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Conserved domains on  [gi|1721879820|ref|XP_030232138|]
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cytosolic Fe-S cluster assembly factor NUBP1 [Gadus morhua]

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 ...
 65-315 1.58e-151

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: 425.33  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEeNLAVMSIG 144
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARL-GYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKE 224
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 225 IRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPA 304
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1721879820 305 ALAYSRIVKSI 315
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 ...
 65-315 1.58e-151

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: 425.33  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEeNLAVMSIG 144
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARL-GYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKE 224
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 225 IRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPA 304
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1721879820 305 ALAYSRIVKSI 315
Cdd:pfam10609 235 AKAFLKIADKV 245
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
65-317 7.80e-131

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 377.24  E-value: 7.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEENLAVMSIG 144
Cdd:NF041136    4 IKHKILVMSGKGGVGKSTVAANLAVALARR-GYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVMSIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKE 224
Cdd:NF041136   83 FLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADVRKS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 225 IRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFPptTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPA 304
Cdd:NF041136  160 INFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPA 237

                         250
                  ....*....|...
gi 1721879820 305 ALAYSRIVKSIQE 317
Cdd:NF041136  238 AKALEKIVDPILE 250
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 67-286 1.36e-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: 371.06  E-value: 1.36e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEeNLAVMSIGFL 146
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKK-GYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 147 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKEIR 226
Cdd:cd02037    79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 227 FCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIG 286
Cdd:cd02037   155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELA 212
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
65-311 1.93e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.28  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDVSKeVAVLDVDICGPSIPRIMGLDGEQ-VHQSGSGWSPVYVEeNLAVMSI 143
Cdd:PRK11670  106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK-VGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 144 GFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLStagIDGAVIITTPQEVSLQDVRK 223
Cdd:PRK11670  184 GYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAKK 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 224 EIRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSP 303
Cdd:PRK11670  260 GIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337


                  ....*...
gi 1721879820 304 AALAYSRI 311
Cdd:PRK11670  338 FTAIYRQL 345
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 44-249 2.03e-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: 161.51  E-value: 2.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  44 ASGATKAPDPAIAEIAEKMLTVKHKILVLSGKGGVGKSTFSAHLAHALAsDVSKEVAVLDVDICGPSIPRIMGLDGEQ-- 121
Cdd:COG0489    70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALA-QSGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 122 --VHQSGSGWSPV---YVEENLAVMSIGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGDLDYLIVDTPPGTSDEHLSIV 196
Cdd:COG0489   149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1721879820 197 QYLstagIDGAVIITTPQEVSLQDVRKEIRFCQKVKLPIIGVVENMsgfVCPK 249
Cdd:COG0489   222 ASL----VDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 69-316 1.19e-10

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: 60.81  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVDICGPSIPRIMGLDGEQVhqsgsgWSPVYVEE------------ 136
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIV------YTLVDVVEgecrlqqalikd 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 137 ----NLAVMSIGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDLDYLIVDTPPGT-SDEHLSIvqylstAGIDGAVIIT 211
Cdd:TIGR01968  77 krlkNLYLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAGIeSGFRNAV------APADEAIVVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 212 TPQEVSLQDVRKeirfcqkvklpIIGVVENMS--------GFVCPK-CKNTSQIfppttgGAERMCEELGLRLLGKVPLD 282
Cdd:TIGR01968 142 TPEVSAVRDADR-----------VIGLLEAKGiekihlivNRLRPEmVKKGDML------SVDDVLEILSIPLIGVIPED 204

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1721879820 283 PRIGRSCDEGRSFLAEvPDSPAALAYSRIVKSIQ 316
Cdd:TIGR01968 205 EAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
ParA_partition NF041546
ParA family partition ATPase;
69-105 8.25e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 51.78  E-value: 8.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVD 105
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARR-GYRVLLVDAD 37
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 65-315 1.58e-151

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: 425.33  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEeNLAVMSIG 144
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARL-GYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKE 224
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 225 IRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPA 304
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 1721879820 305 ALAYSRIVKSI 315
Cdd:pfam10609 235 AKAFLKIADKV 245
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
65-317 7.80e-131

