NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|688508349|gb|AIQ84929|]
View 

caseinolytic protease C, partial (apicoplast) [Plasmodium ashfordi]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-133 7.02e-69

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0542:

Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 223.42  E-value: 7.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 SNLGcpnnyDKYLLnKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:COG0542  699 SNIG-----SELIL-DLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVF 745
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-133 7.02e-69

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 223.42  E-value: 7.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 SNLGcpnnyDKYLLnKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:COG0542  699 SNIG-----SELIL-DLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVF 745
clpC CHL00095
Clp protease ATP binding subunit
1-177 4.22e-61

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 202.21  E-value: 4.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:CHL00095 579 MEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMT 658
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349  81 SNLGCP----NNYD-KYLLNKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDILIFNPLNINNLLLIFDKFINELKYK 155
Cdd:CHL00095 659 SNLGSKvietNSGGlGFELSENQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKR 738
                        170       180
                 ....*....|....*....|..
gi 688508349 156 lyLNKLNININIHNNVKYLLVK 177
Cdd:CHL00095 739 --LNEQGIQLEVTERIKTLLIE 758
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
1-133 5.81e-60

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 199.41  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:TIGR03346 634 MEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMT 713
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688508349   81 SNLGCPnnydkYLLNKMylSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:TIGR03346 714 SNLGSD-----FIQELA--GGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVF 759
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
1-130 1.64e-54

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 170.07  E-value: 1.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:pfam07724  43 MEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMT 122
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 688508349   81 SNLGCpnnyDKYLLNKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDI 130
Cdd:pfam07724 123 GNFGS----EKISDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
1-133 3.60e-51

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 161.96  E-value: 3.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:cd19499   81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 snlgcpnnydkyllnkmylskedlqdiknnikiniSNYFKPELLNRLTDILIF 133
Cdd:cd19499  161 -----------------------------------SNHFRPEFLNRIDEIVVF 178
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-133 7.02e-69

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 223.42  E-value: 7.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 SNLGcpnnyDKYLLnKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:COG0542  699 SNIG-----SELIL-DLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVF 745
clpC CHL00095
Clp protease ATP binding subunit
1-177 4.22e-61

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 202.21  E-value: 4.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:CHL00095 579 MEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMT 658
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349  81 SNLGCP----NNYD-KYLLNKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDILIFNPLNINNLLLIFDKFINELKYK 155
Cdd:CHL00095 659 SNLGSKvietNSGGlGFELSENQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKR 738
                        170       180
                 ....*....|....*....|..
gi 688508349 156 lyLNKLNININIHNNVKYLLVK 177
Cdd:CHL00095 739 --LNEQGIQLEVTERIKTLLIE 758
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
1-133 5.81e-60

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 199.41  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:TIGR03346 634 MEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMT 713
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688508349   81 SNLGCPnnydkYLLNKMylSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:TIGR03346 714 SNLGSD-----FIQELA--GGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVF 759
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
1-130 1.64e-54

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 170.07  E-value: 1.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:pfam07724  43 MEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMT 122
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 688508349   81 SNLGCpnnyDKYLLNKMYLSKEDLQDIKNNIKINISNYFKPELLNRLTDI 130
Cdd:pfam07724 123 GNFGS----EKISDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
1-133 3.60e-51

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 161.96  E-value: 3.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:cd19499   81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 snlgcpnnydkyllnkmylskedlqdiknnikiniSNYFKPELLNRLTDILIF 133
Cdd:cd19499  161 -----------------------------------SNHFRPEFLNRIDEIVVF 178
ClpA TIGR02639
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ...
1-156 1.19e-50

ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274241 [Multi-domain]  Cd Length: 730  Bit Score: 172.90  E-value: 1.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:TIGR02639 520 MEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMT 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   81 SNLGCpnnydkyllnkMYLSKEDLQDIKNNIKIN----ISNYFKPELLNRLTDILIFNPLNINNLLLIFDKFINELKYKL 156
Cdd:TIGR02639 600 SNAGA-----------SEMSKPPIGFGGENRESKslkaIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQL 668
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
1-133 2.35e-47

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 164.63  E-value: 2.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:PRK10865 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508349  81 SNLGCPNNYDKYllnkmylSKEDLQDIKNNIKINISNYFKPELLNRLTDILIF 133
Cdd:PRK10865 718 SNLGSDLIQERF-------GELDYAHMKELVLGVVSHNFRPEFINRIDEVVVF 763
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
1-156 2.14e-43

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 153.07  E-value: 2.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349   1 MEKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLT 80
Cdd:PRK11034 525 MERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMT 604
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688508349  81 SNLGCPNNYDKYL-LNKMYLSKEDLQDIKnniKInisnyFKPELLNRLTDILIFNPLNINNLLLIFDKFINELKYKL 156
Cdd:PRK11034 605 TNAGVRETERKSIgLIHQDNSTDAMEEIK---KI-----FTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQL 673
VI_ClpV1 TIGR03345
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ...
2-130 4.71e-42

type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274528 [Multi-domain]  Cd Length: 852  Bit Score: 149.32  E-value: 4.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508349    2 EKHSISRLIGSPPGYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTDTTGKLVDFTNTIILLTS 81
Cdd:TIGR03345 637 EAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTS 716
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 688508349   82 NLGCPnnydkyLLNKMYLSKE---DLQDIKNNIKINISNYFKPELLNRLTDI 130
Cdd:TIGR03345 717 NAGSD------LIMALCADPEtapDPEALLEALRPELLKVFKPAFLGRMTVI 762
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
20-82 3.20e-05

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 41.51  E-value: 3.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688508349   20 NEGGQLTEQVFK---KPNSVILFDEIEKAHPDIYNIMLQILDEGRL-TDTTGKLVDF--TNTIILLTSN 82
Cdd:pfam07728  50 PGGASWVDGPLVraaREGEIAVLDEINRANPDVLNSLLSLLDERRLlLPDGGELVKAapDGFRLIATMN 118
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
15-82 8.69e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 35.20  E-value: 8.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688508349  15 GYVGYNEGGQLTEQVFKKPNSVILFDEIEKAHPDIYNIMLQILDEGRLTdttgkLVDFTNTIILLTSN 82
Cdd:cd00009   66 ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH