NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446349821|ref|WP_000427676|]
View 

MULTISPECIES: AAA family ATPase [Enterobacteriaceae]

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
HTH_54 pfam18607
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ...
 14-105 2.69e-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: 156.42  E-value: 2.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEASGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 446349821   94 FHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 4.79e-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: 137.68  E-value: 4.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 188 LSDFIVSSIIPGVDVIPASIDdafLAegwkGLCEEHLPGQNIHAVLKEnIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIEQDGHtcnLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLE---ILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446349821 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 2.69e-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: 156.42  E-value: 2.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEASGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 446349821   94 FHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 4.79e-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: 137.68  E-value: 4.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 188 LSDFIVSSIIPGVDVIPASIDdafLAegwkGLCEEHLPGQNIHAVLKEnIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIEQDGHtcnLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLE---ILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446349821 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 5.97e-18

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: 82.01  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  111 IFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLsd 190
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  191 FIVSSIIPGVDVIPASIDdafLAEGWKGLCEEhLPGQNIHAVLKEniidkLRYDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNID---LEKFEKELLGP-RKEERLREALEA-----LKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  271 LTPLPPATVDfhsslkfVASLPALIDSIEQDGHTCNLIG--NVGFmskILNK---SDHKICHSQA--KEVFGADMLDmVL 343
Cdd:pfam01656 144 IIPLEPEVIL-------VEDAKRLGGVIAALVGGYALLGlkIIGV---VLNKvdgDNHGKLLKEAleELLRGLPVLG-VI 212

                         250
                  ....*....|....*.
gi 446349821  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 3.96e-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: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 110 TIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLshensvglventaaqamlqnvsreells 189
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL---------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 dfivssiipgvdvipasiddaflaegwkglceehlpgqnihavlkeniidklrydYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:cd02042   48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                        170       180       190
                 ....*....|....*....|....*....|
gi 446349821 270 MLTPLPPATVDFHSSLKFVASLPALIDSIE 299
Cdd:cd02042   73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 111-392 4.99e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.01  E-value: 4.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 111 IFVCNLKGGGSKTVSTASLSHafrahpQLLFEDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLSD 190
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 191 FIVSSIIPGVDVIPASIDDAFLAEGWKGLCEEHLPGQNIHAVLKENIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:PRK13869 198 VIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 271 LTPLPPATVDFHSSLKFVASLPALIDSIEQDGhtcnliGNV--GFMSKILNK-------------------SDHKICHSQ 329
Cdd:PRK13869 278 VITVHPQMLDIASMSQFLLMTRDLLGVVKEAG------GNLqyDFIRYLLTRyepqdapqtkvaallrnmfEDHVLTNPM 351

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446349821 330 AKEvfgADMLDMVLPRLDGFERCGETFdtvisaNPATYDGSTEALKSAKSAAEDFAKAVFDRI 392
Cdd:PRK13869 352 VKS---AAVSDAGLTKQTLYEIGRENL------TRSTYDRAMESLDAVNSEIEALIKMAWGRA 405
ParA_partition NF041546
ParA family partition ATPase;
110-280 2.34e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.71  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDPQASLTMFlshensvglventaAQAmlqnvsREElls 189
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED--- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 dfivssiipgvdvipasiDDAFLAEGwkglceehLPGQNIHavlKEniIDKLRYDYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:NF041546  52 ------------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADL 100

                        170
                 ....*....|.
gi 446349821 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 2.69e-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: 156.42  E-value: 2.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821   14 AGKLLTSLSESIRQQKEELKLTEFYQEYSKAALYKLPKLSKGSVEYAVAEMEASGYIFKKKPSGNTMKYAMTIQNVIDLY 93
Cdd:pfam18607   1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80

                          90
                  ....*....|..
gi 446349821   94 FHRKVPKYRDRF 105
Cdd:pfam18607  81 KHRGIPKYRDRY 92
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 108-393 4.79e-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: 137.68  E-value: 4.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 108 AFTIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVglVENTAAQAMLQNVSreel 187
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 188 LSDFIVSSIIPGVDVIPASIDdafLAegwkGLCEEHLPGQNIHAVLKEnIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:COG1192   69 LEDAIVPTEIPGLDLIPANID---LA----GAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 268 DLMLTPLPPATVDFHSSLKFVASLPALIDSIEQDGHtcnLIGNVGFMSKILNKSDHKIChSQAKEVFGADMLDMVLPRLD 347
Cdd:COG1192  141 DSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLE---ILGILLTMVDPRTRLSREVL-EELREEFGDKVLDTVIPRSV 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446349821 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 5.97e-18