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 377.24  E-value: 7.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEENLAVMSIG 144
Cdd:NF041136    4 IKHKILVMSGKGGVGKSTVAANLAVALARR-GYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVMSIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKE 224
Cdd:NF041136   83 FLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADVRKS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 225 IRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFPptTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPA 304
Cdd:NF041136  160 INFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPA 237

                         250
                  ....*....|...
gi 1721879820 305 ALAYSRIVKSIQE 317
Cdd:NF041136  238 AKALEKIVDPILE 250
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 67-286 1.36e-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: 371.06  E-value: 1.36e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEeNLAVMSIGFL 146
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKK-GYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 147 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLstaGIDGAVIITTPQEVSLQDVRKEIR 226
Cdd:cd02037    79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 227 FCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIG 286
Cdd:cd02037   155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELA 212
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
65-311 1.93e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.28  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  65 VKHKILVLSGKGGVGKSTFSAHLAHALASDVSKeVAVLDVDICGPSIPRIMGLDGEQ-VHQSGSGWSPVYVEeNLAVMSI 143
Cdd:PRK11670  106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK-VGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 144 GFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDLDYLIVDTPPGTSDEHLSIVQYLStagIDGAVIITTPQEVSLQDVRK 223
Cdd:PRK11670  184 GYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAKK 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 224 EIRFCQKVKLPIIGVVENMSGFVCPKCKNTSQIFppTTGGAERMCEELGLRLLGKVPLDPRIGRSCDEGRSFLAEVPDSP 303
Cdd:PRK11670  260 GIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337


                  ....*...
gi 1721879820 304 AALAYSRI 311
Cdd:PRK11670  338 FTAIYRQL 345
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 44-249 2.03e-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: 161.51  E-value: 2.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  44 ASGATKAPDPAIAEIAEKMLTVKHKILVLSGKGGVGKSTFSAHLAHALAsDVSKEVAVLDVDICGPSIPRIMGLDGEQ-- 121
Cdd:COG0489    70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALA-QSGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 122 --VHQSGSGWSPV---YVEENLAVMSIGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGDLDYLIVDTPPGTSDEHLSIV 196
Cdd:COG0489   149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1721879820 197 QYLstagIDGAVIITTPQEVSLQDVRKEIRFCQKVKLPIIGVVENMsgfVCPK 249
Cdd:COG0489   222 ASL----VDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 69-315 7.01e-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: 94.80  E-value: 7.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDVSKEVAVLDVDICGPSIPRIMGLDGEQ----VHQSGSGWSPVYVEENLAVMSIG 144
Cdd:COG4963   105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgDLDYLIVDTPPGTSDEHLSIvqyLSTAgiDGAVIITTPQEVSLQDV 221
Cdd:COG4963   185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAA--DEVVLVTEPDLPSLRNA 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 222 RKEIRFCQKVKLPI--IGVVENMsgfvcpkckntsqiFPPTTG-GAERMCEELGLRLLGKVPLDPR-IGRSCDEGRSFLA 297
Cdd:COG4963   256 KRLLDLLRELGLPDdkVRLVLNR--------------VPKRGEiSAKDIEEALGLPVAAVLPNDPKaVAEAANQGRPLAE 321

                         250
                  ....*....|....*...
gi 1721879820 298 EVPDSPAALAYSRIVKSI 315
Cdd:COG4963   322 VAPKSPLAKAIRKLAARL 339
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 69-295 4.85e-21

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: 89.71  E-value: 4.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDIcGPSIPRIMGLDGE--QVHQS------GSGW-SPVYVEENLA 139
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 140 VMSIGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGDLDYLIVDTPPGTSDEHLSivqYLSTAgiDGAVIITTPQEV 216
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGELLRN---ALIAA--DYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 217 SLQDVRKEIRFCQKVK-------LPIIGVVENMSGfvcpkckntsqifPPTTGGAER--MCEEL-GLRLLGKVPLDPRIG 286
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD-------------GDNHGKLLKeaLEELLrGLPVLGVIPRDEAVA 219


