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Conserved domains on  [gi|500706951|ref|WP_011977818|]
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MULTISPECIES: AAA family ATPase [Enterobacterales]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 14-105 1.15e-47

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


:

Pssm-ID: 436616  Cd Length: 92  Bit Score: 157.58  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEAGGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 500706951   94 NHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 2.05e-38

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: 138.45  E-value: 2.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 188 LSDFIVPSIIPGVDVIPASIDdafLAegwkGLCEEHLPGKNIHAVLKEnIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIemdGHTCNLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDL---NPKLEILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500706951 348 GFERCGETFDTVIsanpaTYDGSTEALKsaksAAEDFAKAVFDRIE 393
Cdd:COG1192  217 ALAEAPSAGKPVF-----EYDPKSKGAK----AYRALAEELLERLE 253
 
Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 14-105 1.15e-47

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


Pssm-ID: 436616  Cd Length: 92  Bit Score: 157.58  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEAGGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 500706951   94 NHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 2.05e-38

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: 138.45  E-value: 2.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 188 LSDFIVPSIIPGVDVIPASIDdafLAegwkGLCEEHLPGKNIHAVLKEnIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIemdGHTCNLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDL---NPKLEILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500706951 348 GFERCGETFDTVIsanpaTYDGSTEALKsaksAAEDFAKAVFDRIE 393
Cdd:COG1192  217 ALAEAPSAGKPVF-----EYDPKSKGAK----AYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 111-359 8.20e-20

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: 87.40  E-value: 8.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  111 IFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLsd 190
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  191 FIVPSIIPGVDVIPASIDdafLAEGWKGLCEEHLPGKnIHAVLKEniidkLQHDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNID---LEKFEKELLGPRKEER-LREALEA-----LKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  271 LTPLPPATVDfhsslkfVASLPALIDSIEMDGHTCNLIG--NVGFmskILNK---SDHKICHSQA--KEVFGADMLDmVL 343
Cdd:pfam01656 144 IIPLEPEVIL-------VEDAKRLGGVIAALVGGYALLGlkIIGV---VLNKvdgDNHGKLLKEAleELLRGLPVLG-VI 212

                         250
                  ....*....|....*.
gi 500706951  344 PRLDGFERCGETFDTV 359
Cdd:pfam01656 213 PRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 110-299 4.63e-15

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: 71.42  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 110 TIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLshensvglventaaqamlqnvsreells 189
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL---------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 190 dfivpsiipgvdvipasiddaflaegwkglceehlpgknihavlkeniidklqhdYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:cd02042   48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                        170       180       190
                 ....*....|....*....|....*....|
gi 500706951 270 MLTPLPPATVDFHSSLKFVASLPALIDSIE 299
Cdd:cd02042   73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 90-288 1.12e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 68.93  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  90 IDLYNHRKVPKYRDrfdkafTIFVCNLKGGGSKTVSTASLSHafrahpQLLFEDLRILAIDFDPQASLTMFLSHENSVGL 169
Cdd:PRK13869 109 IDFVPHRRGSEHLQ------VIAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDV 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 170 VENTAAQAMLQNVSREELLSDFIVPSIIPGVDVIPASIDDAFLAEGWKGLCEEHLPGKNIHAVLKENIIDKLQHDYDFIF 249
Cdd:PRK13869 177 GANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVV 256

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500706951 250 LDSGPHLDAFLKNCIGAADLMLTPLPPATVDFHSSLKFV 288
Cdd:PRK13869 257 IDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFL 295
ParA_partition NF041546
ParA family partition ATPase;
110-280 2.86e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.71  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDPQASLTMFlshensvglventaAQAmlqnvsREElls 189
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED--- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 190 dfivpsiipgvdvipasiDDAFLAEGwkglceehLPGKNIHavlKEniIDKLQHDYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:NF041546  52 ------------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADL 100

                        170
                 ....*....|.
gi 500706951 270 MLTPLPPATVD 280
Cdd:NF041546 101 VLIPVQPSPYD 111
 
Name Accession Description Interval E-value
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 14-105 1.15e-47

ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.


