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Conserved domains on  [gi|859786154|ref|XP_012910607|]
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cytosolic Fe-S cluster assembly factor NUBP1 isoform X1 [Mustela putorius furo]

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 7.66e-143

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: 402.60  E-value: 7.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSaarLDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  213 ISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQSFLMDAPASAA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 859786154  293 ALAYRSIIQKI 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 7.66e-143

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: 402.60  E-value: 7.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSaarLDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  213 ISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQSFLMDAPASAA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 859786154  293 ALAYRSIIQKI 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 7.23e-129

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: 366.06  E-value: 7.23e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLsaaRLDGAVIITTPQEVSLQDVRKEIS 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 859786154 215 FCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-315 3.20e-120

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 349.89  E-value: 3.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVEDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSAarlDGAVIITTPQEVSLQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 210 RKEISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFPptTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQSFLMDAPA 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250       260
                 ....*....|....*....|....*.
gi 859786154 290 SAAALAYRSIIQKIQEfcgHHQPKEE 315
Cdd:NF041136 235 SPAAKALEKIVDPILE---LLENKKS 257
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-281 6.27e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.03  E-value: 6.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVFVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSAArldGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVT---GAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 859786154 210 RKEISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQ 281
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGT 327
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 9.41e-48

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: 161.89  E-value: 9.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  32 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQvh 111
Cdd:COG0489   70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRP-- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 112 qsgsGWSPVFVED-------------NLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGELDYLIVDTPPGTSD 178
Cdd:COG0489  147 ----GLSDVLAGEasledviqpteveGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGV 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 859786154 179 EHLSVVQylsaARLDGAVIITTPQEVSLQDVRKEISFCHKVKVPIIGVVENMsvfVCPK 237
Cdd:COG0489  216 ADATLLA----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 57-304 7.82e-12

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: 64.28  E-value: 7.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVFVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeLDYLIVDTPPGT-SDEHLSVvqylsaARLDGAVIITTPQEVS 205
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAGIeSGFRNAV------APADEAIVVTTPEVSA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  206 LQDVRKeisfchkvkvpIIGVVENMSVF--------VCPKCKKESQIFppttgGAEVMCQDLKIPLLGKVPLDPHIGKSC 277
Cdd:TIGR01968 148 VRDADR-----------VIGLLEAKGIEkihlivnrLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPEDEAIIVST 211

                         250       260
                  ....*....|....*....|....*..
gi 859786154  278 DKGQSFLMDaPASAAALAYRSIIQKIQ 304
Cdd:TIGR01968 212 NKGEPVVLN-DKSRAGKAFENIARRIL 237
ParA_partition NF041546
ParA family partition ATPase;
57-93 2.43e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 2.43e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDID 93
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYR-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 7.66e-143

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: 402.60  E-value: 7.66e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSaarLDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  213 ISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQSFLMDAPASAA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 859786154  293 ALAYRSIIQKI 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 7.23e-129

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: 366.06  E-value: 7.23e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLsaaRLDGAVIITTPQEVSLQDVRKEIS 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 859786154 215 FCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-315 3.20e-120

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 349.89  E-value: 3.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVEDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSAarlDGAVIITTPQEVSLQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 210 RKEISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFPptTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQSFLMDAPA 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250       260
                 ....*....|....*....|....*.
gi 859786154 290 SAAALAYRSIIQKIQEfcgHHQPKEE 315
Cdd:NF041136 235 SPAAKALEKIVDPILE---LLENKKS 257
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-281 6.27e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 196.03  E-value: 6.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVFVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYLSAArldGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVT---GAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 859786154 210 RKEISFCHKVKVPIIGVVENMSVFVCPKCKKESQIFppTTGGAEVMCQDLKIPLLGKVPLDPHIGKSCDKGQ 281
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGT 327
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 9.41e-48

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: 161.89  E-value: 9.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  32 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQvh 111
Cdd:COG0489   70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRP-- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 112 qsgsGWSPVFVED-------------NLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGELDYLIVDTPPGTSD 178
Cdd:COG0489  147 ----GLSDVLAGEasledviqpteveGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGV 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 859786154 179 EHLSVVQylsaARLDGAVIITTPQEVSLQDVRKEISFCHKVKVPIIGVVENMsvfVCPK 237
Cdd:COG0489  216 ADATLLA----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 57-283 1.46e-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: 85.48  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   57 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVFVEDNLG 127
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGELDYLIVDTPPGTSDehlSVVQYLSAArlDGAVIITTPQEV 204
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  205 SLQDVRKEISFCHKVK-------VPIIGVVENMsvfVCPKCKKESQIfppttggaEVMCQDL-KIPLLGKVPLDPHIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK---VDGDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221


                  ....*..
gi 859786154  277 CDKGQSF 283
Cdd:pfam01656 222 PARGLPV 228
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 57-285 4.11e-18

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: 83.63  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVFVEDNLGVMSVG 132
Cdd:COG4963  105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 133 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgELDYLIVDTPPGTSDEHLSVvqyLSAArlDGAVIITTPQEVSLQDV 209
Cdd:COG4963  185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAA--DEVVLVTEPDLPSLRNA 255

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 859786154 210 RKEISFCHKVKVPI--IGVVENmsvfvcpKCKKESQIfppttgGAEVMCQDLKIPLLGKVPLDP-HIGKSCDKGQSFLM 285
Cdd:COG4963  256 KRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 57-276 1.51e-15

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: 74.53  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVFVEDNL 126
Cdd:cd02038    3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgELDYLIVDTPPGTSDehlSVVQYLSAArlDGAVIITTPQEVSL 206
Cdd:cd02038   78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAA--DEVIVVTTPEPTSI 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 859786154 207 QD---VRKEISfcHKVKVPIIGVVENMSvfvcpKCKKESQifpPTTGGAEVMCQ---DLKIPLLGKVPLDPHIGKS 276
Cdd:cd02038  148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRA 213
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 70-286 6.67e-15

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: 72.61  E-value: 6.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  70 TFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGE----QVHQSGSGWSPVFVEDNLGVmsvgFLLSSPDDAVIWR 145
Cdd:COG0455    1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKatlaDVLAGEADLEDAIVQGPGGL----DVLPGGSGPAELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 146 GPKKNGMIKQFLRDVDwGELDYLIVDTPPGTSDehlSVVQYLSAArlDGAVIITTPQEVSLQD---VRKEISFCHKVKVp 222
Cdd:COG0455   76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDayaLLKLLRRRLGVRR- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 859786154 223 iIGVVENMSvfvcpkckKESQIFPPTTGGAEVMCQ---DLKIPLLGKVPLDPHIGKSCDKGQSFLMD 286
Cdd:COG0455  149 -AGVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLA 206
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 57-303 1.84e-13

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: 68.77  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQV-------------HQSgsgwspvFVE 123
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENRIVytlvdvlegecrlEQA-------LIK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 124 D----NLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGELDYLIVDTPPGTSDEHLSVVqyLSAarlDGAVIIT 199
Cdd:cd02036   75 DkrweNLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFINAI--APA---DEAIIVT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 200 TPQEVSLQDVRKEISFCHKVKVPIIGVVENMsvfVCPKCKKESQIFPPttggaEVMCQDLKIPLLGKVPLDPHIGKSCDK 279
Cdd:cd02036  141 NPEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNR 212

                        250       260
                 ....*....|....*....|....
gi 859786154 280 GQSFLMDAPASAAALAYRSIIQKI 303
Cdd:cd02036  213 GEPLVLYKPNSLAAKAFENIARRL 236
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 55-229 6.75e-13

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: 66.05  E-value: 6.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVFVEDNLGVMS 130
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDVIQSTNIPNLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 131 VGFLLSSPDDAVIWRGPKKngmIKQFLRDVDwGELDYLIVDTPP-GTSDEHLSVvqylsAARLDGAVIITTPQEVSLQDV 209
Cdd:cd05387   99 VLPAGTVPPNPSELLSSPR---FAELLEELK-EQYDYVIIDTPPvLAVADALIL-----APLVDGVLLVVRAGKTRRREV 169

                        170       180
                 ....*....|....*....|
gi 859786154 210 RKEISFCHKVKVPIIGVVEN 229
Cdd:cd05387  170 KEALERLEQAGAKVLGVVLN 189
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 57-218 2.56e-12

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: 65.38  E-value: 2.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVFVEDNLGVMSVG 132
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGELDYLIVDTPPgtsdeHLSVVQYLSAARLDGAVIITTPQEVSLQD 208
Cdd:cd03111   83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152

                        170
                 ....*....|
gi 859786154 209 VRKEISFCHK 218
Cdd:cd03111  153 ARRLLDSLRE 162
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 57-304 7.82e-12

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: 64.28  E-value: 7.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVFVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeLDYLIVDTPPGT-SDEHLSVvqylsaARLDGAVIITTPQEVS 205
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAGIeSGFRNAV------APADEAIVVTTPEVSA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  206 LQDVRKeisfchkvkvpIIGVVENMSVF--------VCPKCKKESQIFppttgGAEVMCQDLKIPLLGKVPLDPHIGKSC 277
Cdd:TIGR01968 148 VRDADR-----------VIGLLEAKGIEkihlivnrLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPEDEAIIVST 211

