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Conserved domains on  [gi|16077222|ref|NP_388035|]
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phosphorylation-dependent (Y327) transcriptional regulator [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

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

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

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

Graphical summary

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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 ...
 109-344 4.00e-121

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: 349.06  E-value: 4.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITV-RPTIEGEKLLPVERFGVKVMSMGFFVE-E 186
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGeRPEQSDGGIIPVEAHGIKVMSIGFLLPdE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   187 NAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDH 266
Cdd:pfam10609  86 DDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMFKKVNV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   267 EVVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLKQPDWDK-DQFAPSV-YDENHPIGEIYQDIAKKI 344
Cdd:pfam10609 166 PVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAgDEGKPFVlADPDSPAAKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 109-344 4.00e-121

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: 349.06  E-value: 4.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITV-RPTIEGEKLLPVERFGVKVMSMGFFVE-E 186
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGeRPEQSDGGIIPVEAHGIKVMSIGFLLPdE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   187 NAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDH 266
Cdd:pfam10609  86 DDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMFKKVNV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   267 EVVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLKQPDWDK-DQFAPSV-YDENHPIGEIYQDIAKKI 344
Cdd:pfam10609 166 PVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAgDEGKPFVlADPDSPAAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 109-318 5.24e-105

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: 306.74  E-value: 5.24e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRP-TIEGEKLLPVERFGVKVMSMGFFVEEN 187
Cdd:cd02037   3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPlHQSEEGIVPVEVGGIKVMSIGFLLPED 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 188 APVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDHE 267
Cdd:cd02037  83 DAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKLNIP 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16077222 268 VVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLKQPDWD 318
Cdd:cd02037 163 VLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
109-344 1.19e-76

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 240.10  E-value: 1.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGIT-VRPTIEGEKLLPVERF-GVKVMSMGFFVE- 185
Cdd:NF041136   8 ILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEgKRLGSEDEGILPVEYSdNLKVMSIGFLLEn 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  186 ENAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTD 265
Cdd:NF041136  88 RDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINFCRKLN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  266 HEVVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLkQPDWDK--DQFAPSVYDEN-HPIGEIYQDIAK 342
Cdd:NF041136 168 IPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPI-DPEIVEagDAGRPFVLDYAwSPAAKALEKIVD 246


                 ..
gi 16077222  343 KI 344
Cdd:NF041136 247 PI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
78-348 7.47e-67

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 214.91  E-value: 7.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   78 FEELPEETVAKFRAPSAEKK----------TLLNMDNPPV------FLAVASGKGGVGKSTVSVNLAISLARLGKKVGLI 141
Cdd:PRK11670  63 FEELKEQCSAELLRITGAKAidwklshniaTLKRVNNQPGvngvknIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGIL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  142 DADIYGFSVPDMMGIT-VRPTI-EGEKLLPVERFGVKVMSMGFFVEENAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLD 219
Cdd:PRK11670 143 DADIYGPSIPTMLGAEdQRPTSpDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLD 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  220 LPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDHEVVGVIENMAYYESAKTGEREYVFGKGGGDKLA 299
Cdd:PRK11670 223 MPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLA 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16077222  300 EELNVPLLGRIPLK---QPDWDKDQfaPSVY-DENHPIGEIYQDIAKKIDAKM 348
Cdd:PRK11670 303 EKYHTQLLGQMPLHislREDLDRGT--PTVVsRPESEFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 99-299 1.21e-49

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: 168.06  E-value: 1.21e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  99 LLNMDNPPVFLAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTIE---------GEKLLP 169
Cdd:COG0489  85 LLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaslEDVIQP 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 170 VERFGVKVMSMGFFVEENApvvwrGPMLGKMLNNFFHEVEwGEVDYIVLDLPPGTGDVALDVHTMLPSCkEIIVSTPHPT 249
Cdd:COG0489 165 TEVEGLDVLPAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVDG-VLLVVRPGKT 237

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16077222 250 AAFVAARAGSMAIKTDHEVVGVIENMAYYESAKT--GEREYVFGKGGGDKLA 299
Cdd:COG0489 238 ALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERYygGGEEYGYREYGDREIA 289
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 109-311 1.80e-13

