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Conserved domains on  [gi|740680866|ref|WP_038466155|]
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AAA family ATPase [Candidatus Paracaedibacter acanthamoebae]

Protein Classification

COG3911 family protein( domain architecture ID 10008129)

COG3911 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
1-177 3.91e-58

Predicted ATPase [General function prediction only];


:

Pssm-ID: 443117  Cd Length: 180  Bit Score: 179.63  E-value: 3.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   1 MKNYILTGAPGSGKTTLLESLKNLNFTIISEAATDIIAQEQAI-GTPEPWTDPS-FIDKIILLQQERHlLSAISGKSVQF 78
Cdd:COG3911    3 TRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIgGDALPWTDPAaFAELMLEGRLRQY-REAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866  79 FDRSPLCTYALALYLEYPPSRLLLTEIERiqqtQCYERNVFFIENLGFITKTDA-RQISFDESLKFEKIHRDVYQQFGFN 157
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAA----FRYDRTVFILPPWPEIYTQDAeRKQSFEEALRTYEALVETYRALGYE 157

                        170       180
                 ....*....|....*....|
gi 740680866 158 CIPVPKAPVPNRINYIIERL 177
Cdd:COG3911  158 LIEVPKGSVEERVDFILSRL 177
 
Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
1-177 3.91e-58

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 179.63  E-value: 3.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   1 MKNYILTGAPGSGKTTLLESLKNLNFTIISEAATDIIAQEQAI-GTPEPWTDPS-FIDKIILLQQERHlLSAISGKSVQF 78
Cdd:COG3911    3 TRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIgGDALPWTDPAaFAELMLEGRLRQY-REAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866  79 FDRSPLCTYALALYLEYPPSRLLLTEIERiqqtQCYERNVFFIENLGFITKTDA-RQISFDESLKFEKIHRDVYQQFGFN 157
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAA----FRYDRTVFILPPWPEIYTQDAeRKQSFEEALRTYEALVETYRALGYE 157

                        170       180
                 ....*....|....*....|
gi 740680866 158 CIPVPKAPVPNRINYIIERL 177
Cdd:COG3911  158 LIEVPKGSVEERVDFILSRL 177
AAA_28 pfam13521
AAA domain;
4-169 1.49e-30

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 108.89  E-value: 1.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866    4 YILTGAPGSGKTTLLESLKN-LNFTIISEAATDIIAQEQAIGTPE-PWTDPSFIDKIILLQQERHLLSAISGKSVQFFDR 81
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAArFGYPVVPEAAREILEELGADGGDAlPWVEDLLAFARGVLEAQLEDEAAAAANDLLFFDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   82 SPLCT--YALALYLEYPPsrllltEIERIQQTQCYERnVFFIENLGFITKTDARQISFDESLKFEKIHRDVYQQFGFNCI 159
Cdd:pfam13521  82 GPLDTlaYSRAYGGPCPP------ELEAAARASRYDL-VFLLPPDPEIVQDGERREDPEERERFHERLREALRELGIPVI 154

                         170
                  ....*....|
gi 740680866  160 PVPKAPVPNR 169
Cdd:pfam13521 155 IVPRGSVEER 164
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 6-46 2.69e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 36.73  E-value: 2.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 740680866   6 LTGAPGSGKTTLLESLKNLNFTIISeaaTDIIA-QEQAIGTP 46
Cdd:cd02022    4 LTGGIGSGKSTVAKLLKELGIPVID---ADKIAhEVYEPGGP 42
 
Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
1-177 3.91e-58

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 179.63  E-value: 3.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   1 MKNYILTGAPGSGKTTLLESLKNLNFTIISEAATDIIAQEQAI-GTPEPWTDPS-FIDKIILLQQERHlLSAISGKSVQF 78
Cdd:COG3911    3 TRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIgGDALPWTDPAaFAELMLEGRLRQY-REAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866  79 FDRSPLCTYALALYLEYPPSRLLLTEIERiqqtQCYERNVFFIENLGFITKTDA-RQISFDESLKFEKIHRDVYQQFGFN 157
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAA----FRYDRTVFILPPWPEIYTQDAeRKQSFEEALRTYEALVETYRALGYE 157

                        170       180
                 ....*....|....*....|
gi 740680866 158 CIPVPKAPVPNRINYIIERL 177
Cdd:COG3911  158 LIEVPKGSVEERVDFILSRL 177
AAA_28 pfam13521
AAA domain;
4-169 1.49e-30

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 108.89  E-value: 1.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866    4 YILTGAPGSGKTTLLESLKN-LNFTIISEAATDIIAQEQAIGTPE-PWTDPSFIDKIILLQQERHLLSAISGKSVQFFDR 81
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAArFGYPVVPEAAREILEELGADGGDAlPWVEDLLAFARGVLEAQLEDEAAAAANDLLFFDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   82 SPLCT--YALALYLEYPPsrllltEIERIQQTQCYERnVFFIENLGFITKTDARQISFDESLKFEKIHRDVYQQFGFNCI 159
Cdd:pfam13521  82 GPLDTlaYSRAYGGPCPP------ELEAAARASRYDL-VFLLPPDPEIVQDGERREDPEERERFHERLREALRELGIPVI 154

                         170
                  ....*....|
gi 740680866  160 PVPKAPVPNR 169
Cdd:pfam13521 155 IVPRGSVEER 164
AAA_17 pfam13207
AAA domain;
7-71 1.26e-05

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 43.00  E-value: 1.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740680866    7 TGAPGSGKTTLLESL-KNLNFTIISeaATDIIAQEQAIGTPEPwtDPSFIDKIILLQQERHLLSAI 71
Cdd:pfam13207   1 TGVPGSGKTTQLKKLaEKLGFPHIS--AGDLLREEAKERGLVE--DRDEMRKLPLEPQKELQKLAA 62
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 1-93 1.11e-04

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 40.57  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740680866   1 MKNYILTGAPGSGKTTLLESLKN-LNFTIISEAATDIIAQEQAIgtpepwTDPSFIDKIILLQQERHLLSAISGKSVQFF 79
Cdd:COG3172    8 VKKIVLLGAESTGKTTLARALAAhYNTPWVPEYGREYLEEKGRA------LTYDDLLAIARGQLALEDAAAKRANKLLFC 81

                         90
                 ....*....|....
gi 740680866  80 DRSPLCTYALALYL 93
Cdd:COG3172   82 DTDALTTKVYSELY 95
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 6-46 2.69e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 36.73  E-value: 2.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 740680866   6 LTGAPGSGKTTLLESLKNLNFTIISeaaTDIIA-QEQAIGTP 46
Cdd:cd02022    4 LTGGIGSGKSTVAKLLKELGIPVID---ADKIAhEVYEPGGP 42
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 3-46 4.46e-03

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 36.45  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 740680866   3 NYILTGAPGSGKTTLLESL-KNLNFTIISeaATDIIAQEQAIGTP 46
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLaKKYGLPHIS--TGDLLREEIASGTE 43
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 3-28 5.81e-03

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 35.68  E-value: 5.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 740680866    3 NYILTGAPGSGKTTLL----ESLKNLNFTI 28
Cdd:pfam03266   1 RIFITGPPGVGKTTLVlkvaELLKSSGVKV 30
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 6-46 5.90e-03

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 35.81  E-value: 5.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 740680866   6 LTGAPGSGKTTLLESLKNLNFTIISeaaTDIIAQE-QAIGTP 46
Cdd:COG0237    6 LTGGIGSGKSTVARMFAELGAPVID---ADAIARElVEPGGP 44
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-46 5.97e-03

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 35.33  E-value: 5.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 740680866    1 MKNYILTGAPGSGKTTLLESLKNLNFTIISEAATDIIaqEQAIGTP 46
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFY--DNAIDTP 44
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
2-21 7.62e-03

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 35.26  E-value: 7.62e-03
                         10        20
                 ....*....|....*....|
gi 740680866   2 KNYILTGAPGSGKTTLLESL 21
Cdd:COG1618    1 MKIFITGRPGVGKTTLLLKV 20
 
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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