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Conserved domains on  [gi|13632127|sp|Q9R060|]
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RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1; AltName: Full=Nucleotide-binding protein 1; Short=NBP 1

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, similar to the yeast cytosolic iron-sulfur (Fe-S) assembly factors, NBP35 and CFD1 (also called NUBP1/NUBP2 in higher eukaryotes), which functions as a heterotetrameric complex to assemble nascent Fe-S clusters and transfer them to apoprotein targets

Gene Ontology:  GO:0005524|GO:0016887|GO:0046872
PubMed:  11916378

Graphical summary

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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 ...
 53-303 1.37e-149

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: 419.94  E-value: 1.37e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 13632127   293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 53-303 1.37e-149

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: 419.94  E-value: 1.37e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 13632127   293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 55-275 7.29e-131

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: 371.06  E-value: 7.29e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037  79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13632127 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-303 1.18e-127

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 368.76  E-value: 1.18e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   50 MKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRG-YKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAAahiDGAVILTTPQEVALQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....
gi 13632127  290 SPATAAYRSIIQRI 303
Cdd:NF041136 235 SPAAKALEKIVDPI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.17e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   51 KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                        250
                 ....*....|....
gi 13632127  290 SPATAAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 7.69e-47

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: 159.58  E-value: 7.69e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  32 ASGAGAAPDPAVEEIREKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489  70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKR-VLLIDADLRGPSLHRMLGLENRPgl 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 110 --VHQSGSGWSPV---YVDDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13632127 185 QylaaAHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 59-303 8.88e-22

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: 92.10  E-value: 8.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQV--HQSGSGWS----PVYVDDNlGVMSVg 132
Cdd:TIGR01969   5 IASGKGGTGKTTITANLGVALAKLGK-KVLALDADITMANLELILGMEDKPVtlHDVLAGEAdikdAIYEGPF-GVKVI- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   133 fllsspDDAVIWRGPKKNGMIKqfLRDV---DWGDVDYLIVDTPPGTSdehLSVVQYLAAAhiDGAVILTTPQEVALQDV 209
Cdd:TIGR01969  82 ------PAGVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSITDA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   210 RKEISFCHKVKLPIIGVVENMSGficpkcKKESQIfppttgGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:TIGR01969 149 LKTKIVAEKLGTAILGVVLNRVT------RDKTEL------GREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPN 216

                         250
                  ....*....|....
gi 13632127   290 SPATAAYRSIIQRI 303
Cdd:TIGR01969 217 SPAAQAFMELAAEL 230
ParA_partition NF041546
ParA family partition ATPase;
59-93 1.70e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.63  E-value: 1.70e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 13632127   59 VLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:NF041546   4 VLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 53-303 1.37e-149

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: 419.94  E-value: 1.37e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    53 VRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 13632127   293 TAAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 55-275 7.29e-131

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: 371.06  E-value: 7.29e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037  79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13632127 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-303 1.18e-127

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 368.76  E-value: 1.18e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   50 MKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRG-YKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAAahiDGAVILTTPQEVALQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....
gi 13632127  290 SPATAAYRSIIQRI 303
Cdd:NF041136 235 SPAAKALEKIVDPI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.17e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   51 KTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                        250
                 ....*....|....
gi 13632127  290 SPATAAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 7.69e-47

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: 159.58  E-value: 7.69e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  32 ASGAGAAPDPAVEEIREKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489  70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKR-VLLIDADLRGPSLHRMLGLENRPgl 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 110 --VHQSGSGWSPV---YVDDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13632127 185 QylaaAHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 42-303 2.08e-22

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: 95.95  E-value: 2.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  42 AVEEIREKMKTVRHKLL-VLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSG 116
Cdd:COG4963  89 ALARLLDPGAARRGRVIaVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDR 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 117 WSPVYVDDNLGVMSVGF-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgDVDYLIVDTPPGTSDEHLSVvqyLAAAHId 193
Cdd:COG4963 169 LDETLLDRALTRHSSGLsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE- 240

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 194 gaVILTTPQEVA-LQDVRKEISFCHKVKLPI--IGVVENMSGficpkckKESQIfppttgGAEAMCQDLRIPLLGKVPLD 270
Cdd:COG4963 241 --VVLVTEPDLPsLRNAKRLLDLLRELGLPDdkVRLVLNRVP-------KRGEI------SAKDIEEALGLPVAAVLPND 305

                       250       260       270
                ....*....|....*....|....*....|....
gi 13632127 271 P-HIGKSCDKGQSFFVEAPDSPATAAYRSIIQRI 303
Cdd:COG4963 306 PkAVAEAANQGRPLAEVAPKSPLAKAIRKLAARL 339
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 70-305 5.01e-22

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: 92.26  E-value: 5.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  70 TFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VDDNLGVmsvgFLLSSPDDAVIWR 145
Cdd:COG0455   1 TVAVNLAAALARLGK-RVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 146 GPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVILTTPQEVALQD---VRKEISFCHKVKlp 222
Cdd:COG0455  76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDayaLLKLLRRRLGVR-- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 223 IIGVVENMSgficpkckKESQIFPPTTGGAEAMCQ---DLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPATAAYRSI 299
Cdd:COG0455 148 RAGVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIREL 219


                ....*.
gi 13632127 300 IQRIRD 305
Cdd:COG0455 220 AARLAG 225
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 59-303 8.88e-22

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: 92.10  E-value: 8.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQV--HQSGSGWS----PVYVDDNlGVMSVg 132
Cdd:TIGR01969   5 IASGKGGTGKTTITANLGVALAKLGK-KVLALDADITMANLELILGMEDKPVtlHDVLAGEAdikdAIYEGPF-GVKVI- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   133 fllsspDDAVIWRGPKKNGMIKqfLRDV---DWGDVDYLIVDTPPGTSdehLSVVQYLAAAhiDGAVILTTPQEVALQDV 209
Cdd:TIGR01969  82 ------PAGVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSITDA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   210 RKEISFCHKVKLPIIGVVENMSGficpkcKKESQIfppttgGAEAMCQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPD 289
Cdd:TIGR01969 149 LKTKIVAEKLGTAILGVVLNRVT------RDKTEL------GREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPN 216

                         250
                  ....*....|....
gi 13632127   290 SPATAAYRSIIQRI 303
Cdd:TIGR01969 217 SPAAQAFMELAAEL 230
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 59-303 4.01e-21

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: 89.95  E-value: 4.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQV-------------HQSgsgwspVYVD-- 123
Cdd:cd02036   5 ITSGKGGVGKTTTTANLGVALAKLGK-KVLLIDADIGLRNLDLILGLENRIVytlvdvlegecrlEQA------LIKDkr 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 124 -DNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSvvqylAAAHIDGAVILTTPQ 202
Cdd:cd02036  78 wENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTNPE 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 203 EVALQDVRKEISFCHKVKLPIIGVVENMsgfICPKCKKESQIFPPttggaEAMCQDLRIPLLGKVPLDPHIGKSCDKGQS 282
Cdd:cd02036 144 ISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRGEP 215

                       250       260
                ....*....|....*....|.
gi 13632127 283 FFVEAPDSPATAAYRSIIQRI 303
Cdd:cd02036 216 LVLYKPNSLAAKAFENIARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 57-283 2.03e-20

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: 87.79  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    57 LLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVDDNLG 127
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRG-LRVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVILTTPQEV 204
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   205 ALQDVRKEISFCHKVK-------LPIIGVVENMSGficPKCKKESQIfppttggaEAMCQDLR-IPLLGKVPLDPHIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLRgLPVLGVIPRDEAVAEA 221


                  ....*..
gi 13632127   277 CDKGQSF 283
Cdd:pfam01656 222 PARGLPV 228
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 59-293 5.65e-18

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: 81.08  E-value: 5.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  59 VLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVDDNLGV 128
Cdd:cd02038   5 VTSGKGGVGKTNVSANLALALSKLGKR-VLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGLDI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 129 MSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgDVDYLIVDTPPGTSDehlSVVQYLAAAHIdgAVILTTPQEVALQD 208
Cdd:cd02038  80 IPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSITD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 209 ---VRKEISfcHKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAEAMCQ---DLRIPLLGKVPLDPHIGKSCDKGQS 282
Cdd:cd02038 150 ayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQKP 219

                       250
                ....*....|.
gi 13632127 283 FFVEAPDSPAT 293
Cdd:cd02038 220 FVLLFPNSKAS 230
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 50-303 2.53e-16

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: 77.21  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  50 MKTVrhklLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 122
Cdd:COG1192   1 MKVI----AVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 123 DDNLGVMSVgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVvqyLAAAhiDGAVIL 198
Cdd:COG1192  75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 199 TTPQEVAL----------QDVRKEisfcHKVKLPIIGVVENMsgficpkckkesqiFPPTTGGAEAMCQDLR----IPLL 264
Cdd:COG1192 147 VQPEYLSLeglaqlletiEEVRED----LNPKLEILGILLTM--------------VDPRTRLSREVLEELReefgDKVL 208

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13632127 265 G-KVPLDPHIGKSCDKGQSFFVEAPDSPATAAYRSIIQRI 303
Cdd:COG1192 209 DtVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEEL 248
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 57-304 2.56e-15

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: 74.30  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    57 LLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQsgsgwspvYVD------------- 123
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGK-KVVLIDADIGLRNLDLLLGLENRIVYT--------LVDvvegecrlqqali 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   124 -----DNLGVMSVGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDVDYLIVDTPPGtsdehLSVVQYLAAAHIDGAVIL 198
Cdd:TIGR01968  75 kdkrlKNLYLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   199 TTPQEVALQDVRKeisfchkvklpIIGVVENMS--------GFICPKCKKESQIFppttgGAEAMCQDLRIPLLGKVPLD 270
Cdd:TIGR01968 141 TTPEVSAVRDADR-----------VIGLLEAKGiekihlivNRLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPED 204

                         250       260       270
                  ....*....|....*....|....*....|....
gi 13632127   271 PHIGKSCDKGQSFFVEaPDSPATAAYRSIIQRIR 304
Cdd:TIGR01968 205 EAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 58-303 2.98e-14

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 70.97  E-value: 2.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  58 LVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----YVDDNLGVMSVG 132
Cdd:COG3640   3 IAVAGKGGVGKTTLSALLARYLAEKGK-PVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPGGG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 133 FLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGDVDYLIVDTPPGTsdEHLSvvqYLA 188
Cdd:COG3640  76 MFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG---RGT 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 189 AAHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENmsgficpKCKKESQIfppttggaEAMCQDLRIPLLGKVP 268
Cdd:COG3640 151 AEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGFIP 215

                       250       260       270
                ....*....|....*....|....*....|....*
gi 13632127 269 LDPHIGKSCDKGQSFFvEAPDSPATAAYRSIIQRI 303
Cdd:COG3640 216 YDEEVREADLEGKPLL-DLPDSPAVAAVEEIAEKL 249
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 58-299 5.06e-14

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: 70.38  E-value: 5.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  58 LVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVDDNLGVMSVGF 133
Cdd:cd03111   4 AVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 134 -LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGDVDYLIVDTPPgtsdeHLSVVQYLAAAHIDGAVILTTPQEVALQDV 209
Cdd:cd03111  84 sLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 210 RKEISFC-------HKVKLpIIGVVENMSGfICPKckkesQIfppttggAEAmcqdLRIPLLGKVPLDPH-IGKSCDKGQ 281
Cdd:cd03111 154 RRLLDSLrelegssDRLRL-VLNRYDKKSE-ISPK-----DI-------EEA----LGLEVFATLPNDYKaVSESANTGR 215

                       250
                ....*....|....*...
gi 13632127 282 SFFVEAPDSPATAAYRSI 299
Cdd:cd03111 216 PLVEVAPRSALVRALQDL 233
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 59-303 1.14e-13

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 69.70  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  59 VLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEgEQVhqsgsgwspVY--VD------------- 123
Cdd:COG2894   7 VTSGKGGVGKTTTTANLGTALALLGK-KVVLIDADIGLRNLDLVMGLE-NRI---------VYdlVDviegecrlkqali 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 124 -----DNLgvmsvgFLLssP-----D-DAViwrgpKKNGMIK--QFLRDvdwgDVDYLIVDTPPGTsdEHLSvvqYLAAA 190
Cdd:COG2894  76 kdkrfENL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIA 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 191 HIDGAVILTTPQEVALQDV-RkeisfchkvklpIIGVVENMSgficpkcKKESQI----FPPT---TGG---AEAMCQDL 259
Cdd:COG2894 134 GADEAIVVTTPEVSSVRDAdR------------IIGLLEAKG-------IRKPHLiinrYRPAmvkRGDmlsVEDVLEIL 194

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 13632127 260 RIPLLGKVPLDPHIGKSCDKGQSfFVEAPDSPATAAYRSIIQRI 303
Cdd:COG2894 195 AIPLLGVVPEDEEVIVSSNRGEP-VVLDEKSKAGQAYRNIARRL 237
PRK10818 PRK10818
septum site-determining protein MinD;
57-303 1.36e-13

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 69.58  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   57 LLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVaLLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVDD----NL 126
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVqYLAaahiDGAVILTTPQEVAL 206
Cdd:PRK10818  84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  207 QDVRKeisfchkvklpIIGVVENMS--GFICPKCKKESQIFPPTTGG---------AEAMCQDLRIPLLGKVPLDPHIGK 275
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219

                        250       260
                 ....*....|....*....|....*...
gi 13632127  276 SCDKGQSFFVEApDSPATAAYRSIIQRI 303
Cdd:PRK10818 220 ASNQGEPVILDI-EADAGKAYADTVDRL 246
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 54-229 7.12e-12

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: 63.36  E-value: 7.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  54 RHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ------VHQSgSGWSPVYVDD--N 125
Cdd:cd05387  19 PKVIAVTSASPGEGKSTVAANLAVALAQSG-KRVLLIDADLRRPSLHRLLGLPNEPglsevlSGQA-SLEDVIQSTNipN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 126 LGVMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgDVDYLIVDTPP--GTSDEHlsvvqyLAAAHIDGAVILTTPQE 203
Cdd:cd05387  97 LDVLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADAL------ILAPLVDGVLLVVRAGK 163

                       170       180
                ....*....|....*....|....*.
gi 13632127 204 VALQDVRKEISFCHKVKLPIIGVVEN 229
Cdd:cd05387 164 TRRREVKEALERLEQAGAKVLGVVLN 189
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 56-268 1.02e-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: 58.17  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  56 KLLVLSGKGGVGKSTFSAHLAHGLAEdgdtqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDD----------- 124
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 159
Cdd:cd03110  76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 160 VDWGDVDYLIVDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkck 239
Cdd:cd03110 155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------- 221

                       250       260
                ....*....|....*....|....*....
gi 13632127 240 kesqIFPPTTGGAEAMCQDLRIPLLGKVP 268
Cdd:cd03110 222 ----INDEISEEIEDFADEEGIPLLGKIP 246
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 55-93 3.66e-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: 51.39  E-value: 3.66e-08
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 13632127  55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 58-303 1.35e-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: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  58 LVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSgwspvyVDD-------NLGVMS 130
Cdd:cd02034   3 IAVAGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKT------IGDirertgaKKGEPP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 131 VGFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGDVDYLIVDTPPGTsdEHLS--VVQ 185
Cdd:cd02034  75 EGMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 186 ylaaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGficpkcKKESQIFPPTTGgaeamcqdLRIPLLG 265
Cdd:cd02034 153 -----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVR------NEEEQELIEELL--------IKLKLIG 213

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 13632127 266 KVPLDPHIGKSCDKGQSFFveAPDSPATAAYRSIIQRI 303
Cdd:cd02034 214 VIPYDEEIMEADLKGKPLF--DLDSAAVKAIEKIVEKL 249
ParA_partition NF041546
ParA family partition ATPase;
59-93 1.70e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.63  E-value: 1.70e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 13632127   59 VLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:NF041546   4 VLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
minD CHL00175
septum-site determining protein; Validated
 48-306 2.00e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 51.31  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   48 EKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyvddnLG 127
Cdd:CHL00175   9 EKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA------------MD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  128 VMSVGFLLsspDDAVI----WRG---------------PKKNgmIKQFLRDVDWGDVDYLIVDTPPGtsdehLSVVQYLA 188
Cdd:CHL00175  76 VLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKN--MNMLVDSLKNRGYDYILIDCPAG-----IDVGFINA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  189 AAHIDGAVILTTPQEVALQDVRK-----EISFCHKVKLPIIGVVENMsgficpkCKKESQIfppTTGGAEAMcqdLRIPL 263
Cdd:CHL00175 146 IAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM---SVRDVQEM---LGIPL 212

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13632127  264 LGKVPLDPHIGKSCDKG--------------------------QSFFVEApDSPataaYRSIIQRIRDF 306
Cdd:CHL00175 213 LGAIPEDENVIISTNRGeplvlnkkltlsgiafenaarrlvgkQDYFIDL-DSP----SKGPLKRLQKF 276
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 56-93 3.22e-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: 45.11  E-value: 3.22e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 13632127  56 KLLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd01983   2 VIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 55-174 6.33e-05

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: 43.88  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    55 HKLLVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVDDNLGVMSVG-- 132
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGK-KVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIDpn 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13632127   133 -----------------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGDVDYLIVDTPP 174
Cdd:pfam02374  71 meleeywqevqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
56-174 9.24e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 43.27  E-value: 9.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  56 KLLVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDIcGPSIPKIMGLEGeqvhqsgsGWSPVYV-DDNLGVMSVgfl 134
Cdd:COG0003   4 RIIFFTGKGGVGKTTVAAATALALAERG-KRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVaVPNLYALEI--- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13632127 135 lsSPDDAV--IWRGPKKN------------------GM--------IKQFLRDVDWgdvDYLIVDTPP 174
Cdd:COG0003  71 --DPEAELeeYWERVRAPlrgllpsagvdelaeslpGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 58-305 1.84e-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: 42.35  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127  58 LVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGSGWSPVYVDDN 125
Cdd:cd02117   3 IVVYGKGGIGKSTTASNLSAALAEGGkkvlhvgcdpkhDSTLLLTG----GKVPPTIDEMLTEDGTAEELRREDLLFSGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 126 LGVMSVGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DW----------GDV---------------DYLIVdtppg 175
Cdd:cd02117  79 NGVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDDdydvvifdvlGDVvcggfaaplrrgfaqKVVIV----- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127 176 TSDEHLSVvqyLAAAHIDGAVilttpQEVALQDVRkeisfchkvklpIIGVVENMSGficpkckkesqifPPTTGGAEAM 255
Cdd:cd02117 149 VSEELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAF 195

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 13632127 256 CQDLRIPLLGKVPLDPHIGKSCDKGQSFFVEAPDSPATAAYRSIIQRIRD 305
Cdd:cd02117 196 AAAVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIAD 245
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 41-83 1.01e-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: 40.84  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 13632127    41 PAVEEIREKMKTVRHKLLVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:TIGR04291 307 PSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKG 349
PHA02518 PHA02518
ParA-like protein; Provisional
 57-123 1.45e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.45  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127   57 LLVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDICG-------------PSIPKI-MGLE-GEQVHQSGSGWSPVY 121
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHK-VLLVDLDPQGsstdwaeareegePLIPVVrMGKSiRADLPKVASGYDYVV 81


                 ..
gi 13632127  122 VD 123
Cdd:PHA02518  82 VD 83
COG3903 COG3903
Predicted ATPase [General function prediction only];
26-91 1.49e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 40.39  E-value: 1.49e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13632127  26 PNQRLCASGAGAAPDPAVEEIREKMKTVRhkLLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLD 91
Cdd:COG3903 149 PPPPAPLAALARRAAALAAAARALLSAAR--LVTLTGPGGVGKTRLALEVAHRLADRFPDGVWFVD 212
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 56-83 1.62e-03

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: 39.41  E-value: 1.62e-03
                        10        20
                ....*....|....*....|....*...
gi 13632127  56 KLLVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02035   1 RIIFFGGKGGVGKTTIAAATAVRLAEQG 28
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
54-92 2.06e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 2.06e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 13632127  54 RHKLLVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDI 92
Cdd:COG5635 179 KKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPI 217
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 63-174 2.23e-03

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: 38.33  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13632127    63 KGGVGKSTFSAHLAHGLAE--------DGDTQVAL-----LDIDICGPSIPKIMGLEG---EQVHQSgsgwspvyVDDNL 126
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKkgkkvlliDLDPQGNAtsglgIDKNNVEKTIYELLIGECnieEAIIKT--------VIENL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 13632127   127 GVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVDwGDVDYLIVDTPP 174
Cdd:pfam13614  82 DLIPSNIDLAGAEIELIGIENREN-ILKEALEPVK-DNYDYIIIDCPP 127
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 62-83 4.01e-03

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


Pssm-ID: 349759  Cd Length: 265  Bit Score: 38.26  E-value: 4.01e-03
                        10        20
                ....*....|....*....|..
gi 13632127  62 GKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02040   7 GKGGIGKSTTASNLSAALAEMG 28
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
62-83 5.15e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 37.81  E-value: 5.15e-03
                          10        20
                  ....*....|....*....|..
gi 13632127    62 GKGGVGKSTFSAHLAHGLAEDG 83
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMG 28
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 47-93 6.49e-03

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: 38.04  E-value: 6.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 13632127    47 REKMKTVRH-----KLLVLS---GKGGVGKSTFSAHLAHGLAEDGdTQVALLDID 93
Cdd:TIGR03453  89 REARRYLPHrrggeHLQVIAvtnFKGGSGKTTTAAHLAQYLALRG-YRVLAIDLD 142
 
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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