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Conserved domains on  [gi|17554384|ref|NP_498806|]
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Proteasome subunit beta type-1 [Caenorhabditis elegans]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 44-258 4.20e-84

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.


The actual alignment was detected with superfamily member cd03757:

Pssm-ID: 469781  Cd Length: 212  Bit Score: 250.25  E-value: 4.20e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  44 WNPYSMEGGSTCAISGENFAIVASDTRMTQnDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYR 123
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSE-GYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 124 SDMSVDLCAELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIGHVTlSE 203
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKN-QN 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17554384 204 GYERPELTLDRAISLMKDSFRGAAEREISTGDKIHLVIAEAgKPVVVKFLPLRED 258
Cdd:cd03757 159 NVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK-DGIEEETFPLRKD 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 ...
 44-258 4.20e-84

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: 250.25  E-value: 4.20e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  44 WNPYSMEGGSTCAISGENFAIVASDTRMTQnDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYR 123
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSE-GYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 124 SDMSVDLCAELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIGHVTlSE 203
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKN-QN 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17554384 204 GYERPELTLDRAISLMKDSFRGAAEREISTGDKIHLVIAEAgKPVVVKFLPLRED 258
Cdd:cd03757 159 NVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK-DGIEEETFPLRKD 212
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 49-241 2.78e-45

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 150.41  E-value: 2.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384    49 MEGGSTC-AISGENFAIVASDTRMTQNDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMS 127
Cdd:pfam00227   1 VKTGTTIvGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384   128 VDLC---AELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEG 204
Cdd:pfam00227  81 VELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE---------KL 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 17554384   205 YeRPELTLDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:pfam00227 152 Y-RPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAV 187
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 49-241 1.55e-25

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 100.22  E-value: 1.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  49 MEGGSTCAISGENFAIVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSV 128
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNL-IASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 129 DLCAELLSRNLY---YRRFFPYYTGAILAGIDEHGkGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEGY 205
Cdd:COG0638 112 EGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLE---------KEY 181

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17554384 206 eRPELTLDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:COG0638 182 -REDLSLDEAVELALRALYSAAERDSASGDGIDVAV 216
 
Name Accession Description Interval E-value
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 44-258 4.20e-84

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: 250.25  E-value: 4.20e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  44 WNPYSMEGGSTCAISGENFAIVASDTRMTQnDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYR 123
Cdd:cd03757   1 FSPYTDNGGTVLAIAGNDFAVIAGDTRLSE-GYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 124 SDMSVDLCAELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIGHVTlSE 203
Cdd:cd03757  80 KEMSTEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRKN-QN 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17554384 204 GYERPELTLDRAISLMKDSFRGAAEREISTGDKIHLVIAEAgKPVVVKFLPLRED 258
Cdd:cd03757 159 NVERTPLSLEEAVSLVKDAFTSAAERDIYTGDSLEIVIITK-DGIEEETFPLRKD 212
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 52-241 4.05e-57

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: 180.72  E-value: 4.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  52 GSTCAISGENFAIVASDTRMTQNdINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLC 131
Cdd:cd01912   1 TTIVGIKGKDGVVLAADTRASAG-SLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 132 AELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIghvtlsegyeRPELT 211
Cdd:cd01912  80 ANLLSNILYSYRGFPYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGY----------KPDMT 149

                       170       180       190
                ....*....|....*....|....*....|
gi 17554384 212 LDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:cd01912 150 LEEAVELVKKAIDSAIERDLSSGGGVDVAV 179
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 49-241 2.78e-45

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


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 150.41  E-value: 2.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384    49 MEGGSTC-AISGENFAIVASDTRMTQNDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMS 127
Cdd:pfam00227   1 VKTGTTIvGIKGKDGVVLAADKRATRGSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384   128 VDLC---AELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEG 204
Cdd:pfam00227  81 VELAariADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLE---------KL 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 17554384   205 YeRPELTLDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:pfam00227 152 Y-RPDLTLEEAVELAVKALKEAIDRDALSGGNIEVAV 187
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 52-241 3.24e-45

