105
Cdd:pfam00227   2 KTGTTIVGIKGKDGVVLAADKRATRGSKLLSKdTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605   106 E---AVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLED 182
Cdd:pfam00227  82 ElaaRIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDLTLEE 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 17737605   183 AdkIKLTKeRAVSvasdtfiSAAERDIYTGDSVLINII 220
Cdd:pfam00227 161 A--VELAV-KALK-------EAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-228 8.40e-35

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: 122.75  E-value: 8.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  32 IVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQM 111
Cdd:cd03764   3 TVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 112 LSIAMYNRRFFPYYVSNILAGIDNEGkGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLEDADKIKLtke 191
Cdd:cd03764  83 LSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEY-KEDMTVEEAKKLAI--- 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17737605 192 RAVSvasdtfiSAAERDIYTGDSVLINIITKDGIEVR 228
Cdd:cd03764 158 RAIK-------SAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-230 8.05e-33

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: 117.73  E-value: 8.05e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  27 SNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTE 106
Cdd:cd03759   1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 107 AVAQMLSIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKAT-YRAGGTAGTLLQPVLDNqIGHKNMNLEDadk 185
Cdd:cd03759  81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYGMCES-LWRPDMEPDE--- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17737605 186 ikltkerAVSVASDTFISAAERDIYTGDSVLINIITKDGIEVRTL 230
Cdd:cd03759 157 -------LFETISQALLSAVDRDALSGWGAVVYIITKDKVTTRTL 194
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 30-183 4.56e-29

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: 107.10  E-value: 4.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  30 GSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVA 109
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17737605 110 QMLSIAMYNRRF-FPYYVSNILAGIDNEGkGVVYSYDPIGHCEKATYR-AGGTAGTLLQPVLDNQIgHKNMNLEDA 183
Cdd:cd01901  81 KELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENPGAvATGSRSQRAKSLLEKLY-KPDMTLEEA 154
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 29-226 2.16e-27

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 104.46  E-value: 2.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  29 GGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAV 108
Cdd:COG0638  35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 109 AQMLSIAMYN---RRFFPYYVSNILAGIDNEGkGVVYSYDPIGHCEKATYRAGGTAGTLLQPVldnqighknmnLEDADK 185
Cdd:COG0638 115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGV-----------LEKEYR 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17737605 186 IKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIE 226
Cdd:COG0638 183 EDLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFR 223
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-230 3.85e-19

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: 81.86  E-value: 3.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  31 SIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQ 110
Cdd:cd03758   3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 111 ML--SIAMYNRRFFPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLEDA----D 184
Cdd:cd03758  83 FTrrELAESLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYY-KPDMTVEEAlelmK 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17737605 185 K-IKLTKERAVsVASDTFIsaaerdiytgdsvlINIITKDGIEVRTL 230
Cdd:cd03758 162 KcIKELKKRFI-INLPNFT--------------VKVVDKDGIRDLEL 193
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 29-227 8.40e-19

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: 81.08  E-value: 8.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  29 GGSIVAIAGDDFAVIAADTRLSSG-----YNIhsrtqSKLFKLSPQTVLGSAGCWADTLSLTGSI--KVRMQSYEHTHLr 101
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTLGSYGslarfKNV-----ERIFKVGDNTLLGASGDYADFQYLKRLLdqLVIDDECLDDGH- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 102 TMTTEAVAQMLSIAMYNRR--FFPYYVSNILAGIDNEGK---GVVysyDPIGHCEKATYRAGGTAGTLLQPVLDNqiGHK 176
Cdd:cd03760  76 SLSPKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEpflGYV---DLLGTAYEDPHVATGFGAYLALPLLRE--AWE 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17737605 177 NmnledadKIKLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIEV 227
Cdd:cd03760 151 K-------KPDLTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVEI 194
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-226 1.02e-16

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: 75.34  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  31 SIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQ 110
Cdd:cd03762   2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 111 MLSIAMYNRRFFpYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHKNMNLEDAdkIKLTK 190
Cdd:cd03762  82 LFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANY-KPGMTLEEC--IKFVK 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17737605 191 eRAVSVasdtfisAAERDIYTGDSVLINIITKDGIE 226
Cdd:cd03762 158 -NALSL-------AMSRDGSSGGVIRLVIITKDGVE 185
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-188 5.74e-11

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: 59.76  E-value: 5.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  27 SNGGSIVAIAGDDFAVIAADTRLSSGYnIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTE 106
Cdd:cd01911  25 KNGSTAVGIKGKDGVVLAVEKKVTSKL-LDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARVEAQNYRYTYGEPIPVE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 107 AVAQmlSIAMYNRRFF------PYYVSNILAGIDNEGKGVVYSYDPIGHCE--KATyrAGG----TAGTLLQpvldnQIG 174
Cdd:cd01911 104 VLVK--RIADLAQVYTqyggvrPFGVSLLIAGYDEEGGPQLYQTDPSGTYFgyKAT--AIGkgsqEAKTFLE-----KRY 174

                       170
                ....*....|....
gi 17737605 175 HKNMNLEDAdkIKL 188
Cdd:cd01911 175 KKDLTLEEA--IKL 186
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-226 1.13e-09

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: 56.05  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  31 SIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQ 110
Cdd:cd03763   2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 111 MLSiamynRRFFPY--YVSN--ILAGIDNEGKGvVYSYDPIGHCEKATYRAGGTAGTLLQPVldnqighknmnLEDADKI 186
Cdd:cd03763  82 MLK-----QHLFRYqgHIGAalVLGGVDYTGPH-LYSIYPHGSTDKLPFVTMGSGSLAAMSV-----------LEDRYKP 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17737605 187 KLTKERAVSVASDTFISAAERDIYTGDSVLINIITKDGIE 226
Cdd:cd03763 145 DMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVE 184
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 29-194 9.86e-08

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: 50.80  E-value: 9.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  29 GGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQsKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAV 108
Cdd:cd03753  27 GSTAIGIKTKEGVVLAVEKRITSPLMEPSSVE-KIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 109 AQMLS------------IAMYNRrffPYYVSNILAGIDNEGKgVVYSYDPIGHCEKATYRAGGTAGTLLQPVLDNQIgHK 176
Cdd:cd03753 106 TQAVSdlalqfgegddgKKAMSR---PFGVALLIAGVDENGP-QLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKY-HK 180

                       170
                ....*....|....*...
gi 17737605 177 NMNLEDADKIKLTKERAV 194
Cdd:cd03753 181 DMTLEEAEKLALSILKQV 198
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 42-224 4.20e-07

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 49.22  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605   42 VIAADTRLSSGYNIHSRTQSKLFKLSPqTVLGS-AGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQMLSIAMYNRR 120
Cdd:PTZ00488  52 IIAVDSKATAGPYIASQSVKKVIEINP-TLLGTmAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  121 FFPYYVSNILAGIDNEGKGVVYsYDPIGHCEKATYRAGGTAGTLLQPVLDNqiGHK-NMNLEDADKIkltKERAVsvasd 199
Cdd:PTZ00488 131 GMGLSMGTMICGWDKKGPGLFY-VDNDGTRLHGNMFSCGSGSTYAYGVLDA--GFKwDLNDEEAQDL---GRRAI----- 199

                        170       180
                 ....*....|....*....|....*
gi 17737605  200 tfISAAERDIYTGDSVLINIITKDG 224
Cdd:PTZ00488 200 --YHATFRDAYSGGAINLYHMQKDG 222
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 29-148 7.49e-07

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: 48.13  E-value: 7.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  29 GGSIVAIAGDDFAVIAADtRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAV 108
Cdd:cd03755  27 GTTAVGVRGKDCVVLGVE-KKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARVLINRARLECQSHRLTVEDPVTVEYI 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17737605 109 AQmlSIAMYNRRFF------PYYVSNILAGIDNEGKGVVYSYDPIG 148
Cdd:cd03755 106 TR--YIAGLQQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSG 149
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 42-224 1.39e-05

proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239730  Cd Length: 188  Bit Score: 44.16  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  42 VIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQMLSIAMYNRRF 121
Cdd:cd03761  13 IVAVDSRATAGSYIASQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNMLYQYKG 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 122 FPYYVSNILAGIDNEGKGVVYSYDPIGHCEKATYRAgGTAGTLLQPVLDnqighknmnleDADKIKLTKERAVSVASDTF 201
Cdd:cd03761  93 MGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSV-GSGSTYAYGVLD-----------SGYRYDLSVEEAYDLARRAI 160

                       170       180
                ....*....|....*....|...
gi 17737605 202 ISAAERDIYTGDSVLINIITKDG 224
Cdd:cd03761 161 YHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-145 4.33e-05

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: 43.05  E-value: 4.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  27 SNGGSIVAIAGDDFAVIAADTRLSSGYnihSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTE 106
Cdd:cd03749  25 KQGSATVGLKSKTHAVLVALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQECLNYRFVYDSPIPVS 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17737605 107 AVAQMLS------IAMYNRRffPYYVSNILAGIDNEG--------KGVVYSYD 145
Cdd:cd03749 102 RLVSKVAekaqinTQRYGRR--PYGVGLLIAGYDESGphlfqtcpSGNYFEYK 152
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-200 4.38e-05

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: 43.10  E-value: 4.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  27 SNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTE 106
Cdd:cd03752  27 SHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSDANILINYARLIAQRYLYSYQEPIPVE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605 107 AVAQMLSIAMYNRRFF----PYYVSNILAGIDNEGKGVVYSYDPIGHCE--KATYRAG--GTAGTLLQpvldnQIGHKNM 178
Cdd:cd03752 107 QLVQRLCDIKQGYTQYgglrPFGVSFLYAGWDKHYGFQLYQSDPSGNYSgwKATAIGNnnQAAQSLLK-----QDYKDDM 181

                       170       180
                ....*....|....*....|..
gi 17737605 179 NLEDAdkikltKERAVSVASDT 200
Cdd:cd03752 182 TLEEA------LALAVKVLSKT 197
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 33-157 7.83e-05

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


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 42.22  E-value: 7.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  33 VAIAGDDFAVIAADTRLSSGYnIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTEAVAQ-M 111
Cdd:cd03754  33 VAVRGKDCAVVVTQKKVPDKL-IDPSTVTHLFRITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGYEMPVDVLAKrI 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17737605 112 LSIA-MYNRRFF--PYYVSNILAGIDNEGKGVVYSYDPIGHCekATYRA 157
Cdd:cd03754 112 ADINqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYF--AGYKA 158
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 27-207 8.35e-04

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 39.45  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605   27 SNGGSIVAIAGDDFAVIAADTRLSSGYNIHSRTQSKLFKLSPQTVLGSAGCWADTLSLTGSIKVRMQSYEHTHLRTMTTE 106
Cdd:PTZ00246  29 NNASLTVGILCKEGVILGADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLTADANILINQCRLYAQRYRYTYGEPQPVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737605  107 A-VAQMLSIAMYNRRF---FPYYVSNILAGIDNEGKGVVYSYDPIGHCE--KATyrAGGTAGTLLQPVLdNQIGHKNMNL 180
Cdd:PTZ00246 109 QlVVQICDLKQSYTQFgglRPFGVSFLFAGYDENLGYQLYHTDPSGNYSgwKAT--AIGQNNQTAQSIL-KQEWKEDLTL 185

                        170       180
                 ....*....|....*....|....*..
gi 17737605  181 EDADKIKLtkeRAVSVASDTFISAAER 207
Cdd:PTZ00246 186 EQGLLLAA---KVLTKSMDSTSPKADK 209
 
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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