Pssm-ID: 436616  Cd Length: 92  Bit Score: 157.58  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEAGGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 500706951   94 NHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 2.05e-38

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: 138.45  E-value: 2.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 188 LSDFIVPSIIPGVDVIPASIDdafLAegwkGLCEEHLPGKNIHAVLKEnIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIemdGHTCNLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDL---NPKLEILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 500706951 348 GFERCGETFDTVIsanpaTYDGSTEALKsaksAAEDFAKAVFDRIE 393
Cdd:COG1192  217 ALAEAPSAGKPVF-----EYDPKSKGAK----AYRALAEELLERLE 253
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 111-359 8.20e-20

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: 87.40  E-value: 8.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  111 IFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLsd 190
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  191 FIVPSIIPGVDVIPASIDdafLAEGWKGLCEEHLPGKnIHAVLKEniidkLQHDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNID---LEKFEKELLGPRKEER-LREALEA-----LKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  271 LTPLPPATVDfhsslkfVASLPALIDSIEMDGHTCNLIG--NVGFmskILNK---SDHKICHSQA--KEVFGADMLDmVL 343
Cdd:pfam01656 144 IIPLEPEVIL-------VEDAKRLGGVIAALVGGYALLGlkIIGV---VLNKvdgDNHGKLLKEAleELLRGLPVLG-VI 212

                         250
                  ....*....|....*.
gi 500706951  344 PRLDGFERCGETFDTV 359
Cdd:pfam01656 213 PRDEAVAEAPARGLPV 228
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 110-276 1.46e-17

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: 79.94  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  110 TIFVCNLKGGGSKTVSTASLSHAfrahpqLLFEDLRILAIDFDPQASLTMflshenSVGLVENTAAQAMLQNVSREELLS 189
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAA------LAKKGKKVLLIDLDPQGNATS------GLGIDKNNVEKTIYELLIGECNIE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  190 DFIVPSIIPGVDVIPASIDdafLAegwkGLCEEHLPGKNIHAVLKEnIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:pfam13614  71 EAIIKTVIENLDLIPSNID---LA----GAEIELIGIENRENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALTASDS 142


                  ....*..
gi 500706951  270 MLTPLPP 276
Cdd:pfam13614 143 VLIPVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 110-299 4.63e-15

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: 71.42  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 110 TIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLshensvglventaaqamlqnvsreells 189
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL---------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 190 dfivpsiipgvdvipasiddaflaegwkglceehlpgknihavlkeniidklqhdYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:cd02042   48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                        170       180       190
                 ....*....|....*....|....*....|
gi 500706951 270 MLTPLPPATVDFHSSLKFVASLPALIDSIE 299
Cdd:cd02042   73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 90-288 1.12e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 68.93  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  90 IDLYNHRKVPKYRDrfdkafTIFVCNLKGGGSKTVSTASLSHafrahpQLLFEDLRILAIDFDPQASLTMFLSHENSVGL 169
Cdd:PRK13869 109 IDFVPHRRGSEHLQ------VIAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDV 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 170 VENTAAQAMLQNVSREELLSDFIVPSIIPGVDVIPASIDDAFLAEGWKGLCEEHLPGKNIHAVLKENIIDKLQHDYDFIF 249
Cdd:PRK13869 177 GANETLYAAIRYDDTRRPLRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVV 256

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 500706951 250 LDSGPHLDAFLKNCIGAADLMLTPLPPATVDFHSSLKFV 288
Cdd:PRK13869 257 IDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFL 295
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 85-302 7.44e-12

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 66.19  E-value: 7.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  85 TIQNVIDLYNHRKVPKYRDRFDKAFTIFVCNLKGGGSKTvstaslSHAFRAHPQLLFEDLRILAID-FDPQASLTMFLSH 163
Cdd:PHA02519  83 TIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKT------SSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 164 ENSVGLVENtaaQAMLQNVSREELLSDF-IVPSIIPGVDVIPASIDdafLAEGWKGLCEEHLPGKNIHA--VLKENIIDK 240
Cdd:PHA02519 157 VPDLHIHAD---DTLLPFYLGERDNAEYaIKPTCWPGLDIIPSCLA---LHRIETDLMQYHDAGKLPHPphLMLRAAIES 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500706951 241 LQHDYDFIFLDSGPHLDAFLKNCIGAADLMLTPLPPATVDFHSSLKFVASLPALIDSIEMDG 302
Cdd:PHA02519 231 VWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGG 292
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 117-302 1.50e-11

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 65.38  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 117 KGGGSKTVSTASLSHafrahpQLLFEDLRILAID-FDPQASLTMFLSHENSVGLVENTAAQAMLqnVSREELLSDFIVPS 195
Cdd:PRK13705 115 KGGVYKTSVSVHLAQ------DLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTLLPFY--LGEKDDATYAIKPT 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 196 IIPGVDVIPASIDDAFLAEGWKGLCEEHLPGKNIHAVLKEnIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAADLMLTPLP 275
Cdd:PRK13705 187 CWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRL-AIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP 265

                        170       180
                 ....*....|....*....|....*..
gi 500706951 276 PATVDFHSSLKFVASLPALIDSIEMDG 302
Cdd:PRK13705 266 AELFDYTSALQFFDMLRDLLKNVDLKG 292
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 107-345 1.08e-08

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: 56.28  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 107 KAFTIFVCNLKGG-GSKTVSTaSLSHAFRAHPqllfeDLRILAIDFDPQA-SLTMFLSHENSVGLVEntaaqaMLQNVSR 184
Cdd:COG4963  101 RGRVIAVVGAKGGvGATTLAV-NLAWALARES-----GRRVLLVDLDLQFgDVALYLDLEPRRGLAD------ALRNPDR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 185 --EELLSDFIVPsIIPGVDVI--PASIDDAFLAEgwkglcEEHLpgknihavlkENIIDKLQHDYDFIFLDSGPHLDAFL 260
Cdd:COG4963  169 ldETLLDRALTR-HSSGLSVLaaPADLERAEEVS------PEAV----------ERLLDLLRRHFDYVVVDLPRGLNPWT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 261 KNCIGAAD---LMLTPLPPATVDFHSSLKFVASLPALIDSIEMdghtcnlignvgfmskILNKSDHK--ICHSQAKEVFG 335
Cdd:COG4963  232 LAALEAADevvLVTEPDLPSLRNAKRLLDLLRELGLPDDKVRL----------------VLNRVPKRgeISAKDIEEALG 295

                        250
                 ....*....|
gi 500706951 336 ADmLDMVLPR 345
Cdd:COG4963  296 LP-VAAVLPN 304
ParA_partition NF041546
ParA family partition ATPase;
110-280 2.86e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.71  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDPQASLTMFlshensvglventaAQAmlqnvsREElls 189
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED--- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 190 dfivpsiipgvdvipasiDDAFLAEGwkglceehLPGKNIHavlKEniIDKLQHDYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:NF041546  52 ------------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADL 100

                        170
                 ....*....|.
gi 500706951 270 MLTPLPPATVD 280
Cdd:NF041546 101 VLIPVQPSPYD 111
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 103-254 4.28e-07

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 50.96  E-value: 4.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 103 DRFDKAFTIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDP-QASLTMFLSHENSVGLVENTAAQAMLQN 181
Cdd:COG0489   87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ------SGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLED 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500706951 182 VsreellsdfIVPSIIPGVDVIPAsiddAFLAEGWKGLceehLPGKNIHAVLKEniidkLQHDYDFIFLDSGP 254
Cdd:COG0489  161 V---------IQPTEVEGLDVLPA----GPLPPNPSEL----LASKRLKQLLEE-----LRGRYDYVIIDTPP 211
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 126-268 4.62e-04

