NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|189054996|dbj|BAG37980|]
View 

unnamed protein product [Homo sapiens]

Protein Classification

Mrp/NBP35 family ATP-binding protein( domain architecture ID 10566257)

Mrp (multiple resistance and pH adaptation)/NBP35 (nucleotide-binding protein 35) family ATP-binding protein is an iron-sulfur (FeS) cluster protein that functions as a scaffold to assemble nascent FeS clusters for transfer to FeS-requiring enzymes

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005524|GO:0051536|GO:0140663|GO:0016226|GO:0016887
PubMed:  8921898

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 12-263 1.61e-141

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: 397.21  E-value: 1.61e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   12 GVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   92 VGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALrpyqPL-GALVVTTPQAVSVGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  171 RRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSP 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 189054996  251 AFAALTSIAQKIL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 12-263 1.61e-141

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: 397.21  E-value: 1.61e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   12 GVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   92 VGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALrpyqPL-GALVVTTPQAVSVGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  171 RRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSP 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 189054996  251 AFAALTSIAQKIL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 15-233 1.10e-125

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: 356.04  E-value: 1.10e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  15 HIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGF 94
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  95 LLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYqplGALVVTTPQAVSVGDVRREL 174
Cdd:cd02037   78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189054996 175 TFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALM 233
Cdd:cd02037  154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
10-266 1.69e-118

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 343.72  E-value: 1.69e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  10 LAGVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreQSISL 89
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYS--DNLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  90 MSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALrpyqPL-GALVVTTPQAVSVG 168
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 169 DVRRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPG 248
Cdd:NF041136 155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....*...
gi 189054996 249 SPAFAALTSIAQKILDAT 266
Cdd:NF041136 235 SPAAKALEKIVDPILELL 252
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
12-239 1.65e-58

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 190.25  E-value: 1.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  12 GVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQG-RAVHQCDRGWAPVFLdreQSISLM 90
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDqRPTSPDGTHMAPIMA---HGLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  91 SVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMaTIEALRPYQplGALVVTTPQAVSVGDV 170
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189054996 171 RRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEG 239
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRG 326
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-191 4.28e-40

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: 140.32  E-value: 4.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   9 NLAGVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRA----VHQCDRGWAPVFL-DR 83
Cdd:COG0489   87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPglsdVLAGEASLEDVIQpTE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  84 EQSISLMSVGFLLEKPDEAVVwrgpkkNALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATIealrpyQPL--GALVVTT 161
Cdd:COG0489  167 VEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL------ASLvdGVLLVVR 233

                        170       180       190
                 ....*....|....*....|....*....|
gi 189054996 162 PQAVSVGDVRRELTFCRKMGLRVMGIVENM 191
Cdd:COG0489  234 PGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 16-263 1.63e-11

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: 62.74  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVH--------QCDRGWAPVFLDREQSI 87
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvegECRLQQALIKDKRLKNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   88 SLMSVGFLLEKpdEAVVWRGPKK--NALIKQFvsdvawgelDYLVVDTPPGtsdehmatIE-----ALRPYQplGALVVT 160
Cdd:TIGR01968  83 YLLPASQTRDK--DAVTPEQMKKlvNELKEEF---------DYVIIDCPAG--------IEsgfrnAVAPAD--EAIVVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  161 TPQAVSVGDVRreltfcrkmglRVMGIVENmSGFTCPHCT------------ECTSVfsrgggEELAQLAGVPFLGSVPL 228
Cdd:TIGR01968 142 TPEVSAVRDAD-----------RVIGLLEA-KGIEKIHLIvnrlrpemvkkgDMLSV------DDVLEILSIPLIGVIPE 203

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 189054996  229 DPALMRTLEEGHDFIQEfPGSPAFAALTSIAQKIL 263
Cdd:TIGR01968 204 DEAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 12-263 1.61e-141

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: 397.21  E-value: 1.61e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   12 GVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   92 VGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALrpyqPL-GALVVTTPQAVSVGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  171 RRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSP 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 189054996  251 AFAALTSIAQKIL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 15-233 1.10e-125

