NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157384956|ref|NP_079428|]
View 

iron-sulfur cluster transfer protein NUBPL isoform 1 precursor [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 65-311 3.49e-136

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: 386.04  E-value: 3.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   65 GVKQVIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSM 144
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLG--YKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  145 GFLVE-ESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAE 223
Cdd:pfam10609  79 GFLLPdEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  224 MFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEAKAY 303
Cdd:pfam10609 159 MFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAF 238


                  ....*...
gi 157384956  304 LRIAVEVV 311
Cdd:pfam10609 239 LKIADKVA 246
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 65-311 3.49e-136

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: 386.04  E-value: 3.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   65 GVKQVIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSM 144
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLG--YKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  145 GFLVE-ESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAE 223
Cdd:pfam10609  79 GFLLPdEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  224 MFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEAKAY 303
Cdd:pfam10609 159 MFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAF 238


                  ....*...
gi 157384956  304 LRIAVEVV 311
Cdd:pfam10609 239 LKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 69-282 1.28e-108

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: 314.82  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  69 VIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSMGFLV 148
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKG--YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGIKVMSIGFLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 149 EESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAEMFRRV 228
Cdd:cd02037   80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157384956 229 HVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIRE 282
Cdd:cd02037  160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
60-314 2.07e-101

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 302.35  E-value: 2.07e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  60 QKPIEGVKQVIVVASGKGGVGKSTTAVNLALALAANDSSkaIGLLDVDVYGPSVPKMMNLKGNPELSQSNL-MRPLLNYG 138
Cdd:PRK11670 100 QPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK--VGILDADIYGPSIPTMLGAEDQRPTSPDGThMAPIMAHG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 139 IACMSMGFLVEESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDA 218
Cdd:PRK11670 178 LATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 219 HKGAEMFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESD 298
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337

                        250
                 ....*....|....*.
gi 157384956 299 EAKAYLRIAVEVVRRL 314
Cdd:PRK11670 338 FTAIYRQLADRVAAQL 353
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
66-317 4.54e-95

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 285.94  E-value: 4.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  66 VKQVIVVASGKGGVGKSTTAVNLALALaaNDSSKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPL-LNYGIACMSM 144
Cdd:NF041136   4 IKHKILVMSGKGGVGKSTVAANLAVAL--ARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVeYSDNLKVMSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 145 GFLVE-ESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAE 223
Cdd:NF041136  82 GFLLEnRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 224 MFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEAKAY 303
Cdd:NF041136 162 FCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKAL 241

                        250
                 ....*....|....
gi 157384956 304 LRIAVEVVRRLPSP 317
Cdd:NF041136 242 EKIVDPILELLENK 255
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 68-255 9.16e-44

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: 151.49  E-value: 9.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAANDSSkaIGLLDVDVYGPSVPKMMNLKGNPELSQ--------SNLMRPLLNYGI 139
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKR--VLLIDADLRGPSLHRMLGLENRPGLSDvlageaslEDVIQPTEVEGL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 140 ACMSMGFLVEESEpvvwrGLMVMSAIEKLLRQVDwGQLDYLVVDMPPGTGDVQLSVSQNIpITGAVIVSTPQDIALMDAH 219
Cdd:COG0489  171 DVLPAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVR 243

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157384956 220 KGAEMFRRVHVPVLGLVQNMSvfqcpkCKHKTHIFG 255
Cdd:COG0489  244 KALEMLEKAGVPVLGVVLNMV------CPKGERYYG 273
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 69-311 2.82e-12

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: 65.52  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   69 VIVVASGKGGVGKSTTAVNLALALAanDSSKAIGLLDVDVYGPSVPKMMN-----------LKGNPELSQSNLMRPllnY 137
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALA--KLGKKVLALDADITMANLELILGmedkpvtlhdvLAGEADIKDAIYEGP---F 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  138 GIACMSMGflveesepVVWRGLMvMSAIEKL---LRQVDwGQLDYLVVDMPPGTGdvQLSVSQNIPITGAVIVSTPQDIA 214
Cdd:TIGR01969  77 GVKVIPAG--------VSLEGLR-KADPDKLedvLKEII-DDTDFLLIDAPAGLE--RDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  215 LMDAHKGAEMFRRVHVPVLGLVQNmsvfqcpkckHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQ 294
Cdd:TIGR01969 145 ITDALKTKIVAEKLGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYN 214

                         250
                  ....*....|....*..
gi 157384956  295 PESDEAKAYLRIAVEVV 311
Cdd:TIGR01969 215 PNSPAAQAFMELAAELA 231
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 65-311 3.49e-136

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: 386.04  E-value: 3.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   65 GVKQVIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSM 144
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLG--YKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAHGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  145 GFLVE-ESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAE 223
Cdd:pfam10609  79 GFLLPdEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  224 MFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEAKAY 303
Cdd:pfam10609 159 MFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAF 238


                  ....*...
gi 157384956  304 LRIAVEVV 311
Cdd:pfam10609 239 LKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 69-282 1.28e-108

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: 314.82  E-value: 1.28e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  69 VIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNYGIACMSMGFLV 148
Cdd:cd02037    2 IIAVLSGKGGVGKSTVAVNLALALAKKG--YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVGGIKVMSIGFLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 149 EESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAEMFRRV 228
Cdd:cd02037   80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157384956 229 HVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIRE 282
Cdd:cd02037  160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
60-314 2.07e-101

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 302.35  E-value: 2.07e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  60 QKPIEGVKQVIVVASGKGGVGKSTTAVNLALALAANDSSkaIGLLDVDVYGPSVPKMMNLKGNPELSQSNL-MRPLLNYG 138
Cdd:PRK11670 100 QPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK--VGILDADIYGPSIPTMLGAEDQRPTSPDGThMAPIMAHG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 139 IACMSMGFLVEESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDA 218
Cdd:PRK11670 178 LATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 219 HKGAEMFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESD 298
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337

                        250
                 ....*....|....*.
gi 157384956 299 EAKAYLRIAVEVVRRL 314
Cdd:PRK11670 338 FTAIYRQLADRVAAQL 353
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
66-317 4.54e-95

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 285.94  E-value: 4.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  66 VKQVIVVASGKGGVGKSTTAVNLALALaaNDSSKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPL-LNYGIACMSM 144
Cdd:NF041136   4 IKHKILVMSGKGGVGKSTVAANLAVAL--ARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVeYSDNLKVMSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 145 GFLVE-ESEPVVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMPPGTGDVQLSVSQNIPITGAVIVSTPQDIALMDAHKGAE 223
Cdd:NF041136  82 GFLLEnRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 224 MFRRVHVPVLGLVQNMSVFQCPKCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEAKAY 303
Cdd:NF041136 162 FCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKAL 241

                        250
                 ....*....|....
gi 157384956 304 LRIAVEVVRRLPSP 317
Cdd:NF041136 242 EKIVDPILELLENK 255
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 68-255 9.16e-44

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: 151.49  E-value: 9.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAANDSSkaIGLLDVDVYGPSVPKMMNLKGNPELSQ--------SNLMRPLLNYGI 139
Cdd:COG0489   93 EVIAVTSGKGGEGKSTVAANLALALAQSGKR--VLLIDADLRGPSLHRMLGLENRPGLSDvlageaslEDVIQPTEVEGL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 140 ACMSMGFLVEESEpvvwrGLMVMSAIEKLLRQVDwGQLDYLVVDMPPGTGDVQLSVSQNIpITGAVIVSTPQDIALMDAH 219
Cdd:COG0489  171 DVLPAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVR 243

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 157384956 220 KGAEMFRRVHVPVLGLVQNMSvfqcpkCKHKTHIFG 255
Cdd:COG0489  244 KALEMLEKAGVPVLGVVLNMV------CPKGERYYG 273
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 70-290 2.69e-13

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: 68.14  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   70 IVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVyGPSVPKMMNLKGNPELSQSNL---------MRPLL----- 135
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRG--LRVLLIDLDP-QSNNSSVEGLEGDIAPALQALaeglkgrvnLDPILlkeks 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  136 NYGIACMSMGFLVEESEPVVWRGLMVMSAIEKLLRQVDwGQLDYLVVDMPPGTGDvqLSVSQNIPITGAVIVSTPQDIAL 215
Cdd:pfam01656  78 DEGGLDLIPGNIDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  216 MDAHKGAEMFRRV-------HVPVLGLVQNMSVfqcpkcKHKTHIFGADGARKLAQtlGLEVLGDIPLHLNIREASDTGQ 288
Cdd:pfam01656 155 EDAKRLGGVIAALvggyallGLKIIGVVLNKVD------GDNHGKLLKEALEELLR--GLPVLGVIPRDEAVAEAPARGL 226


                  ..
gi 157384956  289 PI 290
Cdd:pfam01656 227 PV 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 150-317 7.86e-13

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: 66.84  E-value: 7.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 150 ESEPVVWRGLMVMSAIEKLLRQVDwGQLDYLVVDMPPGTGDV---QLSVSQNIpitgaVIVSTPQDIALMDAHKGAEMFR 226
Cdd:COG0455   68 GSGPAELAELDPEERLIRVLEELE-RFYDVVLVDTGAGISDSvllFLAAADEV-----VVVTTPEPTSITDAYALLKLLR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 227 RVH-VPVLGLVQNMSvfqcpkckhKTHIFGADGARKLAQTLG------LEVLGDIPLHLNIREASDTGQPIVFSQPESDE 299
Cdd:COG0455  142 RRLgVRRAGVVVNRV---------RSEAEARDVFERLEQVAErflgvrLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPA 212

                        170
                 ....*....|....*...
gi 157384956 300 AKAYLRIAVEVVRRLPSP 317
Cdd:COG0455  213 ARAIRELAARLAGWPVPE 230
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 68-313 8.20e-13

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: 68.22  E-value: 8.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAANDSSKAIgLLDVDVYGPSVPKMMNLKGNPELSQsnlmrpllnygiACMSMGFL 147
Cdd:COG4963  103 RVIAVVGAKGGVGATTLAVNLAWALARESGRRVL-LVDLDLQFGDVALYLDLEPRRGLAD------------ALRNPDRL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 148 ----VEESEPVVWRGLMVMSA--------------IEKLLRQVDwGQLDYLVVDMPPGTGDVQLSV---SQNIpitgaVI 206
Cdd:COG4963  170 detlLDRALTRHSSGLSVLAApadleraeevspeaVERLLDLLR-RHFDYVVVDLPRGLNPWTLAAleaADEV-----VL 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 207 VSTPQDIALMDAHKGAEMFRRVHVPV--LGLVQNmsvfQCPKckhkthiFGADGARKLAQTLGLEVLGDIPL-HLNIREA 283
Cdd:COG4963  244 VTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLN----RVPK-------RGEISAKDIEEALGLPVAAVLPNdPKAVAEA 312

                        250       260       270
                 ....*....|....*....|....*....|
gi 157384956 284 SDTGQPIVFSQPESDEAKAYLRIAVEVVRR 313
Cdd:COG4963  313 ANQGRPLAEVAPKSPLAKAIRKLAARLTGR 342
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 69-311 2.82e-12

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: 65.52  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   69 VIVVASGKGGVGKSTTAVNLALALAanDSSKAIGLLDVDVYGPSVPKMMN-----------LKGNPELSQSNLMRPllnY 137
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALA--KLGKKVLALDADITMANLELILGmedkpvtlhdvLAGEADIKDAIYEGP---F 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  138 GIACMSMGflveesepVVWRGLMvMSAIEKL---LRQVDwGQLDYLVVDMPPGTGdvQLSVSQNIPITGAVIVSTPQDIA 214
Cdd:TIGR01969  77 GVKVIPAG--------VSLEGLR-KADPDKLedvLKEII-DDTDFLLIDAPAGLE--RDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  215 LMDAHKGAEMFRRVHVPVLGLVQNmsvfqcpkckHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQ 294
Cdd:TIGR01969 145 ITDALKTKIVAEKLGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYN 214

                         250
                  ....*....|....*..
gi 157384956  295 PESDEAKAYLRIAVEVV 311
Cdd:TIGR01969 215 PNSPAAQAFMELAAELA 231
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 68-298 1.45e-11

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: 62.97  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAanDSSKAIGLLDVDVYGPSVPKMMN----------LKGNPELSQSNLMRPllnY 137
Cdd:cd02038    1 RIIAVTSGKGGVGKTNVSANLALALS--KLGKRVLLLDADLGLANLDILLGlapkktlgdvLKGRVSLEDIIVEGP---E 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 138 GIACMSMGFLVEE---SEPVVWRGLmvmsaIEKLlrQVDWGQLDYLVVDMPPGTGDVQLSVSqnIPITGAVIVSTPQDIA 214
Cdd:cd02038   76 GLDIIPGGSGMEElanLDPEQKAKL-----IEEL--SSLESNYDYLLIDTGAGISRNVLDFL--LAADEVIVVTTPEPTS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 215 LMDAH---KgaEMFRRVHVPVLGLVQNMSvfqcpkckhKTHIFGADGARKLAQTLG------LEVLGDIPLHLNIREASD 285
Cdd:cd02038  147 ITDAYaliK--VLSRRGGKKNFRLIVNMA---------RSPKEGRATFERLKKVAKrfldinLDFVGFIPYDQSVRRAVR 215

                        250
                 ....*....|...
gi 157384956 286 TGQPIVFSQPESD 298
Cdd:cd02038  216 SQKPFVLLFPNSK 228
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 68-314 2.42e-11

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 62.95  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAA-------------NDSSKAIGlLDVDVYGPSVPKMmnLKGNPELSQsnLMRPL 134
Cdd:COG1192    2 KVIAVANQKGGVGKTTTAVNLAAALARrgkrvllidldpqGNLTSGLG-LDPDDLDPTLYDL--LLDDAPLED--AIVPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 135 LNYGIACM--SMGFLVEESEPVvwRGLMVMSAIEKLLRQVDwGQLDYLVVDMPPGtgdvqLSVSQNIPITGA---VIVST 209
Cdd:COG1192   77 EIPGLDLIpaNIDLAGAEIELV--SRPGRELRLKRALAPLA-DDYDYILIDCPPS-----LGLLTLNALAAAdsvLIPVQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 210 PQDIALMDAHKGAEMFRRV------HVPVLGLVQNMsvFQCPKCKHKthifgaDGARKLAQTLGLEVLG-DIPLHLNIRE 282
Cdd:COG1192  149 PEYLSLEGLAQLLETIEEVredlnpKLEILGILLTM--VDPRTRLSR------EVLEELREEFGDKVLDtVIPRSVALAE 220

                        250       260       270
                 ....*....|....*....|....*....|..
gi 157384956 283 ASDTGQPIVFSQPESDEAKAYLRIAVEVVRRL 314
Cdd:COG1192  221 APSAGKPVFEYDPKSKGAKAYRALAEELLERL 252
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 69-314 4.98e-10

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: 58.75  E-value: 4.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  69 VIVVASGKGGVGKSTTAVNLALALAANDSSKA-----IGL--LDV--DVYGPSVPKMMN-LKGNPELSQSNLMRP-LLNY 137
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLlidadIGLrnLDLilGLENRIVYTLVDvLEGECRLEQALIKDKrWENL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 138 GIACMSmgflveesepVVWRGLMV-MSAIEKLLRQVDwGQLDYLVVDMPPGTGdvQLSVSQNIPITGAVIVSTPQDIALM 216
Cdd:cd02036   82 YLLPAS----------QTRDKDALtPEKLEELVKELK-DSFDFILIDSPAGIE--SGFINAIAPADEAIIVTNPEISSVR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 217 DAHKgaemfrrvhvpVLGLVQNMSVfqcpkcKHKTHI---FGADGARK--------LAQTLGLEVLGDIPLHLNIREASD 285
Cdd:cd02036  149 DADR-----------VIGLLESKGI------VNIGLIvnrYRPEMVKSgdmlsvedIQEILGIPLLGVIPEDPEVIVATN 211