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 69.37  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMG-----ITVRPTIEGEKLLP----VERFGVKVMS 179
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGmedkpVTLHDVLAGEADIKdaiyEGPFGVKVIP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   180 MGffveenapVVWRGPMLGK--MLNNFFHEVEwGEVDYIVLDLPPGTGdvaLDVHTMLPSCKE-IIVSTPHPTAAFVAAR 256
Cdd:TIGR01969  83 AG--------VSLEGLRKADpdKLEDVLKEII-DDTDFLLIDAPAGLE---RDAVTALAAADElLLVVNPEISSITDALK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16077222   257 AGSMAIKTDHEVVGVIENMAYYEsaktgereyvFGKGGGDKLAEELNVPLLGRIP 311
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVTRD----------KTELGREEIETILEVPVLGVVP 195
ParA_partition NF041546
ParA family partition ATPase;
109-144 1.57e-10

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 59.87  E-value: 1.57e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 109-344 4.00e-121

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: 349.06  E-value: 4.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITV-RPTIEGEKLLPVERFGVKVMSMGFFVE-E 186
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGeRPEQSDGGIIPVEAHGIKVMSIGFLLPdE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   187 NAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDH 266
Cdd:pfam10609  86 DDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDMFKKVNV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   267 EVVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLKQPDWDK-DQFAPSV-YDENHPIGEIYQDIAKKI 344
Cdd:pfam10609 166 PVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAgDEGKPFVlADPDSPAAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 109-318 5.24e-105

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: 306.74  E-value: 5.24e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRP-TIEGEKLLPVERFGVKVMSMGFFVEEN 187
Cdd:cd02037   3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPlHQSEEGIVPVEVGGIKVMSIGFLLPED 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 188 APVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDHE 267
Cdd:cd02037  83 DAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKLNIP 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16077222 268 VVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLKQPDWD 318
Cdd:cd02037 163 VLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
109-344 1.19e-76

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 240.10  E-value: 1.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGIT-VRPTIEGEKLLPVERF-GVKVMSMGFFVE- 185
Cdd:NF041136   8 ILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEgKRLGSEDEGILPVEYSdNLKVMSIGFLLEn 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  186 ENAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTD 265
Cdd:NF041136  88 RDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINFCRKLN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  266 HEVVGVIENMAYYESAKTGEREYVFGKGGGDKLAEELNVPLLGRIPLkQPDWDK--DQFAPSVYDEN-HPIGEIYQDIAK 342
Cdd:NF041136 168 IPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPI-DPEIVEagDAGRPFVLDYAwSPAAKALEKIVD 246


                 ..
gi 16077222  343 KI 344
Cdd:NF041136 247 PI 248
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
78-348 7.47e-67

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 214.91  E-value: 7.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   78 FEELPEETVAKFRAPSAEKK----------TLLNMDNPPV------FLAVASGKGGVGKSTVSVNLAISLARLGKKVGLI 141
Cdd:PRK11670  63 FEELKEQCSAELLRITGAKAidwklshniaTLKRVNNQPGvngvknIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGIL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  142 DADIYGFSVPDMMGIT-VRPTI-EGEKLLPVERFGVKVMSMGFFVEENAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLD 219
Cdd:PRK11670 143 DADIYGPSIPTMLGAEdQRPTSpDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLD 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  220 LPPGTGDVALDVHTMLPSCKEIIVSTPHPTAAFVAARAGSMAIKTDHEVVGVIENMAYYESAKTGEREYVFGKGGGDKLA 299
Cdd:PRK11670 223 MPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLA 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16077222  300 EELNVPLLGRIPLK---QPDWDKDQfaPSVY-DENHPIGEIYQDIAKKIDAKM 348
Cdd:PRK11670 303 EKYHTQLLGQMPLHislREDLDRGT--PTVVsRPESEFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 99-299 1.21e-49

