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Conserved domains on  [gi|1993813941|ref|XP_039563512|]
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proteasome subunit beta type-1 [Passer montanus]

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 ...
 27-238 4.86e-148

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: 411.27  E-value: 4.86e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  27 FSPYTFNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNK 106
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 107 TMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGFKNMQNV 186
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1993813941 187 EHVPLTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEETVQLRKD 238
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 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 ...
 27-238 4.86e-148

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: 411.27  E-value: 4.86e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  27 FSPYTFNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNK 106
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 107 TMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGFKNMQNV 186
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1993813941 187 EHVPLTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEETVQLRKD 238
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-223 9.74e-46

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 150.80  E-value: 9.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  31 TFNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDS-PKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMT 109
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 110 ---TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIgFKNMqnv 186
Cdd:pfam00227  81 velAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL--- 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1993813941 187 ehvplTLEKALQLVKDVFISAAERDVYTGDALKICIV 223
Cdd:pfam00227 157 -----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 34-232 1.80e-28

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 107.54  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  34 GGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAI 113
Cdd:COG0638    35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 114 AAMLSTILYS---RRFFPYYVYNIIGGLDEQGkGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNqigfknmqnvEHVP 190
Cdd:COG0638   115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEK----------EYRE 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1993813941 191 -LTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEET 232
Cdd:COG0638   184 dLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-230 2.18e-13

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 67.32  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941   7 CGPSRPEAGCGLEaPVQHYRfsPYTFN------------GGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQ 74
Cdd:PTZ00488    3 CGPEHFEHPPGAH-PGDFLA--EYTFDhgdankaiefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  75 TVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGaVYSFDPVGS 154
Cdd:PTZ00488   80 LLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993813941 155 YERDTFKAGGSASAMLQPLLDNqiGFK-NMQNvehvpltlEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKE 230
Cdd:PTZ00488  159 RLHGNMFSCGSGSTYAYGVLDA--GFKwDLND--------EEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKK 225
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 27-238 4.86e-148

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: 411.27  E-value: 4.86e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  27 FSPYTFNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNK 106
Cdd:cd03757     1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 107 TMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGFKNMQNV 186
Cdd:cd03757    81 EMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKNQNNV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1993813941 187 EHVPLTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEETVQLRKD 238
Cdd:cd03757   161 ERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITKDGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-232 3.69e-76

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: 228.10  E-value: 3.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  35 GTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIA 114
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRASAGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 115 AMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGFKnmqnvehvpLTLE 194
Cdd:cd01912    81 NLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD---------MTLE 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1993813941 195 KALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEET 232
Cdd:cd01912   152 EAVELVKKAIDSAIERDLSSGGGVDVAVITKDGVEELR 189
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-223 1.82e-53

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: 170.37  E-value: 1.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  35 GTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIA 114
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 115 AMLSTILYSRRF--FPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGFKnmqnvehvpLT 192
Cdd:cd01906    81 KLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD---------MT 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1993813941 193 LEKALQLVKDVFISAAERDVYTGDALKICIV 223
Cdd:cd01906   152 LEEAIELALKALKSALERDLYSGGNIEVAVI 182
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 31-223 9.74e-46

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 150.80  E-value: 9.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  31 TFNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDS-PKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMT 109
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 110 ---TGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIgFKNMqnv 186
Cdd:pfam00227  81 velAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLY-RPDL--- 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1993813941 187 ehvplTLEKALQLVKDVFISAAERDVYTGDALKICIV 223
Cdd:pfam00227 157 -----TLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-231 3.12e-41

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: 139.31  E-value: 3.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  36 TVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIAA 115
Cdd:cd03764     2 TTVGIVCKDGVVLAADKRASMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 116 MLSTILYSRRFFPYYVYNIIGGLDEQGkGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNqiGFKNmqnvehvPLTLEK 195
Cdd:cd03764    82 LLSNILNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLED--EYKE-------DMTVEE 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1993813941 196 ALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEE 231
Cdd:cd03764   152 AKKLAIRAIKSAIERDSASGDGIDVVVITKDGYKEL 187
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-233 1.02e-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: 120.04  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  32 FNGGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTG 111
Cdd:cd03759     1 YNGGAVVAMAGKDCVAIASDLRLGVQQQTVSTDFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 112 AIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVG--SYERDtFKAGGSASAMLQPLLDNqIGFKNMqNVEHV 189
Cdd:cd03759    81 TFSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGcpSIPSD-FVVSGTASEQLYGMCES-LWRPDM-EPDEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1993813941 190 PLTLEKALqlvkdvfISAAERDVYTGDALKICIVTKDGIKEETV 233
Cdd:cd03759   158 FETISQAL-------LSAVDRDALSGWGAVVYIITKDKVTTRTL 194
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-206 4.68e-32