                  ....*....
gi 1721879820 287 RSCDEGRSF 295
Cdd:pfam01656 220 EAPARGLPV 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 82-315 5.60e-21

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: 89.56  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  82 TFSAHLAHALASdVSKEVAVLDVDICGPSIPRIMGLDGEQ-VHQSGSGWSPVyvEENLAVMSIGF-LLSSPDDAVIWRGP 159
Cdd:COG0455     1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADL--EDAIVQGPGGLdVLPGGSGPAELAEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 160 KKNGMIKQFLRDVDwGDLDYLIVDTPPGTSDEHLSIvqyLSTAgiDGAVIITTPQEVSLQD---VRKEIRfcQKVKLPII 236
Cdd:COG0455    78 DPEERLIRVLEELE-RFYDVVLVDTGAGISDSVLLF---LAAA--DEVVVVTTPEPTSITDayaLLKLLR--RRLGVRRA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 237 GVVENMSGfvcpkcknTSQIFPPTTGGAERMCEE-LG--LRLLGKVPLDPRIGRSCDEGRSFLAEVPDSPAALAYSRIVK 313
Cdd:COG0455   150 GVVVNRVR--------SEAEARDVFERLEQVAERfLGvrLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAA 221


                  ..
gi 1721879820 314 SI 315
Cdd:COG0455   222 RL 223
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 69-315 4.62e-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: 78.78  E-value: 4.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALAsDVSKEVAVLDVDICGPSIPRIMGLDG----------------EQVHQSGSGWspv 132
Cdd:cd02036     3 IVITSGKGGVGKTTTTANLGVALA-KLGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 133 yveENLAVMSIGFllSSPDDAViwrGPKKngmIKQFLRDVDwGDLDYLIVDTPPGTSDEHLSIVqylstAGIDGAVIITT 212
Cdd:cd02036    79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFINAI-----APADEAIIVTN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 213 PQEVSLQDVRKEIRFCQKVKLPIIGVVENMsgfVCPKCKNTSQIFPPttggaERMCEELGLRLLGKVPLDPRIGRSCDEG 292
Cdd:cd02036   142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213

                         250       260
                  ....*....|....*....|...
gi 1721879820 293 RSFLAEVPDSPAALAYSRIVKSI 315
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) ...
 69-305 8.70e-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: 77.99  E-value: 8.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALaSDVSKEVAVLD-------VDIC-GPSIPRIMG--LDGEqvhqSGSGWSPVYVEENL 138
Cdd:cd02038     3 IAVTSGKGGVGKTNVSANLALAL-SKLGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 139 AVMSIGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgDLDYLIVDTPPGTSDEhlsiVQYLSTAgIDGAVIITTPQEVSL 218
Cdd:cd02038    78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN----VLDFLLA-ADEVIVVTTPEPTSI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 219 QDVRKEIRFCQKVKLPI-IGVVENMSG------FVCPKCKNTSQIFppttggaermceeLGLRL--LGKVPLDPRIGRSC 289
Cdd:cd02038   148 TDAYALIKVLSRRGGKKnFRLIVNMARspkegrATFERLKKVAKRF-------------LDINLdfVGFIPYDQSVRRAV 214

                         250
                  ....*....|....*.
gi 1721879820 290 DEGRSFLAEVPDSPAA 305
Cdd:cd02038   215 RSQKPFVLLFPNSKAS 230
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 69-317 1.00e-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: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALAsDVSKEVAVLDVDICGpSIPRIMGLDGEQVHQS-------GSGWSPVYVEENLAVM 141
Cdd:COG1192     4 IAVANQKGGVGKTTTAVNLAAALA-RRGKRVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIVPTEIPGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 142 SIgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGDLDYLIVDTPPGTSdehlsivqYLSTAGI---DGAVIITTPQ 214
Cdd:COG1192    82 DL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLG--------LLTLNALaaaDSVLIPVQPE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 215 EVSLQDVRKEIRFCQKVK------LPIIGVVENMsgfVCPKCKNTSQIfppttggAERMCEELGLRLLG-KVPLDPRIGR 287
Cdd:COG1192   151 YLSLEGLAQLLETIEEVRedlnpkLEILGILLTM---VDPRTRLSREV-------LEELREEFGDKVLDtVIPRSVALAE 220

                         250       260       270
                  ....*....|....*....|....*....|
gi 1721879820 288 SCDEGRSFLAEVPDSPAALAYSRIVKSIQE 317
Cdd:COG1192   221 APSAGKPVFEYDPKSKGAKAYRALAEELLE 250
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 68-315 2.48e-16

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 77.13  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVlSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDIcGPSIPRIMGLDGEQvhqsgSGWSPV-----YVEENLAVMS 142
Cdd:COG3640     2 KIAV-AGKGGVGKTTLSALLARYLAEK-GKPVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 143 IGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGDLDYLIVDTPPGTsdEHLSivqY 198
Cdd:COG3640    74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG---R 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 199 LSTAGIDGAVIITTPQEVSLQDVRKEIRFCQKVKLPIIGVVENmsgfvcpKCKNTSQIfppttggaERMCEELGLRLLGK 278
Cdd:COG3640   149 GTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGF 213

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1721879820 279 VPLDPRIGRSCDEGRSfLAEVPDSPAALAYSRIVKSI 315
Cdd:COG3640   214 IPYDEEVREADLEGKP-LLDLPDSPAVAAVEEIAEKL 249
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 69-312 1.39e-13

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: 69.23  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDVSKEVAVLDVDICGPSIPRIMGLDGEQ----VHQSGSGWSPVYVEENLAVMSIG 144
Cdd:cd03111     3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 145 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGDLDYLIVDTPPgtsdeHLSIVQYLSTAGIDGAVIITTPQEVSLQD 220
Cdd:cd03111    83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 221 VRKEIRFC-------QKVKLpiigvVENmsgfvcpKCKNTSQIFPPTTGgaermcEELGLRLLGKVPLDPR-IGRSCDEG 292
Cdd:cd03111   153 ARRLLDSLrelegssDRLRL-----VLN-------RYDKKSEISPKDIE------EALGLEVFATLPNDYKaVSESANTG 214

                         250       260
                  ....*....|....*....|
gi 1721879820 293 RSFLAEVPDSPAALAYSRIV 312
Cdd:cd03111   215 RPLVEVAPRSALVRALQDLA 234
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 67-241 9.18e-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: 9.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDICGPSIPRIMGLDGEQ----VHQSGSGWSPV---YVEENLA 139
Cdd:cd05387    20 KVIAVTSASPGEGKSTVAANLAVALAQS-GKRVLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 140 VMSIGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgDLDYLIVDTPP-GTSDEHLSIVQYLstagiDGAVIITTPQEVSL 218
Cdd:cd05387    99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvLAVADALILAPLV-----DGVLLVVRAGKTRR 166

                         170       180
                  ....*....|....*....|...
gi 1721879820 219 QDVRKEIRFCQKVKLPIIGVVEN 241
Cdd:cd05387   167 REVKEALERLEQAGAKVLGVVLN 189
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 69-316 6.62e-12

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 64.69  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVDIcGpsiPR----IMGLDgEQVhqsgsgwspVY-----VE---- 135
Cdd:COG2894     5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADI-G---LRnldlVMGLE-NRI---------VYdlvdvIEgecr 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 136 -----------ENLavmsigFLL----SSPDDAViwrgpKKNGMIK--QFLRDvdwgDLDYLIVDTPPGtsdehlsIVQ- 197
Cdd:COG2894    70 lkqalikdkrfENL------YLLpasqTRDKDAL-----TPEQMKKlvEELKE----EFDYILIDSPAG-------IEQg 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 198 -YLSTAGIDGAVIITTPqEVSlqDVRKEIRfcqkvklpIIGVVENMSgfvcpkckntsqIFPP------------TTGG- 263
Cdd:COG2894   128 fKNAIAGADEAIVVTTP-EVS--SVRDADR--------IIGLLEAKG------------IRKPhliinryrpamvKRGDm 184

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721879820 264 --AERMCEELGLRLLGKVPLDPRIGRSCDEGrsflaEV----PDSPAALAYSRIVKSIQ 316
Cdd:COG2894   185 lsVEDVLEILAIPLLGVVPEDEEVIVSSNRG-----EPvvldEKSKAGQAYRNIARRLL 238
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 69-316 1.19e-10

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: 60.81  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVDICGPSIPRIMGLDGEQVhqsgsgWSPVYVEE------------ 136
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIV------YTLVDVVEgecrlqqalikd 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 137 ----NLAVMSIGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDLDYLIVDTPPGT-SDEHLSIvqylstAGIDGAVIIT 211
Cdd:TIGR01968  77 krlkNLYLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAGIeSGFRNAV------APADEAIVVT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 212 TPQEVSLQDVRKeirfcqkvklpIIGVVENMS--------GFVCPK-CKNTSQIfppttgGAERMCEELGLRLLGKVPLD 282
Cdd:TIGR01968 142 TPEVSAVRDADR-----------VIGLLEAKGiekihlivNRLRPEmVKKGDML------SVDDVLEILSIPLIGVIPED 204

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1721879820 283 PRIGRSCDEGRSFLAEvPDSPAALAYSRIVKSIQ 316
Cdd:TIGR01968 205 EAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 68-280 1.85e-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: 60.09  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVLSGKGGVGKSTFSAHLAHALasdvsKEVAVLDVDICGPSIPRIMGLDGEQVHQSGSGWSPVYVEE----------- 136
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLL-----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 137 -------NLAVMSIGF----------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 171
Cdd:cd03110    76 ckfgailEFFQKLIVDeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 172 VDWGDLDYLIVDTPPGTsdeHLSIVQylSTAGIDGAVIITTPQEVSLQDVRKEIRFCQKVKLPIIGVVenmsgfvcpkck 251
Cdd:cd03110   155 ERSKECDLAIIDGPPGT---GCPVVA--SITGADAVLLVTEPTPSGLHDLKRAIELAKHFGIPTGIVI------------ 217

                         250       260
                  ....*....|....*....|....*....
gi 1721879820 252 NTSQIFPPTTGGAERMCEELGLRLLGKVP 280
Cdd:cd03110   218 NRYDINDEISEEIEDFADEEGIPLLGKIP 246
PRK10818 PRK10818
septum site-determining protein MinD;
69-328 2.54e-09

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 57.26  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDVSKEVaVLDVDICGPSIPRIMGLDGEQVH------QSGSGWSPVYVE----ENL 138
Cdd:PRK10818    5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKdkrtENL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 139 AVMSIGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGDLDYLIVDTPPGTSDEHLsIVQYLStagiDGAVIITTPQEVSL 218
Cdd:PRK10818   84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGAL-MALYFA----DEAIITTNPEVSSV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 219 QDVRKeirfcqkvklpIIGVVENMS-----------GFVCPKCKNTSQIFPPTTGGAERMCEELGLRLLGKVPLDPRIGR 287
Cdd:PRK10818  151 RDSDR-----------ILGILASKSrraengeepikEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLR 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1721879820 288 SCDEGRSFLAEVpDSPAALAYSRIVKSI--QEYCSNLLTEEQR 328
Cdd:PRK10818  220 ASNQGEPVILDI-EADAGKAYADTVDRLlgEERPFRFIEEEKK 261
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 68-315 5.15e-09

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: 56.17  E-value: 5.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVlSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDiCGPSIPRIMGLDGEQVHQSGSGWSpvyVEENL----AVMSI 143
Cdd:cd02034     2 KIAV-AGKGGVGKTTIAALLIRYLAKK-GGKVLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTgakkGEPPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 144 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGDLDYLIVDTPPGTsdEHLS--IVQy 198
Cdd:cd02034    76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 199 lstaGIDGAVIITTPQEVSLQDVRKEIRFCQKVKLPIIGVVENMSgfvcPKCKNTSQIfppttggaermcEELG--LRLL 276
Cdd:cd02034   153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----RNEEEQELI------------EELLikLKLI 212