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: 168.06  E-value: 1.21e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  99 LLNMDNPPVFLAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTIE---------GEKLLP 169
Cdd:COG0489  85 LLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaslEDVIQP 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 170 VERFGVKVMSMGFFVEENApvvwrGPMLGKMLNNFFHEVEwGEVDYIVLDLPPGTGDVALDVHTMLPSCkEIIVSTPHPT 249
Cdd:COG0489 165 TEVEGLDVLPAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVDG-VLLVVRPGKT 237

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16077222 250 AAFVAARAGSMAIKTDHEVVGVIENMAYYESAKT--GEREYVFGKGGGDKLA 299
Cdd:COG0489 238 ALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERYygGGEEYGYREYGDREIA 289
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 108-250 9.13e-23

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: 94.94  E-value: 9.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 108 FLAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTI------------------EGEKLLP 169
Cdd:cd02038   2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTLgdvlkgrvslediivegpEGLDIIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 170 -----VERFGVKVMSMGFFVEEnapvvwrgpmLGKMLNNFfhevewgevDYIVLDLPPGTGDVALDvhTMLPSCKEIIVS 244
Cdd:cd02038  82 ggsgmEELANLDPEQKAKLIEE----------LSSLESNY---------DYLLIDTGAGISRNVLD--FLLAADEVIVVT 140


                ....*.
gi 16077222 245 TPHPTA 250
Cdd:cd02038 141 TPEPTS 146
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 122-347 2.58e-18

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: 82.63  E-value: 2.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 122 TVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTI----EGEKllPVERF------GVKVMSMGffveeNAPVV 191
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLadvlAGEA--DLEDAivqgpgGLDVLPGG-----SGPAE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 192 WRGPMLGKMLNNFFHEVEwGEVDYIVLDLPPGTGDVALDvhtMLPSCKE-IIVSTPHPTAAfVAARAGSMAIKTDHEV-- 268
Cdd:COG0455  74 LAELDPEERLIRVLEELE-RFYDVVLVDTGAGISDSVLL---FLAAADEvVVVTTPEPTSI-TDAYALLKLLRRRLGVrr 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 269 VGVIENMAyyESAKTGEREYvfgkgggDKLAE------ELNVPLLGRIPlkqpdWD-------KDQFAPSVYDENHPIGE 335
Cdd:COG0455 149 AGVVVNRV--RSEAEARDVF-------ERLEQvaerflGVRLRVLGVIP-----EDpavreavRRGRPLVLAAPDSPAAR 214

                       250
                ....*....|..
gi 16077222 336 IYQDIAKKIDAK 347
Cdd:COG0455 215 AIRELAARLAGW 226
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 111-344 2.70e-15

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: 74.16  E-value: 2.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 111 VASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIyGFSVPDM-MG------ITVRPTIEGE-----KLLPVERF-GVKV 177
Cdd:cd02036   5 ITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADI-GLRNLDLiLGlenrivYTLVDVLEGEcrleqALIKDKRWeNLYL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 178 MSMGFFVEENApvvwrgpMLGKMLNNFFHEVEwGEVDYIVLDLPPGTGDVALdvHTMLPSCKEIIVSTPHPTAAFVAARA 257
Cdd:cd02036  84 LPASQTRDKDA-------LTPEKLEELVKELK-DSFDFILIDSPAGIESGFI--NAIAPADEAIIVTNPEISSVRDADRV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 258 GSMAIKTDHEVVGVIENMAYYESAKTGEREYVfgkgggDKLAEELNVPLLGRIPlkqpdwdkdqFAPSV----------- 326
Cdd:cd02036 154 IGLLESKGIVNIGLIVNRYRPEMVKSGDMLSV------EDIQEILGIPLLGVIP----------EDPEVivatnrgeplv 217

                       250
                ....*....|....*....
gi 16077222 327 -YDENHPIGEIYQDIAKKI 344
Cdd:cd02036 218 lYKPNSLAAKAFENIARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 109-311 4.12e-15

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: 73.53  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD-------IYGFSVP-DMMGITVRPTIEGEKLL-------PVERF 173
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDpqsnnssVEGLEGDiAPALQALAEGLKGRVNLdpillkeKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   174 GVKVMSMGfFVEENAPVVWRGPMLGKMLNNFFHEVEwGEVDYIVLDLPPGTGDvaLDVHTMLPSCKEIIVSTPHPTAAFV 253
Cdd:pfam01656  81 GLDLIPGN-IDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILVED 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16077222   254 AARAGSMAIKTDH-------EVVGVIENMayYESAKTGEREYVFgkgggdkLAEEL-NVPLLGRIP 311
Cdd:pfam01656 157 AKRLGGVIAALVGgyallglKIIGVVLNK--VDGDNHGKLLKEA-------LEELLrGLPVLGVIP 213
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 109-144 1.42e-13

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: 66.79  E-value: 1.42e-13
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:cd02042   3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 109-311 1.80e-13

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 69.37  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMG-----ITVRPTIEGEKLLP----VERFGVKVMS 179
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGmedkpVTLHDVLAGEADIKdaiyEGPFGVKVIP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   180 MGffveenapVVWRGPMLGK--MLNNFFHEVEwGEVDYIVLDLPPGTGdvaLDVHTMLPSCKE-IIVSTPHPTAAFVAAR 256
Cdd:TIGR01969  83 AG--------VSLEGLRKADpdKLEDVLKEII-DDTDFLLIDAPAGLE---RDAVTALAAADElLLVVNPEISSITDALK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16077222   257 AGSMAIKTDHEVVGVIENMAYYEsaktgereyvFGKGGGDKLAEELNVPLLGRIP 311
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVTRD----------KTELGREEIETILEVPVLGVVP 195
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 109-347 6.36e-13

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 67.75  E-value: 6.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIyGFSVPDM-MGI------TVRPTIEGE---------------- 165
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADI-GLRNLDLlLGLenrivyTLVDVVEGEcrlqqalikdkrlknl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   166 KLLPV----ERFGVKVMSMGFFVEEnapvvwrgpmlgkMLNNFfhevewgevDYIVLDLPPGTgDVALDvHTMLPSCKEI 241
Cdd:TIGR01968  83 YLLPAsqtrDKDAVTPEQMKKLVNE-------------LKEEF---------DYVIIDCPAGI-ESGFR-NAVAPADEAI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   242 IVSTPHPTAAFVAARAGSMAIKTDHEVVGVIENMAYYESAKTGEREYVfgkgggDKLAEELNVPLLGRIPLkqpdwDKD- 320
Cdd:TIGR01968 139 VVTTPEVSAVRDADRVIGLLEAKGIEKIHLIVNRLRPEMVKKGDMLSV------DDVLEILSIPLIGVIPE-----DEAi 207

                         250       260       270
                  ....*....|....*....|....*....|..
gi 16077222   321 -----QFAPSVYDENHPIGEIYQDIAKKIDAK 347
Cdd:TIGR01968 208 ivstnKGEPVVLNDKSRAGKAFENIARRILGE 239
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 109-225 9.08e-13

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: 67.19  E-value: 9.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD-------IYGFSVPDMMG--------------ITVRPTIEGEKL 167
Cdd:COG1192   4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDpqgnltsGLGLDPDDLDPtlydlllddapledAIVPTEIPGLDL 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16077222 168 LP-------VERFGVKVMSMGFFveenapvvwrgpmlgkmLNNFFHEVEwGEVDYIVLDLPPGTG 225
Cdd:COG1192  84 IPanidlagAEIELVSRPGRELR-----------------LKRALAPLA-DDYDYILIDCPPSLG 130
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 109-311 1.40e-12

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: 67.83  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARL-GKKVGLIDADIYGFSVPDMMGITVRPTIEG-------------EKLLPVERFG 174
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDLEPRRGLADalrnpdrldetllDRALTRHSSG 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 175 VKVMSMgffveENAPVVWR-------GPMLGKMLNNFfhevewgevDYIVLDLPPGTGDVALDVhtmLPSCKEI-IVSTP 246
Cdd:COG4963 185 LSVLAA-----PADLERAEevspeavERLLDLLRRHF---------DYVVVDLPRGLNPWTLAA---LEAADEVvLVTEP 247