                        250       260
                 ....*....|....*....|....*....
gi 157384956 286 TGQPIVFSQPESDEAKAYLRIAvevvRRL 314
Cdd:cd02036  212 RGEPLVLYKPNSLAAKAFENIA----RRL 236
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 68-307 1.71e-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: 48.43  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVNLALALAAnDSSKAIGLLDVDVYGPSVPKMMNLK---------GNPelsqSNLMRPLLNyg 138
Cdd:cd03111    1 RVVAVVGAKGGVGASTLAVNLAQELAQ-RAKDKVLLIDLDLPFGDLGLYLNLRpdydladviQNL----DRLDRTLLD-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 139 iacmsmGFLVEESepvvwRGLMVMSA--------------IEKLLrQVDWGQLDYLVVDMPPGTGDVQLSVSQniPITGA 204
Cdd:cd03111   74 ------SAVTRHS-----SGLSLLPApqeledlealgaeqVDKLL-QVLRAFYDHIIVDLGHFLDEVTLAVLE--AADEI 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 205 VIVSTPQDIALMDAHKGAEMFRRVHVPvlglvqnmsvfqcpkcKHKTHI----FGADG---ARKLAQTLGLEVLGDIPL- 276
Cdd:cd03111  140 LLVTQQDLPSLRNARRLLDSLRELEGS----------------SDRLRLvlnrYDKKSeisPKDIEEALGLEVFATLPNd 203

                        250       260       270
                 ....*....|....*....|....*....|.
gi 157384956 277 HLNIREASDTGQPIVFSQPESDEAKAYLRIA 307
Cdd:cd03111  204 YKAVSESANTGRPLVEVAPRSALVRALQDLA 234
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 69-314 4.16e-06

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: 47.33  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   69 VIVVASGKGGVGKSTTAVNLALALAAndSSKAIGLLDVDVYGPSVPKMMNLK------------GNPELSQSnlmrplln 136
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALAR--LGKKVVLIDADIGLRNLDLLLGLEnrivytlvdvveGECRLQQA-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  137 ygiacmsmgfLVEESEpvvWRGLMVMSA-------------IEKLLRQVDwGQLDYLVVDMPPG--TGdVQLSVSqniPI 201
Cdd:TIGR01968  73 ----------LIKDKR---LKNLYLLPAsqtrdkdavtpeqMKKLVNELK-EEFDYVIIDCPAGieSG-FRNAVA---PA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  202 TGAVIVSTPQDIALMDAHKgaemfrrvhvpVLGLVQNMSVFQC--------PKCKHKTHIFGADGARklaQTLGLEVLGD 273
Cdd:TIGR01968 135 DEAIVVTTPEVSAVRDADR-----------VIGLLEAKGIEKIhlivnrlrPEMVKKGDMLSVDDVL---EILSIPLIGV 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 157384956  274 IPLHLNIREASDTGQPIVFsQPESDEAKAYLRIAvevvRRL 314
Cdd:TIGR01968 201 IPEDEAIIVSTNKGEPVVL-NDKSRAGKAFENIA----RRI 236
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 69-87 1.81e-05

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: 43.68  E-value: 1.81e-05
                         10
                 ....*....|....*....
gi 157384956  69 VIVVASGKGGVGKSTTAVN 87
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVN 20
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 75-312 3.02e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 44.79  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  75 GKGGVGKSTTAVNLALALAANDSSKAIGL-----LDVDVYGPSVPKMMN-LKGNPELSQSNLMRPLLNyGIACMSMGflv 148
Cdd:PRK13231   9 GKGGIGKSTTVSNMAAAYSNDHRVLVIGCdpkadTTRTLCGKRIPTVLDtLKDNRKPELEDIIHEGFN-GILCVESG--- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 149 eESEPVV---WRGLMV-MSAIEKLlrQVDWGQLDYLVVDMppgTGDV---QLSVSQNIPITGAV-IVSTPQDIALMDAHK 220
Cdd:PRK13231  85 -GPEPGVgcaGRGVIVaMNLLENL--GVFDEDIDVVIYDV---LGDVvcgGFSVPLREDYADEVyIVTSGEYMSLYAANN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 221 GAEMFRRVHVPVLGLVQNmsvfqCPKCKHKTHIfgadgARKLAQTLGLEVLGDIPLHLNIREASDTGQPIVFSQPESDEA 300
Cdd:PRK13231 159 IARGIKKLKGKLGGIICN-----CRGIDNEVEI-----VSEFASRIGSRIIGVIPRSNLVQESELDAKTVVETFPESEQA 228

                        250
                 ....*....|..
gi 157384956 301 KAYLRIAVEVVR 312
Cdd:PRK13231 229 SVYRKLANNIMN 240
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 74-242 4.72e-05

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: 44.04  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  74 SGKGGVGKSTTAvnlalalaandSSKAIGL---------------------LDVDVyGPSVPKM-------MNLKGNPEL 125
Cdd:cd02035    6 GGKGGVGKTTIA-----------AATAVRLaeqgkrvllvstdpahslsdaFGQKL-GGETPVKgapnlwaMEIDPEEAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 126 SQ--SNLMRPLLNYGIACMSMGFLVEE--SEPvvwrGLMVMSAIEKLLRQVDWGQLDYLVVDMPPgTGD----VQLSVSQ 197
Cdd:cd02035   74 EEywEEVKELLAQYLRLPGLDEVYAEEllSLP----GMDEAAAFDELREYVESGEYDVIVFDTAP-TGHtlrlLSLPLEQ 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157384956 198 ------NIPITGAVIVSTPQDIALMDAHKGAEMFRRVHVPVLGLVQNMSVF 242
Cdd:cd02035  149 vrellrDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLP 199
minD CHL00175
septum-site determining protein; Validated
 57-291 5.86e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 43.99  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  57 LPKQKPIEGVKQVIVVASGKGGVGKSTTAVNLALALAANDSSKA-----IGLLDVD---------VYgpsvPKMMNLKGN 122
Cdd:CHL00175   5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVAlidadIGLRNLDlllglenrvLY----TAMDVLEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 123 PELSQSnLMRPLLNYGIACMSMGfLVEESEPVVWRGL-MVMSAIEKLlrqvdwgQLDYLVVDMPPGTgDVQLSVSQNiPI 201
Cdd:CHL00175  81 CRLDQA-LIRDKRWKNLSLLAIS-KNRQRYNVTRKNMnMLVDSLKNR-------GYDYILIDCPAGI-DVGFINAIA-PA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 202 TGAVIVSTPQDIALMDAHKgaemfrrvhvpVLGLVQNMSVFQC--------PKCKHKTHIFGADGARKLaqtLGLEVLGD 273
Cdd:CHL00175 150 QEAIVVTTPEITAIRDADR-----------VAGLLEANGIYNVkllvnrvrPDMIQANDMMSVRDVQEM---LGIPLLGA 215