                         250       260
                  ....*....|....*....|....*..
gi 859786154  278 DKGQSFLMDaPASAAALAYRSIIQKIQ 304
Cdd:TIGR01968 212 NKGEPVVLN-DKSRAGKAFENIARRIL 237
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 56-303 7.99e-12

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 64.03  E-value: 7.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  56 KILVlSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----FVEDNLGVMS 130
Cdd:COG3640    2 KIAV-AGKGGVGKTTLSALLARYLAE-KGKPVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 131 VGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGELDYLIVDTPPGTsdEHLSvvqY 186
Cdd:COG3640   74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG---R 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 187 LSAARLDGAVIITTPQEVSLQDVRKEISFCHKVKVPIIGVVENmsvfvcpKCKKESQIfppttggaEVMCQDLKIPLLGK 266
Cdd:COG3640  149 GTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGF 213

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 859786154 267 VPLDPHIGKSCDKGQSfLMDAPASAAALAYRSIIQKI 303
Cdd:COG3640  214 IPYDEEVREADLEGKP-LLDLPDSPAVAAVEEIAEKL 249
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 50-230 1.17e-11

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: 63.72  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  50 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVFV 122
Cdd:COG1192    1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 123 EDNLGVMSVgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGELDYLIVDTPPGTSDEHLSVvqyLSAArlDGAVII 198
Cdd:COG1192   75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 859786154 199 TTPQEVSL----------QDVRKEisfcHKVKVPIIGVVENM 230
Cdd:COG1192  147 VQPEYLSLeglaqlletiEEVRED----LNPKLEILGILLTM 184
PRK10818 PRK10818
septum site-determining protein MinD;
57-286 1.37e-11

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 63.81  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVFVED----NL 126
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGELDYLIVDTPPGTSDEHLSVVQYlsaarLDGAVIITTPQEVSL 206
Cdd:PRK10818  84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMALYF-----ADEAIITTNPEVSSV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 207 QDVRKeisfchkvkvpIIGVVENMS--VFVCPKCKKESQIFPPTTGG---------AEVMCQDLKIPLLGKVPLDPHIGK 275
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219

                        250
                 ....*....|.
gi 859786154 276 SCDKGQSFLMD 286
Cdd:PRK10818 220 ASNQGEPVILD 230
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 56-268 5.14e-10

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: 58.94  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  56 KILVLSGKGGVGKSTFSAHLAHGLAEdentqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVFVED----------- 124
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---VDWGEL------------------- 165
Cdd:cd03110   76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggpLVHGRLnigeensgklvtelrkkal 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 166 ------DYLIVDTPPGTsdeHLSVVQYLSAArlDGAVIITTPQEVSLQDVRKEISFCHKVKVPiIGVVENmsvfvcpkck 239
Cdd:cd03110  155 erskecDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVIN---------- 218

                        250       260
                 ....*....|....*....|....*....
gi 859786154 240 kESQIFPPTTGGAEVMCQDLKIPLLGKVP 268
Cdd:cd03110  219 -RYDINDEISEEIEDFADEEGIPLLGKIP 246
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 57-280 2.81e-09

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 56.60  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLE------------GE-QVHQSgsgwspvFVE 123
Cdd:COG2894    5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 124 D----NLgvmsvgFLLssP-----D-DAViwrgpKKNGMIK--QFLRDvdwgELDYLIVDTPPGTsdEH---LSVvqylS 188
Cdd:COG2894   77 DkrfeNL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQgfkNAI----A 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 189 AArlDGAVIITTPQEVSLQDV-RkeisfchkvkvpIIGVVENMSVfvcpkcKKESQI---FPPT---TGG---AEVMCQD 258
Cdd:COG2894  134 GA--DEAIVVTTPEVSSVRDAdR------------IIGLLEAKGI------RKPHLIinrYRPAmvkRGDmlsVEDVLEI 193

                        250       260
                 ....*....|....*....|..
gi 859786154 259 LKIPLLGKVPLDPHIGKSCDKG 280
Cdd:COG2894  194 LAIPLLGVVPEDEEVIVSSNRG 215
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 55-93 2.79e-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: 51.77  E-value: 2.79e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 859786154  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDID 93
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD 38
minD CHL00175
septum-site determining protein; Validated
 44-286 7.97e-08