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: 82.01  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  111 IFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLsd 190
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  191 FIVSSIIPGVDVIPASIDdafLAEGWKGLCEEhLPGQNIHAVLKEniidkLRYDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:pfam01656  73 LKEKSDEGGLDLIPGNID---LEKFEKELLGP-RKEERLREALEA-----LKEDYDYVIIDGAPGLGELLRNALIAADYV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  271 LTPLPPATVDfhsslkfVASLPALIDSIEQDGHTCNLIG--NVGFmskILNK---SDHKICHSQA--KEVFGADMLDmVL 343
Cdd:pfam01656 144 IIPLEPEVIL-------VEDAKRLGGVIAALVGGYALLGlkIIGV---VLNKvdgDNHGKLLKEAleELLRGLPVLG-VI 212

                         250
                  ....*....|....*.
gi 446349821  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 1.28e-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: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  110 TIFVCNLKGGGSKTVSTASLSHAfrahpqLLFEDLRILAIDFDPQASLTMflshenSVGLVENTAAQAMLQNVSREELLS 189
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAA------LAKKGKKVLLIDLDPQGNATS------GLGIDKNNVEKTIYELLIGECNIE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  190 DFIVSSIIPGVDVIPASID----DAFLAEGWKGlceehlpgqniHAVLKEnIIDKLRYDYDFIFLDSGPHLDAFLKNCIG 265
Cdd:pfam13614  71 EAIIKTVIENLDLIPSNIDlagaEIELIGIENR-----------ENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALT 138

                         170
                  ....*....|.
gi 446349821  266 AADLMLTPLPP 276
Cdd:pfam13614 139 ASDSVLIPVQC 149
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 110-299 3.96e-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: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 110 TIFVCNLKGGGSKTVSTASLSHAFRAHpqllfeDLRILAIDFDPQASLTMFLshensvglventaaqamlqnvsreells 189
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL---------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 dfivssiipgvdvipasiddaflaegwkglceehlpgqnihavlkeniidklrydYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:cd02042   48 -------------------------------------------------------YDYILIDTPPSLGLLTRNALAAADL 72

                        170       180       190
                 ....*....|....*....|....*....|
gi 446349821 270 MLTPLPPATVDFHSSLKFVASLPALIDSIE 299
Cdd:cd02042   73 VLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 111-392 4.99e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.01  E-value: 4.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 111 IFVCNLKGGGSKTVSTASLSHafrahpQLLFEDLRILAIDFDPQASLTMFLSHENSVGLVENTAAQAMLQNVSREELLSD 190
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 191 FIVSSIIPGVDVIPASIDDAFLAEGWKGLCEEHLPGQNIHAVLKENIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAADLM 270
Cdd:PRK13869 198 VIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLFFTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 271 LTPLPPATVDFHSSLKFVASLPALIDSIEQDGhtcnliGNV--GFMSKILNK-------------------SDHKICHSQ 329
Cdd:PRK13869 278 VITVHPQMLDIASMSQFLLMTRDLLGVVKEAG------GNLqyDFIRYLLTRyepqdapqtkvaallrnmfEDHVLTNPM 351

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446349821 330 AKEvfgADMLDMVLPRLDGFERCGETFdtvisaNPATYDGSTEALKSAKSAAEDFAKAVFDRI 392
Cdd:PRK13869 352 VKS---AAVSDAGLTKQTLYEIGRENL------TRSTYDRAMESLDAVNSEIEALIKMAWGRA 405
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 117-302 5.79e-09

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 57.30  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 117 KGGGSKTVSTASLSHafrahpQLLFEDLRILAID-FDPQASLTMFLSHENSVGLVENTAAQAMLqnVSREELLSDFIVSS 195
Cdd:PRK13705 115 KGGVYKTSVSVHLAQ------DLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTLLPFY--LGEKDDATYAIKPT 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 196 IIPGVDVIPASIDDAFLAEGWKGLCEE-HLPGQNiHAVLKEnIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAADLMLTPL 274
Cdd:PRK13705 187 CWPGLDIIPSCLALHRIETELMGKFDEgKLPTDP-HLMLRL-AIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPT 264

                        170       180
                 ....*....|....*....|....*...
gi 446349821 275 PPATVDFHSSLKFVASLPALIDSIEQDG 302
Cdd:PRK13705 265 PAELFDYTSALQFFDMLRDLLKNVDLKG 292
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 107-345 2.25e-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: 55.51  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 107 KAFTIFVCNLKGG-GSKTVSTaSLSHAFRAHPqllfeDLRILAIDFDPQA-SLTMFLSHENSVGLVEntaaqaMLQNVSR 184
Cdd:COG4963  101 RGRVIAVVGAKGGvGATTLAV-NLAWALARES-----GRRVLLVDLDLQFgDVALYLDLEPRRGLAD------ALRNPDR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 185 --EELLSDFiVSSIIPGVDVI--PASIDDAFLAEgwkglcEEHLpgqnihavlkENIIDKLRYDYDFIFLDSGPHLDAFL 260
Cdd:COG4963  169 ldETLLDRA-LTRHSSGLSVLaaPADLERAEEVS------PEAV----------ERLLDLLRRHFDYVVVDLPRGLNPWT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 261 KNCIGAAD---LMLTPLPPATVDFHSSLKFVASLPALIDSIEqdghtcnLignvgfmskILNKSDHK--ICHSQAKEVFG 335
Cdd:COG4963  232 LAALEAADevvLVTEPDLPSLRNAKRLLDLLRELGLPDDKVR-------L---------VLNRVPKRgeISAKDIEEALG 295