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: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 126 TASLSHAFRAHpqllfeDLRILAIDFDPQ-ASLTMFLSHENSVGLVEntaaqamlqnVSREEL-LSDFIVPSIiPGVDVI 203
Cdd:COG0455    3 AVNLAAALARL------GKRVLLVDADLGlANLDVLLGLEPKATLAD----------VLAGEAdLEDAIVQGP-GGLDVL 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500706951 204 PASIDDAFLAegwkglceehlpgkNIHAVLK-ENIIDKLQHDYDFIFLDSGPHLDAFLKNCIGAAD 268
Cdd:COG0455   66 PGGSGPAELA--------------ELDPEERlIRVLEELERFYDVVLVDTGAGISDSVLLFLAAAD 117
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 111-281 1.06e-03

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: 40.52  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  111 IFVCNLKGGGSKtvSTASLsHAFRAhpqLLFEDLRILAIDFDP-QASLTMFlshensvglVENTAAQAmlqnvSREELls 189
Cdd:pfam09140   3 IVVGNEKGGSGK--STTAV-HVAVA---LLYKGARVAAIDLDLrQRTFHRY---------FENRSATA-----DRTGL-- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951  190 DFIVPSIIPGVDVIPASIDDaflaegwkglceehlpGKNIHAVLKENIIDKLQHDYDFIFLDS-GPHlDAFLKNCIGAAD 268
Cdd:pfam09140  61 SLPTPEHLNLPDNDVAEVPD----------------GENIDDARLEEAFADLEARCDFIVIDTpGSD-SPLSRLAHSRAD 123

                         170
                  ....*....|...
gi 500706951  269 LMLTPLPPATVDF 281
Cdd:pfam09140 124 TLVTPLNDSFVDF 136
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 113-344 1.44e-03

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: 39.95  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 113 VCNLKGG-GSKTVStASLSHAFRAHPqllfeDLRILAIDFD-PQASLTMFLSHENSVGLVEntaaqaMLQNVSR--EELL 188
Cdd:cd03111    5 VVGAKGGvGASTLA-VNLAQELAQRA-----KDKVLLIDLDlPFGDLGLYLNLRPDYDLAD------VIQNLDRldRTLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 189 SDFIVPsIIPGVDVI--PASIDDaflaegwkglceehlpGKNIHAVLKENIIDKLQHDYDFIFLDSGPHLDAFLKNCIGA 266
Cdd:cd03111   73 DSAVTR-HSSGLSLLpaPQELED----------------LEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEA 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500706951 267 ADLMLTPLPPATvdfhSSLKFVASLPALIDSIEMDGHTCNLIGNvgfmsKILNKSDhkICHSQAKEVFGADMLdMVLP 344
Cdd:cd03111  136 ADEILLVTQQDL----PSLRNARRLLDSLRELEGSSDRLRLVLN-----RYDKKSE--ISPKDIEEALGLEVF-ATLP 201
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 110-287 3.18e-03

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 38.70  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDpqasltMFLShenSVGLVENTAAQAMLQNVSREEL-L 188
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSK------LGKRVLLLDAD------LGLA---NLDILLGLAPKKTLGDVLKGRVsL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500706951 189 SDFIVpSIIPGVDVIPASIDDAFLAegwkglceehlpgkNIHAVLKENIIDKLQH---DYDFIFLDSGPHLDAFLKNCIG 265
Cdd:cd02038   67 EDIIV-EGPEGLDIIPGGSGMEELA--------------NLDPEQKAKLIEELSSlesNYDYLLIDTGAGISRNVLDFLL 131

                        170       180
                 ....*....|....*....|....*
gi 500706951 266 AAD---LMLTPLPPATVDFHSSLKF 287
Cdd:cd02038  132 AADeviVVTTPEPTSITDAYALIKV 156
 
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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