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 52.85  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  44 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQVALLDIDICGPSIPKIMGLE------GEQVHQSGSGW 117
Cdd:CHL00175   5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLEnrvlytAMDVLEGECRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 118 SPVFVED----NLGvmsvgfLLSSPDDAVIWRGPKKN-GMIKQFLRDVDWgelDYLIVDTPPGTSdehlsvVQYLSA-AR 191
Cdd:CHL00175  84 DQALIRDkrwkNLS------LLAISKNRQRYNVTRKNmNMLVDSLKNRGY---DYILIDCPAGID------VGFINAiAP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 192 LDGAVIITTPQEVSLQDVRKeisfchkvkvpIIGVVE-----NMSVFVcpkckkeSQIFPPTTGGAEVM----CQD-LKI 261
Cdd:CHL00175 149 AQEAIVVTTPEITAIRDADR-----------VAGLLEangiyNVKLLV-------NRVRPDMIQANDMMsvrdVQEmLGI 210

                        250       260
                 ....*....|....*....|....*
gi 859786154 262 PLLGKVPLDPHIGKSCDKGQSFLMD 286
Cdd:CHL00175 211 PLLGAIPEDENVIISTNRGEPLVLN 235
ParA_partition NF041546
ParA family partition ATPase;
57-93 2.43e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 2.43e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 859786154  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDID 93
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 56-282 8.21e-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: 49.23  E-value: 8.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDiCGPSIPKIMGLEGEQVHQSG-SGWSPVFVEDNLGVMSVGFL 134
Cdd:cd02034    2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKtIGDIRERTGAKKGEPPEGMS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 135 LSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGELDYLIVDTPPGTsdEHLS--VVQYlsa 189
Cdd:cd02034   79 LNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIRA--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154 190 arLDGAVIITTPQEVSLQDVRKEISFCHKVKVPIIGVVENMSvfvcPKCKKESQIfppttggAEVMcqdLKIPLLGKVPL 269
Cdd:cd02034  154 --VDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----RNEEEQELI-------EELL---IKLKLIGVIPY 217

                        250
                 ....*....|...
gi 859786154 270 DPHIGKSCDKGQS 282
Cdd:cd02034  218 DEEIMEADLKGKP 230
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 56-93 1.28e-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: 43.57  E-value: 1.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 859786154  56 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDID 93
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 55-174 1.68e-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: 45.80  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   55 HKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMG-------------LEGEQVHQSGS---GWS 118
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSE-LGKKVLLISTDP-AHSLSDSFNqkfgheptkvkenLSAMEIDPNMEleeYWQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 859786154  119 PVFVEDNLGVMSVG-------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGELDYLIVDTPP 174
Cdd:pfam02374  79 EVQKYMNALLGLRMlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 46-229 2.19e-04

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 41.65  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154   46 IKEKMKTVKhKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIP-------KIMGLEGEQVHQS--GSG 116
Cdd:TIGR01007  10 IQFSGAEIK-VLLITSVKPGEGKSTTSANIAIAFAQ-AGYKTLLIDGDMRNSVMSgtfksqnKITGLTNFLSGTTdlSDA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  117 WSPVFVEdNLGVMSVGFLlsSPDDAVIWRGPKKNGMIKQFLRdvdwgELDYLIVDTPPgtsdehLSVV--QYLSAARLDG 194
Cdd:TIGR01007  88 ICDTNIE-NLDVITAGPV--PPNPTELLQSSNFKTLIETLRK-----RFDYIIIDTPP------IGTVtdAAIIARACDA 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 859786154  195 AVIITTPQEVSLQDVRKEISFCHKVKVPIIGVVEN 229
Cdd:TIGR01007 154 SILVTDAGKIKKREVKKAKEQLEQAGSNFLGVVLN 188
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
56-174 3.66e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 41.73  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 859786154  56 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDIDIcGPSIPKIMGLEGeqvhqsgsGWSPVFVE-DNLGVMSVgfl 134
Cdd:COG0003    4 RIIFFTGKGGVGKTTVAAATALALAER-GKRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVAvPNLYALEI--- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 859786154 135 lsSPDDAV--IWRGPKKN------------------GM--------IKQFLRDVDWgelDYLIVDTPP 174
Cdd:COG0003   71 --DPEAELeeYWERVRAPlrgllpsagvdelaeslpGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 43-81 1.67e-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: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 859786154   43 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
54-92 2.23e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 2.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 859786154  54 KHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDI 92
Cdd:COG5635  179 KKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPI 217
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 56-81 2.82e-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: 38.89  E-value: 2.82e-03
                         10        20
                 ....*....|....*....|....*.
gi 859786154  56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAE 26
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 56-81 2.90e-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: 2.90e-03
                         10        20
                 ....*....|....*....|....*.
gi 859786154  56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 55-93 6.05e-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: 6.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 859786154   55 HKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDID 93
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.
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