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Conserved domains on  [gi|1561506012|gb|QAT79378|]
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ParA [Cloning vector pDW18]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-264 3.25e-46

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: 155.40  E-value: 3.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   3 AKTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALArtANLDHIDKTIVDGL-NDGDLSTCI-TSI 80
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLlDDAPLEDAIvPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  81 LPNLDLIACNTQFTSFDKYviegFTDEKDRVSVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEES 160
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIE----LVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012 161 LSGVRKYVGYQNFMVEAYGINLQVIDILPCMLTADDKLDYEILDEARKEFGDAVSATVINFQKRLKRYSRDGISLKRHKN 240
Cdd:COG1192   154 LEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDP 233

                         250       260
                  ....*....|....*....|....
gi 1561506012 241 GNidqwdyKAHEKFIDILHEIESR 264
Cdd:COG1192   234 KS------KGAKAYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-264 3.25e-46

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: 155.40  E-value: 3.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   3 AKTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALArtANLDHIDKTIVDGL-NDGDLSTCI-TSI 80
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLlDDAPLEDAIvPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  81 LPNLDLIACNTQFTSFDKYviegFTDEKDRVSVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEES 160
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIE----LVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012 161 LSGVRKYVGYQNFMVEAYGINLQVIDILPCMLTADDKLDYEILDEARKEFGDAVSATVINFQKRLKRYSRDGISLKRHKN 240
Cdd:COG1192   154 LEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDP 233

                         250       260
                  ....*....|....*....|....
gi 1561506012 241 GNidqwdyKAHEKFIDILHEIESR 264
Cdd:COG1192   234 KS------KGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 3-164 1.94e-29

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: 109.60  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   3 AKTFTVGNFKGGVGKTKITTMLAYDNAMINKKkTLVIDIDPQANASDALArtANLDHIDKTIVDGL-NDGDLSTCI-TSI 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKK-VLLIDLDPQGNATSGLG--IDKNNVEKTIYELLiGECNIEEAIiKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  81 LPNLDLIACNTQFTSFDKYVIEgftdEKDRVSVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEES 160
Cdd:pfam13614  78 IENLDLIPSNIDLAGAEIELIG----IENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153


                  ....
gi 1561506012 161 LSGV 164
Cdd:pfam13614 154 LEGL 157
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-207 1.78e-19

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: 81.82  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYDnAMINKKKTLVIDIDPQANASDAlartanldhidktivdglndgdlstcitsilpn 83
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAA-LALRGKRVLLIDLDPQGSLTSW--------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  84 ldliacntqftsfdkyviegftdekdrvsvlaklikplkpLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEESLSG 163
Cdd:cd02042    47 ----------------------------------------LYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1561506012 164 VRKYVGYQNFMVEAYGINLQVIDILPCMLTADDKLDYEILDEAR 207
Cdd:cd02042    87 LAKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
7-56 2.48e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 47.16  E-value: 2.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1561506012   7 TVGNFKGGVGKTKITTMLAyDNAMINKKKTLVIDIDPQANASD-ALARTAN 56
Cdd:NF041546    3 AVLNQKGGVGKTTLATHLA-AALARRGYRVLLVDADPQGSALDwAAAREDE 52
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 4-152 3.42e-06

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 47.75  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALARTANLD-HIDKTIVDGLNDGD----LSTCIT 78
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLAL-QGYRVLAVDLDPQASLSALLGVLPETDvGANETLYAAIRYDDtrrpLRDVIR 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561506012  79 SI-LPNLDLIACNTQFTSFDKYVIEGFTDEKDRVSV----LAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSII 152
Cdd:PRK13869  201 PTyFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-264 3.25e-46

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: 155.40  E-value: 3.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   3 AKTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALArtANLDHIDKTIVDGL-NDGDLSTCI-TSI 80
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLlDDAPLEDAIvPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  81 LPNLDLIACNTQFTSFDKYviegFTDEKDRVSVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEES 160
Cdd:COG1192    78 IPGLDLIPANIDLAGAEIE----LVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012 161 LSGVRKYVGYQNFMVEAYGINLQVIDILPCMLTADDKLDYEILDEARKEFGDAVSATVINFQKRLKRYSRDGISLKRHKN 240
Cdd:COG1192   154 LEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDP 233

                         250       260
                  ....*....|....*....|....
gi 1561506012 241 GNidqwdyKAHEKFIDILHEIESR 264
Cdd:COG1192   234 KS------KGAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 3-164 1.94e-29

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: 109.60  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   3 AKTFTVGNFKGGVGKTKITTMLAYDNAMINKKkTLVIDIDPQANASDALArtANLDHIDKTIVDGL-NDGDLSTCI-TSI 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKK-VLLIDLDPQGNATSGLG--IDKNNVEKTIYELLiGECNIEEAIiKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  81 LPNLDLIACNTQFTSFDKYVIEgftdEKDRVSVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEES 160
Cdd:pfam13614  78 IENLDLIPSNIDLAGAEIELIG----IENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153


                  ....
gi 1561506012 161 LSGV 164
Cdd:pfam13614 154 LEGL 157
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 4-207 1.78e-19

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: 81.82  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYDnAMINKKKTLVIDIDPQANASDAlartanldhidktivdglndgdlstcitsilpn 83
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAA-LALRGKRVLLIDLDPQGSLTSW--------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  84 ldliacntqftsfdkyviegftdekdrvsvlaklikplkpLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEESLSG 163
Cdd:cd02042    47 ----------------------------------------LYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1561506012 164 VRKYVGYQNFMVEAYGINLQVIDILPCMLTADDKLDYEILDEAR 207
Cdd:cd02042    87 LAKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 6-189 5.99e-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: 80.47  E-value: 5.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   6 FTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALARTANLDHIDKTIVDGL-NDGDLSTCITSILP-- 82
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALAR-RGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLkGRVNLDPILLKEKSde 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  83 -NLDLIACNTQFTSFDKYVIEGFTDEKdrvsvLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIAFQTVEESL 161
Cdd:pfam01656  80 gGLDLIPGNIDLEKFEKELLGPRKEER-----LREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILV 154

                         170       180
                  ....*....|....*....|....*...
gi 1561506012 162 SGVRKYVGyqnfMVEAYGINLQVIDILP 189
Cdd:pfam01656 155 EDAKRLGG----VIAALVGGYALLGLKI 178
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 12-220 2.78e-07

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: 50.35  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  12 KGGVGKTKITTMLAYDNAMINKKKTLVIDIDPQanASDAlarTANLDHI-DKTIVDGLNDGD------LSTCITSILPNL 84
Cdd:cd03111     9 KGGVGASTLAVNLAQELAQRAKDKVLLIDLDLP--FGDL---GLYLNLRpDYDLADVIQNLDrldrtlLDSAVTRHSSGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  85 DLIACNTQFtsfdkyviEGFtDEKDRVSVLaKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSIIafqTVEESLSGV 164
Cdd:cd03111    84 SLLPAPQEL--------EDL-EALGAEQVD-KLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILL---VTQQDLPSL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1561506012 165 RKYVGYQNFMVEAYGINLQVIDILPCMLTaddklDYEI-LDEARKEFGDAVSATVIN 220
Cdd:cd03111   151 RNARRLLDSLRELEGSSDRLRLVLNRYDK-----KSEIsPKDIEEALGLEVFATLPN 202
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-165 4.37e-07

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: 50.50  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   2 LAKTFTVGNFKGGVGKTKITTMLAYDNAMINKKKTLVIDIDPQA-NASDALartaNLDHiDKTIVDGLNDGD------LS 74
Cdd:COG4963   101 RGRVIAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFgDVALYL----DLEP-RRGLADALRNPDrldetlLD 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  75 TCITSILPNLDLIACNTQFTSfdkyvIEGFTDEkdrvsVLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDysiIAF 154
Cdd:COG4963   176 RALTRHSSGLSVLAAPADLER-----AEEVSPE-----AVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAAD---EVV 242

                         170
                  ....*....|.
gi 1561506012 155 QTVEESLSGVR 165
Cdd:COG4963   243 LVTEPDLPSLR 253
ParA_partition NF041546
ParA family partition ATPase;
7-56 2.48e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 47.16  E-value: 2.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1561506012   7 TVGNFKGGVGKTKITTMLAyDNAMINKKKTLVIDIDPQANASD-ALARTAN 56
Cdd:NF041546    3 AVLNQKGGVGKTTLATHLA-AALARRGYRVLLVDADPQGSALDwAAAREDE 52
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 12-152 2.94e-06