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: 356.04  E-value: 1.10e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  15 HIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGF 94
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  95 LLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYqplGALVVTTPQAVSVGDVRREL 174
Cdd:cd02037   78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 189054996 175 TFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALM 233
Cdd:cd02037  154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
10-266 1.69e-118

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 343.72  E-value: 1.69e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  10 LAGVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDreQSISL 89
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYS--DNLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  90 MSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALrpyqPL-GALVVTTPQAVSVG 168
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 169 DVRRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPG 248
Cdd:NF041136 155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....*...
gi 189054996 249 SPAFAALTSIAQKILDAT 266
Cdd:NF041136 235 SPAAKALEKIVDPILELL 252
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
12-239 1.65e-58

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 190.25  E-value: 1.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  12 GVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQG-RAVHQCDRGWAPVFLdreQSISLM 90
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDqRPTSPDGTHMAPIMA---HGLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  91 SVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMaTIEALRPYQplGALVVTTPQAVSVGDV 170
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189054996 171 RRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEG 239
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRG 326
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-191 4.28e-40

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: 140.32  E-value: 4.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   9 NLAGVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRA----VHQCDRGWAPVFL-DR 83
Cdd:COG0489   87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPglsdVLAGEASLEDVIQpTE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  84 EQSISLMSVGFLLEKPDEAVVwrgpkkNALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATIealrpyQPL--GALVVTT 161
Cdd:COG0489  167 VEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL------ASLvdGVLLVVR 233

                        170       180       190
                 ....*....|....*....|....*....|
gi 189054996 162 PQAVSVGDVRRELTFCRKMGLRVMGIVENM 191
Cdd:COG0489  234 PGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 16-251 9.81e-21

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: 87.62  E-value: 9.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRavhqcdrgwapvfldreqsISLMSVgFL 95
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPK-------------------KTLGDV-LK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  96 LEKPDEAVVWRGPKKNALI-----------------KQFVSDV--AWGELDYLVVDTPPGTSDEhmaTIEALRPYQPLga 156
Cdd:cd02038   62 GRVSLEDIIVEGPEGLDIIpggsgmeelanldpeqkAKLIEELssLESNYDYLLIDTGAGISRN---VLDFLLAADEV-- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 157 LVVTTPQAVSVGDVRRELTFC-RKMGLRVMGIVENMsgftcphctectsVFSRGGGEELAQ-LAGV---------PFLGS 225
Cdd:cd02038  137 IVVTTPEPTSITDAYALIKVLsRRGGKKNFRLIVNM-------------ARSPKEGRATFErLKKVakrfldinlDFVGF 203

                        250       260
                 ....*....|....*....|....*.
gi 189054996 226 VPLDPALMRTLEEGHDFIQEFPGSPA 251
Cdd:cd02038  204 IPYDQSVRRAVRSQKPFVLLFPNSKA 229
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 30-265 1.71e-19

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: 84.56  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  30 TISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQ-GRAVHQCDRGWAP---VFLDREQSISLMSVGfllekPDEAVVW 105
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEpKATLADVLAGEADledAIVQGPGGLDVLPGG-----SGPAELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 106 RGPKKNALIKQFvsDVAWGELDYLVVDTPPGTSDEHMATIEAlrpyqplgA---LVVTTPQAVSVGDVRREL-TFCRKMG 181
Cdd:COG0455   76 ELDPEERLIRVL--EELERFYDVVLVDTGAGISDSVLLFLAA--------AdevVVVTTPEPTSITDAYALLkLLRRRLG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 182 LRVMGIVENMsgftcphctectsVFSRGGGEEL-AQLAGV---------PFLGSVPLDPALMRTLEEGHDFIQEFPGSPA 251
Cdd:COG0455  146 VRRAGVVVNR-------------VRSEAEARDVfERLEQVaerflgvrlRVLGVIPEDPAVREAVRRGRPLVLAAPDSPA 212

                        250
                 ....*....|....
gi 189054996 252 FAALTSIAQKILDA 265
Cdd:COG0455  213 ARAIRELAARLAGW 226
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 17-242 3.97e-18

