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Conserved domains on  [gi|1417949075|gb|AWY56412|]
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septum site-determining protein MinD [Burkholderia gladioli pv. gladioli]

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 1.02e-169

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


:

Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.15  E-value: 1.02e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLiAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894    81 ENLYLLPASQTRDKDALTPEQMKKLVEEL-KEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 ASKTKRaadggdpiKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:COG2894   160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231
                         250       260
                  ....*....|....*....|....*..
gi 1417949075 241 DVVSRFLGEEKTMRFVDYSKPGLLQRL 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 1.02e-169

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.15  E-value: 1.02e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLiAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894    81 ENLYLLPASQTRDKDALTPEQMKKLVEEL-KEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 ASKTKRaadggdpiKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:COG2894   160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231
                         250       260
                  ....*....|....*....|....*..
gi 1417949075 241 DVVSRFLGEEKTMRFVDYSKPGLLQRL 267
Cdd:COG2894   232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-269 6.06e-157

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 437.45  E-value: 6.06e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLIAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818   81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 ASKTKRAADGGDPIKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:PRK10818  161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240
                         250       260
                  ....*....|....*....|....*....
gi 1417949075 241 DVVSRFLGEEKTMRFVDYSKPGLLQRLFG 269
Cdd:PRK10818  241 DTVDRLLGEERPFRFIEEEKKGFLKRLFG 269
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-271 4.35e-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: 4.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCE 81
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  82 NLFILPASQTRDKDALTREGVEKVINDLIAmDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILA 161
Cdd:TIGR01968  81 NLYLLPASQTRDKDAVTPEQMKKLVNELKE-EFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 162 SKTKRaadggdpiKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYKD 241
Cdd:TIGR01968 160 AKGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFEN 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1417949075 242 VVSRFLGEEKTMRFVDYSKPGLLQRLFGSK 271
Cdd:TIGR01968 232 IARRILGEEVPFEDLTTQKKGFFARIKRFF 261
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
3-246 3.00e-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: 348.04  E-value: 3.00e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCEN 82
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  83 LFILPASQTRDKDALTREGVEKVINDLIAMdFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILAS 162
Cdd:cd02036    81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 163 KtkraadggDPIKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDG-TDVAEAYKD 241
Cdd:cd02036   160 K--------GIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPnSLAAKAFEN 231

                  ....*
gi 1417949075 242 VVSRF 246
Cdd:cd02036   232 IARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-226 4.59e-40

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: 138.63  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   5 IVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  82 NLFILPA---SQTRDKDALTREGVEKVINDL--IAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALeaLKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417949075 157 LGILAS-KTKRAADGGDPIKehLLITRYNPKRVSEGEMLSLEDIgeILRIKLIGVIPESEAVLHASNQGLP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIG--VVLNKVDGDNHGKLLKEALEEL--LRGLPVLGVIPRDEAVAEAPARGLP 227
ParA_partition NF041546
ParA family partition ATPase;
4-182 9.12e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 54.10  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVglrnldlimgcerrvvydlvnviQGEAnlnqalikdkkcenl 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSA--------------- 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  84 fiLPASQTRDKD------ALTREGVEKVINDLiAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRIL 157
Cdd:NF041546   43 --LDWAAAREDErpfpvvGLARPTLHRELPSL-ARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119
                         170       180
                  ....*....|....*....|....*
gi 1417949075 158 GILasktKRAADGGDPIKEHLLITR 182
Cdd:NF041546  120 DLI----KEAREYTPGLKAAFVLNR 140
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
9-189 1.69e-04

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: 42.56  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   9 SGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGlRNLDLIMGceRRVVYDLVNViqGEANLNQALIKDKKCenlfiLPA 88
Cdd:NF041417  339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPA-SHLQDIFG--TEVGHEPTKV--GVENLYAARIDQERA-----LEE 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  89 SQTRDKDALTREGVEKVINDLIAMDFAYIVCDSPAGIESGALHAM--YFADEA--VVV--TNPEVSSVR----DSD-RIL 157
Cdd:NF041417  409 YKTRMLDQVEQSFDKDQIDVEAAKAQVREELESPCAEEMAALEKFvsYFDVDGydVVVfdTAPTGHTLRllelPSDwKGF 488
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1417949075 158 GILASKTKRAADGGDPIKEHLLITRYNPKRVS 189
Cdd:NF041417  489 MDLGSLTKEASDVTGDKYDRVIETMRDPERST 520
 
Name Accession Description Interval E-value
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
1-267 1.02e-169

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 469.15  E-value: 1.02e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:COG2894     1 MGKVIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADIGLRNLDLVMGLENRIVYDLVDVIEGECRLKQALIKDKRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLiAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:COG2894    81 ENLYLLPASQTRDKDALTPEQMKKLVEEL-KEEFDYILIDSPAGIEQGFKNAIAGADEAIVVTTPEVSSVRDADRIIGLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 ASKTKRaadggdpiKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:COG2894   160 EAKGIR--------KPHLIINRYRPAMVKRGDMLSVEDVLEILAIPLLGVVPEDEEVIVSSNRGEPVVLDEKSKAGQAYR 231
                         250       260
                  ....*....|....*....|....*..
gi 1417949075 241 DVVSRFLGEEKTMRFVDYSKPGLLQRL 267
Cdd:COG2894   232 NIARRLLGEEVPLRDLEEEKKGFFSRL 258
PRK10818 PRK10818
septum site-determining protein MinD;
1-269 6.06e-157

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 437.45  E-value: 6.06e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:PRK10818    1 MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLIAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:PRK10818   81 ENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 ASKTKRAADGGDPIKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:PRK10818  161 ASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDIEADAGKAYA 240
                         250       260
                  ....*....|....*....|....*....
gi 1417949075 241 DVVSRFLGEEKTMRFVDYSKPGLLQRLFG 269
Cdd:PRK10818  241 DTVDRLLGEERPFRFIEEEKKGFLKRLFG 269
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-271 4.35e-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: 4.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCE 81
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYTLVDVVEGECRLQQALIKDKRLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  82 NLFILPASQTRDKDALTREGVEKVINDLIAmDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILA 161
Cdd:TIGR01968  81 NLYLLPASQTRDKDAVTPEQMKKLVNELKE-EFDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVRDADRVIGLLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 162 SKTKRaadggdpiKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAEAYKD 241
Cdd:TIGR01968 160 AKGIE--------KIHLIVNRLRPEMVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEPVVLNDKSRAGKAFEN 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1417949075 242 VVSRFLGEEKTMRFVDYSKPGLLQRLFGSK 271
Cdd:TIGR01968 232 IARRILGEEVPFEDLTTQKKGFFARIKRFF 261
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
3-246 3.00e-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: 348.04  E-value: 3.00e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCEN 82
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQALIKDKRWEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  83 LFILPASQTRDKDALTREGVEKVINDLIAMdFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILAS 162
Cdd:cd02036    81 LYLLPASQTRDKDALTPEKLEELVKELKDS-FDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVRDADRVIGLLES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 163 KtkraadggDPIKEHLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDG-TDVAEAYKD 241
Cdd:cd02036   160 K--------GIVNIGLIVNRYRPEMVKSGDMLSVEDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKPnSLAAKAFEN 231

                  ....*
gi 1417949075 242 VVSRF 246
Cdd:cd02036   232 IARRL 236
minD CHL00175
septum-site determining protein; Validated
1-268 2.31e-78

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 238.52  E-value: 2.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQGEANLNQALIKDKKC 80
Cdd:CHL00175   14 MSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLEGECRLDQALIRDKRW 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ENLFILPASQTRDKDALTREGVEKVINDLIAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:CHL00175   94 KNLSLLAISKNRQRYNVTRKNMNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPEITAIRDADRVAGLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 161 asktkrAADGGDPIKehLLITRYNPKRVSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTDVAE-AY 239
Cdd:CHL00175  174 ------EANGIYNVK--LLVNRVRPDMIQANDMMSVRDVQEMLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGiAF 245
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1417949075 240 KDVVSRFLGEEKtmRFVDYSKP--GLLQRLF 268
Cdd:CHL00175  246 ENAARRLVGKQD--YFIDLDSPskGPLKRLQ 274
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
5-226 4.59e-40

