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Conserved domains on  [gi|446438375|ref|WP_000516230|]
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MULTISPECIES: division plane positioning ATPase MipZ [Gammaproteobacteria]

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;
4-215 2.51e-21

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.22  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   4 IITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTNARLS--EIPYFECYTDIPamaqKLAARF 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELP----SLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  82 DYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446438375 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNNGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
4-215 2.51e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.22  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   4 IITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTNARLS--EIPYFECYTDIPamaqKLAARF 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELP----SLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  82 DYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446438375 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNNGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 3-216 3.02e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 82.21  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTNARLseIPYFECYTDIPAMAQKLAARFD 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  83 YVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQP-SPFDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446438375 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNNGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-215 5.69e-17

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: 76.82  E-value: 5.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQG---------------SIKDFIEDRKTNARL---SEIPYF 64
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  65 ECytdIPAMA-----------------------QKLAARFDYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTL 121
Cdd:COG1192   82 DL---IPANIdlagaeielvsrpgrelrlkralAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNNGMGVHEYD 198
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*..
gi 446438375 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192  233 --PKSKGAKAYRALAEE 247
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-164 9.15e-17

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: 73.34  E-value: 9.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIkdfiedrktnarlseipyfecytdipamaqkLAARFD 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  83 YVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126


                 ...
gi 446438375 162 RQL 164
Cdd:cd02042  127 EEL 129
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-194 2.19e-08

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: 52.73  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375    5 ITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGS---------------------------IKDFIEDRKT--- 54
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILLKEKSdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   55 -------NARLSEIPYFECYTD----IPAMAQKLAARFDYVFVDTPGmkSPAF--VKALSCAHILFTFIEPgSGIEINTL 121
Cdd:pfam01656  81 gldlipgNIDLEKFEKELLGPRkeerLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEP-EVILVEDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446438375  122 GRLVFDIKTAQAGVNPS--MKAWIVLNKC-STNPSDSEASELRRQLNDDPDWLPVPRqriymRTAHKKAYNNGMGV 194
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNKVdGDNHGKLLKEALEELLRGLPVLGVIPR-----DEAVAEAPARGLPV 228
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
4-215 2.51e-21

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 87.22  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   4 IITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTNARLS--EIPYFECYTDIPamaqKLAARF 81
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPvvGLARPTLHRELP----SLARDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  82 DYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPsdSEASELR 161
Cdd:NF041546  77 DFVVIDGPPRAEDLARSAIKAADLVLIPVQP-SPYDLWASADTVDLIKEARE-YTPGLKAAFVLNRAIART--ALGREVA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446438375 162 RQLNDDPdwLPVPRQRIYMRTAHKKAYNNGMGVHEYDdkRGNKARGEIELLLKE 215
Cdd:NF041546 153 EALAEYG--LPVLKTRIGQRVAFAESAAEGLTVFEAE--PDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 3-216 3.02e-19

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 82.21  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTNARLseIPYFECYTDIPAMAQKLAARFD 82
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPL--IPVVRMGKSIRADLPKVASGYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  83 YVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAgVNPSMKAWIVLNKCSTNPSDSEAsELRR 162
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQP-SPFDIWAAPDLVELIKARQE-VTDGLPKFAFIISRAIKNTQLYR-EARK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446438375 163 QLNDDPdwLPVPRQRIYMRTAHKKAYNNGMGVHEYDDKrgNKARGEIELLLKET 216
Cdd:PHA02518 156 ALAGYG--LPILRNGTTQRVAYADAAEAGGSVLELPED--DKAAEEIIQLVKEL 205
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 3-215 5.69e-17

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: 76.82  E-value: 5.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQG---------------SIKDFIEDRKTNARL---SEIPYF 64
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGnltsglgldpddldpTLYDLLLDDAPLEDAivpTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  65 ECytdIPAMA-----------------------QKLAARFDYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTL 121
Cdd:COG1192   82 DL---IPANIdlagaeielvsrpgrelrlkralAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQP-EYLSLEGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375 122 GRLVFDIKTAQAGVNPSMK-AWIVLNKC--STNPSDSEASELRRQLNDdpdwlPVPRQRIYMRTAHKKAYNNGMGVHEYD 198
Cdd:COG1192  158 AQLLETIEEVREDLNPKLEiLGILLTMVdpRTRLSREVLEELREEFGD-----KVLDTVIPRSVALAEAPSAGKPVFEYD 232

