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Conserved domains on  [gi|753938939|ref|WP_041652327|]
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MULTISPECIES: septum site-determining protein MinD [Achromobacter]

Protein Classification

septum site-determining protein MinD( domain architecture ID 11458413)

septum site-determining protein MinD, one of the three protein products of the min operon, is a membrane ATPase required for proper placement of the cell division site at the midcell position through the activation and regulation of MinC and MinE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-267 4.09e-168

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


:

Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 464.92  E-value: 4.09e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRavegdepvKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYK 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 753938939 241 DVVARYLGEDKALRFTDYEKPGFLKRL 267
Cdd:COG2894  232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-267 4.09e-168

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 464.92  E-value: 4.09e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRavegdepvKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYK 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 753938939 241 DVVARYLGEDKALRFTDYEKPGFLKRL 267
Cdd:COG2894  232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-270 5.42e-156

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 435.14  E-value: 5.42e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRAVEGDEPVKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYK 240
Cdd:PRK10818 161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 753938939 241 DVVARYLGEDKALRFTDYEKPGFLKRLFGG 270
Cdd:PRK10818 241 DTVDRLLGEERPFRFIEEEKKGFLKRLFGG 270
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-269 5.55e-120

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: 343.55  E-value: 5.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLEN 82
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   83 LFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAA 162
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  163 KSKRavegdepvKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYKDV 242
Cdd:TIGR01968 161 KGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFENI 232

                         250       260
                  ....*....|....*....|....*..
gi 753938939  243 VARYLGEDKALRFTDYEKPGFLKRLFG 269
Cdd:TIGR01968 233 ARRILGEEVPFEDLTTQKKGFFARIKR 259
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-245 1.71e-119

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: 341.10  E-value: 1.71e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLEN 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 LFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAA 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 163 KSkravegdePVKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLR-DTDVSEAYKD 241
Cdd:cd02036  160 KG--------IVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKpNSLAAKAFEN 231


                 ....
gi 753938939 242 VVAR 245
Cdd:cd02036  232 IARR 235
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-226 1.36e-36

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: 129.77  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    5 VVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   82 NLFILPA---SQTRDKDALTQEGVEKVINDLKGM--GFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753938939  157 LGILAA-KSKRAVEGDEPVkeYLLLTRYSPKRVVDGEMLslgDIEDILR-IKLIGVIPESEAVLQASNQGLP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKII--GVVLNKVDGDNHGKLLKE---ALEELLRgLPVLGVIPRDEAVAEAPARGLP 227
ParA_partition NF041546
ParA family partition ATPase;
4-193 1.49e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.32  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   4 IVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVglrnldlimgcerrvvydfvnviQGEATLNQALIKDKQLenl 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSALDWAAAREDERP--- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  84 fiLPASqtrdkdALTQEGVEKVINDLKGmGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILaak 163
Cdd:NF041546  55 --FPVV------GLARPTLHRELPSLAR-DYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLI--- 122

                        170       180       190
                 ....*....|....*....|....*....|
gi 753938939 164 sKRAVEGDEPVKEYLLLTRYSPKRVVDGEM 193
Cdd:NF041546 123 -KEAREYTPGLKAAFVLNRAIARTALGREV 151
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 2-138 2.34e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.09  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   2 TRIVVVTsGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGlRNLDLIMGceRRVVYDFVNViqGEATLNQALI-KDKQL 80
Cdd:NF041417 333 TRYLFFT-GKGGVGKSTIASTTATYLAEEGYETLIVTTDPA-SHLQDIFG--TEVGHEPTKV--GVENLYAARIdQERAL 406

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMgfdyivCDSPAGIETGAL--MAAYFADD 138
Cdd:NF041417 407 EEYKTRMLDQVEQSFDKDQIDVEAAKAQVREE------LESPCAEEMAALekFVSYFDVD 460
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-267 4.09e-168

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 464.92  E-value: 4.09e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRavegdepvKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYK 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 753938939 241 DVVARYLGEDKALRFTDYEKPGFLKRL 267
Cdd:COG2894  232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-270 5.42e-156