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: 138.63  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   5 IVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNL--DLIMGCERRVVYDLVNVIQGEANLNQALIKDKKCE- 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsvEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  82 NLFILPA---SQTRDKDALTREGVEKVINDL--IAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRI 156
Cdd:pfam01656  81 GLDLIPGnidLEKFEKELLGPRKEERLREALeaLKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417949075 157 LGILAS-KTKRAADGGDPIKehLLITRYNPKRVSEGEMLSLEDIgeILRIKLIGVIPESEAVLHASNQGLP 226
Cdd:pfam01656 161 GGVIAAlVGGYALLGLKIIG--VVLNKVDGDNHGKLLKEALEEL--LRGLPVLGVIPRDEAVAEAPARGLP 227
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
3-250 5.42e-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: 131.39  E-value: 5.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVyDLVNVIQGEANLNQALIKDKkcEN 82
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPV-TLHDVLAGEADIKDAIYEGP--FG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  83 LFILPAsqtrdkdALTREGVEKVINDL-------IAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDR 155
Cdd:TIGR01969  78 VKVIPA-------GVSLEGLRKADPDKledvlkeIIDDTDFLLIDAPAGLERDAVTALAAADELLLVVNPEISSITDALK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 156 IlGILASKTKRAADGgdpikehLLITRYNpkrvSEGEMLSLEDIGEILRIKLIGVIPESEAVLHASNQGLPAVHLDGTD- 234
Cdd:TIGR01969 151 T-KIVAEKLGTAILG-------VVLNRVT----RDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSp 218
                         250
                  ....*....|....*.
gi 1417949075 235 VAEAYKDVVSRFLGEE 250
Cdd:TIGR01969 219 AAQAFMELAAELAGIE 234
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
2-252 2.31e-35

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: 129.85  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALR-GHKTAVIDFDVGLRNLDLIMGCERRvvYDLVNVIQGEANLNQALIKD--K 78
Cdd:COG4963   102 GRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPR--RGLADALRNPDRLDETLLDRalT 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  79 KCE-NLFILPASQTRDK-DALTREGVEKVInDLIAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRI 156
Cdd:COG4963   180 RHSsGLSVLAAPADLERaEEVSPEAVERLL-DLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPDLPSLRNAKRL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 157 LGILASKtkraadGGDPIKEHLLITRYNPKRvsegeMLSLEDIGEILRIKLIGVIP-ESEAVLHASNQGLPAVHLD-GTD 234
Cdd:COG4963   259 LDLLREL------GLPDDKVRLVLNRVPKRG-----EISAKDIEEALGLPVAAVLPnDPKAVAEAANQGRPLAEVApKSP 327
                         250
                  ....*....|....*...
gi 1417949075 235 VAEAYKDVVSRFLGEEKT 252
Cdd:COG4963   328 LAKAIRKLAARLTGRPAA 345
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
2-251 1.42e-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: 122.27  E-value: 1.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDV-GlrNLDLIMGCERRVV-YDLVNVIQGEANLNQAlIKDKK 79
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqG--NLTSGLGLDPDDLdPTLYDLLLDDAPLEDA-IVPTE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  80 CENLFILPASQ---TRDKDALTREGVEKVINDLIAM---DFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDS 153
Cdd:COG1192    78 IPGLDLIPANIdlaGAEIELVSRPGRELRLKRALAPladDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 154 DRILGILasKTKRAADGGDPIKEHLLITRYNPKRVSEGEMlsLEDIGEILRIKLIG-VIPESEAVLHASNQGLPAVHLD- 231
Cdd:COG1192   158 AQLLETI--EEVREDLNPKLEILGILLTMVDPRTRLSREV--LEELREEFGDKVLDtVIPRSVALAEAPSAGKPVFEYDp 233
                         250       260
                  ....*....|....*....|
gi 1417949075 232 GTDVAEAYKDVVSRFLGEEK 251
Cdd:COG1192   234 KSKGAKAYRALAEELLERLE 253
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
18-250 4.93e-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: 112.68  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  18 TTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRvvYDLVNVIQGEANLNQALIKDKkcENLFILPASQ--TRDKD 95
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPK--ATLADVLAGEADLEDAIVQGP--GGLDVLPGGSgpAELAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  96 ALTREGVEKVINDLIAmDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILasktkRAADGGDPIk 175
Cdd:COG0455    77 LDPEERLIRVLEELER-FYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLL-----RRRLGVRRA- 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1417949075 176 eHLLITRYNPKRVSEGEMLSLED-IGEIL--RIKLIGVIPESEAVLHASNQGLPAVHLD-GTDVAEAYKDVVSRFLGEE 250
Cdd:COG0455   150 -GVVVNRVRSEAEARDVFERLEQvAERFLgvRLRVLGVIPEDPAVREAVRRGRPLVLAApDSPAARAIRELAARLAGWP 227
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
3-217 1.43e-25

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: 100.72  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRvvYDLVNVIQGEANLNQALIKDKkcEN 82
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK--KTLGDVLKGRVSLEDIIVEGP--EG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  83 LFILPASQ-TRDKDALTREGVEKVINDL--IAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGI 159
Cdd:cd02038    77 LDIIPGGSgMEELANLDPEQKAKLIEELssLESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPEPTSITDAYALIKV 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1417949075 160 LASKtkraaDGGDPIkeHLLITRYnpKRVSEGemlslEDIGEIL----------RIKLIGVIPESEAV 217
Cdd:cd02038   157 LSRR-----GGKKNF--RLIVNMA--RSPKEG-----RATFERLkkvakrfldiNLDFVGFIPYDQSV 210
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
3-226 8.01e-23

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: 93.50  E-value: 8.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALR-GHKTAVIDFDVGLRNLDLIMGCERRvvYDLVNVIQGEANLNQALIKD--KK 79
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPD--YDLADVIQNLDRLDRTLLDSavTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  80 CEN-LFILPASQTRDK-DALTREGVEKVInDLIAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRIL 157
Cdd:cd03111    79 HSSgLSLLPAPQELEDlEALGAEQVDKLL-QVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 158 GILasktKRAADGGDPIkeHLLITRYNPKrvSEgemLSLEDIGEILRIKLIGVIP-ESEAVLHASNQGLP 226
Cdd:cd03111   158 DSL----RELEGSSDRL--RLVLNRYDKK--SE---ISPKDIEEALGLEVFATLPnDYKAVSESANTGRP 216
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
4-162 4.18e-22

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: 92.94  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVvyDLVNVIQGEANLNQALIKDKKcENL 83
Cdd:COG0489    94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP--GLSDVLAGEASLEDVIQPTEV-EGL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  84 FILPASQTRDKDA--LTREGVEKVINDLIAmDFAYIVCDSPAGIE-SGALHAMYFADEAVVVTNPEVSSVRDSDRILGIL 160
Cdd:COG0489   171 DVLPAGPLPPNPSelLASKRLKQLLEELRG-RYDYVIIDTPPGLGvADATLLASLVDGVLLVVRPGKTALDDVRKALEML 249

                  ..
gi 1417949075 161 AS 162
Cdd:COG0489   250 EK 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-146 1.39e-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: 75.31  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLrNLDLIMGCERRVVY-DLVNVIQGEANLNQALIKDKKc 80
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQG-NATSGLGIDKNNVEkTIYELLIGECNIEEAIIKTVI- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1417949075  81 ENLFILPAS-----------QTRDKDALTREGVEKVINdliamDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPE 146
Cdd:pfam13614  79 ENLDLIPSNidlagaeieliGIENRENILKEALEPVKD-----NYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
2-160 3.94e-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: 3.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDvgLRN--LDLIMGCERRVvyDLVNVIQGEANLNQAlIKDKK 79
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDAD--LRRpsLHRLLGLPNEP--GLSEVLSGQASLEDV-IQSTN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  80 CENLFILPASQTRDK--DALTREGVEKVINDLiAMDFAYIVCDSPA-GIESGALHAMYFADEAVVVTNPEVSSVRDSDRI 156
Cdd:cd05387    94 IPNLDVLPAGTVPPNpsELLSSPRFAELLEEL-KEQYDYVIIDTPPvLAVADALILAPLVDGVLLVVRAGKTRRREVKEA 172