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: 80.85  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   17 ILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD-------LCGPSIPRMLGAQGRAVHQCDRGW-APVFLD---REQ 85
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnnssVEGLEGDIAPALQALAEGLKGRVNlDPILLKeksDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   86 SISLMSVGFLLEKPDEavVWRGPKKNALIKQFVSDVAwGELDYLVVDTPPGTsdeHMATIEALRPYQplGALVVTTPQAV 165
Cdd:pfam01656  81 GLDLIPGNIDLEKFEK--ELLGPRKEERLREALEALK-EDYDYVIIDGAPGL---GELLRNALIAAD--YVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  166 SVGDVRRELTFCRKMG-------LRVMGIVENMsgftcphctectsVFSRGGGEELAQ-----LAGVPFLGSVPLDPALM 233
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK-------------VDGDNHGKLLKEaleelLRGLPVLGVIPRDEAVA 219


                  ....*....
gi 189054996  234 RTLEEGHDF 242
Cdd:pfam01656 220 EAPARGLPV 228
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 16-262 1.17e-16

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: 76.86  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVH--------QCDRGWAPVFLDREQSI 87
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYtlvdvlegECRLEQALIKDKRWENL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  88 SLMSVGFLLEKpDEAvvwrGPKKnalIKQFVSDVAwGELDYLVVDTPPGT-SDEHMATIEALRpyqplgALVVTTPQAVS 166
Cdd:cd02036   82 YLLPASQTRDK-DAL----TPEK---LEELVKELK-DSFDFILIDSPAGIeSGFINAIAPADE------AIIVTNPEISS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 167 VGDVRRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVfsrgggEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEF 246
Cdd:cd02036  147 VRDADRVIGLLESKGIVNIGLIVNRYRPEMVKSGDMLSV------EDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYK 220

                        250
                 ....*....|....*.
gi 189054996 247 PGSPAFAALTSIAQKI 262
Cdd:cd02036  221 PNSLAAKAFENIARRL 236
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 15-268 6.81e-16

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: 76.31  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  15 HIILVLSGKGGVGRSTISTELALAL-RHAGKKVGILDVDLCGPSIPRMLGAQGR-----AVHQCDRgwapvfLDR---EQ 85
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDVALYLDLEPRrgladALRNPDR------LDEtllDR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  86 SISLMSVGF-LLEKPDEAVVWRGPKKNALIKqfVSDVAWGELDYLVVDTPPGTSDEHMATIEAlrpyqplgA---LVVTT 161
Cdd:COG4963  177 ALTRHSSGLsVLAAPADLERAEEVSPEAVER--LLDLLRRHFDYVVVDLPRGLNPWTLAALEA--------AdevVLVTE 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 162 PQAVSVGDVRRELTFCRKMGLRV--MGIVENMsgftCPHCTECTSvfsrgggEELAQLAGVPFLGSVPLDPALMRT-LEE 238
Cdd:COG4963  247 PDLPSLRNAKRLLDLLRELGLPDdkVRLVLNR----VPKRGEISA-------KDIEEALGLPVAAVLPNDPKAVAEaANQ 315

                        250       260       270
                 ....*....|....*....|....*....|
gi 189054996 239 GHDFIQEFPGSPAFAALTSIAQKILDATPA 268
Cdd:COG4963  316 GRPLAEVAPKSPLAKAIRKLAARLTGRPAA 345
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 16-263 1.63e-11

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: 62.74  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVH--------QCDRGWAPVFLDREQSI 87
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvegECRLQQALIKDKRLKNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   88 SLMSVGFLLEKpdEAVVWRGPKK--NALIKQFvsdvawgelDYLVVDTPPGtsdehmatIE-----ALRPYQplGALVVT 160
Cdd:TIGR01968  83 YLLPASQTRDK--DAVTPEQMKKlvNELKEEF---------DYVIIDCPAG--------IEsgfrnAVAPAD--EAIVVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  161 TPQAVSVGDVRreltfcrkmglRVMGIVENmSGFTCPHCT------------ECTSVfsrgggEELAQLAGVPFLGSVPL 228
Cdd:TIGR01968 142 TPEVSAVRDAD-----------RVIGLLEA-KGIEKIHLIvnrlrpemvkkgDMLSV------DDVLEILSIPLIGVIPE 203

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 189054996  229 DPALMRTLEEGHDFIQEfPGSPAFAALTSIAQKIL 263
Cdd:TIGR01968 204 DEAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-262 1.19e-10

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 60.18  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  17 ILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDlcgP--SIPRMLGAqgravhqcdrgwaPVFLDREQSISLM---- 90
Cdd:COG3640    2 KIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDAD---PnaNLAEALGL-------------EVEADLIKPLGEMreli 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  91 -------SVGFLLEKP------DEAVVWRG---------PKK---------NALIKQFVSDVAWGELDYLVVDTPPGTsd 139
Cdd:COG3640   66 kertgapGGGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 140 EHMA--TIE---ALrpyqplgaLVVTTPQAVSVGDVRRELTFCRKMGLRVMGIVENMsgftcphctectsVFSRGGGEEL 214
Cdd:COG3640  144 EHLGrgTAEgvdLL--------LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNK-------------VREEEDEEFL 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 189054996 215 AQLAGVPFLGSVPLDPALMRtLEEGHDFIQEFPGSPAFAALTSIAQKI 262
Cdd:COG3640  203 RELLGLELLGFIPYDEEVRE-ADLEGKPLLDLPDSPAVAAVEEIAEKL 249
PRK10818 PRK10818
septum site-determining protein MinD;
16-243 3.60e-10

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 59.18  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQcdrgwapvFLDREQSISLMSVGFL 95
Cdd:PRK10818   4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYD--------FVNVIQGDATLNQALI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  96 LEKPDEAV----VWRGPKKNAL----IKQFVSDVAWGELDYLVVDTPPGTSDEHMATIealrpYQPLGALVVTTPQAVSV 167
Cdd:PRK10818  76 KDKRTENLyilpASQTRDKDALtregVAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-----YFADEAIITTNPEVSSV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 168 GDVRRELTFCRKMGLRvmgiVENMSGFTCPHCTEC---TSVFSRG---GGEELAQLAGVPFLGSVPLDPALMRTLEEGHD 241
Cdd:PRK10818 151 RDSDRILGILASKSRR----AENGEEPIKEHLLLTrynPGRVSRGdmlSMEDVLEILRIKLVGVIPEDQSVLRASNQGEP 226


                 ..
gi 189054996 242 FI 243
Cdd:PRK10818 227 VI 228
minD CHL00175
septum-site determining protein; Validated
 9-230 3.66e-10

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 59.01  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   9 NLAGVRHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVH--------QCDRGWAPVF 80
Cdd:CHL00175  10 KSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYtamdvlegECRLDQALIR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  81 LDREQSISLMSVGFLLEKpdeavvWRGPKKNalIKQFVSDVAWGELDYLVVDTPPGTSdehMATIEALRPYQPlgALVVT 160
Cdd:CHL00175  90 DKRWKNLSLLAISKNRQR------YNVTRKN--MNMLVDSLKNRGYDYILIDCPAGID---VGFINAIAPAQE--AIVVT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 161 TPQAVSVGDVRRELTFCRKMGLRVMGIVENMSGFTCPHCTECTSVfsrgggEELAQLAGVPFLGSVPLDP 230
Cdd:CHL00175 157 TPEITAIRDADRVAGLLEANGIYNVKLLVNRVRPDMIQANDMMSV------RDVQEMLGIPLLGAIPEDE 220
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 16-259 8.54e-10

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: 57.67  E-value: 8.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRH-AGKKVGILDVDLCGPSIPRMLGAqgravhQCDRGWAPVF-----LDREQSISL 89
Cdd:cd03111    2 VVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDLPFGDLGLYLNL------RPDYDLADVIqnldrLDRTLLDSA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  90 M---SVGF-LLEKPDEAVVWRGPKKNALIKqfVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPyqplgALVVTTPQAV 165
Cdd:cd03111   76 VtrhSSGLsLLPAPQELEDLEALGAEQVDK--LLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADE-----ILLVTQQDLP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 166 SVGDVRRELTFCRKMGLR------VMGIVENMSGFTCphctectsvfsrgggEELAQLAGVPFLGSVPLDP-ALMRTLEE 238
Cdd:cd03111  149 SLRNARRLLDSLRELEGSsdrlrlVLNRYDKKSEISP---------------KDIEEALGLEVFATLPNDYkAVSESANT 213

                        250       260
                 ....*....|....*....|.
gi 189054996 239 GHDFIQEFPGSPAFAALTSIA 259
Cdd:cd03111  214 GRPLVEVAPRSALVRALQDLA 234
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 14-190 1.97e-08

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: 52.96  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  14 RHIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRA------VHQCDrgWAPVFLDREQS- 86
Cdd:cd05387   19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPglsevlSGQAS--LEDVIQSTNIPn 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  87 ISLMSVGFLLEKPDEAVvwRGPKKNALIKQFVsdvawGELDYLVVDTPP--GTSDEHMATiealrpyqPL--GALVVTTP 162
Cdd:cd05387   97 LDVLPAGTVPPNPSELL--SSPRFAELLEELK-----EQYDYVIIDTPPvlAVADALILA--------PLvdGVLLVVRA 161

                        170       180
                 ....*....|....*....|....*...
gi 189054996 163 QAVSVGDVRRELTFCRKMGLRVMGIVEN 190
Cdd:cd05387  162 GKTRRREVKEALERLEQAGAKVLGVVLN 189
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 15-52 4.06e-08

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: 51.00  E-value: 4.06e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189054996  15 HIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 15-264 7.66e-08

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: 52.17  E-value: 7.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  15 HIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGpSIPRMLGAQGRAVhqcDRGWAPVFLDR---EQSISLMS 91
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLDPDDL---DPTLYDLLLDDaplEDAIVPTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  92 VGFL--------LEKPDEAVVwRGPKKNALIKQFVSDVAwGELDYLVVDTPPGTSdehMATIEALRpyqplgA----LVV 159
Cdd:COG1192   78 IPGLdlipanidLAGAEIELV-SRPGRELRLKRALAPLA-DDYDYILIDCPPSLG---LLTLNALA------AadsvLIP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 160 TTPQAVS----------VGDVRRELtfcrKMGLRVMGIVENMsgftcphcTECTSVFSRGGGEELAQLAGVPFLGS-VPL 228
Cdd:COG1192  147 VQPEYLSleglaqlletIEEVREDL----NPKLEILGILLTM--------VDPRTRLSREVLEELREEFGDKVLDTvIPR 214

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 189054996 229 DPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILD 264
Cdd:COG1192  215 SVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 16-262 1.20e-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: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDlCGPSIPRMLGaqgraVHQCDRGWAPVFLD-RE---QSISLMS 91
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDAD-PNSNLAETLG-----VEVEKLPLIKTIGDiRErtgAKKGEPP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  92 VGFLLE-----KPDEAVVWRG---------PKK---------NALIKQFVSDVAWGELDYLVVDTPPGTsdEHM--ATIE 146
Cdd:cd02034   75 EGMSLNpyvddIIKEIIVEPDgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLsrGTIR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 147 ALRPYqplgaLVVTTPQAVSVGDVRR--ELTfcRKMGLRVMGIVENmsgftcphctectsvfsRGGGEELAQLA-----G 219
Cdd:cd02034  153 AVDLL-----IIVIEPSKRSIQTAKRikELA--EELGIKKIYLIVN-----------------KVRNEEEQELIeelliK 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 189054996 220 VPFLGSVPLDPALMRTLEEGHDFIQEfpGSPAFAALTSIAQKI 262
Cdd:cd02034  209 LKLIGVIPYDEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 16-227 1.84e-07

