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Conserved domains on  [gi|446454293|ref|WP_000532148|]
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MULTISPECIES: division plane positioning ATPase MipZ [Enterobacteriaceae]

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;
7-216 1.50e-24

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 96.08  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   7 VASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNGLLPVpVYEEYGDVSEVIKRLKKICEVLIID 86
Cdd:NF041546   4 VLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFVVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  87 CPGHDSKEFRSALTVADILLTLVKPSS-DFEA--ETLthvtEKVRTAQQINPDLQPWVLftrINTTKPRHRKAAiDLDKL 163
Cdd:NF041546  83 GPPRAEDLARSAIKAADLVLIPVQPSPyDLWAsaDTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EVAEA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446454293 164 LRENPVWIqpLRTRISDLDIFEAACNEGAGVHDVRRASSlstAKAQIELLAQE 216
Cdd:NF041546 155 LAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
7-216 1.50e-24

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 96.08  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   7 VASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNGLLPVpVYEEYGDVSEVIKRLKKICEVLIID 86
Cdd:NF041546   4 VLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFVVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  87 CPGHDSKEFRSALTVADILLTLVKPSS-DFEA--ETLthvtEKVRTAQQINPDLQPWVLftrINTTKPRHRKAAiDLDKL 163
Cdd:NF041546  83 GPPRAEDLARSAIKAADLVLIPVQPSPyDLWAsaDTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EVAEA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446454293 164 LRENPVWIqpLRTRISDLDIFEAACNEGAGVHDVRRASSlstAKAQIELLAQE 216
Cdd:NF041546 155 LAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 5-217 1.87e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 87.98  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNGLLpVPVYEEYGDVSEVIKRLKKICEVLI 84
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL-IPVVRMGKSIRADLPKVASGYDYVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  85 IDCPGHDSKEFRSALTVADILLTLVKPSSdFEAETLTHVTEKVRTAQQINpDLQPWVLFTRINTTKPRHRKAaiDLDKLL 164
Cdd:PHA02518  82 VDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQEVT-DGLPKFAFIISRAIKNTQLYR--EARKAL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446454293 165 REnpVWIQPLRTRISDLDIFEAACNEGAGVHDVRRAsslSTAKAQIELLAQEL 217
Cdd:PHA02518 158 AG--YGLPILRNGTTQRVAYADAAEAGGSVLELPED---DKAAEEIIQLVKEL 205
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-157 1.74e-18

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: 77.97  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWnekrkqngllpvpvyeeygdvsevikrlkkICEVLI 84
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------------------------LYDYIL 52

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446454293  85 IDCPGHDSKEFRSALTVADILLTLVKPsSDFEAETLTHVTEKVRTAQ-QINPDLQPW-VLFTRINTTKPRHRKAA 157
Cdd:cd02042   53 IDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKkQLNPPLLILgILLTRVDPRTKLAREVL 126
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 7-217 1.74e-14

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: 69.89  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   7 VASDKGGVGKSTTATNLASYLVN-NSRTVII--------------LKTDKNNDILSW--NEKRKQNGLLP--------VP 61
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARrGKRVLLIdldpqgnltsglglDPDDLDPTLYDLllDDAPLEDAIVPteipgldlIP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  62 -------VYEEYGDVSEVIKRLKKICE-------VLIIDCPGHDSKEFRSALTVADILLTLVKPsSDFEAETLTHVTEKV 127
Cdd:COG1192   86 anidlagAEIELVSRPGRELRLKRALApladdydYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGLAQLLETI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293 128 RTAQ-QINPDLQPW-VLFTRINTTKPRHRKAAIDLDKLLREnPVwiqpLRTRISDLDIFEAACNEGAGVHDVRRASSlst 205
Cdd:COG1192  165 EEVReDLNPKLEILgILLTMVDPRTRLSREVLEELREEFGD-KV----LDTVIPRSVALAEAPSAGKPVFEYDPKSK--- 236

                        250
                 ....*....|..
gi 446454293 206 AKAQIELLAQEL 217
Cdd:COG1192  237 GAKAYRALAEEL 248
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-166 6.03e-12

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: 63.24  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    3 RALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKN--------NDILSWNEKRK--------------QNGLLPV 60
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRqrtfhryfENRSATADRTGlslptpehlnlpdnDVAEVPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   61 PVYEEYGDVSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKPS-SDF------EAETL-----THVTEKVR 128
Cdd:pfam09140  81 GENIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSfVDFdllgqvDPETFkvkrpSFYAEMVW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446454293  129 TAQQINP--DLQP--W-VLFTRINTTKPRHRKaaiDLDKLLRE 166
Cdd:pfam09140 161 EARKKRAkaDRAPmdWiVLRNRLGTLEARNKR---RVERALAE 200
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-111 7.85e-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: 48.49  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    2 GRALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD---KNNDILSWNE------------------------KRKQ 54
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglRNLDLLLGLEnrivytlvdvvegecrlqqalikdKRLK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446454293   55 N-GLLPVP-------VYEEygDVSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKP 111
Cdd:TIGR01968  81 NlYLLPASqtrdkdaVTPE--QMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTP 143
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
7-216 1.50e-24

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 96.08  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   7 VASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNGLLPVpVYEEYGDVSEVIKRLKKICEVLIID 86
Cdd:NF041546   4 VLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPV-VGLARPTLHRELPSLARDYDFVVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  87 CPGHDSKEFRSALTVADILLTLVKPSS-DFEA--ETLthvtEKVRTAQQINPDLQPWVLftrINTTKPRHRKAAiDLDKL 163
Cdd:NF041546  83 GPPRAEDLARSAIKAADLVLIPVQPSPyDLWAsaDTV----DLIKEAREYTPGLKAAFV---LNRAIARTALGR-EVAEA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446454293 164 LRENPVWIqpLRTRISDLDIFEAACNEGAGVHDVRRASSlstAKAQIELLAQE 216
Cdd:NF041546 155 LAEYGLPV--LKTRIGQRVAFAESAAEGLTVFEAEPDGK---AAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 5-217 1.87e-21

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 87.98  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNGLLpVPVYEEYGDVSEVIKRLKKICEVLI 84
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL-IPVVRMGKSIRADLPKVASGYDYVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  85 IDCPGHDSKEFRSALTVADILLTLVKPSSdFEAETLTHVTEKVRTAQQINpDLQPWVLFTRINTTKPRHRKAaiDLDKLL 164
Cdd:PHA02518  82 VDGAPQDSELARAALRIADMVLIPVQPSP-FDIWAAPDLVELIKARQEVT-DGLPKFAFIISRAIKNTQLYR--EARKAL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446454293 165 REnpVWIQPLRTRISDLDIFEAACNEGAGVHDVRRAsslSTAKAQIELLAQEL 217
Cdd:PHA02518 158 AG--YGLPILRNGTTQRVAYADAAEAGGSVLELPED---DKAAEEIIQLVKEL 205
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 5-157 1.74e-18

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: 77.97  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWnekrkqngllpvpvyeeygdvsevikrlkkICEVLI 84
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSW------------------------------LYDYIL 52

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446454293  85 IDCPGHDSKEFRSALTVADILLTLVKPsSDFEAETLTHVTEKVRTAQ-QINPDLQPW-VLFTRINTTKPRHRKAA 157
Cdd:cd02042   53 IDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKkQLNPPLLILgILLTRVDPRTKLAREVL 126
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 7-217 1.74e-14

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: 69.89  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   7 VASDKGGVGKSTTATNLASYLVN-NSRTVII--------------LKTDKNNDILSW--NEKRKQNGLLP--------VP 61
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARrGKRVLLIdldpqgnltsglglDPDDLDPTLYDLllDDAPLEDAIVPteipgldlIP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  62 -------VYEEYGDVSEVIKRLKKICE-------VLIIDCPGHDSKEFRSALTVADILLTLVKPsSDFEAETLTHVTEKV 127
Cdd:COG1192   86 anidlagAEIELVSRPGRELRLKRALApladdydYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGLAQLLETI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293 128 RTAQ-QINPDLQPW-VLFTRINTTKPRHRKAAIDLDKLLREnPVwiqpLRTRISDLDIFEAACNEGAGVHDVRRASSlst 205
Cdd:COG1192  165 EEVReDLNPKLEILgILLTMVDPRTRLSREVLEELREEFGD-KV----LDTVIPRSVALAEAPSAGKPVFEYDPKSK--- 236

                        250
                 ....*....|..
gi 446454293 206 AKAQIELLAQEL 217
Cdd:COG1192  237 GAKAYRALAEEL 248
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-166 6.03e-12

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: 63.24  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    3 RALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKN--------NDILSWNEKRK--------------QNGLLPV 60
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRqrtfhryfENRSATADRTGlslptpehlnlpdnDVAEVPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   61 PVYEEYGDVSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKPS-SDF------EAETL-----THVTEKVR 128
Cdd:pfam09140  81 GENIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSfVDFdllgqvDPETFkvkrpSFYAEMVW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446454293  129 TAQQINP--DLQP--W-VLFTRINTTKPRHRKaaiDLDKLLRE 166
Cdd:pfam09140 161 EARKKRAkaDRAPmdWiVLRNRLGTLEARNKR---RVERALAE 200
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-185 1.10e-11

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: 61.98  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD--KNNDILSWNEKRKQNG-------------------------- 56
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqSNNSSVEGLEGDIAPAlqalaeglkgrvnldpillkeksdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   57 ---LLPVPVYEEYGD-----------VSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKPS----SDfeAE 118
Cdd:pfam01656  81 gldLIPGNIDLEKFEkellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEvilvED--AK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446454293  119 TLTHVTEKVRTAQQINPDLQPWVLFTRINTTKpRHRKAAIDLDKLLRENPVW-IQPLRTRISDLDIFE 185
Cdd:pfam01656 159 RLGGVIAALVGGYALLGLKIIGVVLNKVDGDN-HGKLLKEALEELLRGLPVLgVIPRDEAVAEAPARG 225
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 5-88 3.02e-08

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: 52.12  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD------------KNNDILSwnekrKQNGLLPVPVYE-------- 64
Cdd:cd02037    3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADiygpsiprllgvEGKPLHQ-----SEEGIVPVEVGGikvmsigf 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446454293  65 --EYGD--------VSEVIKRLKKICE-----VLIIDCP 88
Cdd:cd02037   78 llPEDDaviwrgpmKSGAIKQFLKDVDwgeldYLIIDLP 116
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-111 7.85e-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: 48.49  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    2 GRALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD---KNNDILSWNE------------------------KRKQ 54
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADiglRNLDLLLGLEnrivytlvdvvegecrlqqalikdKRLK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446454293   55 N-GLLPVP-------VYEEygDVSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKP 111
Cdd:TIGR01968  81 NlYLLPASqtrdkdaVTPE--QMKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVVTTP 143
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-111 9.54e-07

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: 9.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   3 RALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD---KNNDILSWNE------------------------KRKQN 55
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiglRNLDLILGLEnrivytlvdvlegecrleqalikdKRWEN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446454293  56 -GLLPVPVYEEYGDVS-----EVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKP 111
Cdd:cd02036   81 lYLLPASQTRDKDALTpekleELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIVTNP 142
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 5-40 1.11e-06

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: 47.83  E-value: 1.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446454293    5 LLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD 40
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-41 2.07e-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: 42.42  E-value: 2.07e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446454293   3 RALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDK 41
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-37 1.23e-04

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


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 42.10  E-value: 1.23e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446454293   3 RALLVASDKGGVGKSTTATNLASYLVNNSRTVIIL 37
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLI 127
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-27 1.65e-04

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 41.58  E-value: 1.65e-04
                         10        20
                 ....*....|....*....|....*..
gi 446454293   1 MGRALLVASDKGGVGKSTTATNLASYL 27
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTAL 27
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 6-43 3.32e-04

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 39.63  E-value: 3.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446454293   6 LVASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNN 43
Cdd:cd05386    4 FVLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDPVN 41
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
7-40 4.24e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 40.41  E-value: 4.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446454293   7 VASDKGGVGKSTTATNLASYLVNNSRTVIILKTD 40
Cdd:PRK11670 112 VSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 8-56 6.89e-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: 39.48  E-value: 6.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446454293    8 ASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNG 56
Cdd:pfam07015   7 CSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWRENALRKG 55
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-138 8.31e-04

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: 38.72  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293    2 GRALLVASDKGGVGKSTTATNLASYLVNNSRTVII------------LKTDKNN-------------DILSWNEKRKQNG 56
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLidldpqgnatsgLGIDKNNvektiyelligecNIEEAIIKTVIEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   57 L--LP------------VPVYEEYGDVSEVIKRLKKICEVLIIDCPGHDSKEFRSALTVADILLTLVKPS--SDFEAETL 120
Cdd:pfam13614  81 LdlIPsnidlagaeielIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEyyALEGLSQL 160

                         170
                  ....*....|....*...
gi 446454293  121 THVTEKVRtaQQINPDLQ 138
Cdd:pfam13614 161 LNTIKLVK--KRLNPSLE 176
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 7-46 2.19e-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: 2.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446454293   7 VASDKGGVGKSTTATNLASYLVNNSRTVIILKTD---KNNDIL 46
Cdd:cd02038    5 VTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglANLDIL 47
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-36 2.77e-03

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: 38.17  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446454293   2 GRALLVASDKGGVGKSTTATNLASYLVNNS--RTVII 36
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAWALARESgrRVLLV 138
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 13-90 4.39e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 36.75  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293   13 GVGKSTTATNLASYLVNNSRTVIILKTDKNN----DILSWNEKRkqnglLPVPVYEEYGDVSEV------IKRLK-KICE 81
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLVAADTFRaaaiEQLKQLAEK-----LGVPVFGSKTGADPAavafdaVEKAKaENYD 84


                  ....*....
gi 446454293   82 VLIIDCPGH 90
Cdd:pfam00448  85 VVLVDTAGR 93
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
8-56 4.59e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 37.13  E-value: 4.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446454293   8 ASDKGGVGKSTTATNLASYLVNNSRTVIILKTDKNNDILSWNEKRKQNG 56
Cdd:PRK13849   7 CSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKENALRSN 55
PRK10818 PRK10818
septum site-determining protein MinD;
1-52 5.14e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 37.23  E-value: 5.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446454293   1 MGRALLVASDKGGVGKSTTATNLASYLVNNSRTVIILKTD---KNNDILSWNEKR 52
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiglRNLDLIMGCERR 55
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 11-42 6.40e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 36.68  E-value: 6.40e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446454293  11 KGGVGKSTTATNLASYLVNNSRTVIILKTDKN 42
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPN 39
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 11-44 6.52e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 36.67  E-value: 6.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446454293  11 KGGVGKSTTATNLASYLVNNSRTVIILKTDKNND 44
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKAD 42
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 15-123 7.47e-03

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 36.12  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446454293  15 GKSTTATNLASYLVNNSR--TVIILKTDKNNDilswnEKRKQNGLLPVPVYEEYGDvsevikrlkkiCEVLIIDCPGHD- 91
Cdd:cd00881   11 GKTTLTGSLLYQTGAIDRrgTRKETFLDTLKE-----ERERGITIKTGVVEFEWPK-----------RRINFIDTPGHEd 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446454293  92 -SKEFRSALTVADILLTLVKPSSDFEAETLTHV 123
Cdd:cd00881   75 fSKETVRGLAQADGALLVVDANEGVEPQTREHL 107
 
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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