                  ....
gi 1417949075 157 LGIL 160
Cdd:cd05387   173 LERL 176
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-194 3.07e-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: 64.87  E-value: 3.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDvglrnldlimgcerrvvydlvnvIQGeaNLNQALikdkkcen 82
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD-----------------------PQG--SLTSWL-------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  83 lfilpasqtrdkdaltregvekvindliamdFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILGILas 162
Cdd:cd02042    48 -------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTL-- 94
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1417949075 163 KTKRAADGGDPIKEHLLITRYNPKRVSEGEML 194
Cdd:cd02042    95 EELKKQLNPPLLILGILLTRVDPRTKLAREVL 126
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
3-245 1.03e-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: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVvtSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLrNLDLIMGCErrVVYDLVNVIqGEanlNQALIKDKKC-- 80
Cdd:COG3640     2 KIAV--AGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNA-NLAEALGLE--VEADLIKPL-GE---MRELIKERTGap 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  81 ------ENLFI--LPASQTRDKD--------ALTREG----------VEKVINDLIAMDFAYIVCDSPAGIESgalhamy 134
Cdd:COG3640    73 gggmfkLNPKVddIPEEYLVEGDgvdllvmgTIEEGGsgcycpenalLRALLNHLVLGNYEYVVVDMEAGIEH------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 135 FA-------DEAVVVTNPEVSSVRDSDRILGIlasktkrAADGGdpIKEHLLITryNpkRVSEGEMLslEDIGEILRIKL 207
Cdd:COG3640   146 LGrgtaegvDLLLVVSEPSRRSIETARRIKEL-------AEELG--IKKIYLVG--N--KVREEEDE--EFLRELLGLEL 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1417949075 208 IGVIPESEAVLHASNQGLPAVHLDGTDVAEAYKDVVSR 245
Cdd:COG3640   211 LGFIPYDEEVREADLEGKPLLDLPDSPAVAAVEEIAEK 248
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
3-146 1.11e-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: 59.76  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDvgLRN-LDLIMGCERRVVYDLVNVIQGEANLNQAlIKDKKCE 81
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGD--MRNsVMSGTFKSQNKITGLTNFLSGTTDLSDA-ICDTNIE 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1417949075  82 NLFILPASQTR-DKDALTREGVEKVINDLIAMDFAYIVCDS-PAGIESGALHAMYFADEAVVVTNPE 146
Cdd:TIGR01007  95 NLDVITAGPVPpNPTELLQSSNFKTLIETLRKRFDYIIIDTpPIGTVTDAAIIARACDASILVTDAG 161
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
2-229 2.30e-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: 59.28  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   2 AKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDV----------------GLRNLDLIMGCERRVVYDLVN--- 62
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPqnllrlhfgmdwsvrdGWARALLNGADWAAAAYRSPDgvl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  63 -VIQGEANLNQALikdkkcenlfilpASQTRDKDALTREgVEKVinDLIAMDFAYIvcDSPAGIESGALHAMYFADEAVV 141
Cdd:TIGR03371  81 fLPYGDLSADERE-------------AYQAHDAGWLARL-LQQL--DLAARDWVLI--DLPRGPSPITRQALAAADLVLV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 142 VTNPEVSSVRDSDRILGILasktkrAADGGDPIKEHLLITRYNPKRVSEGEMLSL--EDIGEILrikLIGVIPESEAVLH 219
Cdd:TIGR03371 143 VVNADAACYATLHQLALAL------FAGSGPRDGPRFLINQFDPARQLSRDVRAVlrQTLGSRL---LPFVIHRDEAVSE 213
                         250
                  ....*....|
gi 1417949075 220 ASNQGLPAVH 229
Cdd:TIGR03371 214 ALARGTPVLN 223
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
3-41 6.43e-10

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: 57.85  E-value: 6.43e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDV 41
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADI 42
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
3-59 7.60e-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: 57.51  E-value: 7.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGCERRVVYD 59
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ 57
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 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLAlrghKTAVIDFDVGLRNLDLIMGCERRVVYDLVNVIQgeANLNQ----------- 72
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLLY----NVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKK--AFIDQekcircgncer 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  73 -----ALIKDKK--------CEN----LFILPASQTRDKDALT---------------------REGVEKVINDLI---- 110
Cdd:cd03110    75 vckfgAILEFFQklivdeslCEGcgacVIICPRGAIYLKDRDTgkifisssdggplvhgrlnigEENSGKLVTELRkkal 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 111 --AMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRILgilasktKRAADGGDPIKehLLITRY--NPK 186
Cdd:cd03110   155 erSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAI-------ELAKHFGIPTG--IVINRYdiNDE 225
                         250       260
                  ....*....|....*....|....*.
gi 1417949075 187 RVSEgemlsLEDIGEILRIKLIGVIP 212
Cdd:cd03110   226 ISEE-----IEDFADEEGIPLLGKIP 246
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
1-53 3.59e-09