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: 50.85  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALrhagKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPvFLDREQSIS------- 88
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKA-FIDQEKCIRcgncerv 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  89 -----LMSVG-------FLLEK--------PDEAVVWRgPKKNALIKQFVSD---VAWGEL------------------- 126
Cdd:cd03110   76 ckfgaILEFFqklivdeSLCEGcgacviicPRGAIYLK-DRDTGKIFISSSDggpLVHGRLnigeensgklvtelrkkal 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 127 ------DYLVVDTPPGTsdeHMATIEALRpyqplGA---LVVTTPQAVSVGDVRRELTFCRKMGLRVMgIVENMSGFTcP 197
Cdd:cd03110  155 erskecDLAIIDGPPGT---GCPVVASIT-----GAdavLLVTEPTPSGLHDLKRAIELAKHFGIPTG-IVINRYDIN-D 224

                        250       260       270
                 ....*....|....*....|....*....|
gi 189054996 198 HCTECTsvfsrgggEELAQLAGVPFLGSVP 227
Cdd:cd03110  225 EISEEI--------EDFADEEGIPLLGKIP 246
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 16-263 6.76e-07

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 49.29  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD--LcgpsipR----MLGAQGRAVHqcdrgwapvfldreqsiSL 89
Cdd:COG2894    4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADigL------RnldlVMGLENRIVY-----------------DL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  90 MSVgflLE---KPDEAVVW--RGPK-----------KNALIKQFVSDVAwGEL----DYLVVDTPPGtsdehmatIE--- 146
Cdd:COG2894   61 VDV---IEgecRLKQALIKdkRFENlyllpasqtrdKDALTPEQMKKLV-EELkeefDYILIDSPAG--------IEqgf 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 147 --ALRPYQplGALVVTTPQAVSVGDVRreltfcrkmglRVMGIVENMsGFTCPHCtectsVFSR-------GGG----EE 213
Cdd:COG2894  129 knAIAGAD--EAIVVTTPEVSSVRDAD-----------RIIGLLEAK-GIRKPHL-----IINRyrpamvkRGDmlsvED 189

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 189054996 214 LAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEfPGSPAFAALTSIAQKIL 263
Cdd:COG2894  190 VLEILAIPLLGVVPEDEEVIVSSNRGEPVVLD-EKSKAGQAYRNIARRLL 238
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 15-134 1.82e-06

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: 47.83  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   15 HIILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQgravhqcdRGWApvfldREQSISL-MSVG 93
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFENR--------SATA-----DRTGLSLpTPEH 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 189054996   94 FLLEKPDEAVVWRGpkKNALIKQF---VSDVAwGELDYLVVDTP 134
Cdd:pfam09140  68 LNLPDNDVAEVPDG--ENIDDARLeeaFADLE-ARCDFIVIDTP 108
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 16-52 2.01e-06

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: 45.50  E-value: 2.01e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 16-190 8.21e-06

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: 45.96  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  16 IILVLsGKGGVGRSTISTELALALRHAGKKV------------GILDVDLcGPSI--------------PRMLGAQGRA- 68
Cdd:cd02035    2 IIFFG-GKGGVGKTTIAAATAVRLAEQGKRVllvstdpahslsDAFGQKL-GGETpvkgapnlwameidPEEALEEYWEe 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  69 VHQCDRGWAPVFLDREQSISLMSVGfllekP--DEAVvwrgpkknAL--IKQFVSDvawGELDYLVVDTPPgtsdehmaT 144
Cdd:cd02035   80 VKELLAQYLRLPGLDEVYAEELLSL-----PgmDEAA--------AFdeLREYVES---GEYDVIVFDTAP--------T 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 145 IEALR----PYQPLGAL----------VVTTPQAVSVGDVRRELTFCRKMGLRVMGIVEN 190
Cdd:cd02035  136 GHTLRllslPLEQVRELlrdperttfvLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 10-190 2.37e-05

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 45.48  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   10 LAGVRHIILVLSGK-GGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRA----VHQCDRGWaPVFLDRE 84
Cdd:TIGR01005 548 LADAENNLIAIAGAlPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPglldLLAGEASI-EAGIHRD 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   85 QSISLMSV---GFLLEKPDEAVVWRGPKKNALIKQFVSdvawgELDYLVVDTPPgtsdehMATIEALRPYQPL--GALVV 159
Cdd:TIGR01005 627 QRPGLAFIaagGASHFPHNPNELLANPAMAELIDNARN-----AFDLVLVDLAA------LAAVADAAAFAALadGILFV 695

                         170       180       190
                  ....*....|....*....|....*....|.
gi 189054996  160 TTPQAVSVGDVRRELTFCRKMGLRVMGIVEN 190
Cdd:TIGR01005 696 TEFERSPLGEIRDLIHQEPHANSDVLGVIFN 726
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 16-52 2.41e-05

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: 43.73  E-value: 2.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 189054996   16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
17-52 8.62e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 43.27  E-value: 8.62e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 189054996  17 ILVLSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:COG0003    5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTD 40
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 16-64 1.97e-04

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 41.79  E-value: 1.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDlcgPSIPRMLGA 64
Cdd:cd03114   47 FRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVD---PSSPRSGGS 92
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 17-268 7.02e-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: 40.04  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  17 ILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGaqGRAVHQCDRGWAPVFLDRE---QSISLMSVG 93
Cdd:cd02117    2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTG--GKVPPTIDEMLTEDGTAEElrrEDLLFSGFN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996  94 --FLLE----KPDEAVVWRGP-------KKNALIKQ--------FVSDVAWGEL----------DYLVVdtppgTSDEHM 142
Cdd:cd02117   80 gvDCVEaggpEPGVGCGGRGIgtmlellEEHGLLDDdydvvifdVLGDVVCGGFaaplrrgfaqKVVIV-----VSEELM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996 143 ATIEALRpyqpLGALVVTTpqavsvgdvrreltfcRKMGLRVMGIVENMSGftcphctectsvfSRGGG--EELAQLAGV 220
Cdd:cd02117  155 SLYAANN----IVKAVENY----------------SKNGVRLAGLVANLRD-------------PAGTEeiQAFAAAVGT 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 189054996 221 PFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPA 268
Cdd:cd02117  202 KILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIADAVPP 249
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 16-73 7.97e-04

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


Pssm-ID: 349771  Cd Length: 155  Bit Score: 38.86  E-value: 7.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDlcgPSIPRMLGAQGRAVHQCD 73
Cdd:cd05386    2 IHFVLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTD---PVNKTFAGYKALNVQRIN 56
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 16-52 1.48e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 39.26  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 189054996   16 IILVlSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:pfam02374   3 WIFF-GGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 18-52 2.17e-03

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: 39.30  E-value: 2.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 189054996   18 LVLSGKGGVGRSTISTELALALRHAGKKVGILDVD 52
Cdd:TIGR04291   6 LFFTGKGGVGKTSIACATAINLADQGKRVLLVSTD 40
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 17-46 2.49e-03

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 38.43  E-value: 2.49e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 189054996  17 ILVLSGKGGVGRSTISTELALALRHAGKKV 46
Cdd:cd02032    2 VIAVYGKGGIGKSTTSSNLSAAFAKRGKKV 31
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 16-68 2.64e-03

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: 38.29  E-value: 2.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189054996  16 IILVLSGKGGVGRSTISTELALALRHAGKKVGILDVDLCGpSIPRMLGAQGRA 68
Cdd:cd17869    5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQ-STDVFFGASGRY 56
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 22-62 7.07e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 37.06  E-value: 7.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 189054996  22 GKGGVGRSTISTELALALRHAGKKVGILDVD--------LCGPSIPRML 62
Cdd:PRK13230   8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVL 56
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 13-105 9.97e-03

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


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 36.20  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189054996   13 VRHIILVLSGKGGVGRSTISTELALAL---------RHAGKKVGILDVDLCGPS--IPRMLGAQGRAVHQCDRgwaPVFL 81
Cdd:pfam13481  31 PAGGLGLLAGAPGTGKTTLALDLAAAVatgkpwlggPRVPEQGKVLYVSAEGPAdeLRRRLRAAGADLDLPAR---LLFL 107

                          90       100
                  ....*....|....*....|....
gi 189054996   82 DREQSISLMSVGFLLEKPDEAVVW 105
Cdd:pfam13481 108 SLVESLPLFFLDRGGPLLDADVDA 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH