NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1147372655|ref|XP_020035438|]
View 

cytosolic Fe-S cluster assembly factor NUBP1 isoform X1 [Castor canadensis]

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

 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 ...
 92-342 1.27e-146

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: 413.77  E-value: 1.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  92 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 171
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 FLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 251
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 252 ISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPA 331
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1147372655 332 TLAYRSVIKRI 342
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 ...
 92-342 1.27e-146

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: 413.77  E-value: 1.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  92 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 171
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 FLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 251
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 252 ISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPA 331
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1147372655 332 TLAYRSVIKRI 342
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 94-314 2.54e-130

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: 371.45  E-value: 2.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 173
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVIITTPQEVSLQDVRKEIS 253
Cdd:cd02037    79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147372655 254 FCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGK 314
Cdd:cd02037   155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
89-355 5.22e-127

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 368.76  E-value: 5.22e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  89 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 168
Cdd:NF041136    1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAAahiDGAVIITTPQEVSLQDV 248
Cdd:NF041136   80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFPptTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:NF041136  157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                         250       260
                  ....*....|....*....|....*..
gi 1147372655 329 SPATLAYRSVIKRIQEFCSAQQSNKEN 355
Cdd:NF041136  235 SPAAKALEKIVDPILELLENKKSLTEE 261
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
90-342 8.48e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.80  E-value: 8.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  90 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 168
Cdd:PRK11670  104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDV 248
Cdd:PRK11670  182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:PRK11670  258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                         250
                  ....*....|....
gi 1147372655 329 SPATLAYRSVIKRI 342
Cdd:PRK11670  336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 71-276 1.51e-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: 162.66  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  71 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-- 148
Cdd:COG0489    70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 149 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVV 223
Cdd:COG0489   149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1147372655 224 QylaaAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENMsgfVCPK 276
Cdd:COG0489   222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 96-335 1.11e-20

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: 89.79  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQV--HQSGSGWSPVyvEDNLGVMSVGFL 173
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDKPVtlHDVLAGEADI--KDAIYEGPFGVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSSPddAVIWRGPKKSGMIKqfLRDV---DWGDVDYLIVDTPPGTSdehLSVVQYLAAAhiDGAVIITTPQEVSLQDVRK 250
Cdd:TIGR01969  80 VIPA--GVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSITDALK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 251 EISFCHKVKLPIIGVVENMSGfvcpkckKESQIFPPTTggAEIMcqdLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSP 330
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVT-------RDKTELGREE--IETI---LEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSP 218


                  ....*
gi 1147372655 331 ATLAY 335
Cdd:TIGR01969 219 AAQAF 223
ParA_partition NF041546
ParA family partition ATPase;
96-237 7.62e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 52.17  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 175
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147372655 176 SPDdaviwrgpkksgmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVVQylaAAHIdgaVII 237
Cdd:NF041546   62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK---AADL---VLI 103
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 92-342 1.27e-146

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: 413.77  E-value: 1.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  92 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 171
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 FLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 251
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 252 ISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPA 331
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1147372655 332 TLAYRSVIKRI 342
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 94-314 2.54e-130

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: 371.45  E-value: 2.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 173
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVIITTPQEVSLQDVRKEIS 253
Cdd:cd02037    79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147372655 254 FCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGK 314
Cdd:cd02037   155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
89-355 5.22e-127

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 368.76  E-value: 5.22e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  89 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 168
Cdd:NF041136    1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAAahiDGAVIITTPQEVSLQDV 248
Cdd:NF041136   80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFPptTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:NF041136  157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                         250       260
                  ....*....|....*....|....*..
gi 1147372655 329 SPATLAYRSVIKRIQEFCSAQQSNKEN 355
Cdd:NF041136  235 SPAAKALEKIVDPILELLENKKSLTEE 261
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
90-342 8.48e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.80  E-value: 8.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  90 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 168
Cdd:PRK11670  104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDV 248
Cdd:PRK11670  182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:PRK11670  258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                         250
                  ....*....|....
gi 1147372655 329 SPATLAYRSVIKRI 342
Cdd:PRK11670  336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 71-276 1.51e-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: 162.66  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  71 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-- 148
Cdd:COG0489    70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 149 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVV 223
Cdd:COG0489   149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1147372655 224 QylaaAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENMsgfVCPK 276
Cdd:COG0489   222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 96-342 1.03e-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: 97.49  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 171
Cdd:COG4963   105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 F-LLSSPDDAVIWR--GPKKSGMIKQFLRDvdwgDVDYLIVDTPPGTSDEHLSVvqyLAAAHIdgaVIITTPQEV-SLQD 247
Cdd:COG4963   185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 248 VRKEISFCHKVKLPI--IGVVENmsgfvcpKCKKESQIfppttgGAEIMCQDLKVPLLAKVPLDP-HIGKSCDKGQSFFV 324
Cdd:COG4963   255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321

                         250
                  ....*....|....*...
gi 1147372655 325 EAPGSPATLAYRSVIKRI 342
Cdd:COG4963   322 VAPKSPLAKAIRKLAARL 339
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 96-335 1.11e-20

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: 89.79  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQV--HQSGSGWSPVyvEDNLGVMSVGFL 173
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDKPVtlHDVLAGEADI--KDAIYEGPFGVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSSPddAVIWRGPKKSGMIKqfLRDV---DWGDVDYLIVDTPPGTSdehLSVVQYLAAAhiDGAVIITTPQEVSLQDVRK 250
Cdd:TIGR01969  80 VIPA--GVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSITDALK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 251 EISFCHKVKLPIIGVVENMSGfvcpkckKESQIFPPTTggAEIMcqdLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSP 330
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVT-------RDKTELGREE--IETI---LEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSP 218


                  ....*
gi 1147372655 331 ATLAY 335
Cdd:TIGR01969 219 AAQAF 223
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 109-342 2.05e-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: 85.71  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 109 TFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VEDNLGVmsvgFLLSSPDDAVIWR 184
Cdd:COG0455     1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 185 GPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEVSLQD---VRKEISFCHKVKlp 261
Cdd:COG0455    76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDayaLLKLLRRRLGVR-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 262 IIGVVENMSgfvcpkckKESQIFPPTTGGAEIMCQ---DLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSV 338
Cdd:COG0455   148 RAGVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIREL 219


                  ....
gi 1147372655 339 IKRI 342
Cdd:COG0455   220 AARL 223
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 96-322 5.58e-19

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: 84.70  E-value: 5.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 166
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 167 VMSVGFLLSSPD---DAVIWRGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEV 243
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 244 SLQDVRKEISFCHKVK-------LPIIGVVENMSGfvcPKCKKESQIfppttggaEIMCQDL-KVPLLAKVPLDPHIGKS 315
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221


                  ....*..
gi 1147372655 316 CDKGQSF 322
Cdd:pfam01656 222 PARGLPV 228
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 96-342 2.82e-17

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: 79.94  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 159
Cdd:cd02036     3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 160 yveDNLGVMSVGFllSSPDDAViwrGPKKsgmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSvvqylAAAHIDGAVIITT 239
Cdd:cd02036    79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 240 PQEVSLQDVRKEISFCHKVKLPIIGVVENMsgfVCPKCKKESQIFPPttggaEIMCQDLKVPLLAKVPLDPHIGKSCDKG 319
Cdd:cd02036   142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213

                         250       260
                  ....*....|....*....|...
gi 1147372655 320 QSFFVEAPGSPATLAYRSVIKRI 342
Cdd:cd02036   214 EPLVLYKPNSLAAKAFENIARRL 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 96-332 4.73e-17

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: 79.15  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 165
Cdd:cd02038     3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGfllSSPDDAVIWRGPKKSGMIKQFLRDVDwgDVDYLIVDTPPGTSDehlSVVQYLAAAHIdgAVIITTPQEVSL 245
Cdd:cd02038    78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QD---VRKEISfcHKVKLPIIGVVENMSgfvcpKCKKESQifpPTTGGAEIMCQ---DLKVPLLAKVPLDPHIGKSCDKG 319
Cdd:cd02038   148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQ 217

                         250
                  ....*....|...
gi 1147372655 320 QSFFVEAPGSPAT 332
Cdd:cd02038   218 KPFVLLFPNSKAS 230
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 89-344 1.28e-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: 78.36  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  89 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 161
Cdd:COG1192     1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 162 EDNLGVMSVgfLLSSPD----DAVIWRGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVvqyLAAAhiDGAVII 237
Cdd:COG1192    75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 238 TTPQEVSL----------QDVRKEisfcHKVKLPIIGVVENMsgfvcpkckkesqiFPPTTGGAEIMCQDLK----VPLL 303
Cdd:COG1192   147 VQPEYLSLeglaqlletiEEVRED----LNPKLEILGILLTM--------------VDPRTRLSREVLEELReefgDKVL 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1147372655 304 -AKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRIQE 344
Cdd:COG1192   209 dTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 96-338 9.46e-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: 70.00  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 171
Cdd:cd03111     3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 F-LLSSP---DDAVIWRGPKKSGMIkQFLRdvdwGDVDYLIVDTPPgtsdeHLSVVQYLAAAHIDGAVIITTPQEVSLQD 247
Cdd:cd03111    83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 248 VRKEISFCHKVKLPI--IGVVENmsgfvcpKCKKESQIFPPTTGGAeimcqdLKVPLLAKVPLDPH-IGKSCDKGQSFFV 324
Cdd:cd03111   153 ARRLLDSLRELEGSSdrLRLVLN-------RYDKKSEISPKDIEEA------LGLEVFATLPNDYKaVSESANTGRPLVE 219

                         250
                  ....*....|....
gi 1147372655 325 EAPGSPATLAYRSV 338
Cdd:cd03111   220 VAPRSALVRALQDL 233
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 95-344 7.12e-13

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 67.50  E-value: 7.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  95 KILVlSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----YVEDNLGVMS 169
Cdd:COG3640     2 KIAV-AGKGGVGKTTLSALLARYLAE-KGKPVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 170 VGFLLSSP------DDAVIWRG---------PKKSG---------MIKQFLRDVDWGDVDYLIVDTPPGTsdEHLSvvqY 225
Cdd:COG3640    74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEGGsgcycpenaLLRALLNHLVLGNYEYVVVDMEAGI--EHLG---R 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 226 LAAAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENmsgfvcpKCKKESQIfppttggaEIMCQDLKVPLLAK 305
Cdd:COG3640   149 GTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGF 213

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1147372655 306 VPLDPHIGKSCDKGQSFFvEAPGSPAtlayRSVIKRIQE 344
Cdd:COG3640   214 IPYDEEVREADLEGKPLL-DLPDSPA----VAAVEEIAE 247
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 96-343 7.86e-13

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: 67.75  E-value: 7.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 165
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGPKKsgMIKQFLRdvdwgDVDYLIVDTPPGtsdehLSVVQYLAAAHIDGAVIITTPQEVSL 245
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QDVRKeisfchkvklpIIGVVENMSgfvcpkCKKESQIF----PPTTGGAEIMCQD-----LKVPLLAKVPLDPHIGKSC 316
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKG------IEKIHLIVnrlrPEMVKKGDMLSVDdvleiLSIPLIGVIPEDEAIIVST 211

                         250       260
                  ....*....|....*....|....*..
gi 1147372655 317 DKGQSFFVEaPGSPATLAYRSVIKRIQ 343
Cdd:TIGR01968 212 NKGEPVVLN-DKSRAGKAFENIARRIL 237
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 94-268 2.29e-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: 64.90  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 166
Cdd:cd05387    20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 167 VMSVGFLLSSPDDAViwRGPKKSGMIKQFLRDVDwgdvdYLIVDTPP--GTSDEHLsvvqylAAAHIDGAVIITTPQEVS 244
Cdd:cd05387    99 VLPAGTVPPNPSELL--SSPRFAELLEELKEQYD-----YVIIDTPPvlAVADALI------LAPLVDGVLLVVRAGKTR 165

                         170       180
                  ....*....|....*....|....
gi 1147372655 245 LQDVRKEISFCHKVKLPIIGVVEN 268
Cdd:cd05387   166 RREVKEALERLEQAGAKVLGVVLN 189
PRK10818 PRK10818
septum site-determining protein MinD;
96-342 4.18e-11

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 62.65  E-value: 4.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 165
Cdd:PRK10818    5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGpkksgmIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVqYLAaahiDGAVIITTPQEVSL 245
Cdd:PRK10818   84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QDVRKeisfchkvklpIIGVVENMS--GFVCPKCKKESQIFPPTTGG---------AEIMCQDLKVPLLAKVPLDPHIGK 314
Cdd:PRK10818  151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219

                         250       260
                  ....*....|....*....|....*...
gi 1147372655 315 SCDKGQSFFVEAPgSPATLAYRSVIKRI 342
Cdd:PRK10818  220 ASNQGEPVILDIE-ADAGKAYADTVDRL 246
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 96-343 1.68e-10

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 60.84  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLE------------GE-QVHQSgsgwspvYVE 162
Cdd:COG2894     5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 163 D----NLgvmsvgFLLssP-----D-DAViwrgpKKSGMIK--QFLRDvdwgDVDYLIVDTPPGTsdEHLSvvqYLAAAH 230
Cdd:COG2894    77 DkrfeNL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIAG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 231 IDGAVIITTPQEVSLQDV-RkeisfchkvklpIIGVVENMSgfvcpkcKKESQI----FPPT---TGG---AEIMCQDLK 299
Cdd:COG2894   135 ADEAIVVTTPEVSSVRDAdR------------IIGLLEAKG-------IRKPHLiinrYRPAmvkRGDmlsVEDVLEILA 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1147372655 300 VPLLAKVPLDPHIGKSCDKGQSfFVEAPGSPATLAYRSVIKRIQ 343
Cdd:COG2894   196 IPLLGVVPEDEEVIVSSNRGEP-VVLDEKSKAGQAYRNIARRLL 238
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 95-307 6.32e-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: 55.85  E-value: 6.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  95 KILVLSGKGGVGKSTFSAHLAHGLAEdentqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED----------- 163
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 164 -NLGVMSVGF----------------LLSSPDDAVIWR------------------------GPKKSGMIKQFLR---DV 199
Cdd:cd03110    76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLKdrdtgkifisssdggplvhgrlniGEENSGKLVTELRkkaLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 200 DWGDVDYLIVDTPPGTsdeHLSVVQYLAAAhiDGAVIITTPQEVSLQDVRKEISFCHKVKLPiIGVVENMSGfvcpkckk 279
Cdd:cd03110   156 RSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD-------- 221

                         250       260
                  ....*....|....*....|....*...
gi 1147372655 280 esqIFPPTTGGAEIMCQDLKVPLLAKVP 307
Cdd:cd03110   222 ---INDEISEEIEDFADEEGIPLLGKIP 246
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 94-269 1.26e-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: 52.93  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 173
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 lsspdDAVIWRgpkksgmikqflrdvdwgdVDYLIVDTPPGTSDEHLSVvqyLAAAHIdgaVII-TTPQEVSLQDVRKEI 252
Cdd:cd02042    42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLL 91

                         170       180
                  ....*....|....*....|...
gi 1147372655 253 SFCHKVK------LPIIGVVENM 269
Cdd:cd02042    92 DTLEELKkqlnppLLILGILLTR 114
ParA_partition NF041546
ParA family partition ATPase;
96-237 7.62e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 52.17  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 175
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147372655 176 SPDdaviwrgpkksgmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVVQylaAAHIdgaVII 237
Cdd:NF041546   62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK---AADL---VLI 103
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 95-323 1.72e-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: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  95 KILVlSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 170
Cdd:cd02034     2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 171 GFLLSSPDDAVIWRG--------------PKKSG---------MIKQFLRDVDWGDVDYLIVDTPPGTsdEHLS--VVQy 225
Cdd:cd02034    76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGGGsgcycpvnaLLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 226 laaaHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENmsgfvcpKCKKESQIfppttggAEIMCQDLKVPLLAK 305
Cdd:cd02034   153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVN-------KVRNEEEQ-------ELIEELLIKLKLIGV 214

                         250
                  ....*....|....*...
gi 1147372655 306 VPLDPHIGKSCDKGQSFF 323
Cdd:cd02034   215 IPYDEEIMEADLKGKPLF 232
minD CHL00175
septum-site determining protein; Validated
 83-342 3.75e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 50.92  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  83 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 162
Cdd:CHL00175    5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 163 dnLGVMSVGFLLsspDDAVI----WRG----------------PKKSGMIKQFLRDVDWgdvDYLIVDTPPGtsdehLSV 222
Cdd:CHL00175   74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvtRKNMNMLVDSLKNRGY---DYILIDCPAG-----IDV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 223 VQYLAAAHIDGAVIITTPQEVSLQDVRK-----EISFCHKVKLPIIGVVENMsgfvcpkCKKESQIfpPTTGGAEImcqd 297
Cdd:CHL00175  141 GFINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM--SVRDVQEM---- 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1147372655 298 LKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRI 342
Cdd:CHL00175  208 LGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENAARRL 252
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 95-132 1.11e-05

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: 43.96  E-value: 1.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1147372655  95 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDID 132
Cdd:cd01983     2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 94-213 4.02e-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: 44.65  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVEDNLGVMSV--- 170
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSE-LGKKVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIdpn 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1147372655 171 ----------------GFLLSSPDDAV-----IWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPP 213
Cdd:pfam02374  71 meleeywqevqkymnaLLGLRMLEGILaeelaSLPGIDEAASFDEFKKYMDEGEYDVVVFDTAP 134
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
95-213 4.52e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.73  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  95 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDIDIcGPSIPKIMGLEGeqvhqsgsGWSPVYVE-DNLGVMSVgfl 173
Cdd:COG0003     4 RIIFFTGKGGVGKTTVAAATALALAER-GKRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVAvPNLYALEI--- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147372655 174 lsSPDDAV--IWRGPKK------------------SGM--------IKQFLRDVDWgdvDYLIVDTPP 213
Cdd:COG0003    71 --DPEAELeeYWERVRAplrgllpsagvdelaeslPGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 95-343 1.74e-03

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 39.66  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655  95 KILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDID--------ICGPSIPK-IMGLEGEQVHQSGSGWSPVYVEDNL 165
Cdd:cd02117     1 ESIVVYGKGGIGKSTTASNLSAALAE-GGKKVLHVGCDpkhdstllLTGGKVPPtIDEMLTEDGTAEELRREDLLFSGFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGPKKSGMIKqFLRDV---DW----------GDV---------------DYLIVdtppgTSD 217
Cdd:cd02117    80 GVDCVE--AGGPEPGVGCGGRGIGTMLE-LLEEHgllDDdydvvifdvlGDVvcggfaaplrrgfaqKVVIV-----VSE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 218 EHLSVvqyLAAAHIDGAViittpQEVSLQDVRkeisfchkvklpIIGVVENMSGfvcpkckkesqifPPTTGGAEIMCQD 297
Cdd:cd02117   152 ELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAFAAA 198

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1147372655 298 LKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRIQ 343
Cdd:cd02117   199 VGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIA 244
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 82-120 2.04e-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: 40.07  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1147372655  82 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 120
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
93-131 2.71e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 2.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1147372655  93 KHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDI 131
Cdd:COG5635   179 KKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPI 217
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 95-120 3.46e-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: 38.64  E-value: 3.46e-03
                          10        20
                  ....*....|....*....|....*.
gi 1147372655  95 KILVLSGKGGVGKSTFSAHLAHGLAE 120
Cdd:cd02035     1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 94-132 7.21e-03

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: 37.82  E-value: 7.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1147372655  94 HKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDID 132
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALL-YKGARVAAIDLD 38
 
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