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Conserved domains on  [gi|66395523|ref|YP_239858|]
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head maturation protease [Staphylococcus phage 42E]

Protein Classification

Clp protease ClpP( domain architecture ID 10161508)

Clp protease ClpP is a serine protease, involved in several cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins

CATH:  3.90.226.10
Gene Ontology:  GO:0004176|GO:0006508|GO:0004252
MEROPS:  S14
SCOP:  4003574

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-182 1.10e-78

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. This subfamily only contains bacterial sequences. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


:

Pssm-ID: 132927 [Multi-domain]  Cd Length: 160  Bit Score: 234.35  E-value: 1.10e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  18 GEIFIYGDIVSDkwfeSDVTATDFKNKLDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVI 97
Cdd:cd07016   1 AEIYIYGDIGSD----WGVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  98 AMSGDTIFMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYLDKAKdLDQEHLKQMLDAETWLTAEEALSFG 177
Cdd:cd07016  77 AMAGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTG-LSEEEISALMDAETWLTAQEAVELG 155


                ....*
gi 66395523 178 LIDEI 182
Cdd:cd07016 156 FADEI 160
 
Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-182 1.10e-78

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. This subfamily only contains bacterial sequences. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


Pssm-ID: 132927 [Multi-domain]  Cd Length: 160  Bit Score: 234.35  E-value: 1.10e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  18 GEIFIYGDIVSDkwfeSDVTATDFKNKLDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVI 97
Cdd:cd07016   1 AEIYIYGDIGSD----WGVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  98 AMSGDTIFMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYLDKAKdLDQEHLKQMLDAETWLTAEEALSFG 177
Cdd:cd07016  77 AMAGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTG-LSEEEISALMDAETWLTAQEAVELG 155


                ....*
gi 66395523 178 LIDEI 182
Cdd:cd07016 156 FADEI 160
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 20-184 6.25e-29

Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.


Pssm-ID: 425759 [Multi-domain]  Cd Length: 181  Bit Score: 107.65  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523    20 IFIYGDIvsDKWFESDVTATDFKnkLDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAM 99
Cdd:pfam00574  19 IFLGGEI--DDEVANLIIAQLLF--LEAEDPDKDIYLYINSPGGSVTAGLAIYDTMQYIKPDVSTICLGLAASMGSFLLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   100 SGDT--IFMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYlDKAKDLDQEHLKQMLDAETWLTAEEALSFG 177
Cdd:pfam00574  95 AGAKgkRFALPNARIMIHQPLGGAQGQASDIEIQAKEILKIKERLNEIY-AKHTGQSLEKIEKDTDRDFFMSAEEAKEYG 173


                  ....*..
gi 66395523   178 LIDEILG 184
Cdd:pfam00574 174 LIDEVIE 180
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 20-183 6.47e-25

ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440503  Cd Length: 194  Bit Score: 97.46  E-value: 6.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  20 IFIYGDIvsdkwfeSDVTATDFKNKLDEL---GDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASV 96
Cdd:COG0740  29 IFLGGEI-------DDHVANLIIAQLLFLeaeDPDKDILLYINSPGGSVTAGLAIYDTMQFIKPDVSTICLGQAASMGAF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  97 IAMSGDTI--FMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYldkAKDLDQ--EHLKQMLDAETWLTAEE 172
Cdd:COG0740 102 LLAAGTKGkrFALPNARIMIHQPSGGAQGQASDIEIQAREILKMRERLNEIL---AEHTGQplEKIEKDTDRDTWMTAEE 178

                       170
                ....*....|.
gi 66395523 173 ALSFGLIDEIL 183
Cdd:COG0740 179 AVEYGLIDEVI 189
PRK12553 PRK12553
ATP-dependent Clp protease proteolytic subunit; Reviewed
 20-183 1.32e-17

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 237133  Cd Length: 207  Bit Score: 78.45  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   20 IFIYGDIvsdkwfeSDVTATDFKNKLDELGDIS---EIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASV 96
Cdd:PRK12553  38 IFLGGQV-------DDASANDVMAQLLVLESIDpdrDITLYINSPGGSVTAGDAIYDTIQFIRPDVQTVCTGQAASAGAV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   97 IAMSGD--TIFMHKNSFLMIHNSWVMTVGN---------AEELRKTADLLEKTdavsnsayLDKAKDLDQEHLKQMLDAE 165
Cdd:PRK12553 111 LLAAGTpgKRFALPNARILIHQPSLGGGIRgqasdleiqAREILRMRERLERI--------LAEHTGQSVEKIRKDTDRD 182

                        170
                 ....*....|....*...
gi 66395523  166 TWLTAEEALSFGLIDEIL 183
Cdd:PRK12553 183 KWLTAEEAKDYGLVDQII 200
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
 35-182 1.83e-05

signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273227 [Multi-domain]  Cd Length: 208  Bit Score: 44.28  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523    35 DVTATDFKNKLDELGD---ISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDA--LAASIASVIAMSGDTIFMHKn 109
Cdd:TIGR00706  13 DVSPEDFDKKLERIKDdktIKALVLRINSPGGTVVASEEIYKKLEKLKAKKPVVASMggMAASGGYYISMAADEIFANP- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   110 sflmihNSWVMTVGNAEELRKTADLLEK----TDAVSNSAYLD--------------------------------KAKDL 153
Cdd:TIGR00706  92 ------GTITGSIGVILQGANVEKLAEKlgisFEVIKSGAYKDigsptreltpeeknilqslvnesyeqfvqvvsKGRNL 165

                         170       180
                  ....*....|....*....|....*....
gi 66395523   154 DQEHLKQMLDAETWlTAEEALSFGLIDEI 182
Cdd:TIGR00706 166 PVEEVKKFADGRVF-TGRQALKLRLVDKL 193
 
Name Accession Description Interval E-value
S14_ClpP_1 cd07016
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 18-182 1.10e-78

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. This subfamily only contains bacterial sequences. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


Pssm-ID: 132927 [Multi-domain]  Cd Length: 160  Bit Score: 234.35  E-value: 1.10e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  18 GEIFIYGDIVSDkwfeSDVTATDFKNKLDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVI 97
Cdd:cd07016   1 AEIYIYGDIGSD----WGVTAKEFKDALDALGDDSDITVRINSPGGDVFAGLAIYNALKRHKGKVTVKIDGLAASAASVI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  98 AMSGDTIFMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYLDKAKdLDQEHLKQMLDAETWLTAEEALSFG 177
Cdd:cd07016  77 AMAGDEVEMPPNAMLMIHNPSTGAAGNADDLRKAADLLDKIDESIANAYAEKTG-LSEEEISALMDAETWLTAQEAVELG 155


                ....*
gi 66395523 178 LIDEI 182
Cdd:cd07016 156 FADEI 160
S14_ClpP cd07013
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 19-182 9.75e-33

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. Additionally, they are implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


Pssm-ID: 132924 [Multi-domain]  Cd Length: 162  Bit Score: 117.37  E-value: 9.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  19 EIFIYGDiVSDKWFESDVTATDFKNKLDELGDISeidVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIA 98
Cdd:cd07013   2 EIMLTGE-VEDISANQFAAQLLFLGAVNPEKDIY---LYINSPGGDVFAGMAIYDTIKFIKADVVTIIDGLAASMGSVIA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  99 MSGDTI--FMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYLDKAkDLDQEHLKQMLDAETWLTAEEALSF 176
Cdd:cd07013  78 MAGAKGkrFILPNAMMMIHQPWGGTLGDATDMRIYADLLLKVEGNLVSAYAHKT-GQSEEELHADLERDTWLSAREAVEY 156


                ....*.
gi 66395523 177 GLIDEI 182
Cdd:cd07013 157 GFADTI 162
CLP_protease pfam00574
Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ...
 20-184 6.25e-29

Clp protease; The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.


Pssm-ID: 425759 [Multi-domain]  Cd Length: 181  Bit Score: 107.65  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523    20 IFIYGDIvsDKWFESDVTATDFKnkLDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAM 99
Cdd:pfam00574  19 IFLGGEI--DDEVANLIIAQLLF--LEAEDPDKDIYLYINSPGGSVTAGLAIYDTMQYIKPDVSTICLGLAASMGSFLLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   100 SGDT--IFMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYlDKAKDLDQEHLKQMLDAETWLTAEEALSFG 177
Cdd:pfam00574  95 AGAKgkRFALPNARIMIHQPLGGAQGQASDIEIQAKEILKIKERLNEIY-AKHTGQSLEKIEKDTDRDFFMSAEEAKEYG 173


                  ....*..
gi 66395523   178 LIDEILG 184
Cdd:pfam00574 174 LIDEVIE 180
ClpP COG0740
ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein ...
 20-183 6.47e-25

ATP-dependent protease ClpP, protease subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440503  Cd Length: 194  Bit Score: 97.46  E-value: 6.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  20 IFIYGDIvsdkwfeSDVTATDFKNKLDEL---GDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASV 96
Cdd:COG0740  29 IFLGGEI-------DDHVANLIIAQLLFLeaeDPDKDILLYINSPGGSVTAGLAIYDTMQFIKPDVSTICLGQAASMGAF 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  97 IAMSGDTI--FMHKNSFLMIHNSWVMTVGNAEELRKTADLLEKTDAVSNSAYldkAKDLDQ--EHLKQMLDAETWLTAEE 172
Cdd:COG0740 102 LLAAGTKGkrFALPNARIMIHQPSGGAQGQASDIEIQAREILKMRERLNEIL---AEHTGQplEKIEKDTDRDTWMTAEE 178

                       170
                ....*....|.
gi 66395523 173 ALSFGLIDEIL 183
Cdd:COG0740 179 AVEYGLIDEVI 189
PRK12553 PRK12553
ATP-dependent Clp protease proteolytic subunit; Reviewed
 20-183 1.32e-17

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 237133  Cd Length: 207  Bit Score: 78.45  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   20 IFIYGDIvsdkwfeSDVTATDFKNKLDELGDIS---EIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASV 96
Cdd:PRK12553  38 IFLGGQV-------DDASANDVMAQLLVLESIDpdrDITLYINSPGGSVTAGDAIYDTIQFIRPDVQTVCTGQAASAGAV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   97 IAMSGD--TIFMHKNSFLMIHNSWVMTVGN---------AEELRKTADLLEKTdavsnsayLDKAKDLDQEHLKQMLDAE 165
Cdd:PRK12553 111 LLAAGTpgKRFALPNARILIHQPSLGGGIRgqasdleiqAREILRMRERLERI--------LAEHTGQSVEKIRKDTDRD 182

                        170
                 ....*....|....*...
gi 66395523  166 TWLTAEEALSFGLIDEIL 183
Cdd:PRK12553 183 KWLTAEEAKDYGLVDQII 200
S14_ClpP_2 cd07017
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp ...
 45-182 1.74e-17

Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease; Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.


Pssm-ID: 132928 [Multi-domain]  Cd Length: 171  Bit Score: 77.48  E-value: 1.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  45 LDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGDTI--FMHKNSFLMIHNSWVMTV 122
Cdd:cd07017  33 LESEDPKKPIYLYINSPGGSVTAGLAIYDTMQYIKPPVSTICLGLAASMGALLLAAGTKGkrYALPNSRIMIHQPLGGAG 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523 123 GNAEELRKTADLLEKTDAVSNSaYLDKAKDLDQEHLKQMLDAETWLTAEEALSFGLIDEI 182
Cdd:cd07017 113 GQASDIEIQAKEILRLRRRLNE-ILAKHTGQPLEKIEKDTDRDRYMSAEEAKEYGLIDKI 171
clpP PRK00277
ATP-dependent Clp protease proteolytic subunit; Reviewed
 53-183 4.63e-13

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 178955  Cd Length: 200  Bit Score: 65.96  E-value: 4.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   53 EIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGDT--IFMHKNSFLMIHNSWVMTVG------- 123
Cdd:PRK00277  63 DIYLYINSPGGSVTAGLAIYDTMQFIKPDVSTICIGQAASMGAFLLAAGAKgkRFALPNSRIMIHQPLGGFQGqatdiei 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66395523  124 NAEELRKTADLLEKTDAVSNSAYLDK-AKDLDQEHlkqmldaetWLTAEEALSFGLIDEIL 183
Cdd:PRK00277 143 HAREILKLKKRLNEILAEHTGQPLEKiEKDTDRDN---------FMSAEEAKEYGLIDEVL 194
Clp_protease_like cd00394
Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ...
 20-182 8.18e-13

Caseinolytic protease (ClpP) is an ATP-dependent protease; Clp protease (caseinolytic protease; ClpP; endopeptidase Clp; Peptidase S14; ATP-dependent protease, ClpAP)-like enzymes are highly conserved serine proteases and belong to the ClpP/Crotonase superfamily. Included in this family are Clp proteases that are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. The functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP. Active site consists of the triad Ser, His and Asp, preferring hydrophobic or non-polar residues at P1 or P1' positions. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function. Another family included in this class of enzymes is the signal peptide peptidase A (SppA; S49) which is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Mutagenesis studies suggest that the catalytic center of SppA comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. In addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members, the E. coli SppA contains an amino-terminal domain. Others, including sohB peptidase, protein C, protein 1510-N and archaeal signal peptide peptidase, do not contain the amino-terminal domain. The third family included in this hierarchy is nodulation formation efficiency D (NfeD) which is a membrane-bound Clp-class protease and only found in bacteria and archaea. Majority of the NfeD genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named stomatin operon partner protein (STOPP). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 from Pyrococcus horikoshii has been shown to possess serine protease activity having a Ser-Lys catalytic dyad.


Pssm-ID: 132923 [Multi-domain]  Cd Length: 161  Bit Score: 64.34  E-value: 8.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  20 IFIYGDIvsdkwfeSDVTATDFKNKLDEL---GDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASV 96
Cdd:cd00394   2 IFINGVI-------EDVSADQLAAQIRFAeadNSVKAIVLEVNTPGGRVDAGMNIVDALQASRKPVIAYVGGQAASAGYY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  97 IAMSGDTIFMHKNSFLMIHNSWVMTVGNAEELRKTAD--LLEKTDAVSNSAYLDKAKDlDQEHLKQMLDAETWLTAEEAL 174
Cdd:cd00394  75 IATAANKIVMAPGTRVGSHGPIGGYGGNGNPTAQEADqrIILYFIARFISLVAENRGQ-TTEKLEEDIEKDLVLTAQEAL 153


                ....*...
gi 66395523 175 SFGLIDEI 182
Cdd:cd00394 154 EYGLVDAL 161
PRK14514 PRK14514
ATP-dependent Clp endopeptidase proteolytic subunit ClpP;
45-183 1.32e-11

ATP-dependent Clp endopeptidase proteolytic subunit ClpP;


Pssm-ID: 184722  Cd Length: 221  Bit Score: 62.24  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   45 LDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGD--TIFMHKNSFLMIHNSWVMTV 122
Cdd:PRK14514  78 LDSVDPGKDISIYINSPGGSVYAGLGIYDTMQFISSDVATICTGMAASMASVLLVAGTkgKRSALPHSRVMIHQPLGGAQ 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66395523  123 GNAEELRKTADLLEKtdaVSNSAYLDKAKDLDQEHLKQMLDAET--WLTAEEALSFGLIDEIL 183
Cdd:PRK14514 158 GQASDIEITAREIQK---LKKELYTIIADHSGTPFDKVWADSDRdyWMTAQEAKEYGMIDEVL 217
PRK14513 PRK14513
ATP-dependent Clp protease proteolytic subunit; Provisional
 45-183 1.79e-11

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237742 [Multi-domain]  Cd Length: 201  Bit Score: 61.49  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   45 LDELGDISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGD--TIFMHKNSFLMIHNSWVMTV 122
Cdd:PRK14513  51 LDSQNPEQEIQMYINCPGGEVYAGLAIYDTMRYIKAPVSTICVGIAMSMGSVLLMAGDkgKRMALPNSRIMIHQGSAGFR 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66395523  123 GNAEELRKTA-DLLEKTDAVSNsaYLDKAKDLDQEHLKQMLDAETWLTAEEALSFGLIDEIL 183
Cdd:PRK14513 131 GNTPDLEVQAkEVLFLRDTLVD--IYHRHTDLPHEKLLRDMERDYFMSPEEAKAYGLIDSVI 190
SppA COG0616
Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, ...
 11-182 4.31e-10

Periplasmic serine protease, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440381 [Multi-domain]  Cd Length: 215  Bit Score: 57.88  E-value: 4.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  11 KRKSKSKGEIF---IYGDIVSDKW-FESDVTATDFKNKLDEL---GDISEIDVHINSSGGSVFEGHAIYNMLKMHPAK-- 81
Cdd:COG0616   3 ARPPKVKPSIAvidLEGTIVDGGGpPSGEIGLEDILAALRKAaedPDVKAVVLRINSPGGSVAASEEIRDALRRLRAKgk 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  82 -INIYVDALAASIASVIAMSGDTIFMHKNS------FLMIHNSW------------VMTVG------------NAEELRK 130
Cdd:COG0616  83 pVVASMGDVAASGGYYIASAADKIYANPTTitgsigVIAQGPNFkglleklgveveVVTAGeykdalspfrplSEEEREQ 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66395523 131 TADLLEKT-----DAVSnsayldKAKDLDQEHLKQMLDAETWlTAEEALSFGLIDEI 182
Cdd:COG0616 163 LQALLDDIydqfvEDVA------EGRGLSLEEVREIADGRVW-TGEQALELGLVDEL 212
S49_Sppa_N_C cd07023
Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal ...
 18-182 5.35e-10

Signal peptide peptidase A (SppA), a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV): SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. This subfamily contains members with either a single domain (sometimes referred to as 36K type), such as sohB peptidase, protein C and archaeal signal peptide peptidase, or an amino-terminal domain in addition to the carboxyl-terminal protease domain that is conserved in all the S49 family members (sometimes referred to as 67K type), similar to E. coli and Arabidopsis thaliana SppA peptidases. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases. Interestingly, the single membrane spanning E. coli SppA carries out catalysis using a Ser-Lys dyad with the serine located in the conserved carboxy-terminal protease domain and the lysine in the non-conserved amino-terminal domain.


Pssm-ID: 132934 [Multi-domain]  Cd Length: 208  Bit Score: 57.50  E-value: 5.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  18 GEIFIYGDIVSDkwfeSDVTATDFKNKLDELGDISEID---VHINSSGGSVFEGHAIYNMLKMHPAK---INIYVDALAA 91
Cdd:cd07023   3 AVIDIEGTISDG----GGIGADSLIEQLRKAREDDSVKavvLRINSPGGSVVASEEIYREIRRLRKAkkpVVASMGDVAA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  92 SIASVIAMSGDTIFMHKNSF---------------LM----IHNSWVMTVGNAEELRKTADL----LEKTDAVSNSAYLD 148
Cdd:cd07023  79 SGGYYIAAAADKIVANPTTItgsigvigqgpnleeLLdklgIERDTIKSGPGKDKGSPDRPLteeeRAILQALVDDIYDQ 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66395523 149 ------KAKDLDQEHLKQMLDAETWlTAEEALSFGLIDEI 182
Cdd:cd07023 159 fvdvvaEGRGMSGERLDKLADGRVW-TGRQALELGLVDEL 197
PRK14512 PRK14512
ATP-dependent Clp protease proteolytic subunit; Provisional
 54-182 2.46e-07

ATP-dependent Clp protease proteolytic subunit; Provisional


Pssm-ID: 237741  Cd Length: 197  Bit Score: 49.79  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   54 IDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVI--AMSGDTIFMHKNSFLMIHNSWVMTVGNAEELRKT 131
Cdd:PRK14512  56 IFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTIGVGLVASAAALIflAAKKESRFSLPNARYLLHQPLSGFKGVATDIEIY 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 66395523  132 ADLLEKTDAVSNsAYLDKAKDLDQEHLKQMLDAETWLTAEEALSFGLIDEI 182
Cdd:PRK14512 136 ANELNKVKSELN-DIIAKETGQELDKVEKDTDRDFWLDSSSAVKYGLVFEV 185
COG3904 COG3904
Predicted periplasmic protein [Function unknown];
24-185 7.74e-07

Predicted periplasmic protein [Function unknown];


Pssm-ID: 443110 [Multi-domain]  Cd Length: 197  Bit Score: 48.48  E-value: 7.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  24 GDIVSDkwfesdvTATDFKNKLDELGDISEIdVHINSSGGSVFEGHAIYNMLKMHpaKINIYV--DALAASIASVIAMSG 101
Cdd:COG3904  43 GEITPG-------DAARLEALLETRGPGVAT-VVLNSPGGSVAEALALGRLIRAR--GLDTAVpaGAYCASACVLAFAGG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523 102 DTIFMHKNSFLMIHNSWVMTvgnaEELRKTADLLEKTDAVSN--SAYLDKAkDLDQEHLKQML----DAETWLTAEEALS 175
Cdd:COG3904 113 VERYVEPGARVGVHQPYLGG----GDALPAAEAVSDTQRATArlARYLREM-GVDPELLELALstppDDMRYLTPEELLR 187

                       170
                ....*....|
gi 66395523 176 FGLIDEILGA 185
Cdd:COG3904 188 YGLVTGPLPA 197
clpP CHL00028
ATP-dependent Clp protease proteolytic subunit
 53-187 1.15e-06

ATP-dependent Clp protease proteolytic subunit


Pssm-ID: 214340  Cd Length: 200  Bit Score: 47.93  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   53 EIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIaMSGDTI---FMHKNSFLMIHN---SWVMtvGNAE 126
Cdd:CHL00028  62 DLYLFINSPGGSVISGLAIYDTMQFVKPDVHTICLGLAASMASFI-LAGGEItkrLAFPHARVMIHQpasSFYE--GQAS 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66395523  127 ELRKTADLLEKT-DAVSNSAYLDKAKDLDQehLKQMLDAETWLTAEEALSFGLIDEILGANE 187
Cdd:CHL00028 139 EFVLEAEELLKLrETITRVYAQRTGKPLWV--ISEDMERDVFMSATEAKAYGIVDLVAVNNE 198
PRK12551 PRK12551
ATP-dependent Clp protease proteolytic subunit; Reviewed
 53-183 2.88e-06

ATP-dependent Clp protease proteolytic subunit; Reviewed


Pssm-ID: 139060  Cd Length: 196  Bit Score: 46.75  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   53 EIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSG----DTIFMHknSFLMIHNSWVMTVGNAEEL 128
Cdd:PRK12551  57 DIYLYINSPGGSVYDGLGIFDTMQHVKPDVHTVCVGLAASMGAFLLCAGakgkRSSLQH--SRIMIHQPLGGARGQASDI 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 66395523  129 RKTAD-LLEKTDAVSNSAYLDKAKDLDQehLKQMLDAETWLTAEEALSFGLIDEIL 183
Cdd:PRK12551 135 RIQADeILFLKERLNTELSERTGQPLER--IQEDTDRDFFMSPSEAVEYGLIDLVI 188
SppA_dom TIGR00706
signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein ...
 35-182 1.83e-05

signal peptide peptidase SppA, 36K type; The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273227 [Multi-domain]  Cd Length: 208  Bit Score: 44.28  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523    35 DVTATDFKNKLDELGD---ISEIDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDA--LAASIASVIAMSGDTIFMHKn 109
Cdd:TIGR00706  13 DVSPEDFDKKLERIKDdktIKALVLRINSPGGTVVASEEIYKKLEKLKAKKPVVASMggMAASGGYYISMAADEIFANP- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523   110 sflmihNSWVMTVGNAEELRKTADLLEK----TDAVSNSAYLD--------------------------------KAKDL 153
Cdd:TIGR00706  92 ------GTITGSIGVILQGANVEKLAEKlgisFEVIKSGAYKDigsptreltpeeknilqslvnesyeqfvqvvsKGRNL 165

                         170       180
                  ....*....|....*....|....*....
gi 66395523   154 DQEHLKQMLDAETWlTAEEALSFGLIDEI 182
Cdd:TIGR00706 166 PVEEVKKFADGRVF-TGRQALKLRLVDKL 193
SDH_sah pfam01972
Serine dehydrogenase proteinase; This family of archaebacterial proteins, formerly known as ...
 54-112 6.05e-05

Serine dehydrogenase proteinase; This family of archaebacterial proteins, formerly known as DUF114, has been found to be a serine dehydrogenase proteinase distantly related to ClpP proteinases that belong to the serine proteinase superfamily. The family has a catalytic triad of Ser, Asp, His residues, which shows an altered residue ordering compared with the ClpP proteinases but similar to that of the carboxypeptidase clan.


Pssm-ID: 110924  Cd Length: 286  Bit Score: 43.30  E-value: 6.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 66395523    54 IDVHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGDTIFMHKNSFL 112
Cdd:pfam01972  94 IDLIIHTPGGLALAATQIAKALKEHKAKTTVIVPHYAMSGGTLIALAADEIIMDENAVL 152
NfeD COG1030
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
 56-182 8.18e-05

Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 43.31  E-value: 8.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66395523  56 VHINSSGGSVFEGHAIYNMLKMHPAKINIYV--DALAASIASVIAMSGDTIFMHKNSflmihnswvmTVGNAE------E 127
Cdd:COG1030  62 LELDTPGGLVDSAREIVDAILASPVPVIVYVasGARAASAGAYILLASHIAAMAPGT----------NIGAATpvqiggG 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66395523 128 LRKTADllEKT--DAVSNSAYLDKAKDLDQEHLKQMLDAETWLTAEEALSFGLIDEI 182
Cdd:COG1030 132 IDEAME--EKVinDAVAYIRSLAELRGRNADWAEAMVRESVSLTAEEALELGVIDLI 186
Clp_protease_NfeD_like cd07021
Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation ...
 56-110 5.51e-03

Nodulation formation efficiency D (NfeD) is a membrane-bound ClpP-class protease; Nodulation formation efficiency D (NfeD; stomatin operon partner protein, STOPP; DUF107) is a member of membrane-anchored ClpP-class proteases. Currently, more than 300 NfeD homologs have been identified - all of which are bacterial or archaeal in origin. Majority of these genomes have been shown to possess operons containing a homologous NfeD/stomatin gene pair, causing NfeD to be previously named STOPP (stomatin operon partner protein). NfeD homologs can be divided into two groups: long and short forms. Long-form homologs have a putative ClpP-class serine protease domain while the short form homologs do not. Downstream from the ClpP-class domain is the so-called NfeD or DUF107 domain. N-terminal region of the NfeD homolog PH1510 (1510-N or PH1510-N) from Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. Difference in oligomeric form and catalytic residues between 1510-N (forming a dimer) and ClpP (forming a tetradecamer) shows a possible functional difference: 1510-N is likely to have a regulatory function while ClpP is involved in protein quality control.


Pssm-ID: 132932 [Multi-domain]  Cd Length: 178  Bit Score: 36.80  E-value: 5.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66395523  56 VHINSSGGSVFEGHAIYNMLKMHPAKINIYVDALAASIASVIAMSGDTIFMHKNS 110
Cdd:cd07021  35 LDIDTPGGRVDSALEIVDLILNSPIPTIAYVNDRAASAGALIALAADEIYMAPGA 89
 
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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