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 435.14  E-value: 5.42e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRAVEGDEPVKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYK 240
Cdd:PRK10818 161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 753938939 241 DVVARYLGEDKALRFTDYEKPGFLKRLFGG 270
Cdd:PRK10818 241 DTVDRLLGEERPFRFIEEEKKGFLKRLFGG 270
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-269 5.55e-120

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: 343.55  E-value: 5.55e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLEN 82
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   83 LFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAA 162
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  163 KSKRavegdepvKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSEAYKDV 242
Cdd:TIGR01968 161 KGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFENI 232

                         250       260
                  ....*....|....*....|....*..
gi 753938939  243 VARYLGEDKALRFTDYEKPGFLKRLFG 269
Cdd:TIGR01968 233 ARRILGEEVPFEDLTTQKKGFFARIKR 259
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-245 1.71e-119

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: 341.10  E-value: 1.71e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLEN 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 LFILPASQTRDKDALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAA 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 163 KSkravegdePVKEYLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLR-DTDVSEAYKD 241
Cdd:cd02036  160 KG--------IVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKpNSLAAKAFEN 231


                 ....
gi 753938939 242 VVAR 245
Cdd:cd02036  232 IARR 235
minD CHL00175
septum-site determining protein; Validated
 1-268 1.09e-76

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 234.28  E-value: 1.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKQL 80
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGIL 160
Cdd:CHL00175  94 KNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADRVAGLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 161 AAKSKRAVEgdepvkeyLLLTRYSPKRVVDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLRDTDVSE-AY 239
Cdd:CHL00175 174 EANGIYNVK--------LLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGiAF 245

                        250       260       270
                 ....*....|....*....|....*....|.
gi 753938939 240 KDVVARYLGedKALRFTDYEKP--GFLKRLF 268
Cdd:CHL00175 246 ENAARRLVG--KQDYFIDLDSPskGPLKRLQ 274
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-268 1.80e-39

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 137.94  E-value: 1.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVyDFVNVIQGEATLNQALIKDKqlEN 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPV-TLHDVLAGEADIKDAIYEGP--FG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   83 LFILPAsqtrdkdALTQEGVEK--------VINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSD 154
Cdd:TIGR01969  78 VKVIPA-------GVSLEGLRKadpdkledVLKEIIDD-TDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDAL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  155 RIlGILAAKSKRAVEGdepvkeyLLLTRYSPkrvvDGEMLSLGDIEDILRIKLIGVIPESEAVLQASNQGLPAIHLR-DT 233
Cdd:TIGR01969 150 KT-KIVAEKLGTAILG-------VVLNRVTR----DKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNpNS 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 753938939  234 DVSEAYKDVVARYLGEDKALRFTDYEkpGFLKRLF 268
Cdd:TIGR01969 218 PAAQAFMELAAELAGIEYEPKEPKKE--GFIAKVI 250
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-226 1.36e-36

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: 129.77  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    5 VVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDFVNVIQGEATLNQALIKDKQLE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   82 NLFILPA---SQTRDKDALTQEGVEKVINDLKGM--GFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753938939  157 LGILAA-KSKRAVEGDEPVkeYLLLTRYSPKRVVDGEMLslgDIEDILR-IKLIGVIPESEAVLQASNQGLP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKII--GVVLNKVDGDNHGKLLKE---ALEELLRgLPVLGVIPRDEAVAEAPARGLP 227
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-267 1.13e-33

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: 125.23  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLA-MRGHKTAVIDFDVGLRNLDLIMGCERRvvYDFVNVIQGEATLNQALIKD---K 78
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYLDLEPR--RGLADALRNPDRLDETLLDRaltR 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  79 QLENLFILPASQTRDK-DALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRIL 157
Cdd:COG4963  181 HSSGLSVLAAPADLERaEEVSPEAVERLLDLLRRH-FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 158 GILAAkskravEGDEPVKEYLLLTRYSPKRvvdgeMLSLGDIEDILRIKLIGVIP-ESEAVLQASNQGLP-AIHLRDTDV 235
Cdd:COG4963  260 DLLRE------LGLPDDKVRLVLNRVPKRG-----EISAKDIEEALGLPVAAVLPnDPKAVAEAANQGRPlAEVAPKSPL 328

                        250       260       270
                 ....*....|....*....|....*....|..
gi 753938939 236 SEAYKDVVARYLGEDKALRftDYEKPGFLKRL 267
Cdd:COG4963  329 AKAIRKLAARLTGRPAAAA--AKAGGKLLKRL 358
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-247 1.94e-31

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: 116.88  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   2 TRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD--------VGLRNLDLimgceRRVVYDfvnVIQGEATLNQA 73
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDpqgnltsgLGLDPDDL-----DPTLYD---LLLDDAPLEDA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  74 lIKDKQLENLFILPASQ---TRDKDALTQEGVE----KVINDLKGmGFDYIVCDSPAGIETGALMAAYFADDALVVTNPE 146
Cdd:COG1192   73 -IVPTEIPGLDLIPANIdlaGAEIELVSRPGRElrlkRALAPLAD-DYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 147 VSSVRDSDRILGILaaKSKRAVEGDEPVKEYLLLTRYSPKRVVDGEMLSlgDIEDILRIKLIG-VIPESEAVLQASNQGL 225
Cdd:COG1192  151 YLSLEGLAQLLETI--EEVREDLNPKLEILGILLTMVDPRTRLSREVLE--ELREEFGDKVLDtVIPRSVALAEAPSAGK 226

                        250       260
                 ....*....|....*....|...
gi 753938939 226 PAIHL-RDTDVSEAYKDVVARYL 247
Cdd:COG1192  227 PVFEYdPKSKGAKAYRALAEELL 249
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-250 4.62e-29

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 109.98  E-value: 4.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  18 TTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRvvYDFVNVIQGEATLNQALIKDKqlENLFILPASQ--TRDKD 95
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLPGGSgpAELAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  96 ALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAAKSKRAvegdepvK 175
Cdd:COG0455   77 LDPEERLIRVLEELERF-YDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRLGVR-------R 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 176 EYLLLTRYSPKRVvdgEMLSLGDIEDIL------RIKLIGVIPESEAVLQASNQGLPAIHLR-DTDVSEAYKDVVARYLG 248
Cdd:COG0455  149 AGVVVNRVRSEAE---ARDVFERLEQVAerflgvRLRVLGVIPEDPAVREAVRRGRPLVLAApDSPAARAIRELAARLAG 225


                 ..
gi 753938939 249 ED 250
Cdd:COG0455  226 WP 227
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-220 7.24e-27

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: 104.19  E-value: 7.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRvvYDFVNVIQGEATLNQALIKDKqlEN 82
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK--KTLGDVLKGRVSLEDIIVEGP--EG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 LFILPASQ-TRDKDALTQEGVEKVINDLKGMG--FDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGI 159
Cdd:cd02038   77 LDIIPGGSgMEELANLDPEQKAKLIEELSSLEsnYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753938939 160 LAAKSKRA-----VEGDEPVKEYLLLTRySPKRVVDgEMLSlgdiediLRIKLIGVIPESEAVLQA 220
Cdd:cd02038  157 LSRRGGKKnfrliVNMARSPKEGRATFE-RLKKVAK-RFLD-------INLDFVGFIPYDQSVRRA 213
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-160 2.46e-23

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: 96.02  E-value: 2.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVvyDFVNVIQGEATLNQALIKDkQLEN 82
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLEDVIQPT-EVEG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 LFILPASQTRDKDA--LTQEGVEKVINDLKGmGFDYIVCDSPAGIE-TGALMAAYFADDALVVTNPEVSSVRDSDRILGI 159
Cdd:COG0489  170 LDVLPAGPLPPNPSelLASKRLKQLLEELRG-RYDYVIIDTPPGLGvADATLLASLVDGVLLVVRPGKTALDDVRKALEM 248


                 .
gi 753938939 160 L 160
Cdd:COG0489  249 L 249
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-228 2.74e-21

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 89.26  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMR-GHKTAVIDFDVGLRNLDLIMGCERRvvYDFVNVIQGEATLNQALIKD---K 78
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavtR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  79 QLENLFILPASQTRDK-DALTQEGVEKVINDLKGMgFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRIL 157
Cdd:cd03111   79 HSSGLSLLPAPQELEDlEALGAEQVDKLLQVLRAF-YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753938939 158 GILaaksKRAVEGDEPVKeyLLLTRYSpkrvVDGEMlSLGDIEDILRIKLIGVIP-ESEAVLQASNQGLPAI 228
Cdd:cd03111  158 DSL----RELEGSSDRLR--LVLNRYD----KKSEI-SPKDIEEALGLEVFATLPnDYKAVSESANTGRPLV 218
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-160 1.82e-17

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 78.00  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDvgLRN--LDLIMGCERRVvyDFVNVIQGEATLNQAlIKDKQL 80
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD--LRRpsLHRLLGLPNEP--GLSEVLSGQASLEDV-IQSTNI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDK--DALTQEGVEKVINDLKGMgFDYIVCDSPA-GIETGALMAAYFADDALVVTNPEVSSVRDSDRIL 157
Cdd:cd05387   95 PNLDVLPAGTVPPNpsELLSSPRFAELLEELKEQ-YDYVIIDTPPvLAVADALILAPLVDGVLLVVRAGKTRRREVKEAL 173


                 ...
gi 753938939 158 GIL 160
Cdd:cd05387  174 ERL 176
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-146 1.27e-15

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: 72.62  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    2 TRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLrNLDLIMGCERRVVY-DFVNVIQGEATLNQALIKDKqL 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG-NATSGLGIDKNNVEkTIYELLIGECNIEEAIIKTV-I 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 753938939   81 ENLFILPAS-----------QTRDKDALTQEGVEKVINDlkgmgFDYIVCDSPAGIETGALMAAYFADDALVVTNPE 146
Cdd:pfam13614  79 ENLDLIPSNidlagaeieliGIENRENILKEALEPVKDN-----YDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-194 6.70e-13

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: 64.10  E-value: 6.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDvglrnldlimgcerrvvydfvnvIQGEATLnqalikdkqlen 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD-----------------------PQGSLTS------------ 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 lfilpasqtrdkdaltqegvekvindlkgMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILAA 162
Cdd:cd02042   46 -----------------------------WLYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEE 96

                        170       180       190
                 ....*....|....*....|....*....|..
gi 753938939 163 ksKRAVEGDEPVKEYLLLTRYSPKRVVDGEML 194
Cdd:cd02042   97 --LKKQLNPPLLILGILLTRVDPRTKLAREVL 126
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 1.17e-12

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 65.15  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDvgLRN-LDLIMGCERRVVYDFVNVIQGEATLNQAlIKDKQLE 81
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD--MRNsVMSGTFKSQNKITGLTNFLSGTTDLSDA-ICDTNIE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753938939   82 NLFILPASQTR-DKDALTQ-EGVEKVINDLKGMgFDYIVCDS-PAGIETGALMAAYFADDALVVTNPE 146
Cdd:TIGR01007  95 NLDVITAGPVPpNPTELLQsSNFKTLIETLRKR-FDYIIIDTpPIGTVTDAAIIARACDASILVTDAG 161
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-245 1.23e-12

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 65.96  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVvtSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLrNLDLIMGCErrVVYDFVNVIqGEatlNQALIKDKQ--- 79
Cdd:COG3640    2 KIAV--AGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNA-NLAEALGLE--VEADLIKPL-GE---MRELIKERTgap 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  80 -----LENLFI--LPASQTRDKD--------ALTQEG----------VEKVINDLKGMGFDYIVCDSPAGIET-GALMAA 133
Cdd:COG3640   73 gggmfKLNPKVddIPEEYLVEGDgvdllvmgTIEEGGsgcycpenalLRALLNHLVLGNYEYVVVDMEAGIEHlGRGTAE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 134 YFaDDALVVTNPEVSSVRDSDRILGiLAAKSKravegdepVKE-YLLLTRYSPKRVVDgemlslgDIEDILRIKLIGVIP 212
Cdd:COG3640  153 GV-DLLLVVSEPSRRSIETARRIKE-LAEELG--------IKKiYLVGNKVREEEDEE-------FLRELLGLELLGFIP 215

                        250       260       270
                 ....*....|....*....|....*....|...
gi 753938939 213 ESEAVLQASNQGLPAIHLRDTDVSEAYKDVVAR 245
Cdd:COG3640  216 YDEEVREADLEGKPLLDLPDSPAVAAVEEIAEK 248
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-152 1.76e-10

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: 59.05  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQGEATLNQALIKDKqlen 82
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGIKVMSIG---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 lFILPASQT-----RDKDALTQEGVEKVI-NDLkgmgfDYIVCDSPAGieTG----ALMAAYFADDALVVTNPEVSSVRD 152
Cdd:cd02037   77 -FLLPEDDAviwrgPMKSGAIKQFLKDVDwGEL-----DYLIIDLPPG--TGdehlSLVQLIPIDGAVVVTTPQEVSLID 148
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-229 5.51e-10

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 58.13  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    1 MTRIVVVtSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVG--LR---NLDLimgcerrvvydfvNVIQG--EATLNQA 73
Cdd:TIGR03371   1 MKVIAIV-SVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQnlLRlhfGMDW-------------SVRDGwaRALLNGA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   74 LIKDKQLEN----LFI----LPASQTRDKDALTQEGVEKVINDLKGMGFDYIVCDSPAG---IETGALMAayfADDALVV 142
Cdd:TIGR03371  67 DWAAAAYRSpdgvLFLpygdLSADEREAYQAHDAGWLARLLQQLDLAARDWVLIDLPRGpspITRQALAA---ADLVLVV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  143 TNPEVSSVRDSDRILGILAAKSKravegdEPVKEYLLLTRYSPKRVVDgemlslGDIEDILRIK-----LIGVIPESEAV 217
Cdd:TIGR03371 144 VNADAACYATLHQLALALFAGSG------PRDGPRFLINQFDPARQLS------RDVRAVLRQTlgsrlLPFVIHRDEAV 211

                         250
                  ....*....|..
gi 753938939  218 LQASNQGLPAIH 229
Cdd:TIGR03371 212 SEALARGTPVLN 223
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-41 1.93e-09

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: 56.69  E-value: 1.93e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 753938939    2 TRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDV 41
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADI 42
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-212 2.49e-09

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 56.24  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   4 IVVVTSGKGGVGKTTTSASFSAGLAmrghKTAVIDFDVGLRNLDLIMGCERRVVYDFVNVIQgeATLNQ----------- 72
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLLY----NVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKK--AFIDQekcircgncer 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  73 -----ALIKDKQLENLF------------ILPASQTRDKDALT---------------------QEGVEKVINDLK---- 110
Cdd:cd03110   75 vckfgAILEFFQKLIVDeslcegcgacviICPRGAIYLKDRDTgkifisssdggplvhgrlnigEENSGKLVTELRkkal 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 111 --GMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILgilaaksKRAVEGDEPVKeyLLLTRYSPKRV 188
Cdd:cd03110  155 erSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAI-------ELAKHFGIPTG--IVINRYDINDE 225

                        250       260
                 ....*....|....*....|....
gi 753938939 189 VDGEMLSLGDIEDilrIKLIGVIP 212
Cdd:cd03110  226 ISEEIEDFADEEG---IPLLGKIP 246
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-40 7.42e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 55.21  E-value: 7.42e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 753938939   1 MTRIVVVTsGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:COG0003    2 MTRIIFFT-GKGGVGKTTVAAATALALAERGKRTLLVSTD 40
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 3-161 8.52e-09

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: 54.82  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTsGKGGVGKTTTSASFSAGLAMRGHKTAVI--D--------FDVGLRNLDLIMGCE---------RRVVYDFVNV 63
Cdd:cd02035    1 RIIFFG-GKGGVGKTTIAAATAVRLAEQGKRVLLVstDpahslsdaFGQKLGGETPVKGAPnlwameidpEEALEEYWEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  64 IQGEAT--LNQALIKDKQLENLFILPAsqtrdkdalTQEGV--EKVINDLKGMGFDYIVCDS-PAGiETGALMA------ 132
Cdd:cd02035   80 VKELLAqyLRLPGLDEVYAEELLSLPG---------MDEAAafDELREYVESGEYDVIVFDTaPTG-HTLRLLSlpleqv 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 753938939 133 -AYFADD----ALVVTNPEVSSVRDSDRILGILA 161
Cdd:cd02035  150 rELLRDPerttFVLVTIPEKLSIYETERLWGELQ 183
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-165 9.47e-09

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: 52.05  E-value: 9.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDvglrnldlimgcerrvvydfvnviqgeatlnqalikdkqlen 82
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  83 lfilpasqtrdkdaltqegvekvindlkgmgfDYIVCDSPAGIETGA-------LMAAYFADDALVVTNPEVSSVRDSDR 155
Cdd:cd01983   39 --------------------------------DYVLIDGGGGLETGLllgtivaLLALKKADEVIVVVDPELGSLLEAVK 86

                        170
                 ....*....|
gi 753938939 156 ILGILAAKSK 165
Cdd:cd01983   87 LLLALLLLGI 96
ParA_partition NF041546
ParA family partition ATPase;
4-193 1.49e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.32  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   4 IVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVglrnldlimgcerrvvydfvnviQGEATLNQALIKDKQLenl 83
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSALDWAAAREDERP--- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  84 fiLPASqtrdkdALTQEGVEKVINDLKGmGFDYIVCDSPAGIETGALMAAYFADDALVVTNPEVSSVRDSDRILGILaak 163
Cdd:NF041546  55 --FPVV------GLARPTLHRELPSLAR-DYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLI--- 122

                        170       180       190
                 ....*....|....*....|....*....|
gi 753938939 164 sKRAVEGDEPVKEYLLLTRYSPKRVVDGEM 193
Cdd:NF041546 123 -KEAREYTPGLKAAFVLNRAIARTALGREV 151
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 9-245 1.82e-07

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


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 50.77  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   9 SGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLrNLDLIMGC--ERRVVYDFV-----NVIQGEATLNQALIKDKQLE 81
Cdd:cd02034    6 AGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS-NLAETLGVevEKLPLIKTIgdireRTGAKKGEPPEGMSLNPYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  82 NLFILPASQTRDKDALT----QEGVE-----------KVINDLKGMGFDYIVCDSPAGIETGALMAAYFADDALVVTNPE 146
Cdd:cd02034   85 DIIKEIIVEPDGIDLLVmgrpEGGGSgcycpvnallrELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDLLIIVIEPS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939 147 VSSVRDSDRIlgilaakskRAVEGDEPVKE-YLLLTryspkRVVDGEMLSLGDiEDILRIKLIGVIPESEAVLQASNQGL 225
Cdd:cd02034  165 KRSIQTAKRI---------KELAEELGIKKiYLIVN-----KVRNEEEQELIE-ELLIKLKLIGVIPYDEEIMEADLKGK 229

                        250       260
                 ....*....|....*....|
gi 753938939 226 PAIHLRDTDVSEAyKDVVAR 245
Cdd:cd02034  230 PLFDLDSAAVKAI-EKIVEK 248
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-126 2.91e-07

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 49.85  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   2 TRIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDvGLRNLDLIMGCERR-----VVYDFVNVIQGEATLNQALIK 76
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFGASGRylmsdHLYTLKSRKANLADKLESCVK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 753938939  77 DKQLENLFILPASQTRDKDALTQEGVEKVINDLKGMG-FDYIVCDSPAGIE 126
Cdd:cd17869   82 QHESGVYYFSPFKSALDILEIKKDDILHMITKLVEAHaYDYIIMDLSFEFS 132
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 2-40 6.14e-06

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: 46.57  E-value: 6.14e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 753938939    2 TRIVVVTsGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:pfam02374   1 MRWIFFG-GKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-41 1.13e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 46.19  E-value: 1.13e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 753938939   4 IVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDV 41
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 3-143 2.07e-05

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: 44.75  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMgcERRVvydfvnviqgeATLNQALIKDKQLEN 82
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYF--ENRS-----------ATADRTGLSLPTPEH 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 753938939   83 LFILPA--SQTRDKDALTQEGVEKVINDLkGMGFDYIVCDSPAGIETGALMAAYFADdaLVVT 143
Cdd:pfam09140  68 LNLPDNdvAEVPDGENIDDARLEEAFADL-EARCDFIVIDTPGSDSPLSRLAHSRAD--TLVT 127
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 5-33 3.02e-05

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 45.08  E-value: 3.02e-05
                          10        20
                  ....*....|....*....|....*....
gi 753938939    5 VVVTSGKGGVGKTTTSASFSAGLAMRGHK 33
Cdd:TIGR04291 323 LIMTMGKGGVGKTTVAAAIAVRLANKGLD 351
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-40 6.01e-05

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 43.81  E-value: 6.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 753938939    4 IVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLD 142
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-40 7.31e-05

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 43.51  E-value: 7.31e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLD 159
PHA02518 PHA02518
ParA-like protein; Provisional
 3-40 1.55e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 41.76  E-value: 1.55e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 753938939   3 RIVVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD 38
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 10-37 6.51e-04

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 40.19  E-value: 6.51e-04
                         10        20
                 ....*....|....*....|....*...
gi 753938939  10 GKGGVGKTTTSASFSAGLAMRGHKTAVI 37
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHV 34
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 10-33 7.60e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.95  E-value: 7.60e-04
                         10        20
                 ....*....|....*....|....
gi 753938939  10 GKGGVGKTTTSASFSAGLAMRGHK 33
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKK 32
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 5-221 1.84e-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: 38.89  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   5 VVVTSGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGLRNLDLIMGceRRVVYDFVNVIQGEATLNQALIKDKQLE--- 81
Cdd:cd02117    2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTG--GKVPPTIDEMLTEDGTAEELRREDLLFSgfn 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  82 NLFILPAS-----------------QTRDKDALTQEGVEKVINDLKGmgfDyIVCDSPAgietgALMAAYFADDALVVTN 144
Cdd:cd02117   80 GVDCVEAGgpepgvgcggrgigtmlELLEEHGLLDDDYDVVIFDVLG---D-VVCGGFA-----APLRRGFAQKVVIVVS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 753938939 145 PEVSSVRDSDRILGILAAKSKRAVegdepvkeYLLLTRYSPKRVVDGEMLSlgDIEDILRIKLIGVIPESEAVLQAS 221
Cdd:cd02117  151 EELMSLYAANNIVKAVENYSKNGV--------RLAGLVANLRDPAGTEEIQ--AFAAAVGTKILAVIPRDPAVRRAE 217
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 2-138 2.34e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.09  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939   2 TRIVVVTsGKGGVGKTTTSASFSAGLAMRGHKTAVIDFDVGlRNLDLIMGceRRVVYDFVNViqGEATLNQALI-KDKQL 80
Cdd:NF041417 333 TRYLFFT-GKGGVGKSTIASTTATYLAEEGYETLIVTTDPA-SHLQDIFG--TEVGHEPTKV--GVENLYAARIdQERAL 406

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939  81 ENLFILPASQTRDKDALTQEGVEKVINDLKGMgfdyivCDSPAGIETGAL--MAAYFADD 138
Cdd:NF041417 407 EEYKTRMLDQVEQSFDKDQIDVEAAKAQVREE------LESPCAEEMAALekFVSYFDVD 460
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 10-33 2.45e-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: 38.43  E-value: 2.45e-03
                         10        20
                 ....*....|....*....|....
gi 753938939  10 GKGGVGKTTTSASFSAGLAMRGHK 33
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKK 30
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-40 2.81e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 38.19  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 753938939   10 GKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCD 37
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 4-85 3.58e-03

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 38.08  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753938939    4 IVVVtsGKGGVGKTTTSASFSAGLAMR--GHKTAVIDFD---VG----LRNLDLIMGCERRVVYDfvnviqgEATLNQAL 74
Cdd:TIGR03499 197 IALV--GPTGVGKTTTLAKLAARFALEhgKKKVALITTDtyrIGaveqLKTYAEILGIPVKVARD-------PKELREAL 267

                          90
                  ....*....|.
gi 753938939   75 IKDKQLENLFI 85
Cdd:TIGR03499 268 DRLRDKDLILI 278
chlL CHL00072
photochlorophyllide reductase subunit L
 10-40 4.41e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 37.79  E-value: 4.41e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 753938939  10 GKGGVGKTTTSASFSAGLAMRGHKTAVIDFD 40
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCD 37
 
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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