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 56.37  E-value: 3.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1417949075   1 MAKIIVVTsGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGlRNLDLIMGCE 53
Cdd:COG0003     2 MTRIIFFT-GKGGVGKTTVAAATALALAERGKRTLLVSTDPA-HSLGDVLGTE 52
ParA_partition NF041546
ParA family partition ATPase;
4-182 9.12e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 54.10  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVglrnldlimgcerrvvydlvnviQGEAnlnqalikdkkcenl 83
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADP-----------------------QGSA--------------- 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  84 fiLPASQTRDKD------ALTREGVEKVINDLiAMDFAYIVCDSPAGIESGALHAMYFADEAVVVTNPEVSSVRDSDRIL 157
Cdd:NF041546   43 --LDWAAAREDErpfpvvGLARPTLHRELPSL-ARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTV 119
                         170       180
                  ....*....|....*....|....*
gi 1417949075 158 GILasktKRAADGGDPIKEHLLITR 182
Cdd:NF041546  120 DLI----KEAREYTPGLKAAFVLNR 140
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
3-40 9.28e-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: 9.28e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
3-37 1.62e-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: 54.05  E-value: 1.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1417949075   3 KIIVVTsGKGGVGKTTTSASFASGLALRGHKTAVI 37
Cdd:cd02035     1 RIIFFG-GKGGVGKTTIAAATAVRLAEQGKRVLLV 34
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
5-240 1.19e-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: 51.54  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   5 IVVTsGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLrNLDLIMGCERrvvyDLVNVIQGEANLNQALIKDKKCE-NL 83
Cdd:cd02034     3 IAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNS-NLAETLGVEV----EKLPLIKTIGDIRERTGAKKGEPpEG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  84 FILpasQTRDKDALTREGVEKVINDLIAM----------------------------DFAYIVCDSPAGIE---SGALHA 132
Cdd:cd02034    77 MSL---NPYVDDIIKEIIVEPDGIDLLVMgrpegggsgcycpvnallrellrhlalkNYEYVVIDMEAGIEhlsRGTIRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075 133 MyfaDEAVVVTNPEVSSVRDSDRILGiLASKTkraadggdPIKEHLLITRYNPKRVSEGEMLSLedigeILRIKLIGVIP 212
Cdd:cd02034   154 V---DLLIIVIEPSKRSIQTAKRIKE-LAEEL--------GIKKIYLIVNKVRNEEEQELIEEL-----LIKLKLIGVIP 216
                         250       260
                  ....*....|....*....|....*...
gi 1417949075 213 ESEAVLHASNQGLPAVHLDGTDVAEAYK 240
Cdd:cd02034   217 YDEEIMEADLKGKPLFDLDSAAVKAIEK 244
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
3-144 1.66e-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: 50.62  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDvGLRNLDLIMGCERR-----VVYDLVNVIQGEANLNQALIKD 77
Cdd:cd17869     4 SVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNME-RLQSTDVFFGASGRylmsdHLYTLKSRKANLADKLESCVKQ 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1417949075  78 KKCENLFILPASQTRDKDALTREGVEKVINDLIAMD-FAYIVCDSPAGIESGALHAMYFADEAVVVTN 144
Cdd:cd17869    83 HESGVYYFSPFKSALDILEIKKDDILHMITKLVEAHaYDYIIMDLSFEFSSTVCKLLQASHNNVVIAL 150
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
3-196 2.41e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 51.21  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGlRNLDLIMGC-------ERRVVYDLVNVIQGEANLNQaLI 75
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQ-ASLSALLGVlpetdvgANETLYAAIRYDDTRRPLRD-VI 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  76 KDKKCENLFILPAS-------QTRDK---DALTREG-----VEKVINDlIAMDFAYIVCDSPAGIESGALHAMYFADEAV 140
Cdd:PRK13869  200 RPTYFDGLHLVPGNlelmefeHTTPKalsDKGTRDGlfftrVAQAFDE-VADDYDVVVIDCPPQLGFLTLSGLCAATSMV 278
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1417949075 141 VVTNPEVSSVRDSDRILGILASKTKRAADGGDPIKEHL---LITRYNPKRVSEGEMLSL 196
Cdd:PRK13869  279 ITVHPQMLDIASMSQFLLMTRDLLGVVKEAGGNLQYDFiryLLTRYEPQDAPQTKVAAL 337
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
4-41 7.39e-07

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 49.66  E-value: 7.39e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDV 41
Cdd:PRK11670  109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
PHA02518 PHA02518
ParA-like protein; Provisional
3-40 8.45e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 48.69  E-value: 8.45e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1417949075   3 KIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD 38
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
4-40 1.07e-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: 49.21  E-value: 1.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLD 142
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
3-40 4.93e-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: 46.96  E-value: 4.93e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1417949075   3 KIIVVTsGKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:pfam02374   2 RWIFFG-GKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
5-33 2.29e-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: 2.29e-05
                          10        20
                  ....*....|....*....|....*....
gi 1417949075   5 IVVTSGKGGVGKTTTSASFASGLALRGHK 33
Cdd:TIGR04291 323 LIMTMGKGGVGKTTVAAAIAVRLANKGLD 351
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
4-144 4.32e-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: 43.98  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   4 IIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGLRNLDLIMGcerrvvydlvNVIQGEANLNQALiKDKKCENL 83
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFE----------NRSATADRTGLSL-PTPEHLNL 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1417949075  84 FILPASQTRDKDALTREGVEKVINDLIAmDFAYIVCDSPAGIESGALHAMYFADEAVVVTN 144
Cdd:pfam09140  71 PDNDVAEVPDGENIDDARLEEAFADLEA-RCDFIVIDTPGSDSPLSRLAHSRADTLVTPLN 130
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
13-85 1.38e-04

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


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 42.32  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  13 GVGKTTTSASFASGLALR--GHKTAVIDFD---VG----LRNLDLIMGCERRVVYDlvnviqgEANLNQALIKDKKCENL 83
Cdd:TIGR03499 204 GVGKTTTLAKLAARFALEhgKKKVALITTDtyrIGaveqLKTYAEILGIPVKVARD-------PKELREALDRLRDKDLI 276

                  ..
gi 1417949075  84 FI 85
Cdd:TIGR03499 277 LI 278
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
9-189 1.69e-04

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: 42.56  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075   9 SGKGGVGKTTTSASFASGLALRGHKTAVIDFDVGlRNLDLIMGceRRVVYDLVNViqGEANLNQALIKDKKCenlfiLPA 88
Cdd:NF041417  339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPA-SHLQDIFG--TEVGHEPTKV--GVENLYAARIDQERA-----LEE 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  89 SQTRDKDALTREGVEKVINDLIAMDFAYIVCDSPAGIESGALHAM--YFADEA--VVV--TNPEVSSVR----DSD-RIL 157
Cdd:NF041417  409 YKTRMLDQVEQSFDKDQIDVEAAKAQVREELESPCAEEMAALEKFvsYFDVDGydVVVfdTAPTGHTLRllelPSDwKGF 488
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1417949075 158 GILASKTKRAADGGDPIKEHLLITRYNPKRVS 189
Cdd:NF041417  489 MDLGSLTKEASDVTGDKYDRVIETMRDPERST 520
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
1-33 7.47e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.95  E-value: 7.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1417949075   1 MAKIIVVTsGKGGVGKTTTSASFASGLALRGHK 33
Cdd:PRK13185    1 MALVLAVY-GKGGIGKSTTSSNLSAAFAKLGKK 32
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
13-85 1.04e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.85  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417949075  13 GVGKTTTSASFASGLALRGHKT-AVIDFD---VG----LRNLDLIMGCERRVVYDlvnviqgEANLNQALIKDKKCENLF 84
Cdd:COG1419   174 GVGKTTTIAKLAARFVLRGKKKvALITTDtyrIGaveqLKTYARILGVPVEVAYD-------PEELKEALERLRDKDLVL 246

                  .
gi 1417949075  85 I 85
Cdd:COG1419   247 I 247
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
1-40 1.06e-03

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 39.71  E-value: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1417949075   1 MAKIIVVTSGKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:PRK13886    1 MAKIHMVLQGKGGVGKSFIAATIAQYKASKGQKPLCIDTD 40
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
1-47 9.54e-03

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 36.54  E-value: 9.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1417949075   1 MAKIIVVTsGKGGVGKTTTSASFAsglalrghKTAVIDFDVGLRNLD 47
Cdd:pfam13479   1 KKLKILIY-GPSGIGKTTFAKTLP--------KPLFLDTEKGSKALD 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
10-40 9.98e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 36.65  E-value: 9.98e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1417949075  10 GKGGVGKTTTSASFASGLALRGHKTAVIDFD 40
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCD 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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