                        250
                 ....*....|....*..
gi 446438375 199 dkRGNKARGEIELLLKE 215
Cdd:COG1192  233 --PKSKGAKAYRALAEE 247
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-164 9.15e-17

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: 73.34  E-value: 9.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIkdfiedrktnarlseipyfecytdipamaqkLAARFD 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSL-------------------------------TSWLYD 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  83 YVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVFDIKTAQAGVNPS-MKAWIVLNKCSTNPsdSEASELR 161
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQP-SPFDLDGLAKLLDTLEELKKQLNPPlLILGILLTRVDPRT--KLAREVL 126


                 ...
gi 446438375 162 RQL 164
Cdd:cd02042  127 EEL 129
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-194 2.19e-08

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: 52.73  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375    5 ITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGS---------------------------IKDFIEDRKT--- 54
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssveglegdiapalqalaeglkgrvnLDPILLKEKSdeg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   55 -------NARLSEIPYFECYTD----IPAMAQKLAARFDYVFVDTPGmkSPAF--VKALSCAHILFTFIEPgSGIEINTL 121
Cdd:pfam01656  81 gldlipgNIDLEKFEKELLGPRkeerLREALEALKEDYDYVIIDGAP--GLGEllRNALIAADYVIIPLEP-EVILVEDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446438375  122 GRLVFDIKTAQAGVNPS--MKAWIVLNKC-STNPSDSEASELRRQLNDDPDWLPVPRqriymRTAHKKAYNNGMGV 194
Cdd:pfam01656 158 KRLGGVIAALVGGYALLglKIIGVVLNKVdGDNHGKLLKEALEELLRGLPVLGVIPR-----DEAVAEAPARGLPV 228
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-187 3.41e-08

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: 52.46  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375    4 IITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDS-QGSIKDFIEDRKTNARLSEI----PYFECYTDIP------- 71
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSATADRTGLslptPEHLNLPDNDvaevpdg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   72 ---------AMAQKLAARFDYVFVDTPGMKSPAFVKALSCAHILFTFIEpGSGIEINTLGRL---VFDIKtaqagvNPSM 139
Cdd:pfam09140  82 eniddarleEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLN-DSFVDFDLLGQVdpeTFKVK------RPSF 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446438375  140 KAWIVLnkcstnpsdsEASELRRQLNDDP-DWLpVPRQRIYMRTAHKKA 187
Cdd:pfam09140 155 YAEMVW----------EARKKRAKADRAPmDWI-VLRNRLGTLEARNKR 192
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-114 1.82e-07

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: 49.88  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETD-------------SQGSIKDFIEDRK--------TNARLSEI 61
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVslediiveGPEGLDII 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446438375  62 PY---FECYTDIPAMAQK--------LAARFDYVFVDTPGMKSPAFVKALSCAH--ILFTFIEPGS 114
Cdd:cd02038   81 PGgsgMEELANLDPEQKAklieelssLESNYDYLLIDTGAGISRNVLDFLLAADevIVVTTPEPTS 146
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 2-215 2.31e-06

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: 47.42  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   2 GKIITVAGHKGGIGKSTVLCSLC----------VCVI----KKGKTACFLETDSQGSIKDFIEDR-------------KT 54
Cdd:COG4963  102 GRVIAVVGAKGGVGATTLAVNLAwalaresgrrVLLVdldlQFGDVALYLDLEPRRGLADALRNPdrldetlldraltRH 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  55 NARLS--------EIPYFECYTDIPAMAQKLAARFDYVFVDTPGMKSPAFVKALSCAHILFTFIEPgSGIEINTLGRLVF 126
Cdd:COG4963  182 SSGLSvlaapadlERAEEVSPEAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEP-DLPSLRNAKRLLD 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375 127 DIKtaQAGVNPSmKAWIVLNKCSTNPsDSEASELRRQLNDDPDWLpVPRQRIYMRTahkkAYNNGMGVHEydDKRGNKAR 206
Cdd:COG4963  261 LLR--ELGLPDD-KVRLVLNRVPKRG-EISAKDIEEALGLPVAAV-LPNDPKAVAE----AANQGRPLAE--VAPKSPLA 329


                 ....*....
gi 446438375 207 GEIELLLKE 215
Cdd:COG4963  330 KAIRKLAAR 338
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 3-136 2.73e-06

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 46.21  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGgIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKdfIEDRKTNARLSEIPYFECYT-----DIpAMAQKL 77
Cdd:cd03115    1 NVILLVGLQG-SGKTTTLAKLARYYQEKGKKVLLIAADTFRAAA--VEQLKTLAEKLGVPVFESYTgtdpaSI-AQEAVE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446438375  78 AAR---FDYVFVDTPG--MKSPAFVKALSCAHilfTFIEPgsgieINTLgrLVFDIKTAQAGVN 136
Cdd:cd03115   77 KAKlegYDVLLVDTAGrlQKDEPLMEELKKVK---EVESP-----DEVL--LVLDATTGQEALS 130
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 13-91 1.05e-04

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 41.38  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  13 GIGKSTVLCSLC-VCVIKKGKTACFLETDSQ--GSIkdfiEDRKTNARLSEIPYFECYtDIPAMAQKLAA--RFDYVFVD 87
Cdd:cd17873   10 GVGKTTTLAKLAaRYVLKKGKKVALITTDTYriGAV----EQLKTYAEIMGIPVEVAE-DPEDLADALERlsDRDLILID 84


                 ....
gi 446438375  88 TPGM 91
Cdd:cd17873   85 TAGR 88
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
 3-93 3.01e-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: 40.63  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375    3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTN---------ARLSEIPYFEcytdiPAM 73
Cdd:pfam07015   2 QLITFCSFKGGAGKTTALMGLCSALASDGKRVALFEADENRPLTKWRENALRKgtwdpaceiFNADELPLLE-----QAY 76

                          90       100
                  ....*....|....*....|
gi 446438375   74 AQKLAARFDYVFVDTPGMKS 93
Cdd:pfam07015  77 EHAEGSGFDYALADTHGGSS 96
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-43 6.57e-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: 39.10  E-value: 6.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446438375    2 GKIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQG 43
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG 42
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
13-118 1.05e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.46  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375  13 GIGKSTVLCSLC-VCVIKKGKTACFLETDSQgsikdfiedR-------KTNARLSEIPYFECYT--DIPAMAQKLAaRFD 82
Cdd:COG1419  174 GVGKTTTIAKLAaRFVLRGKKKVALITTDTY---------RigaveqlKTYARILGVPVEVAYDpeELKEALERLR-DKD 243

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446438375  83 YVFVDTPGM--KSPAFVKALScahilfTFIEPGSGIEI 118
Cdd:COG1419  244 LVLIDTAGRspRDPELIEELK------ALLDAGPPIEV 275
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
3-93 1.47e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 38.67  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKDFIEDRKTN---------ARLSEIPYFEcytdiPAM 73
Cdd:PRK13849   2 KLLTFCSFKGGAGKTTALMGLCAALASDGKRVALFEADENRPLTRWKENALRSntwdpacevYAADELPLLE-----AAY 76

                         90       100
                 ....*....|....*....|
gi 446438375  74 AQKLAARFDYVFVDTPGMKS 93
Cdd:PRK13849  77 EDAELQGFDYALADTHGGSS 96
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-32 1.96e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 38.40  E-value: 1.96e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446438375   1 MGKIITVAGhKGGIGKSTVLCSLCVCVIKKGK 32
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGK 31
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 3-47 1.99e-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: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446438375    3 KIITVAGhKGGIGKSTVLCSLCVCVIKKGKTACFLETDSQGSIKD 47
Cdd:pfam02374   2 RWIFFGG-KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSD 45
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-40 2.04e-03

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: 37.87  E-value: 2.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETD 40
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-40 3.57e-03

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: 37.18  E-value: 3.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446438375   3 KIITVAGHKGGIGKSTVLCSLCVCVIKKGKTACFLETD 40
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 7-59 6.89e-03

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 36.42  E-value: 6.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446438375   7 VAGHKGGiGKSTVLCSLCVCVIKKGKTacfleTDSQGSIKDFIEDRKTNARLS 59
Cdd:cd03276   26 IVGNNGS-GKSAILTALTIGLGGKASD-----TNRGSSLKDLIKDGESSAKIT 72
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 3-32 8.08e-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: 36.51  E-value: 8.08e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 446438375   3 KIITVAGhKGGIGKSTVLCSLCVCVIKKGK 32
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGK 29
 
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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