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16077222 247 HPTAAFVAARA----GSMAIKTDHevVGVIENMAyyeSAKTGEREyvfgkgggDKLAEELNVPLLGRIP 311
Cdd:COG4963 248 DLPSLRNAKRLldllRELGLPDDK--VRLVLNRV---PKRGEISA--------KDIEEALGLPVAAVLP 303
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 111-145 1.65e-12

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 66.62  E-value: 1.65e-12
                        10        20        30
                ....*....|....*....|....*....|....*
gi 16077222 111 VASGKGGVGKSTVSVNLAISLARLGKKVGLIDADI 145
Cdd:COG2894   7 VTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI 41
minD CHL00175
septum-site determining protein; Validated
 109-311 2.12e-12

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 66.72  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGI------TVRPTIEGE-----KLLPVERFgvKV 177
Cdd:CHL00175  18 IVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLenrvlyTAMDVLEGEcrldqALIRDKRW--KN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  178 MSMgFFVEENAPvvwRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTgDVALdVHTMLPSCKEIIVSTPHPTAAFVAARA 257
Cdd:CHL00175  96 LSL-LAISKNRQ---RYNVTRKNMNMLVDSLKNRGYDYILIDCPAGI-DVGF-INAIAPAQEAIVVTTPEITAIRDADRV 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16077222  258 GSMAIKTDHEVVGVIENMAYYESAKTGEREYVfgkgggDKLAEELNVPLLGRIP 311
Cdd:CHL00175 170 AGLLEANGIYNVKLLVNRVRPDMIQANDMMSV------RDVQEMLGIPLLGAIP 217
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 110-144 3.33e-11

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 61.45  E-value: 3.33e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 16077222   110 AVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:pfam13614   5 AIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
ParA_partition NF041546
ParA family partition ATPase;
109-144 1.57e-10

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 59.87  E-value: 1.57e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
114-345 9.21e-10

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 58.61  E-value: 9.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   114 GKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTI--EGEKLLPVERFGVK-VMSMGF----FVEE 186
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQPTVldTAREKGYVEDVEVEdVVYKGYggvkCVES 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   187 NAPVVWRG----------PMLGKmlNNFFHevewgEVDYIVLDLppgTGDV-----ALDVHTMLPScKEIIVSTPHPTAA 251
Cdd:pfam00142  87 GGPEPGVGcagrgvitaiNLLEE--LGAYD-----DLDFVLYDV---LGDVvcggfAMPIREGKAQ-EIYIVTSNEMMAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   252 FVAARAGSMAIKTDH----EVVGVIENmayyesaktgEREYVFGKGGGDKLAEELNVPLLGRIPLkQPDWDKDQFAPSV- 326
Cdd:pfam00142 156 YAANNIAKGIQKYAKsggvRLGGIICN----------SRKVDDERELIDAFAEELGTQVLHFVPR-DNIVRKAELRKQTv 224

                         250       260
                  ....*....|....*....|.
gi 16077222   327 --YDENHPIGEIYQDIAKKID 345
Cdd:pfam00142 225 ieYAPDSEQAQEYRELARKIL 245
PHA02518 PHA02518
ParA-like protein; Provisional
 109-279 2.26e-09

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 56.78  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPdmmGITVRPtiEGEKLLPVERFGVKVmsmgffveena 188
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTD---WAEARE--EGEPLIPVVRMGKSI----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  189 pvvwRGPMLgKMLNNFfhevewgevDYIVLDLPPGTGDV---ALDVHTM-----LPS------CKEII--------VSTP 246
Cdd:PHA02518  67 ----RADLP-KVASGY---------DYVVVDGAPQDSELaraALRIADMvlipvQPSpfdiwaAPDLVelikarqeVTDG 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 16077222  247 HPTAAFVAARagsmAIKTDHEVVGVIENMAYYE 279
Cdd:PHA02518 133 LPKFAFIISR----AIKNTQLYREARKALAGYG 161
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 109-222 6.32e-09

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: 54.88  E-value: 6.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTIE---------GEKLLPVERFGVKVMS 179
Cdd:cd05387  22 IAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSevlsgqaslEDVIQSTNIPNLDVLP 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16077222 180 MGFFVEENAPVVwRGPMLGKMLNnffhevEW-GEVDYIVLDLPP 222
Cdd:cd05387 102 AGTVPPNPSELL-SSPRFAELLE------ELkEQYDYVIIDTPP 138
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 109-144 2.02e-08

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: 51.66  E-value: 2.02e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:cd01983   3 IAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 109-342 6.15e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 52.86  E-value: 6.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 109 LAVAsGKGGVGKSTVSVNLAISLARLGKKVGLIDADIyGFSVPDMMGITV-----------RPTIEGEKLLP-------- 169
Cdd:COG3640   3 IAVA-GKGGVGKTTLSALLARYLAEKGKPVLAVDADP-NANLAEALGLEVeadlikplgemRELIKERTGAPgggmfkln 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 170 -----------VERFGVKVMSMGffveenapVVWRG------PMlGKMLNNFFHEVEWGEVDYIVLDLPPGT-----GdV 227
Cdd:COG3640  81 pkvddipeeylVEGDGVDLLVMG--------TIEEGgsgcycPE-NALLRALLNHLVLGNYEYVVVDMEAGIehlgrG-T 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 228 ALDVHTMlpsckeIIVSTPHPTAAFVAARAGSMAIKTDHEVVGVIENMAYYESAKtgereyvfgkgggDKLAEELNVPLL 307
Cdd:COG3640 151 AEGVDLL------LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDE-------------EFLRELLGLELL 211

                       250       260       270
                ....*....|....*....|....*....|....*
gi 16077222 308 GRIPLKQPDWDKDQFAPSVYDEnhPIGEIYQDIAK 342
Cdd:COG3640 212 GFIPYDEEVREADLEGKPLLDL--PDSPAVAAVEE 244
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 109-145 8.49e-08

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: 52.05  E-value: 8.49e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADI 145
Cdd:TIGR01007  20 LLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDM 56
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 114-311 1.08e-07

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: 52.37  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 114 GKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRPTI-------------EGEKLLPVERFGVkvmsm 180
Cdd:cd02117   7 GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTIdemltedgtaeelRREDLLFSGFNGV----- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 181 gFFVEENAPVVWR---GPMLGKMLNNF--FHEVEWGeVDYIVLDLppgTGDVAldvhtmlpsC-------------KEII 242
Cdd:cd02117  82 -DCVEAGGPEPGVgcgGRGIGTMLELLeeHGLLDDD-YDVVIFDV---LGDVV---------CggfaaplrrgfaqKVVI 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16077222 243 VSTPHPTAAFVAARAGSMAIKTDHEVV---GVIENmayyeSAKTGEREYVfgkgggDKLAEELNVPLLGRIP 311
Cdd:cd02117 148 VVSEELMSLYAANNIVKAVENYSKNGVrlaGLVAN-----LRDPAGTEEI------QAFAAAVGTKILAVIP 208
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 114-151 1.18e-06

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 49.22  E-value: 1.18e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16077222 114 GKGGVGKSTVSVNLAISLARLGKKVGLIDAD--------IYGFSVP 151
Cdd:cd02032   7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDpkhdstftLTGFLIP 52
chlL CHL00072
photochlorophyllide reductase subunit L
 109-162 1.67e-06

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 48.96  E-value: 1.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16077222  109 LAVaSGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVrPTI 162
Cdd:CHL00072   3 LAV-YGKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFLI-PTI 54
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 109-222 2.96e-06

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


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 48.95  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222   109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVRP----TIEGEKLLPV-----ERFGVKVMS 179
Cdd:TIGR01005 556 IAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPglldLLAGEASIEAgihrdQRPGLAFIA 635

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 16077222   180 MG--FFVEENAPVVWRGPMLGKMLNNFFHevewgEVDYIVLDLPP 222
Cdd:TIGR01005 636 AGgaSHFPHNPNELLANPAMAELIDNARN-----AFDLVLVDLAA 675
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 110-256 3.30e-06