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: 114.80  E-value: 4.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  35 GTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIA 114
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 115 AMLSTILYSRRF-FPYYVYNIIGGLDEQGkGAVYSFDPVGSY-ERDTFKAGGSASAMLQPLLDNQIGFKnmqnvehvpLT 192
Cdd:cd01901    81 KELAKLLQVYTQgRPFGVNLIVAGVDEGG-GNLYYIDPSGPViENPGAVATGSRSQRAKSLLEKLYKPD---------MT 150

                         170
                  ....*....|....
gi 1993813941 193 LEKALQLVKDVFIS 206
Cdd:cd01901   151 LEEAVELALKALKS 164
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 34-232 1.80e-28

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 107.54  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  34 GGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAI 113
Cdd:COG0638    35 GTTTVGIKTKDGVVLAADRRATMGNLIASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 114 AAMLSTILYS---RRFFPYYVYNIIGGLDEQGkGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNqigfknmqnvEHVP 190
Cdd:COG0638   115 AKLLSDLLQGytqYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEK----------EYRE 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1993813941 191 -LTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEET 232
Cdd:COG0638   184 dLSLDEAVELALRALYSAAERDSASGDGIDVAVITEDGFRELS 226
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-233 6.62e-23

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: 91.88  E-value: 6.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  36 TVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIAA 115
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 116 MLSTIL--YSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNqigfknmqnvEHVP-LT 192
Cdd:cd03758    83 FTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDR----------YYKPdMT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1993813941 193 LEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEETV 233
Cdd:cd03758   153 VEEALELMKKCIKELKKRFIINLPNFTVKVVDKDGIRDLEL 193
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 34-229 8.74e-22

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: 89.17  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  34 GGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIE-ARLKMYKHSNNKTMTTGA 112
Cdd:cd03760     2 GTSVIAIKYKDGVIIAADTLGSYGSLARFKNVERIFKVGDNTLLGASGDYADFQYLKRLLDqLVIDDECLDDGHSLSPKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 113 IAAMLSTILYSRR--FFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNqiGFKNMQNvehvp 190
Cdd:cd03760    82 IHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGEPFLGYVDLLGTAYEDPHVATGFGAYLALPLLRE--AWEKKPD----- 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1993813941 191 LTLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIK 229
Cdd:cd03760   155 LTEEEARALIEECMKVLYYRDARSINKYQIAVVTKEGVE 193
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-231 7.68e-15

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: 70.33  E-value: 7.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  36 TVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIAA 115
Cdd:cd03762     2 TIIAVEYDGGVVLGADSRTSTGSYVANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 116 MLSTILYSRRFFpYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQIGfKNMqnvehvplTLEK 195
Cdd:cd03762    82 LFKNLCYNYKEM-LSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYK-PGM--------TLEE 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1993813941 196 ALQLVKDVFISAAERDVYTGDALKICIVTKDGIKEE 231
Cdd:cd03762   152 CIKFVKNALSLAMSRDGSSGGVIRLVIITKDGVERK 187
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 7-230 2.18e-13

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 67.32  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941   7 CGPSRPEAGCGLEaPVQHYRfsPYTFN------------GGTVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQ 74
Cdd:PTZ00488    3 CGPEHFEHPPGAH-PGDFLA--EYTFDhgdankaiefahGTTTLAFKYGGGIIIAVDSKATAGPYIASQSVKKVIEINPT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  75 TVIGCTGFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEQGKGaVYSFDPVGS 154
Cdd:PTZ00488   80 LLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAASKILANIVWNYKGMGLSMGTMICGWDKKGPG-LFYVDNDGT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993813941 155 YERDTFKAGGSASAMLQPLLDNqiGFK-NMQNvehvpltlEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKE 230
Cdd:PTZ00488  159 RLHGNMFSCGSGSTYAYGVLDA--GFKwDLND--------EEAQDLGRRAIYHATFRDAYSGGAINLYHMQKDGWKK 225
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-230 5.65e-08

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: 51.04  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  36 TVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTEQTVIGCTGFHGDCLTLTKIIEARLKMykHSNNKTMTTGAIAA 115
Cdd:cd03763     2 TIVGVVFKDGVVLGADTRATEGPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLEL--HRLNTGRKPRVVTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 116 MlsTILySRRFFPY--YV--YNIIGGLDEQGKgAVYSFDPVGSYERDTFKAGGSASAMLQPLLDNQigFKNmqnvehvPL 191
Cdd:cd03763    80 L--TML-KQHLFRYqgHIgaALVLGGVDYTGP-HLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDR--YKP-------DM 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1993813941 192 TLEKALQLVKDVFISAAERDVYTGDALKICIVTKDGIKE 230
Cdd:cd03763   147 TEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDGVEY 185
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 36-227 3.45e-07

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: 48.78  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  36 TVLAIAGEDFCIVASDTRLSEGYSIHSRDSPKCYKLTeQTVIGCT-GFHGDCLTLTKIIEARLKMYKHSNNKTMTTGAIA 114
Cdd:cd03761     2 TTLAFIFQGGVIVAVDSRATAGSYIASQTVKKVIEIN-PYLLGTMaGGAADCQYWERVLGRECRLYELRNKERISVAAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 115 AMLSTILYSRRFFPYYVYNIIGGLDEQGKGAVYSFDPVGSYERDTFKAGgSASAMLQPLLDNQIGFKnmqnvehvpLTLE 194
Cdd:cd03761    81 KLLSNMLYQYKGMGLSMGTMICGWDKTGPGLYYVDSDGTRLKGDLFSVG-SGSTYAYGVLDSGYRYD---------LSVE 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1993813941 195 KALQLVKDVFISAAERDVYTGDALKICIVTKDG 227
Cdd:cd03761   151 EAYDLARRAIYHATHRDAYSGGNVNLYHVREDG 183
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-155 4.48e-07

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 48.98  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  27 FSP--------YTF----NGGTVLAIAGEDFCIVASD----TRLSEGYSIHsrdspKCYKLTEQTVIGCTGFHGDCLTLT 90
Cdd:cd01911     8 FSPegrlfqveYALeavkNGSTAVGIKGKDGVVLAVEkkvtSKLLDPSSVE-----KIFKIDDHIGCAVAGLTADARVLV 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993813941  91 KIieARLKM--YKHSNNKTMTTGAIAAMLSTIL------YSRRffPYYVYNIIGGLDEQGKGAVYSFDPVGSY 155
Cdd:cd01911    83 NR--ARVEAqnYRYTYGEPIPVEVLVKRIADLAqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDPSGTY 151
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 27-223 1.39e-03

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: 38.75  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  27 FSP--------YTF----NGG-TVLAIAGEDFCIVASDTRLSEGYsIHSRDSPKCYKLTEQtvIGC--TGFHGDCLTLtk 91
Cdd:cd03754     9 FSPegrlyqveYAFkavkNAGlTSVAVRGKDCAVVVTQKKVPDKL-IDPSTVTHLFRITDE--IGCvmTGMIADSRSQ-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  92 IIEARLKM--YKHSNNKTMTTGAIAAMLSTI--LYSRRFF--PYYVYNIIGGLDEQGKGAVYSFDPVGSYErdTFKAggS 165
Cdd:cd03754    84 VQRARYEAaeFKYKYGYEMPVDVLAKRIADInqVYTQHAYmrPLGVSMILIGIDEELGPQLYKCDPAGYFA--GYKA--T 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993813941 166 ASAMLQPLLDNQIGfKNMQNVEHVPLTLEKALQLVKDVFISAAERDVYTGDaLKICIV 223
Cdd:cd03754   160 AAGVKEQEATNFLE-KKLKKKPDLIESYEETVELAISCLQTVLSTDFKATE-IEVGVV 215
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 34-203 4.20e-03

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: 37.32  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941  34 GGTVLAIAGEDFCIVASDTRLS----EGYSIHsrdspkcyKLTE-QTVIGCT--GFHGDCLTLtkIIEARLKMYKH--SN 104
Cdd:cd03753    27 GSTAIGIKTKEGVVLAVEKRITsplmEPSSVE--------KIMEiDDHIGCAmsGLIADARTL--IDHARVEAQNHrfTY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993813941 105 NKTMTTGAIAAMLSTI------------LYSRrffPYYVYNIIGGLDEQGKgAVYSFDPVGSYERDTFKAGGSASAMLQP 172
Cdd:cd03753    97 NEPMTVESVTQAVSDLalqfgegddgkkAMSR---PFGVALLIAGVDENGP-QLFHTDPSGTFTRCDAKAIGSGSEGAQS 172

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1993813941 173 LLdnqigfknmQNVEHVPLTLEKA----LQLVKDV 203
Cdd:cd03753   173 SL---------QEKYHKDMTLEEAeklaLSILKQV 198
 
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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