                        250
                 ....*....|
gi 446349821 336 ADmLDMVLPR 345
Cdd:COG4963  296 LP-VAAVLPN 304
ParA_partition NF041546
ParA family partition ATPase;
110-280 2.34e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.71  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDPQASLTMFlshensvglventaAQAmlqnvsREElls 189
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED--- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 dfivssiipgvdvipasiDDAFLAEGwkglceehLPGQNIHavlKEniIDKLRYDYDFIFLDSGPHLDAFLKNCIGAADL 269
Cdd:NF041546  52 ------------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADL 100

                        170
                 ....*....|.
gi 446349821 270 MLTPLPPATVD 280
Cdd:NF041546 101 VLIPVQPSPYD 111
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 85-302 3.13e-08

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 55.02  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821  85 TIQNVIDLYFHRKVPKYRDRFDKAFTIFVCNLKGGGSKTvstaslSHAFRAHPQLLFEDLRILAID-FDPQASLTMFLSH 163
Cdd:PHA02519  83 TIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKT------SSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 164 ENSVGLVENtaaQAMLQNVSREELLSDF-IVSSIIPGVDVIPASIDdafLAEGWKGLCEEHLPGQNIHA--VLKENIIDK 240
Cdd:PHA02519 157 VPDLHIHAD---DTLLPFYLGERDNAEYaIKPTCWPGLDIIPSCLA---LHRIETDLMQYHDAGKLPHPphLMLRAAIES 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446349821 241 LRYDYDFIFLDSGPHLDAFLKNCIGAADLMLTPLPPATVDFHSSLKFVASLPALIDSIEQDG 302
Cdd:PHA02519 231 VWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGG 292
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 113-344 1.03e-06

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: 49.58  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 113 VCNLKGG-GSKTVStASLSHAFRAHPqllfeDLRILAIDFD-PQASLTMFLSHENSVGLVEntaaqaMLQNVSR-EELLS 189
Cdd:cd03111    5 VVGAKGGvGASTLA-VNLAQELAQRA-----KDKVLLIDLDlPFGDLGLYLNLRPDYDLAD------VIQNLDRlDRTLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 DFIVSSIIPGVDVI--PASIDDaflaegwkglceehlpGQNIHAVLKENIIDKLRYDYDFIFLDSGPHLDAFLKNCIGAA 267
Cdd:cd03111   73 DSAVTRHSSGLSLLpaPQELED----------------LEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAA 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446349821 268 DLMLTPLPPATvdfhSSLKFVASlpaLIDSIEQDGhtcnliGNVGFMSKILNKSDHK--ICHSQAKEVFGADMLdMVLP 344
Cdd:cd03111  137 DEILLVTQQDL----PSLRNARR---LLDSLRELE------GSSDRLRLVLNRYDKKseISPKDIEEALGLEVF-ATLP 201
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 126-268 2.47e-03

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: 39.10  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 126 TASLSHAFRAHpqllfeDLRILAIDFDPQ-ASLTMFLSHENSVGLVEntaaqamlqnVSREEL-LSDFIVSSIiPGVDVI 203
Cdd:COG0455    3 AVNLAAALARL------GKRVLLVDADLGlANLDVLLGLEPKATLAD----------VLAGEAdLEDAIVQGP-GGLDVL 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446349821 204 PASIDDAFLAEgwkglceeHLPGQNIHAVLKEniidkLRYDYDFIFLDSGPHLDAFLKNCIGAAD 268
Cdd:COG0455   66 PGGSGPAELAE--------LDPEERLIRVLEE-----LERFYDVVLVDTGAGISDSVLLFLAAAD 117
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 110-287 5.64e-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: 37.93  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 110 TIFVCNLKGGGSKTVSTASLSHAFRAhpqllfEDLRILAIDFDpqasltmflshensVGLventAAQAMLQNVSREELLS 189
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSK------LGKRVLLLDAD--------------LGL----ANLDILLGLAPKKTLG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446349821 190 DFI-----VSSII----PGVDVIPASIDDAFLAegwkglceehlpgqNIHAVLKENIID---KLRYDYDFIFLDSGPHLD 257
Cdd:cd02038   58 DVLkgrvsLEDIIvegpEGLDIIPGGSGMEELA--------------NLDPEQKAKLIEelsSLESNYDYLLIDTGAGIS 123

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446349821 258 AFLKNCIGAAD---LMLTPLPPATVDFHSSLKF 287
Cdd:cd02038  124 RNVLDFLLAADeviVVTTPEPTSITDAYALIKV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH