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Conserved domains on  [gi|1604347244|gb|QBQ85106|]
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plasmid partition protein A (plasmid) [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
4-216 2.34e-21

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.61  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   4 ILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNGLLTIpVHAAYGNVSNEIKRLSKLCEVL 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  84 IVDCPGHDSQEFRSALTVSDIVVTLVKPSS-DFE--SETLtsvtEKIRTAQKANAALEPWVLftrINSAKPRHRKAAiDL 160
Cdd:NF041546   80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPyDLWasADTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244 161 DKLLRSDNIWIqpLKTRISELDVYESACNEGAGVHDVSRASSlstAKAQIELVAQE 216
Cdd:NF041546  152 AEALAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
4-216 2.34e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.61  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   4 ILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNGLLTIpVHAAYGNVSNEIKRLSKLCEVL 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  84 IVDCPGHDSQEFRSALTVSDIVVTLVKPSS-DFE--SETLtsvtEKIRTAQKANAALEPWVLftrINSAKPRHRKAAiDL 160
Cdd:NF041546   80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPyDLWasADTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244 161 DKLLRSDNIWIqpLKTRISELDVYESACNEGAGVHDVSRASSlstAKAQIELVAQE 216
Cdd:NF041546  152 AEALAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 3-216 2.03e-20

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 85.29  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNGLLtIPVHAAYGNVSNEIKRLSKLCEV 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL-IPVVRMGKSIRADLPKVASGYDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  83 LIVDCPGHDSQEFRSALTVSDIVVTLVKPSSdFESETLTSVTEKIRTAQKANAALEpwvLFTRINSA--KPRHRKAaiDL 160
Cdd:PHA02518   80 VVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQEVTDGLP---KFAFIISRaiKNTQLYR--EA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244 161 DKLLrsDNIWIQPLKTRISELDVYESACNEGAGVHDVSRAsslSTAKAQIELVAQE 216
Cdd:PHA02518  154 RKAL--AGYGLPILRNGTTQRVAYADAAEAGGSVLELPED---DKAAEEIIQLVKE 204
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-157 1.84e-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: 69.88  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWnekrtdnglltipvhaaygnvsneikrlskLCEV 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------------------------LYDY 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604347244  83 LIVDCPGHDSQEFRSALTVSDIVVTLVKPsSDFESETLTSVTEKIRTAQKA-NAALEPW-VLFTRINSAKPRHRKAA 157
Cdd:cd02042    51 ILIDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKKQlNPPLLILgILLTRVDPRTKLAREVL 126
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-217 4.99e-12

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: 63.34  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDL---LSWNEKRTDNGLLT-------------------- 59
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLtsgLGLDPDDLDPTLYDlllddapledaivpteipgl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  60 --IPVHAAYGNVSNEI-------KRLSKLCE-------VLIVDCPGHDSQEFRSALTVSDIVVTLVKPsSDFESETLTSV 123
Cdd:COG1192    82 dlIPANIDLAGAEIELvsrpgreLRLKRALApladdydYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244 124 TEKIRTAQKA-NAALEPW-VLFTRINSAKPRHRKAAIDLDKLLrSDNIwiqpLKTRISELDVYESACNEGAGVHDVSRAS 201
Cdd:COG1192   161 LETIEEVREDlNPKLEILgILLTMVDPRTRLSREVLEELREEF-GDKV----LDTVIPRSVALAEAPSAGKPVFEYDPKS 235

                         250
                  ....*....|....*.
gi 1604347244 202 SlstAKAQIELVAQEI 217
Cdd:COG1192   236 K---GAKAYRALAEEL 248
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-107 5.62e-07

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 48.87  E-value: 5.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   2 GKILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLLSWNE------------------------KRTD 54
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglRNLDLLLGLEnrivytlvdvvegecrlqqalikdKRLK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604347244  55 N-GLLTIPVHAAYGNVSNE-----IKRLSKLCEVLIVDCPGHDSQEFRSALTVSD--IVVT 107
Cdd:TIGR01968  81 NlYLLPASQTRDKDAVTPEqmkklVNELKEEFDYVIIDCPAGIESGFRNAVAPADeaIVVT 141
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-114 6.29e-07