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1721879820 277 GKVPLDPRIGRSCDEGRSFLAEvpDSPAALAYSRIVKSI 315
Cdd:cd02034   213 GVIPYDEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 67-242 2.81e-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: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDicgpsiprimgldgeqvHQSgsgwspvyveenlavmsigfl 146
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR-GKRVLLIDLD-----------------PQG--------------------- 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 147 lsspdDAVIWRgpkkngmikqflrdvdwgdLDYLIVDTPPGTSDEHLSIvqyLSTAgiDGAVIITTPQEVSLQDVRKEIR 226
Cdd:cd02042    42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAA--DLVLIPVQPSPFDLDGLAKLLD 92

                         170       180
                  ....*....|....*....|..
gi 1721879820 227 FCQKVK------LPIIGVVENM 242
Cdd:cd02042    93 TLEELKkqlnppLLILGILLTR 114
ParA_partition NF041546
ParA family partition ATPase;
69-105 8.25e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 51.78  E-value: 8.25e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVD 105
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARR-GYRVLLVDAD 37
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 67-186 4.16e-06

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 47.73  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALaSDVSKEVAVLDVDIcGPSIPRIMGLDgeqvhqsgSGWSPVYVEENLAVMSIG-- 144
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQL-SELGKKVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIDpn 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721879820 145 -----------------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGDLDYLIVDTPP 186
Cdd:pfam02374  71 meleeywqevqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 69-241 5.94e-06

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: 46.28  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVDICGPSIP-------RIMGLDGEQVHQSGSGWSPVYVE-ENLAV 140
Cdd:TIGR01007  20 LLITSVKPGEGKSTTSANIAIAFAQ-AGYKTLLIDGDMRNSVMSgtfksqnKITGLTNFLSGTTDLSDAICDTNiENLDV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 141 MSIGFLlsSPDDAVIWRGPKKNGMIKQFLRDvdwgdLDYLIVDTPP-GTSDEHLSIVQYlstagIDGAVIITTPQEVSLQ 219
Cdd:TIGR01007  99 ITAGPV--PPNPTELLQSSNFKTLIETLRKR-----FDYIIIDTPPiGTVTDAAIIARA-----CDASILVTDAGKIKKR 166

                         170       180
                  ....*....|....*....|..
gi 1721879820 220 DVRKEIRFCQKVKLPIIGVVEN 241
Cdd:TIGR01007 167 EVKKAKEQLEQAGSNFLGVVLN 188
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 68-105 8.44e-06

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 43.96  E-value: 8.44e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1721879820  68 KILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVD 105
Cdd:cd01983     2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 68-316 1.50e-05

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: 45.82  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVD--------ICGPSIPR-IMGLDGEQVHQSGSGWSPVYVEENL 138
Cdd:cd02117     1 ESIVVYGKGGIGKSTTASNLSAALAE-GGKKVLHVGCDpkhdstllLTGGKVPPtIDEMLTEDGTAEELRREDLLFSGFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 139 AVMSIGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DWgDLDYLIVD-----------TPpgtsdehlsivqyLSTA 202
Cdd:cd02117    80 GVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDD-DYDVVIFDvlgdvvcggfaAP-------------LRRG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 203 GIDGAVIITTPQEVSL---QDVRKEIRFCQKVKLPIIGVVENMSGfvcpkckntsqifPPTTGGAERMCEELGLRLLGKV 279
Cdd:cd02117   141 FAQKVVIVVSEELMSLyaaNNIVKAVENYSKNGVRLAGLVANLRD-------------PAGTEEIQAFAAAVGTKILAVI 207