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 47.20  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  12 KGGVGKTKITTMLAYDNAMINKKkTLVIDIDpqanasdalARTANLD-------HIDKTIVDGLN-DGDLSTCI--TSIL 81
Cdd:cd02036     9 KGGVGKTTTTANLGVALAKLGKK-VLLIDAD---------IGLRNLDlilglenRIVYTLVDVLEgECRLEQALikDKRW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561506012  82 PNLDLIACntqftsfdkyvieGFTDEKDRVS--VLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSII 152
Cdd:cd02036    79 ENLYLLPA-------------SQTRDKDALTpeKLEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAII 138
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 4-152 3.42e-06

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 47.75  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDALARTANLD-HIDKTIVDGLNDGD----LSTCIT 78
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLAL-QGYRVLAVDLDPQASLSALLGVLPETDvGANETLYAAIRYDDtrrpLRDVIR 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561506012  79 SI-LPNLDLIACNTQFTSFDKYVIEGFTDEKDRVSV----LAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSII 152
Cdd:PRK13869  201 PTyFDGLHLVPGNLELMEFEHTTPKALSDKGTRDGLfftrVAQAFDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVI 279
PHA02518 PHA02518
ParA-like protein; Provisional
 4-50 2.61e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 44.07  E-value: 2.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDA 50
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHA-DGHKVLLVDLDPQGSSTDW 46
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 12-51 1.20e-04

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.46  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1561506012  12 KGGVGKTKITTMLAydNAMI-NKKKTLVIDIDPQANASDAL 51
Cdd:COG3640     8 KGGVGKTTLSALLA--RYLAeKGKPVLAVDADPNANLAEAL 46
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 12-66 4.59e-04

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 40.76  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1561506012  12 KGGVGKTKITTMLAYdnAMINK-KKTLVIDIDPQANASDALARTANLDHIDKTIVD 66
Cdd:cd02034     8 KGGVGKTTIAALLIR--YLAKKgGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGD 61
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 4-152 7.73e-04

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: 39.86  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012   4 KTFTVGNFKGGVGKTKITTMLAYdnAMINK-KKTLVIDIDPQAnasdalartANLD-----HIDKTIVDGLNDG-DLSTC 76
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLAL--ALSKLgKRVLLLDADLGL---------ANLDillglAPKKTLGDVLKGRvSLEDI 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561506012  77 ITSILPNLDLIACNTQftsfdkyvIEGFTDEKDrvSVLAKLIKPLKPL---YETIYIDVPPTISVYSDNAMAASDYSII 152
Cdd:cd02038    70 IVEGPEGLDIIPGGSG--------MEELANLDP--EQKAKLIEELSSLesnYDYLLIDTGAGISRNVLDFLLAADEVIV 138
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 12-68 2.26e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 38.64  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1561506012  12 KGGVGKTKITTMLAYDNAMINKKkTLVIDIDPQANASDALARTanLDHIDKT-IVDGL 68
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKR-VLLVSTDPAHSLSDAFGQK--LGGETPVkGAPNL 62
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-51 3.23e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.48  E-value: 3.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1561506012  12 KGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDAL 51
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSE-LGKKVLLISTDPAHSLSDSF 47
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
12-51 4.45e-03

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 37.88  E-value: 4.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1561506012  12 KGGVGKTKITTMLAYDNAMiNKKKTLVIDIDPQANASDAL 51
Cdd:COG0003    11 KGGVGKTTVAAATALALAE-RGKRTLLVSTDPAHSLGDVL 49
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 34-152 6.78e-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: 37.18  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561506012  34 KKTLVIDIDPQ-ANASDALartaNLDHiDKTIVDGLNDG-DLSTCITSILPNLDLIACNTQFTSFDKYviegftDEKDRv 111
Cdd:COG0455    15 KRVLLVDADLGlANLDVLL----GLEP-KATLADVLAGEaDLEDAIVQGPGGLDVLPGGSGPAELAEL------DPEER- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1561506012 112 svLAKLIKPLKPLYETIYIDVPPTISVYSDNAMAASDYSII 152
Cdd:COG0455    83 --LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVV 121
 
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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