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: 47.66  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 110 AVASGKGGVGKSTVSVNLAISLA-RLGKKVGLIDADIYGFSVPDMMGITVRPTI-----EGEKLLPVERFGVKV-MSMGF 182
Cdd:cd03111   4 AVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLadviqNLDRLDRTLLDSAVTrHSSGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 183 FV-------EENAPVvwRGPMLGKMLN---NFFhevewgevDYIVLDLPPGTGDVALDVhtmLPSCKEIIVSTPHPTAAF 252
Cdd:cd03111  84 SLlpapqelEDLEAL--GAEQVDKLLQvlrAFY--------DHIIVDLGHFLDEVTLAV---LEAADEILLVTQQDLPSL 150


                ....
gi 16077222 253 VAAR 256
Cdd:cd03111 151 RNAR 154
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 113-141 3.36e-06

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 47.89  E-value: 3.36e-06
                        10        20
                ....*....|....*....|....*....
gi 16077222 113 SGKGGVGKSTVSVNLAISLARLGKKVGLI 141
Cdd:cd02035   6 GGKGGVGKTTIAAATAVRLAEQGKRVLLV 34
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 108-144 3.89e-06

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 47.83  E-value: 3.89e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 16077222   108 FLAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
PRK10818 PRK10818
septum site-determining protein MinD;
109-344 5.94e-06

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 47.24  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVR------PTIEGEKLLPVERFGVKvMSMGF 182
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRvvydfvNVIQGDATLNQALIKDK-RTENL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  183 FVEENAPVVWRGPMLGKMLNNFFHEVEWGEVDYIVLDLPPGTGDVALdvhTMLPSCKEIIVSTpHPTAAfvaaragsmAI 262
Cdd:PRK10818  84 YILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGAL---MALYFADEAIITT-NPEVS---------SV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  263 KTDHEVVGVIENMAyyESAKTGE---REYVF------GK-GGGDKLAEE-----LNVPLLGRIPLKQPDW-DKDQFAPSV 326
Cdd:PRK10818 151 RDSDRILGILASKS--RRAENGEepiKEHLLltrynpGRvSRGDMLSMEdvleiLRIKLVGVIPEDQSVLrASNQGEPVI 228

                        250
                 ....*....|....*...
gi 16077222  327 YDENHPIGEIYQDIAKKI 344
Cdd:PRK10818 229 LDIEADAGKAYADTVDRL 246
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 109-145 8.72e-06

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: 46.61  E-value: 8.72e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 16077222 109 LAVASGKGGVGKSTVSVNLAISLarlgKKVGLIDADI 145
Cdd:cd03110   2 IAVLSGKGGTGKTTITANLAVLL----YNVILVDCDV 34
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 114-144 1.71e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 45.72  E-value: 1.71e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 16077222  114 GKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCD 39
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 104-252 2.02e-05

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 46.12  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  104 NPPVfLAVASGKGGVGKSTVSVNLAISLARLGKKVGLID-------ADIYGFSVPDM------------MG------ITV 158
Cdd:PRK13705 105 FPPV-IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgndpqgtASMYHGWVPDLhihaedtllpfyLGekddatYAI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  159 RPTI-EGEKLLP----VERFGVKVmsMGFFVEENAPVvwrGPMLgkMLNNFFHEVeWGEVDYIVLDLPPGTGdvaldVHT 233
Cdd:PRK13705 184 KPTCwPGLDIIPsclaLHRIETEL--MGKFDEGKLPT---DPHL--MLRLAIETV-AHDYDVIVIDSAPNLG-----IGT 250

                        170
                 ....*....|....*....
gi 16077222  234 MLPSCKEIIVSTPHPTAAF 252
Cdd:PRK13705 251 INVVCAADVLIVPTPAELF 269
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 113-144 2.52e-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: 45.42  E-value: 2.52e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 16077222   113 SGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:pfam02374   7 GGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
113-141 3.24e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 45.20  E-value: 3.24e-05
                        10        20
                ....*....|....*....|....*....
gi 16077222 113 SGKGGVGKSTVSVNLAISLARLGKKVGLI 141
Cdd:COG0003   9 TGKGGVGKTTVAAATALALAERGKRTLLV 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 104-144 7.83e-05