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: 149.95  E-value: 3.24e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  52 GSTCAISGENFAIVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLC 131
Cdd:cd01906   1 TTIVGIKGKDGVVLAADKRVTSGLL-VASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 132 AELLSRNLYYRRF--FPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIghvtlsegyeRPE 209
Cdd:cd01906  80 AKLLANLLYEYTQslRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLY----------KPD 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 17554384 210 LTLDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:cd01906 150 MTLEEAIELALKALKSALERDLYSGGNIEVAV 181
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 64-241 7.51e-33

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: 118.12  E-value: 7.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  64 IVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLCAELLSRNLYYRR 143
Cdd:cd03764  13 VLAADKRASMGNF-IASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 144 FFPYYTGAILAGIDEHGkGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEGYeRPELTLDRAISLMKDSF 223
Cdd:cd03764  92 YFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLE---------DEY-KEDMTVEEAKKLAIRAI 160

                       170
                ....*....|....*...
gi 17554384 224 RGAAEREISTGDKIHLVI 241
Cdd:cd03764 161 KSAIERDSASGDGIDVVV 178
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 52-224 3.47e-27

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: 102.86  E-value: 3.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  52 GSTCAISGENFAIVASDTRMTQnDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLC 131
Cdd:cd01901   1 STSVAIKGKGGVVLAADKRLSS-GLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 132 AELLSRNLY-YRRFFPYYTGAILAGIDEHGkGAVFSYDPIGC-IERLGYSASGAAEPMIIPFLdcqighvtlsEGYERPE 209
Cdd:cd01901  80 AKELAKLLQvYTQGRPFGVNLIVAGVDEGG-GNLYYIDPSGPvIENPGAVATGSRSQRAKSLL----------EKLYKPD 148

                       170
                ....*....|....*
gi 17554384 210 LTLDRAISLMKDSFR 224
Cdd:cd01901 149 MTLEEAVELALKALK 163
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 49-241 1.55e-25

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 100.22  E-value: 1.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  49 MEGGSTCAISGENFAIVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSV 128
Cdd:COG0638  33 KRGTTTVGIKTKDGVVLAADRRATMGNL-IASKSIEKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISV 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 129 DLCAELLSRNLY---YRRFFPYYTGAILAGIDEHGkGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEGY 205
Cdd:COG0638 112 EGLAKLLSDLLQgytQYGVRPFGVALLIGGVDDGG-PRLFSTDPSGGLYEEKAVAIGSGSPFARGVLE---------KEY 181

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17554384 206 eRPELTLDRAISLMKDSFRGAAEREISTGDKIHLVI 241
Cdd:COG0638 182 -REDLSLDEAVELALRALYSAAERDSASGDGIDVAV 216
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 49-220 3.38e-22

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: 90.34  E-value: 3.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  49 MEggSTCAISGENFAIVASDTrMTQNDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSV 128
Cdd:cd03758   1 ME--TLIGIKGKDFVILAADT-SAARSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 129 DLCAELLSRNL--YYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlseGYE 206
Cdd:cd03758  78 KAAANFTRRELaeSLRSRTPYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILD----------RYY 147

                       170
                ....*....|....
gi 17554384 207 RPELTLDRAISLMK 220
Cdd:cd03758 148 KPDMTVEEALELMK 161
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 51-234 3.77e-20

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: 84.99  E-value: 3.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  51 GGSTCAISGENFAIVASDTRMTQNDINILTrDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDL 130
Cdd:cd03759   3 GGAVVAMAGKDCVAIASDLRLGVQQQTVST-DFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 131 CAELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLG-YSASGAAEPMIIPfldcqighvtLSEGYERPE 209
Cdd:cd03759  82 FSSLISSLLYEKRFGPYFVEPVVAGLDPDGKPFICTMDLIGCPSIPSdFVVSGTASEQLYG----------MCESLWRPD 151

                       170       180
                ....*....|....*....|....*
gi 17554384 210 LTLDRAISLMKDSFRGAAEREISTG 234
Cdd:cd03759 152 MEPDELFETISQALLSAVDRDALSG 176
proteasome_beta_type_4 cd03760
proteasome beta type-4 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 51-242 1.19e-11

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: 61.82  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  51 GGSTCAISGENFAIVASDT-----RMTQndinilTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHK-YRFDYRS 124
Cdd:cd03760   2 GTSVIAIKYKDGVIIAADTlgsygSLAR------FKNVERIFKVGDNTLLGASGDYADFQYLKRLLDQLVIDdECLDDGH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 125 DMSVDLCAELLSRNLYYRR--FFPYYTGAILAGIDEHGKgavfSYdpIGCIERLG------YSASGAAEPMIIPFldcqi 196
Cdd:cd03760  76 SLSPKEIHSYLTRVLYNRRskMNPLWNTLVVGGVDNEGE----PF--LGYVDLLGtayedpHVATGFGAYLALPL----- 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17554384 197 ghvtLSEGYE-RPELTLDRAISLMKDSFRGAAEREISTGDKIHLVIA 242
Cdd:cd03760 145 ----LREAWEkKPDLTEEEARALIEECMKVLYYRDARSINKYQIAVV 187
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-171 7.45e-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: 7.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  38 QIErqrwnpYSME---GGSTC-AISGENFAIVASDTRMTqnDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQS 113
Cdd:cd01911  16 QVE------YALEavkNGSTAvGIKGKDGVVLAVEKKVT--SKLLDPSSVEKIFKIDDHIGCAVAGLTADARVLVNRARV 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554384 114 RLHKYRFDYRSDMSVDLCAELLSrNL-------YYRRffPYYTGAILAGIDEHGKGAVFSYDPIG 171
Cdd:cd01911  88 EAQNYRYTYGEPIPVEVLVKRIA-DLaqvytqyGGVR--PFGVSLLIAGYDEEGGPQLYQTDPSG 149
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 64-245 7.35e-10

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: 56.85  E-value: 7.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  64 IVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLCAELLsRNLYYRR 143
Cdd:cd03762  13 VLGADSRTSTGSY-VANRVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLF-KNLCYNY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 144 FFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIghvtlsegyeRPELTLDRAISLMKDSF 223
Cdd:cd03762  91 KEMLSAGIIVAGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANY----------KPGMTLEECIKFVKNAL 160

                       170       180
                ....*....|....*....|...
gi 17554384 224 RGAAEREISTGDKIHLV-IAEAG 245
Cdd:cd03762 161 SLAMSRDGSSGGVIRLViITKDG 183
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 38-168 3.74e-06

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 46.51  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  38 QIErqrwnpYSME----GGSTCAISGENFAIVASDTRMTQNdiniLTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQS 113
Cdd:cd03749  16 QVE------YAMEavkqGSATVGLKSKTHAVLVALKRATSE----LSSYQKKIFKVDDHIGIAIAGLTADARVLSRYMRQ 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554384 114 RLHKYRFDYRSDMSVDLCAELLSRNL------YYRRffPYYTGAILAGIDEHG--------KGAVFSYD 168
Cdd:cd03749  86 ECLNYRFVYDSPIPVSRLVSKVAEKAqintqrYGRR--PYGVGLLIAGYDESGphlfqtcpSGNYFEYK 152
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 55-246 1.15e-05

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: 44.88  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  55 CAISGENFAIVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLCAEL 134
Cdd:cd03763   4 VGVVFKDGVVLGADTRATEGPI-VADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 135 LSRNLyyrrfFPY--YTGA--ILAGIDEhgKGA-VFSYDPIGCIERLGYSA--SGAAEPMIIpfldcqighvtLSEGYeR 207
Cdd:cd03763  83 LKQHL-----FRYqgHIGAalVLGGVDY--TGPhLYSIYPHGSTDKLPFVTmgSGSLAAMSV-----------LEDRY-K 143

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17554384 208 PELTLDRAISLMKDSFRGAAEREISTGDKIHLVIAEAGK 246
Cdd:cd03763 144 PDMTEEEAKKLVCEAIEAGIFNDLGSGSNVDLCVITKDG 182
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 64-244 1.48e-05

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


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 44.63  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  64 IVASDTRMTQNDINIltRDAEKIQILNDNIILTTSGFYGDVLQLkkVLQSRL--HKYRFDYRSDMSVDLCAELLSRNLY- 140
Cdd:cd03756  41 VLAVDKRITSKLVEP--ESIEKIYKIDDHVGAATSGLVADARVL--IDRARVeaQIHRLTYGEPIDVEVLVKKICDLKQq 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 141 YRRF---FPYYTGAILAGIDEHGKgAVFSYDPIGCIERLGYSASGAAEPMIIPFLDcqighvtlsEGYeRPELTLDRAIS 217
Cdd:cd03756 117 YTQHggvRPFGVALLIAGVDDGGP-RLFETDPSGAYNEYKATAIGSGRQAVTEFLE---------KEY-KEDMSLEEAIE 185

                       170       180
                ....*....|....*....|....*..
gi 17554384 218 LMKDSFrGAAEREISTGDKIHLVIAEA 244
Cdd:cd03756 186 LALKAL-YAALEENETPENVEIAYVTV 211
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 64-239 5.57e-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: 42.62  E-value: 5.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  64 IVASDTRMTQNDInILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVL--QSRLHKYRfdYRSDMSVDLCAELLSRNLYY 141
Cdd:cd03761  13 IVAVDSRATAGSY-IASQTVKKVIEINPYLLGTMAGGAADCQYWERVLgrECRLYELR--NKERISVAAASKLLSNMLYQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 142 RRFFPYYTGAILAGIDEHGKGaVFSYDPIGciERLG---YSAsGAAEPMIIPFLDcqighvtlsEGYeRPELTLDRAISL 218
Cdd:cd03761  90 YKGMGLSMGTMICGWDKTGPG-LYYVDSDG--TRLKgdlFSV-GSGSTYAYGVLD---------SGY-RYDLSVEEAYDL 155

                       170       180
                ....*....|....*....|.
gi 17554384 219 MKDSFRGAAEREISTGDKIHL 239
Cdd:cd03761 156 ARRAIYHATHRDAYSGGNVNL 176
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 47-218 1.05e-03

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: 39.27  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  47 YSME----GGSTCAISGENFAIVASDTRMT---QNDiniltRDAEKIQILNDNIILTTSGFYGDVLQLkkVLQSRL--HK 117
Cdd:cd03755  19 YAQEavrkGTTAVGVRGKDCVVLGVEKKSVaklQDP-----RTVRKICMLDDHVCLAFAGLTADARVL--INRARLecQS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384 118 YRFDYRSDMSVDLCAELLSRnlYYRRFF------PYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPF 191
Cdd:cd03755  92 HRLTVEDPVTVEYITRYIAG--LQQRYTqsggvrPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIGRNSKTVREF 169

                       170       180
                ....*....|....*....|....*..
gi 17554384 192 LDcqighvtlsEGYERpELTLDRAISL 218
Cdd:cd03755 170 LE---------KNYKE-EMTRDDTIKL 186
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 50-171 3.60e-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: 37.60  E-value: 3.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  50 EGGSTCAISGENFAIVAS-----DTRMTQNDINILTRdaekiqiLNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRS 124
Cdd:cd03754  28 AGLTSVAVRGKDCAVVVTqkkvpDKLIDPSTVTHLFR-------ITDEIGCVMTGMIADSRSQVQRARYEAAEFKYKYGY 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17554384 125 DMSVD-LC------AELLSRNLYYRrffPYYTGAILAGIDEHGKGAVFSYDPIG 171
Cdd:cd03754 101 EMPVDvLAkriadiNQVYTQHAYMR---PLGVSMILIGIDEELGPQLYKCDPAG 151
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 84-218 9.65e-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: 36.16  E-value: 9.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554384  84 EKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLCAELLSrNLYYRrfF------------PYYTGA 151
Cdd:cd03753  58 EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVTQAVS-DLALQ--FgegddgkkamsrPFGVAL 134

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554384 152 ILAGIDEHGKgAVFSYDPIGCIERLGYSASGAAEpmiipfldcQIGHVTLSEGYeRPELTLDRAISL 218
Cdd:cd03753 135 LIAGVDENGP-QLFHTDPSGTFTRCDAKAIGSGS---------EGAQSSLQEKY-HKDMTLEEAEKL 190
 
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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