                        250
                 ....*....|....*...
gi 157384956 274 IPLHLNIREASDTGQPIV 291
Cdd:CHL00175 216 IPEDENVIISTNRGEPLV 233
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 68-87 7.02e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 43.51  E-value: 7.02e-05
                         10        20
                 ....*....|....*....|
gi 157384956  68 QVIVVASGKGGVGKSTTAVN 87
Cdd:COG2894    3 KVIVVTSGKGGVGKTTTTAN 22
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 68-315 8.02e-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: 43.51  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  68 QVIVVAsGKGGVGKSTTAVNLALALAAndSSKAIGLLDVDVYGPS---------VPKMMNLKGNPELSQSNLMRPLL--- 135
Cdd:cd02117    1 ESIVVY-GKGGIGKSTTASNLSAALAE--GGKKVLHVGCDPKHDStllltggkvPPTIDEMLTEDGTAEELRREDLLfsg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 136 NYGIACMSMGflveESEPVVWRGLMVMSAIEKLLRQV---DWGqLDYLVVDMppgTGDV---------QLSVSQNipitg 203
Cdd:cd02117   78 FNGVDCVEAG----GPEPGVGCGGRGIGTMLELLEEHgllDDD-YDVVIFDV---LGDVvcggfaaplRRGFAQK----- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 204 AVIVSTPQDIALMDAH---KGAEMFRRVHVPVLGLVQNMSvfqcpkckhktHIFGADGARKLAQTLGLEVLGDIPLHLNI 280
Cdd:cd02117  145 VVIVVSEELMSLYAANnivKAVENYSKNGVRLAGLVANLR-----------DPAGTEEIQAFAAAVGTKILAVIPRDPAV 213

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157384956 281 REASDTGQPIVFSQPESDEAKAYLRIAVEVVRRLP 315
Cdd:cd02117  214 RRAELARVTVFEHDPVSPAASEFARLAAKIADAVP 248
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
75-307 9.34e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.12  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956   75 GKGGVGKSTTAVNLALALAanDSSKAIGLLDVDVYGPSVPKMMNLKGNPELSQSNLMRPLLNY------------GIACM 142
Cdd:pfam00142   7 GKGGIGKSTTSQNLSAALA--EMGKKVLVVGCDPKADSTRLLLGGKLQPTVLDTAREKGYVEDvevedvvykgygGVKCV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  143 SMGflveESEP-VVWRGLMVMSAIEKLLRQVDWGQLDYLVVDMppgTGDV---------QLSVSQNIpitgaVIVSTPQD 212
Cdd:pfam00142  85 ESG----GPEPgVGCAGRGVITAINLLEELGAYDDLDFVLYDV---LGDVvcggfampiREGKAQEI-----YIVTSNEM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  213 IALMDAH---KGAEMFRRVH-VPVLGLVqnmsvfqcpkCKHKTHIFGADGARKLAQTLGLEVLGDIPLHLNIREASDTGQ 288
Cdd:pfam00142 153 MALYAANniaKGIQKYAKSGgVRLGGII----------CNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQ 222

                         250
                  ....*....|....*....
gi 157384956  289 PIVFSQPESDEAKAYLRIA 307
Cdd:pfam00142 223 TVIEYAPDSEQAQEYRELA 241
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 68-87 1.01e-03

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


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 39.49  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|
gi 157384956   68 QVIVVASGKGGVGKSTTAVN 87
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVN 21
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 43-238 4.35e-03

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: 37.55  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956  43 ETLKQRRTQIMSRGLPKQKpiegvkQVIVVASGKGGVGKSTTAVNLALALAANDssKAIGLLDVDVYGPSVPKMMNLKGN 122
Cdd:cd05387    1 EAFRTLRTNLLFAGSDAGP------KVIAVTSASPGEGKSTVAANLAVALAQSG--KRVLLIDADLRRPSLHRLLGLPNE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157384956 123 PELSQSNLMRPLLNYGIACM-SMGFLVEESEPVVWRG--LMVMSAIEKLLRQVDwGQLDYLVVDMPP--GTGDVQLsVSQ 197
Cdd:cd05387   73 PGLSEVLSGQASLEDVIQSTnIPNLDVLPAGTVPPNPseLLSSPRFAELLEELK-EQYDYVIIDTPPvlAVADALI-LAP 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157384956 198 NipITGAVIV----STPQDialmDAHKGAEMFRRVHVPVLGLVQN 238
Cdd:cd05387  151 L--VDGVLLVvragKTRRR----EVKEALERLEQAGAKVLGVVLN 189
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 70-124 7.81e-03

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: 37.36  E-value: 7.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157384956  70 IVVASGKGGVGKSTTAVNLALalaandSSKAIGLLDVDVYGPSVPKMMNLKGNPE 124
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAV------LLYNVILVDCDVDAPNLHLLLGPEPEEE 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH