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Conserved domains on  [gi|2185807952|ref|WP_236711376|]
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AAA family ATPase [Novosphingobium barchaimii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02518 super family cl33680
ParA-like protein; Provisional
5-145 4.70e-31

ParA-like protein; Provisional


The actual alignment was detected with superfamily member PHA02518:

Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 110.71  E-value: 4.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   5 GAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLRAVAVLNGA 84
Cdd:PHA02518   63 GKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISR 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2185807952  85 DAQGADNEAALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEqTPRDPKAIDELTALI 145
Cdd:PHA02518  143 AIKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLE-LPEDDKAAEEIIQLV 202
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
5-145 4.70e-31

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 110.71  E-value: 4.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   5 GAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLRAVAVLNGA 84
Cdd:PHA02518   63 GKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISR 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2185807952  85 DAQGADNEAALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEqTPRDPKAIDELTALI 145
Cdd:PHA02518  143 AIKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLE-LPEDDKAAEEIIQLV 202
ParA_partition NF041546
ParA family partition ATPase;
2-145 3.67e-29

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 105.33  E-value: 3.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   2 ALTGAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLRAVAVL 81
Cdd:NF041546   59 GLARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVL 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2185807952  82 NGADAQGADNEAALEMIGDIdGIEVLPTSIVRRKAFPNAAAEGRAVIEQTPRDpKAIDELTALI 145
Cdd:NF041546  139 NRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG-KAAREIRALA 200
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
8-145 1.76e-16

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 73.35  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   8 LRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEARE-INEGLRAVAVL-NGAD 85
Cdd:COG1192   107 LKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREdLNPKLEILGILlTMVD 186
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185807952  86 AQGADNEAALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEQTPRDP--KAIDELTALI 145
Cdd:COG1192   187 PRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKgaKAYRALAEEL 248
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
19-98 1.08e-13

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 63.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952  19 YDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEG--LRAVAVLNGADAQGADNEAALE 96
Cdd:cd02042    48 YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLAREVLE 127

                  ..
gi 2185807952  97 MI 98
Cdd:cd02042   128 EL 129
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-127 6.46e-06

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 44.26  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   5 GAALRSQVRQLASKYDDIIID-VGGRDTGsLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLR---AVAV 80
Cdd:pfam01656 104 EERLREALEALKEDYDYVIIDgAPGLGEL-LRNALIAADYVIIPLEPEVILVEDAKRLGGVIAALVGGYALLGlkiIGVV 182
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2185807952  81 LN--GADAQGADNEAALEMIgdIDGIEVLPtSIVRRKAFPNAAAEGRAV 127
Cdd:pfam01656 183 LNkvDGDNHGKLLKEALEEL--LRGLPVLG-VIPRDEAVAEAPARGLPV 228
 
Name Accession Description Interval E-value
PHA02518 PHA02518
ParA-like protein; Provisional
5-145 4.70e-31

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 110.71  E-value: 4.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   5 GAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLRAVAVLNGA 84
Cdd:PHA02518   63 GKSIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISR 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2185807952  85 DAQGADNEAALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEqTPRDPKAIDELTALI 145
Cdd:PHA02518  143 AIKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGSVLE-LPEDDKAAEEIIQLV 202
ParA_partition NF041546
ParA family partition ATPase;
2-145 3.67e-29

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 105.33  E-value: 3.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   2 ALTGAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLRAVAVL 81
Cdd:NF041546   59 GLARPTLHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVL 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2185807952  82 NGADAQGADNEAALEMIGDIdGIEVLPTSIVRRKAFPNAAAEGRAVIEQTPRDpKAIDELTALI 145
Cdd:NF041546  139 NRAIARTALGREVAEALAEY-GLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG-KAAREIRALA 200
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
8-145 1.76e-16

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 73.35  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   8 LRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEARE-INEGLRAVAVL-NGAD 85
Cdd:COG1192   107 LKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREdLNPKLEILGILlTMVD 186
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185807952  86 AQGADNEAALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEQTPRDP--KAIDELTALI 145
Cdd:COG1192   187 PRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKgaKAYRALAEEL 248
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
19-98 1.08e-13

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 63.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952  19 YDDIIIDVGGRDTGSLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEG--LRAVAVLNGADAQGADNEAALE 96
Cdd:cd02042    48 YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPplLILGILLTRVDPRTKLAREVLE 127

                  ..
gi 2185807952  97 MI 98
Cdd:cd02042   128 EL 129
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-127 6.46e-06

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 44.26  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   5 GAALRSQVRQLASKYDDIIID-VGGRDTGsLRAALTVADTLLVPVQPRSFDVWALDQVSALVAEAREINEGLR---AVAV 80
Cdd:pfam01656 104 EERLREALEALKEDYDYVIIDgAPGLGEL-LRNALIAADYVIIPLEPEVILVEDAKRLGGVIAALVGGYALLGlkiIGVV 182
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2185807952  81 LN--GADAQGADNEAALEMIgdIDGIEVLPtSIVRRKAFPNAAAEGRAV 127
Cdd:pfam01656 183 LNkvDGDNHGKLLKEALEEL--LRGLPVLG-VIPRDEAVAEAPARGLPV 228
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
15-143 2.43e-05

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 42.65  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952  15 LASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPrsfDVWALDQVSALVAEAREINEGLRAVA-VLNGADaqgADNEA 93
Cdd:cd03111   110 LRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQ---DLPSLRNARRLLDSLRELEGSSDRLRlVLNRYD---KKSEI 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2185807952  94 ALEMIGDIDGIEVLPTSIVRRKAFPNAAAEGRAVIEQTPRDP--KAIDELTA 143
Cdd:cd03111   184 SPKDIEEALGLEVFATLPNDYKAVSESANTGRPLVEVAPRSAlvRALQDLAA 235
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
6-145 5.58e-05

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 41.41  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   6 AALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPrsfDVWALDQVSALVAEAREINEGLRAVAVLNGAD 85
Cdd:COG0455    81 ERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTP---EPTSITDAYALLKLLRRRLGVRRAGVVVNRVR 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2185807952  86 AQGADNEAALEMIGDID---GIEVLPTSIVRR-KAFPNAAAEGRAVIEQTPRDP--KAIDELTALI 145
Cdd:COG0455   158 SEAEARDVFERLEQVAErflGVRLRVLGVIPEdPAVREAVRRGRPLVLAAPDSPaaRAIRELAARL 223
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-145 1.10e-04

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 40.87  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185807952   2 ALTGAALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVPVQPrsfDVWALDQVSALVAEAREIN-EGLRAVAV 80
Cdd:COG4963   199 EVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP---DLPSLRNAKRLLDLLRELGlPDDKVRLV 275
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185807952  81 LNGADAQGADNEAALEMIGDIDGIEVLPTSivrRKAFPNAAAEGRAVIEQTPRDP--KAIDELTALI 145
Cdd:COG4963   276 LNRVPKRGEISAKDIEEALGLPVAAVLPND---PKAVAEAANQGRPLAEVAPKSPlaKAIRKLAARL 339
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
6-69 2.80e-04

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 39.74  E-value: 2.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185807952   6 AALRSQVRQLASKYDDIIIDVGGRDTGSLRAALTVADTLLVP-------------VQPRSFDVWALDQVSALVAEAR 69
Cdd:pfam09140  87 ARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPlndsfvdfdllgqVDPETFKVKRPSFYAEMVWEAR 163
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
7-75 2.52e-03

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 36.41  E-value: 2.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2185807952   7 ALRSQVRQLASKYDDIIIDVggrdTGSL----RAALTVADTLLVPVQPrsfDVWALDQVSALVAEAREINEGL 75
Cdd:pfam13614 106 ILKEALEPVKDNYDYIIIDC----PPSLglltINALTASDSVLIPVQC---EYYALEGLSQLLNTIKLVKKRL 171
 
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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