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Conserved domains on  [gi|499312472|ref|WP_011003247|]
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MULTISPECIES: septum site-determining protein MinD [Ralstonia solanacearum species complex]

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 4.27e-170

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


:

Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.92  E-value: 4.27e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRaiegkepiQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYA 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 499312472 241 DVIDRFLGKEKPLRYVEYSKPGFLQRL 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 4.27e-170

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.92  E-value: 4.27e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRaiegkepiQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYA 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 499312472 241 DVIDRFLGKEKPLRYVEYSKPGFLQRL 267
Cdd:COG2894  232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-270 2.42e-160

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 445.92  E-value: 2.42e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRAIEGKEPIQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYA 240
Cdd:PRK10818 161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 499312472 241 DVIDRFLGKEKPLRYVEYSKPGFLQRLFGG 270
Cdd:PRK10818 241 DTVDRLLGEERPFRFIEEEKKGFLKRLFGG 270
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-269 4.25e-124

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: 353.95  E-value: 4.25e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKCEN 82
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   83 LFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILSS 162
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  163 KSRRaiegkepiQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYADV 242
Cdd:TIGR01968 161 KGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFENI 232

                         250       260
                  ....*....|....*....|....*..
gi 499312472  243 IDRFLGKEKPLRYVEYSKPGFLQRLFG 269
Cdd:TIGR01968 233 ARRILGEEVPFEDLTTQKKGFFARIKR 259
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-246 1.21e-122

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: 349.19  E-value: 1.21e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKCEN 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  83 LFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILSS 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 163 KsrraieGKEPIqeHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAA-AYAD 241
Cdd:cd02036  160 K------GIVNI--GLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAkAFEN 231


                 ....*
gi 499312472 242 VIDRF 246
Cdd:cd02036  232 IARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-226 7.70e-38

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: 132.85  E-value: 7.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    5 IVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDLINVIHGEANLNQALIKDKKCE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   82 NLFILPA---SQTRDKDALTREGVEKVISGLTDM--GFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499312472  157 LGILSS-KSRRAIEGKEPIQehLLLTRYNPKRVSEGEMLSLTdvQEILRIKLIGVIPESEAVLQASNQGIP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIG--VVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLP 227
ParA_partition NF041546
ParA family partition ATPase;
4-40 6.28e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 51.78  E-value: 6.28e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499312472   4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 9-40 9.12e-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: 37.17  E-value: 9.12e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499312472   9 SGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTD 370
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 1-267 4.27e-170

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.92  E-value: 4.27e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:COG2894    1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894   81 ENLYLLPASQTRDKDALTPEQMKKLVEELKEE-FDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRaiegkepiQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYA 240
Cdd:COG2894  160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231

                        250       260
                 ....*....|....*....|....*..
gi 499312472 241 DVIDRFLGKEKPLRYVEYSKPGFLQRL 267
Cdd:COG2894  232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-270 2.42e-160

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 445.92  E-value: 2.42e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:PRK10818   1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818  81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRAIEGKEPIQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYA 240
Cdd:PRK10818 161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 499312472 241 DVIDRFLGKEKPLRYVEYSKPGFLQRLFGG 270
Cdd:PRK10818 241 DTVDRLLGEERPFRFIEEEKKGFLKRLFGG 270
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-269 4.25e-124

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: 353.95  E-value: 4.25e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKCEN 82
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLKN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   83 LFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILSS 162
Cdd:TIGR01968  82 LYLLPASQTRDKDAVTPEQMKKLVNELKEE-FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  163 KSRRaiegkepiQEHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYADV 242
Cdd:TIGR01968 161 KGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFENI 232

                         250       260
                  ....*....|....*....|....*..
gi 499312472  243 IDRFLGKEKPLRYVEYSKPGFLQRLFG 269
Cdd:TIGR01968 233 ARRILGEEVPFEDLTTQKKGFFARIKR 259
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-246 1.21e-122

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: 349.19  E-value: 1.21e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKCEN 82
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  83 LFILPASQTRDKDALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILSS 162
Cdd:cd02036   81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 163 KsrraieGKEPIqeHLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAA-AYAD 241
Cdd:cd02036  160 K------GIVNI--GLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAkAFEN 231


                 ....*
gi 499312472 242 VIDRF 246
Cdd:cd02036  232 IARRL 236
minD CHL00175
septum-site determining protein; Validated
 1-268 6.18e-79

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 240.06  E-value: 6.18e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   1 MTKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIHGEANLNQALIKDKKC 80
Cdd:CHL00175  14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDKDALTREGVEKVISGLTDMGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:CHL00175  94 KNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADRVAGLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 161 SSKSRRAIEgkepiqehLLLTRYNPKRVSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAA-AY 239
Cdd:CHL00175 174 EANGIYNVK--------LLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGiAF 245

                        250       260
                 ....*....|....*....|....*....
gi 499312472 240 ADVIDRFLGKEKPLRYVEYSKPGFLQRLF 268
Cdd:CHL00175 246 ENAARRLVGKQDYFIDLDSPSKGPLKRLQ 274
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-226 7.70e-38

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: 132.85  E-value: 7.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    5 IVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDLINVIHGEANLNQALIKDKKCE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   82 NLFILPA---SQTRDKDALTREGVEKVISGLTDM--GFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499312472  157 LGILSS-KSRRAIEGKEPIQehLLLTRYNPKRVSEGEMLSLTdvQEILRIKLIGVIPESEAVLQASNQGIP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIG--VVLNKVDGDNHGKLLKEALE--ELLRGLPVLGVIPRDEAVAEAPARGLP 227
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 3-268 3.50e-37

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: 131.78  E-value: 3.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVyDLINVIHGEANLNQALIKDKkcEN 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPV-TLHDVLAGEADIKDAIYEGP--FG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   83 LFILPASQTRDKDALTR-EGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRIlGILS 161
Cdd:TIGR01969  78 VKVIPAGVSLEGLRKADpDKLEDVLKEIIDD-TDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALKT-KIVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  162 SKSRRAIEGkepiqehLLLTRYNpkrvSEGEMLSLTDVQEILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAA-AYA 240
Cdd:TIGR01969 156 EKLGTAILG-------VVLNRVT----RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAqAFM 224

                         250       260
                  ....*....|....*....|....*...
gi 499312472  241 DVIDRFLGKEKPLRyvEYSKPGFLQRLF 268
Cdd:TIGR01969 225 ELAAELAGIEYEPK--EPKKEGFIAKVI 250
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-252 2.65e-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: 124.07  E-value: 2.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALR-GHKTAVIDFDVGLRNLDLIMGCE-RRVVYDLINVIHG--EANLNQALIKDK 78
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEpRRGLADALRNPDRldETLLDRALTRHS 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  79 kcENLFILPASQTRDK-DALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRIL 157
Cdd:COG4963  183 --SGLSVLAAPADLERaEEVSPEAVERLLDLLRRH-FDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRLL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 158 GILSSksrraiEGKEPIQEHLLLTRYNPKRvsegeMLSLTDVQEILRIKLIGVIP-ESEAVLQASNQGIPAIHLD-GTDV 235
Cdd:COG4963  260 DLLRE------LGLPDDKVRLVLNRVPKRG-----EISAKDIEEALGLPVAAVLPnDPKAVAEAANQGRPLAEVApKSPL 328

                        250
                 ....*....|....*..
gi 499312472 236 AAAYADVIDRFLGKEKP 252
Cdd:COG4963  329 AKAIRKLAARLTGRPAA 345
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 2-251 3.42e-33

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: 121.50  E-value: 3.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   2 TKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDV-GlrNLDLIMGCERRVV-YDLINVIHGEANLNQAlIKDKK 79
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqG--NLTSGLGLDPDDLdPTLYDLLLDDAPLEDA-IVPTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  80 CENLFILPASQ---TRDKDALTREGVE----KVISGLTDmGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRD 152
Cdd:COG1192   78 IPGLDLIPANIdlaGAEIELVSRPGRElrlkRALAPLAD-DYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 153 SDRILGILssKSRRAIEGKEPIQEHLLLTRYNPKRVSEGEMLSltDVQEILRIKLIG-VIPESEAVLQASNQGIPAIHLD 231
Cdd:COG1192  157 LAQLLETI--EEVREDLNPKLEILGILLTMVDPRTRLSREVLE--ELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYD 232

                        250       260
                 ....*....|....*....|.
gi 499312472 232 -GTDVAAAYADVIDRFLGKEK 251
Cdd:COG1192  233 pKSKGAKAYRALAEELLERLE 253
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 18-252 5.04e-30

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: 112.29  E-value: 5.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  18 TTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRvvYDLINVIHGEANLNQALIKDKkcENLFILPASQ--TRDKD 95
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLPGGSgpAELAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  96 ALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILSSKSrraieGKEPIq 175
Cdd:COG0455   77 LDPEERLIRVLEELERF-YDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRRRL-----GVRRA- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 176 eHLLLTRYNPKRVSEGEMLSLTDV-QEIL--RIKLIGVIPESEAVLQASNQGIPAIHLD-GTDVAAAYADVIDRFLGKEK 251
Cdd:COG0455  150 -GVVVNRVRSEAEARDVFERLEQVaERFLgvRLRVLGVIPEDPAVREAVRRGRPLVLAApDSPAARAIRELAARLAGWPV 228


                 .
gi 499312472 252 P 252
Cdd:COG0455  229 P 229
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-226 2.01e-28

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: 108.43  E-value: 2.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRvvYDLINVIHGEANLNQALIKDKkcEN 82
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK--KTLGDVLKGRVSLEDIIVEGP--EG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  83 LFILPASQ-TRDKDALTREGVEKVISGLTDMG--FEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGI 159
Cdd:cd02038   77 LDIIPGGSgMEELANLDPEQKAKLIEELSSLEsnYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499312472 160 LSSKsrraiEGKEPIqeHLLLTRYnpKRVSEGEML--SLTDVQEI---LRIKLIGVIPESEAVLQASNQGIP 226
Cdd:cd02038  157 LSRR-----GGKKNF--RLIVNMA--RSPKEGRATfeRLKKVAKRfldINLDFVGFIPYDQSVRRAVRSQKP 219
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 4-162 2.74e-21

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: 90.63  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVvyDLINVIHGEANLNQALIKDKKcENL 83
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLEDVIQPTEV-EGL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  84 FILPASQTRDKDA--LTREGVEKVISGLTDmGFEYIVCDSPAGIE-SGALMAMYFADEAIVVTNPEVSSVRDSDRILGIL 160
Cdd:COG0489  171 DVLPAGPLPPNPSelLASKRLKQLLEELRG-RYDYVIIDTPPGLGvADATLLASLVDGVLLVVRPGKTALDDVRKALEML 249


                 ..
gi 499312472 161 SS 162
Cdd:COG0489  250 EK 251
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 3-228 3.47e-17

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: 78.47  E-value: 3.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALR-GHKTAVIDFDVGLRNLDLIMGCERRvvYDLINVIHGEANLNQALIKD--KK 79
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavTR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  80 CEN-LFILPASQTRDK-DALTREGVEKVISGLTDMgFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRIL 157
Cdd:cd03111   79 HSSgLSLLPAPQELEDlEALGAEQVDKLLQVLRAF-YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499312472 158 GILssksRRAIEGKEPIqeHLLLTRYNPKrvSEgemLSLTDVQEILRIKLIGVIP-ESEAVLQASNQGIPAI 228
Cdd:cd03111  158 DSL----RELEGSSDRL--RLVLNRYDKK--SE---ISPKDIEEALGLEVFATLPnDYKAVSESANTGRPLV 218
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-146 3.28e-16

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: 74.16  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    2 TKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLrNLDLIMGCERRVVYDLI-NVIHGEANLNQALIKDKKc 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG-NATSGLGIDKNNVEKTIyELLIGECNIEEAIIKTVI- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499312472   81 ENLFILPAS-----------QTRDKDALTREGVEKVISgltdmGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPE 146
Cdd:pfam13614  79 ENLDLIPSNidlagaeieliGIENRENILKEALEPVKD-----NYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 3-194 9.48e-15

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 69.11  E-value: 9.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDvglrnldlimgcerrvvydlinvihgeanlnqalikdkkcen 82
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD------------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  83 lfilpaSQtrdkdaltregvekviSGLTDMGFEYIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRILGILss 162
Cdd:cd02042   39 ------PQ----------------GSLTSWLYDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTL-- 94

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499312472 163 KSRRAIEGKEPIQEHLLLTRYNPKRVSEGEML 194
Cdd:cd02042   95 EELKKQLNPPLLILGILLTRVDPRTKLAREVL 126
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-163 4.10e-14

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: 68.75  E-value: 4.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDvgLRN--LDLIMGCERRVvyDLINVIHGEANLNQAlIKDKKC 80
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD--LRRpsLHRLLGLPNEP--GLSEVLSGQASLEDV-IQSTNI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ENLFILPASQTRDK--DALTREGVEKVISGLTDMgFEYIVCDSPA-GIESGALMAMYFADEAIVVTNPEVSSVRDSDRIL 157
Cdd:cd05387   95 PNLDVLPAGTVPPNpsELLSSPRFAELLEELKEQ-YDYVIIDTPPvLAVADALILAPLVDGVLLVVRAGKTRRREVKEAL 173


                 ....*.
gi 499312472 158 GILSSK 163
Cdd:cd05387  174 ERLEQA 179
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 3-245 3.06e-13

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 67.50  E-value: 3.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVvtSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLrNLDLIMGCErrVVYDLINVIhGEanlNQALIKDKKC-- 80
Cdd:COG3640    2 KIAV--AGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNA-NLAEALGLE--VEADLIKPL-GE---MRELIKERTGap 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  81 ------ENLFI--LPASQTRDKD--------ALTREG----------VEKVISGLTDMGFEYIVCDSPAGIESgalmamy 134
Cdd:COG3640   73 gggmfkLNPKVddIPEEYLVEGDgvdllvmgTIEEGGsgcycpenalLRALLNHLVLGNYEYVVVDMEAGIEH------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 135 FA-------DEAIVVTNPEVSSVRDSDRI------LGIlssksrraiegkEPIqeHLLLTRYNPKRVSEgemlsltDVQE 201
Cdd:COG3640  146 LGrgtaegvDLLLVVSEPSRRSIETARRIkelaeeLGI------------KKI--YLVGNKVREEEDEE-------FLRE 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499312472 202 ILRIKLIGVIPESEAVLQASNQGIPAIHLDGTDVAAAYADVIDR 245
Cdd:COG3640  205 LLGLELLGFIPYDEEVREADLEGKPLLDLPDSPAVAAVEEIAEK 248
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 3-152 5.89e-11

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: 60.59  E-value: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDlinvihgeanlNQALIKDKKCEN 82
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ-----------SEEGIVPVEVGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  83 L------FILPASQT-----RDKDALTREGVEKVISGLTDmgfeYIVCDSPAGI--ESGALMAMYFADEAIVVTNPEVSS 149
Cdd:cd02037   70 IkvmsigFLLPEDDAviwrgPMKSGAIKQFLKDVDWGELD----YLIIDLPPGTgdEHLSLVQLIPIDGAVVVTTPQEVS 145


                 ...
gi 499312472 150 VRD 152
Cdd:cd02037  146 LID 148
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-146 5.97e-10

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: 57.45  E-value: 5.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDvgLRN-LDLIMGCERRVVYDLINVIHGEANLNQAlIKDKKCE 81
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD--MRNsVMSGTFKSQNKITGLTNFLSGTTDLSDA-ICDTNIE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499312472   82 NLFILPASQT--RDKDALTREGVEKVISGLTDMgFEYIVCDS-PAGIESGALMAMYFADEAIVVTNPE 146
Cdd:TIGR01007  95 NLDVITAGPVppNPTELLQSSNFKTLIETLRKR-FDYIIIDTpPIGTVTDAAIIARACDASILVTDAG 161
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-53 1.17e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 57.91  E-value: 1.17e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499312472   1 MTKIIVVTsGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGlRNLDLIMGCE 53
Cdd:COG0003    2 MTRIIFFT-GKGGVGKTTVAAATALALAERGKRTLLVSTDPA-HSLGDVLGTE 52
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 3-237 2.28e-09

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: 56.59  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472    3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDV----------------GLRNLDLIMGCERRVVY----DLIN 62
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPqnllrlhfgmdwsvrdGWARALLNGADWAAAAYrspdGVLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   63 VIHGEANLNQALikdkkcenlfilpASQTRDKDALTREgvekvisgLTDMGFE---YIVCDSPAGIESGALMAMYFADEA 139
Cdd:TIGR03371  82 LPYGDLSADERE-------------AYQAHDAGWLARL--------LQQLDLAardWVLIDLPRGPSPITRQALAAADLV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  140 IVVTNPEVSSVRDSDRILGILSSKSrraiegKEPIQEHLLLTRYNPKRVSEgemlslTDVQEILRIK-----LIGVIPES 214
Cdd:TIGR03371 141 LVVVNADAACYATLHQLALALFAGS------GPRDGPRFLINQFDPARQLS------RDVRAVLRQTlgsrlLPFVIHRD 208

                         250       260
                  ....*....|....*....|...
gi 499312472  215 EAVLQASNQGIPAIHLDGTDVAA 237
Cdd:TIGR03371 209 EAVSEALARGTPVLNYAPHSQAA 231
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-41 2.85e-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: 55.92  E-value: 2.85e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499312472    2 TKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDV 41
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADI 42
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-40 7.38e-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: 52.43  E-value: 7.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 4-157 2.78e-08

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: 53.16  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   4 IIVVTSGKGGVGKTTTSAAFSagLALRGHktAVIDFDVGLRNLDLIMGCERRVVYDlinVIHGE-ANLNQ---------- 72
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLA--VLLYNV--ILVDCDVDAPNLHLLLGPEPEEEED---FVGGKkAFIDQekcircgnce 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  73 ------ALIKDKK--------CEN----LFILPASQTRDKDALT---------------------REGVEKVISGLTDMG 113
Cdd:cd03110   74 rvckfgAILEFFQklivdeslCEGcgacVIICPRGAIYLKDRDTgkifisssdggplvhgrlnigEENSGKLVTELRKKA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 499312472 114 FE------YIVCDSPAGIESGALMAMYFADEAIVVTNPEVSSVRDSDRIL 157
Cdd:cd03110  154 LErskecdLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAI 203
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 3-37 2.88e-08

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: 53.28  E-value: 2.88e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 499312472   3 KIIVVTsGKGGVGKTTTSAAFSAGLALRGHKTAVI 37
Cdd:cd02035    1 RIIFFG-GKGGVGKTTIAAATAVRLAEQGKRVLLV 34
ParA_partition NF041546
ParA family partition ATPase;
4-40 6.28e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 51.78  E-value: 6.28e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499312472   4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 5-238 1.44e-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: 51.16  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   5 IVVTsGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLrNLDLIMGCERRVVY-----DLI--NVIHGEANLNQALIKD 77
Cdd:cd02034    3 IAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS-NLAETLGVEVEKLPliktiGDIreRTGAKKGEPPEGMSLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  78 KKCENLFILPASQTRDKDALTREGVEKVISG---------------LTDMGFEYIVCDSPAGIE---SGALMAMyfaDEA 139
Cdd:cd02034   81 PYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGcycpvnallrellrhLALKNYEYVVIDMEAGIEhlsRGTIRAV---DLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 140 IVVTNPEVSSVRDSDRILGI---LSSKSRRAIEGKepiqehllltrynpkrVSEGEMLSLTDvQEILRIKLIGVIPESEA 216
Cdd:cd02034  158 IIVIEPSKRSIQTAKRIKELaeeLGIKKIYLIVNK----------------VRNEEEQELIE-ELLIKLKLIGVIPYDEE 220

                        250       260
                 ....*....|....*....|..
gi 499312472 217 VLQASNQGIPAIHLDGTDVAAA 238
Cdd:cd02034  221 IMEADLKGKPLFDLDSAAVKAI 242
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 2-144 3.86e-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: 49.46  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   2 TKIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDvGLRNLDLIMGCERR-----VVYDLINVIHGEANLNQALIK 76
Cdd:cd17869    3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFGASGRylmsdHLYTLKSRKANLADKLESCVK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499312472  77 DKKCENLFILPASQTRDKDALTREGVEKVISGLTDMG-FEYIVCDSPAGIESGALMAMYFADEAIVVTN 144
Cdd:cd17869   82 QHESGVYYFSPFKSALDILEIKKDDILHMITKLVEAHaYDYIIMDLSFEFSSTVCKLLQASHNNVVIAL 150
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 2-40 2.48e-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: 47.73  E-value: 2.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 499312472    2 TKIIVVTsGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:pfam02374   1 MRWIFFG-GKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-196 5.53e-06

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 46.98  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGlRNLDLIMGC-------ERRVVYDLINVIHGEANLNQaLI 75
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQ-ASLSALLGVlpetdvgANETLYAAIRYDDTRRPLRD-VI 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  76 KDKKCENLFILPAS-------QTRDK---DALTREGV--EKVISGLTDMGFEY--IVCDSPAGIESGALMAMYFADEAIV 141
Cdd:PRK13869 200 RPTYFDGLHLVPGNlelmefeHTTPKalsDKGTRDGLffTRVAQAFDEVADDYdvVVIDCPPQLGFLTLSGLCAATSMVI 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499312472 142 VTNPEVSSVRDSDRILGILSSKSRRAIEGKEPIQEHL---LLTRYNPKRVSEGEMLSL 196
Cdd:PRK13869 280 TVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFiryLLTRYEPQDAPQTKVAAL 337
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-41 6.15e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 46.96  E-value: 6.15e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499312472   4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDV 41
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 4-40 7.87e-06

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: 46.51  E-value: 7.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 499312472    4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLD 142
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 5-33 2.33e-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: 45.46  E-value: 2.33e-05
                          10        20
                  ....*....|....*....|....*....
gi 499312472    5 IVVTSGKGGVGKTTTSAAFSAGLALRGHK 33
Cdd:TIGR04291 323 LIMTMGKGGVGKTTVAAAIAVRLANKGLD 351
PHA02518 PHA02518
ParA-like protein; Provisional
 3-40 2.72e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 44.07  E-value: 2.72e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499312472   3 KIIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD 38
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-33 1.66e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.26  E-value: 1.66e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 499312472   1 MTKIIVVTsGKGGVGKTTTSAAFSAGLALRGHK 33
Cdd:PRK13185   1 MALVLAVY-GKGGIGKSTTSSNLSAAFAKLGKK 32
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 4-40 2.37e-04

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: 41.67  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 499312472    4 IIVVTSGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 13-85 3.52e-04

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


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 41.17  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   13 GVGKTTTSAAFSAGLALR--GHKTAVIDFD---VG----LRNLDLIMGCERRVVYDlinvihgEANLNQALIKDKKCENL 83
Cdd:TIGR03499 204 GVGKTTTLAKLAARFALEhgKKKVALITTDtyrIGaveqLKTYAEILGIPVKVARD-------PKELREALDRLRDKDLI 276


                  ..
gi 499312472   84 FI 85
Cdd:TIGR03499 277 LI 278
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 3-240 5.54e-04

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: 40.43  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472   3 KIIVVTsGKGGVGKTTTSAAFSAGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYD--LINVIHGEANLNQALIKDKK- 79
Cdd:cd02117    1 ESIVVY-GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIDemLTEDGTAEELRREDLLFSGFn 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  80 ---------------CENLFILPASQTRDKDALTREGVEKVI-SGLTDmgfeyIVCDSPAgiesgALMAMYFADEAIVVT 143
Cdd:cd02117   80 gvdcveaggpepgvgCGGRGIGTMLELLEEHGLLDDDYDVVIfDVLGD-----VVCGGFA-----APLRRGFAQKVVIVV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472 144 NPEVSSVRDSDRILGILSSKSRRAIegkepiqeHLLLTRYNPKRVSEGEMLSltDVQEILRIKLIGVIPESEAVLQASNQ 223
Cdd:cd02117  150 SEELMSLYAANNIVKAVENYSKNGV--------RLAGLVANLRDPAGTEEIQ--AFAAAVGTKILAVIPRDPAVRRAELA 219

                        250
                 ....*....|....*...
gi 499312472 224 GIPAIHLD-GTDVAAAYA 240
Cdd:cd02117  220 RVTVFEHDpVSPAASEFA 237
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 10-33 2.10e-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: 38.82  E-value: 2.10e-03
                         10        20
                 ....*....|....*....|....
gi 499312472  10 GKGGVGKTTTSAAFSAGLALRGHK 33
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKK 30
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 10-37 2.50e-03

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: 38.65  E-value: 2.50e-03
                         10        20
                 ....*....|....*....|....*...
gi 499312472  10 GKGGVGKTTTSAAFSAGLALRGHKTAVI 37
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHV 34
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
13-85 6.31e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 37.54  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499312472  13 GVGKTTTSAAFSAGLALRGHKT-AVIDFD---VG----LRNLDLIMGCERRVVYDlinvihgEANLNQALIKDKKCENLF 84
Cdd:COG1419  174 GVGKTTTIAKLAARFVLRGKKKvALITTDtyrIGaveqLKTYARILGVPVEVAYD-------PEELKEALERLRDKDLVL 246


                 .
gi 499312472  85 I 85
Cdd:COG1419  247 I 247
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-40 6.64e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 37.42  E-value: 6.64e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 499312472   10 GKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCD 37
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 9-40 9.12e-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: 37.17  E-value: 9.12e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499312472   9 SGKGGVGKTTTSAAFSAGLALRGHKTAVIDFD 40
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTD 370
 
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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