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: 44.31  E-value: 7.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16077222   104 NPPVFLaVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:TIGR04291   1 ELPPYL-FFTGKGGVGKTSIACATAINLADQGKRVLLVSTD 40
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 103-246 1.59e-04

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 43.08  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  103 DNPPVFLAVASGKGGVGKSTVSVNLAISLARLGKKVGLID-------ADIYGFSVPDM---MGITVRPTIEGEK------ 166
Cdd:PHA02519 103 DKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgndpqgtASMYHGYVPDLhihADDTLLPFYLGERdnaeya 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  167 --------------LLPVERFGVKVMSmgFFVEENAPVvwrGPMLgkMLNNFFHEVeWGEVDYIVLDLPPGTGDVALDVh 232
Cdd:PHA02519 183 ikptcwpgldiipsCLALHRIETDLMQ--YHDAGKLPH---PPHL--MLRAAIESV-WDNYDIIVIDSAPNLGTGTINV- 253

                        170
                 ....*....|....
gi 16077222  233 tmLPSCKEIIVSTP 246
Cdd:PHA02519 254 --VCAADVIVVATP 265
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 114-138 1.64e-04

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


Pssm-ID: 349759  Cd Length: 265  Bit Score: 42.89  E-value: 1.64e-04
                        10        20
                ....*....|....*....|....*
gi 16077222 114 GKGGVGKSTVSVNLAISLARLGKKV 138
Cdd:cd02040   7 GKGGIGKSTTASNLSAALAEMGKKV 31
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 114-190 2.23e-04

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 41.47  E-value: 2.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16077222   114 GKGGVGKSTVSVNLAISLARLGKKVGLIDADIY--GFSVPDMMGITVrptIEgEKLLPVERFGVKvMSMGFFVEENAPV 190
Cdd:pfam16575   1 GPKDSGKSTLCRILLNYAVRKGRKPVYVDLDVGqsEIGPPGTISLAL---VE-RPIDVPEGFSLD-APLVYFFGHTSPS 74
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 114-144 2.79e-04

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: 42.77  E-value: 2.79e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 16077222   114 GKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:TIGR04291 328 GKGGVGKTTVAAAIAVRLANKGLDVHLTTSD 358
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 114-162 4.32e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 41.68  E-value: 4.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 16077222  114 GKGGVGKSTVSVNLAISLARLGKKVGLIDADIYGFSVPDMMGITVrPTI 162
Cdd:PRK13230   8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKI-PTV 55
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 108-144 8.88e-04

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: 40.37  E-value: 8.88e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 16077222 108 FLAVAsGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:cd02034   2 KIAVA-GKGGVGKTTIAALLIRYLAKKGGKVLAVDAD 37
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 87-227 3.30e-03

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 39.04  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222  87 AKFRAPSAEKKTLLNMDNPPV----FLAVaSGKGGVGKSTVSVNLAISLARLGKKVGLIDAD---------IYGFSVPDM 153
Cdd:cd02033   8 ARLRDEAAIEPSLEIPTGPPTketqIIAI-YGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDpksdttsllFGGKACPTI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077222 154 MGITVRPTIEGEKL----LPVERFGVKVMSMGffveenAPVVWRGPMLGKMLNNF-------FHevEWGeVDYIVLDLpp 222
Cdd:cd02033  87 IETSTRKKLAGEEVkigdVCFKRGGVFAMELG------GPEVGRGCGGRGIIHGFelleklgFH--DWG-FDYVLLDF-- 155


                ....*
gi 16077222 223 gTGDV 227
Cdd:cd02033 156 -LGDV 159
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
109-144 4.15e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 38.28  E-value: 4.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 16077222  109 LAVASGKGGVGKSTVSVNLAISLARLGKKVGLIDAD 144
Cdd:PRK13849   4 LTFCSFKGGAGKTTALMGLCAALASDGKRVALFEAD 39
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 114-150 7.95e-03

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 37.15  E-value: 7.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16077222  114 GKGGVGKSTVSVNLAISLARLGKKVGLIDADiyGFSV 150
Cdd:PRK09361  30 GPPGSGKTNICLQLAVEAAKNGKKVIYIDTE--GLSP 64
 
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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