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: 48.60  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   4 ILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNH--------DLLSWNEKRtdnGL-LTIPVHA---------A 65
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQrtfhryfeNRSATADRT---GLsLPTPEHLnlpdndvaeV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244  66 YGNVSNEIKRLSKL-------CEVLIVDCPGHDSQEFRSALTVSDivvTLVKPSSD 114
Cdd:pfam09140  79 PDGENIDDARLEEAfadlearCDFIVIDTPGSDSPLSRLAHSRAD---TLVTPLND 131
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
4-216 2.34e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.61  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   4 ILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNGLLTIpVHAAYGNVSNEIKRLSKLCEVL 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  84 IVDCPGHDSQEFRSALTVSDIVVTLVKPSS-DFE--SETLtsvtEKIRTAQKANAALEPWVLftrINSAKPRHRKAAiDL 160
Cdd:NF041546   80 VIDGPPRAEDLARSAIKAADLVLIPVQPSPyDLWasADTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244 161 DKLLRSDNIWIqpLKTRISELDVYESACNEGAGVHDVSRASSlstAKAQIELVAQE 216
Cdd:NF041546  152 AEALAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 3-216 2.03e-20

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 85.29  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNGLLtIPVHAAYGNVSNEIKRLSKLCEV 82
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL-IPVVRMGKSIRADLPKVASGYDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  83 LIVDCPGHDSQEFRSALTVSDIVVTLVKPSSdFESETLTSVTEKIRTAQKANAALEpwvLFTRINSA--KPRHRKAaiDL 160
Cdd:PHA02518   80 VVVDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQEVTDGLP---KFAFIISRaiKNTQLYR--EA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244 161 DKLLrsDNIWIQPLKTRISELDVYESACNEGAGVHDVSRAsslSTAKAQIELVAQE 216
Cdd:PHA02518  154 RKAL--AGYGLPILRNGTTQRVAYADAAEAGGSVLELPED---DKAAEEIIQLVKE 204
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-157 1.84e-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: 69.88  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWnekrtdnglltipvhaaygnvsneikrlskLCEV 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------------------------LYDY 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604347244  83 LIVDCPGHDSQEFRSALTVSDIVVTLVKPsSDFESETLTSVTEKIRTAQKA-NAALEPW-VLFTRINSAKPRHRKAA 157
Cdd:cd02042    51 ILIDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKKQlNPPLLILgILLTRVDPRTKLAREVL 126
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-217 4.99e-12

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: 63.34  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDL---LSWNEKRTDNGLLT-------------------- 59
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLtsgLGLDPDDLDPTLYDlllddapledaivpteipgl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  60 --IPVHAAYGNVSNEI-------KRLSKLCE-------VLIVDCPGHDSQEFRSALTVSDIVVTLVKPsSDFESETLTSV 123
Cdd:COG1192    82 dlIPANIDLAGAEIELvsrpgreLRLKRALApladdydYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGLAQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244 124 TEKIRTAQKA-NAALEPW-VLFTRINSAKPRHRKAAIDLDKLLrSDNIwiqpLKTRISELDVYESACNEGAGVHDVSRAS 201
Cdd:COG1192   161 LETIEEVREDlNPKLEILgILLTMVDPRTRLSREVLEELREEF-GDKV----LDTVIPRSVALAEAPSAGKPVFEYDPKS 235

                         250
                  ....*....|....*.
gi 1604347244 202 SlstAKAQIELVAQEI 217
Cdd:COG1192   236 K---GAKAYRALAEEL 248
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-46 3.99e-07

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 49.29  E-value: 3.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1604347244   1 MGKILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLL 46
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADiglRNLDLV 49
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-107 5.62e-07

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 48.87  E-value: 5.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   2 GKILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLLSWNE------------------------KRTD 54
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglRNLDLLLGLEnrivytlvdvvegecrlqqalikdKRLK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604347244  55 N-GLLTIPVHAAYGNVSNE-----IKRLSKLCEVLIVDCPGHDSQEFRSALTVSD--IVVT 107
Cdd:TIGR01968  81 NlYLLPASQTRDKDAVTPEqmkklVNELKEEFDYVIIDCPAGIESGFRNAVAPADeaIVVT 141
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-114 6.29e-07

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: 48.60  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   4 ILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNH--------DLLSWNEKRtdnGL-LTIPVHA---------A 65
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQrtfhryfeNRSATADRT---GLsLPTPEHLnlpdndvaeV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244  66 YGNVSNEIKRLSKL-------CEVLIVDCPGHDSQEFRSALTVSDivvTLVKPSSD 114
Cdd:pfam09140  79 PDGENIDDARLEEAfadlearCDFIVIDTPGSDSPLSRLAHSRAD---TLVTPLND 131
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-113 1.08e-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: 47.97  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLLSWNE------------------------KRTDN 55
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiglRNLDLILGLEnrivytlvdvlegecrleqalikdKRWEN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604347244  56 -GLLTIPVHAAYGNVSNE-----IKRLSKLCEVLIVDCPGHDSQEFRSALTVSD--IVVTLVKPSS 113
Cdd:cd02036    81 lYLLPASQTRDKDALTPEkleelVKELKDSFDFILIDSPAGIESGFINAIAPADeaIIVTNPEISS 146
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 3.99e-06

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 45.96  E-value: 3.99e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD 40
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 3-40 1.94e-05

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 43.98  E-value: 1.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD 40
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-182 2.99e-05

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: 43.49  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   5 LLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD--KNHDLLSWNEKRTDNGLLT---------------IPVHAAYG 67
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqSNNSSVEGLEGDIAPALQAlaeglkgrvnldpilLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244  68 N-------------------------VSNEIKRLSKLCEVLIVDCPGHDSQEFRSALTVSDIVVTLVKPS----SDFESe 118
Cdd:pfam01656  81 GldlipgnidlekfekellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEvilvEDAKR- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604347244 119 tLTSVTEKIRTAQKANAALEPWVLFTRINSAKpRHRKAAIDLDKLLRSDNIW-IQPLKTRISELD 182
Cdd:pfam01656 160 -LGGVIAALVGGYALLGLKIIGVVLNKVDGDN-HGKLLKEALEELLRGLPVLgVIPRDEAVAEAP 222
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-41 3.11e-05

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 41.65  E-value: 3.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDK 41
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
PRK10818 PRK10818
septum site-determining protein MinD;
1-52 7.00e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 42.62  E-value: 7.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1604347244   1 MGKILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLLSWNEKR 52
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiglRNLDLIMGCERR 55
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 8-45 7.68e-05

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: 42.72  E-value: 7.68e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1604347244   8 VSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDL 45
Cdd:pfam02374   6 FGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSL 43
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-40 8.87e-05

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: 42.17  E-value: 8.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD 40
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
11-44 1.95e-04

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 41.28  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1604347244  11 KGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHD 44
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD 41
minD CHL00175
septum-site determining protein; Validated
 1-52 3.16e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.91  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1604347244   1 MGKILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTD---KNHDLLSWNEKR 52
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiglRNLDLLLGLENR 68
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 3-56 5.41e-04

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 39.86  E-value: 5.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNG 56
Cdd:pfam07015   2 QLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWRENALRKG 55
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-44 6.69e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 39.75  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1604347244  11 KGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHD 44
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKAD 42
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
3-56 8.12e-04

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 39.44  E-value: 8.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1604347244   3 KILLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDLLSWNEKRTDNG 56
Cdd:PRK13849    2 KLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKENALRSN 55
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 6-44 1.98e-03

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 38.12  E-value: 1.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1604347244   6 LVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHD 44
Cdd:cd02117     3 IVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHD 41
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 3-45 6.56e-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: 36.72  E-value: 6.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1604347244   3 KILLVvSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHDL 45
Cdd:cd02035     1 RIIFF-GGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSL 42
PRK12377 PRK12377
putative replication protein; Provisional
 7-86 9.21e-03

putative replication protein; Provisional


Pssm-ID: 183482 [Multi-domain]  Cd Length: 248  Bit Score: 36.35  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604347244   7 VVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDknhDLLSwnekrtdnglltiPVHAAYGNVSNEIKRLSKLCEV--LI 84
Cdd:PRK12377  105 VFSGKPGTGKNHLAAAIGNRLLAKGRSVIVVTVP---DVMS-------------RLHESYDNGQSGEKFLQELCKVdlLV 168


                  ..
gi 1604347244  85 VD 86
Cdd:PRK12377  169 LD 170
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 5-44 9.36e-03

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 36.12  E-value: 9.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1604347244   5 LLVVSDKGGVGKSTYVANTGSMLVNKGKSVIILKTDKNHD 44
Cdd:cd02032     2 VIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHD 41
 
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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