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1721879820 280 PLDPRIGRSCDEGRSFLAEVPDSPAALAYSRIVKSIQ 316
Cdd:cd02117   208 PRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIA 244
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
68-186 3.37e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 44.81  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVLSGKGGVGKSTFSAHLAHALASDvSKEVAVLDVDIcGPSIPRIMGLDGeqvhqsgsGWSPVYVE-ENLAVMSIgfl 146
Cdd:COG0003     4 RIIFFTGKGGVGKTTVAAATALALAER-GKRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVAvPNLYALEI--- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721879820 147 lsSPDDAV--IWRGPKKN------------------GM--------IKQFLRDVDWgdlDYLIVDTPP 186
Cdd:COG0003    71 --DPEAELeeYWERVRAPlrgllpsagvdelaeslpGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 68-210 1.30e-04

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: 42.88  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  68 KILVLSGKGGVGKSTFSAHLAHALASD------VSKEVA-----VLDVDIcGPSIP-----------------------R 113
Cdd:cd02035     1 RIIFFGGKGGVGKTTIAAATAVRLAEQgkrvllVSTDPAhslsdAFGQKL-GGETPvkgapnlwameidpeealeeyweE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 114 IMGLDGEQVHQSGSGwsPVYVEEnlavmsigfLLSSP--DDAViwrgpkkngMIKQFLRDVDWGDLDYLIVDTPPG---- 187
Cdd:cd02035    80 VKELLAQYLRLPGLD--EVYAEE---------LLSLPgmDEAA---------AFDELREYVESGEYDVIVFDTAPTghtl 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1721879820 188 -------------------------TSDEHLSI------VQYLSTAGID-GAVII 210
Cdd:cd02035   140 rllslpleqvrellrdperttfvlvTIPEKLSIyeterlWGELQQYGIPvDGVVV 194
minD CHL00175
septum-site determining protein; Validated
 69-220 1.81e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.45  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  69 ILVLSGKGGVGKSTFSAHLAHALASdVSKEVAVLDVDICGPSIPRIMGLDG----------------EQVHQSGSGWSpv 132
Cdd:CHL00175   18 IVITSGKGGVGKTTTTANLGMSIAR-LGYRVALIDADIGLRNLDLLLGLENrvlytamdvlegecrlDQALIRDKRWK-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820 133 yveeNLAVMSIGfllSSPDDAVIWRgpKKNGMIKQFLRDVDWgdlDYLIVDTPPGTSdehLSIVQYLSTAgiDGAVIITT 212
Cdd:CHL00175   95 ----NLSLLAIS---KNRQRYNVTR--KNMNMLVDSLKNRGY---DYILIDCPAGID---VGFINAIAPA--QEAIVVTT 157


                  ....*...
gi 1721879820 213 PQEVSLQD 220
Cdd:CHL00175  158 PEITAIRD 165
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 67-105 1.02e-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: 40.13  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1721879820  67 HKILVLSGKGGVGKSTFSAHLAHALAsDVSKEVAVLDVD 105
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALL-YKGARVAAIDLD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 55-186 1.61e-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: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  55 IAEIAEKmltvKHKILVLSGKGGVGKSTFSAHLAHALA----------SDVSKEVAV-LDVDICGPSIPRImglDGEQVH 123
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAnkgldvhlttSDPAAHLSVtLTGSLNNLQVSRI---DPKQET 385

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721879820 124 QSgsgwspvYVEENLAVMSIGflLSSPDDAVI---WRGP--KKNGMIKQFLRDVDWGDLDYLIVDTPP 186
Cdd:TIGR04291 386 ER-------YRQEVLATKGKE--LDEDGKAYLeedLRSPctEEIAVFQAFSRIIREAGDRFVVMDTAP 444
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
63-94 2.17e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 2.17e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1721879820  63 LTVKHKILVLSGKGGVGKSTFSAHLAHALASD 94
Cdd:COG5635   176 LEAKKKRLLILGEPGSGKTTLLRYLALELAER 207
aroK PRK00131
shikimate kinase; Reviewed
 66-120 4.40e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.48  E-value: 4.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879820  66 KHKILVLSGKGGVGKSTFSAHLAHALAsdvskeVAVLDVDI-----CGPSIPRIMGLDGE 120
Cdd:PRK00131    3 KGPNIVLIGFMGAGKSTIGRLLAKRLG------YDFIDTDHliearAGKSIPEIFEEEGE 56
 
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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