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Conserved domains on  [gi|58865352|ref|NP_001011891|]
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cytosolic Fe-S cluster assembly factor NUBP2 [Rattus norvegicus]

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 ...
 12-263 2.91e-141

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: 396.82  E-value: 2.91e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    12 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDqeqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    92 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   171 RRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPKST 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 58865352   251 AYSALTSIAHKVL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 12-263 2.91e-141

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: 396.82  E-value: 2.91e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    12 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDqeqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    92 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   171 RRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPKST 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 58865352   251 AYSALTSIAHKVL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 15-233 4.78e-127

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: 359.51  E-value: 4.78e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  15 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDqeqSISLMSVGF 94
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  95 LLEnPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALRPYkplGALVVTTPQAVSIGDVRREL 174
Cdd:cd02037  78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 58865352 175 TFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLT 233
Cdd:cd02037 154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
10-265 3.75e-118

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 342.57  E-value: 3.75e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   10 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDQeqSISL 89
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSD--NLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   90 MSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIG 168
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  169 DVRRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPK 248
Cdd:NF041136 155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....*..
gi 58865352  249 STAYSALTSIAHKVLHQ 265
Cdd:NF041136 235 SPAAKALEKIVDPILEL 251
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
12-266 9.81e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 193.72  E-value: 9.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   12 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWV-PVfvdQEQSISLM 90
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPI---MAHGLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   91 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIGD 169
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNI----PVtGAVVVTTPQDIALID 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  170 VRRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPKS 249
Cdd:PRK11670 257 AKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPES 336

                        250
                 ....*....|....*..
gi 58865352  250 TAYSALTSIAHKVLHQM 266
Cdd:PRK11670 337 EFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-198 2.22e-42

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: 146.49  E-value: 2.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   9 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAvhqcdsGWVPVFVDQ----- 83
Cdd:COG0489  87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP------GLSDVLAGEasled 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  84 ------EQSISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATVEALRPykplGAL 157
Cdd:COG0489 161 viqpteVEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVL 229

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 58865352 158 VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfACPH 198
Cdd:COG0489 230 LVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 16-265 2.57e-09

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: 56.58  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQcdsgwvpvFVDqeqsislmsvgfL 95
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYT--------LVD------------V 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    96 LE---NPDEAVVW--RGPKKHAL---------------IKQFVSDVAwGELDYLVVDTPPGT-SDEHMATVEALRpykpl 154
Cdd:TIGR01968  63 VEgecRLQQALIKdkRLKNLYLLpasqtrdkdavtpeqMKKLVNELK-EEFDYVIIDCPAGIeSGFRNAVAPADE----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   155 gALVVTTPQAVSIGDVRReltfckktglqVIGVIENMSGFAC--------PHCAECTNVFSSgggEELARLAGVPFLGSV 226
Cdd:TIGR01968 137 -AIVVTTPEVSAVRDADR-----------VIGLLEAKGIEKIhlivnrlrPEMVKKGDMLSV---DDVLEILSIPLIGVI 201

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 58865352   227 PLDPQLTRSLEEGRDFIQEfPKSTAYSALTSIAHKVLHQ 265
Cdd:TIGR01968 202 PEDEAIIVSTNKGEPVVLN-DKSRAGKAFENIARRILGE 239
ParA_partition NF041546
ParA family partition ATPase;
16-147 1.84e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.32  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPsiphmlhaQGKAvhqcdSGWvpvfvdQEQSislmsvgfl 95
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD---P--------QGSA-----LDW------AAAR--------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 58865352   96 LENPDEAVV-WRGPKKHALIKQFVSDVawgelDYLVVDTPPGTSDEHMATVEA 147
Cdd:NF041546  50 EDERPFPVVgLARPTLHRELPSLARDY-----DFVVIDGPPRAEDLARSAIKA 97
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 12-263 2.91e-141

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: 396.82  E-value: 2.91e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    12 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDqeqSISLMS 91
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    92 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIGDV 170
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   171 RRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPKST 250
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|...
gi 58865352   251 AYSALTSIAHKVL 263
Cdd:pfam10609 234 AAKAFLKIADKVA 246
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 15-233 4.78e-127

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: 359.51  E-value: 4.78e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  15 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDqeqSISLMSVGF 94
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  95 LLEnPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALRPYkplGALVVTTPQAVSIGDVRREL 174
Cdd:cd02037  78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 58865352 175 TFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLT 233
Cdd:cd02037 154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELA 212
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
10-265 3.75e-118

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 342.57  E-value: 3.75e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   10 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPVFVDQeqSISL 89
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSD--NLKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   90 MSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIG 168
Cdd:NF041136  79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  169 DVRRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPK 248
Cdd:NF041136 155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|....*..
gi 58865352  249 STAYSALTSIAHKVLHQ 265
Cdd:NF041136 235 SPAAKALEKIVDPILEL 251
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
12-266 9.81e-60

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 193.72  E-value: 9.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   12 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWV-PVfvdQEQSISLM 90
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPI---MAHGLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   91 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALrpykPL-GALVVTTPQAVSIGD 169
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNI----PVtGAVVVTTPQDIALID 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  170 VRRELTFCKKTGLQVIGVIENMSGFACPHCAECTNVFSSGGGEELARLAGVPFLGSVPLDPQLTRSLEEGRDFIQEFPKS 249
Cdd:PRK11670 257 AKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPES 336

                        250
                 ....*....|....*..
gi 58865352  250 TAYSALTSIAHKVLHQM 266
Cdd:PRK11670 337 EFTAIYRQLADRVAAQL 353
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 9-198 2.22e-42

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: 146.49  E-value: 2.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   9 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAvhqcdsGWVPVFVDQ----- 83
Cdd:COG0489  87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP------GLSDVLAGEasled 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  84 ------EQSISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATVEALRPykplGAL 157
Cdd:COG0489 161 viqpteVEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVL 229

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 58865352 158 VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfACPH 198
Cdd:COG0489 230 LVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 16-251 3.47e-21

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: 89.17  E-value: 3.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGK-AVHQCDSGWVPVF---VDQEQSISLMS 91
Cdd:cd02038   2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKkTLGDVLKGRVSLEdiiVEGPEGLDIIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  92 VGFLLEnpdEAVVWRGPKKHALIKQFVSDVAwgELDYLVVDTPPGTSDEHMATVEALRPykplgALVVTTPQAVSIGD-- 169
Cdd:cd02038  82 GGSGME---ELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRNVLDFLLAADE-----VIVVTTPEPTSITDay 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 170 ------VRRELTFckktglqVIGVIENMsgfacphcaectnVFSSGGGEELA-RLAGV---------PFLGSVPLDPQLT 233
Cdd:cd02038 152 alikvlSRRGGKK-------NFRLIVNM-------------ARSPKEGRATFeRLKKVakrfldinlDFVGFIPYDQSVR 211

                       250
                ....*....|....*...
gi 58865352 234 RSLEEGRDFIQEFPKSTA 251
Cdd:cd02038 212 RAVRSQKPFVLLFPNSKA 229
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 30-265 2.03e-17

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: 78.78  E-value: 2.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  30 TISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGK---------------AVHQCDSGwvpvfvdqeqsISLMSVGf 94
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKatladvlageadledAIVQGPGG-----------LDVLPGG- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  95 llenPDEAVVWRGPKKHALIKQFvsDVAWGELDYLVVDTPPGTSDEHMATVEAlrpykplgA---LVVTTPQAVSIGDVR 171
Cdd:COG0455  69 ----SGPAELAELDPEERLIRVL--EELERFYDVVLVDTGAGISDSVLLFLAA--------AdevVVVTTPEPTSITDAY 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 172 ReltFCK----KTGLQVIGVIENMsgfacphcaectnVFSSGGGEEL-ARLAGV---------PFLGSVPLDPQLTRSLE 237
Cdd:COG0455 135 A---LLKllrrRLGVRRAGVVVNR-------------VRSEAEARDVfERLEQVaerflgvrlRVLGVIPEDPAVREAVR 198

                       250       260
                ....*....|....*....|....*...
gi 58865352 238 EGRDFIQEFPKSTAYSALTSIAHKVLHQ 265
Cdd:COG0455 199 RGRPLVLAAPDSPAARAIRELAARLAGW 226
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 17-242 2.79e-17

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: 78.54  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    17 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQ-------CDSGWV-PVFVD---QEQ 85
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqalaeglKGRVNLdPILLKeksDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    86 SISLMSVGFLLENPDEavVWRGPKKHALIKQFVSDVAwGELDYLVVDTPPGTsdeHMATVEALRPykPLGALVVTTPQAV 165
Cdd:pfam01656  81 GLDLIPGNIDLEKFEK--ELLGPRKEERLREALEALK-EDYDYVIIDGAPGL---GELLRNALIA--ADYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   166 SIGDVRRELTFCKKTG-------LQVIGVIENMsgfacphcaectnvFSSGGGEEL------ARLAGVPFLGSVPLDPQL 232
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK--------------VDGDNHGKLlkealeELLRGLPVLGVIPRDEAV 218

                         250
                  ....*....|
gi 58865352   233 TRSLEEGRDF 242
Cdd:pfam01656 219 AEAPARGLPV 228
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 15-264 4.81e-17

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: 79.77  E-value: 4.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  15 HIILVLSGKGGVGKSTISTELALAL-RHQGKKVGILDVDLCGPSIPHMLhaqgkavhqcdsgwvpvfvDQEQSISLMSVG 93
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDVALYL-------------------DLEPRRGLADAL 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  94 FLLENPDEAVVWRGPKKH---------------------ALIKQFVsDVAWGELDYLVVDTPPGTSDEHMATVEAlrpyk 152
Cdd:COG4963 164 RNPDRLDETLLDRALTRHssglsvlaapadleraeevspEAVERLL-DLLRRHFDYVVVDLPRGLNPWTLAALEA----- 237

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 153 plgA---LVVTTPQAVSIGDVRRELTFCKKTGLQV--IGVIENMSGfacphcaectnVFSSGGGEELARLAGVPFLGSVP 227
Cdd:COG4963 238 ---AdevVLVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNRVP-----------KRGEISAKDIEEALGLPVAAVLP 303

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 58865352 228 LDPQ-LTRSLEEGRDFIQEFPKSTAYSALTSIAHKVLH 264
Cdd:COG4963 304 NDPKaVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTG 341
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 16-262 1.27e-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: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDL----------CGPSIPHMLH--AQGKA-VHQCdsgwvpVFVD 82
Cdd:cd02036   2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIglrnldlilgLENRIVYTLVdvLEGECrLEQA------LIKD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  83 QEQ-SISLMSVGFLLENpDEAvvwrGPKKhalIKQFVSDVAwGELDYLVVDTPPGT-SDEHMATVEALRpykplgALVVT 160
Cdd:cd02036  76 KRWeNLYLLPASQTRDK-DAL----TPEK---LEELVKELK-DSFDFILIDSPAGIeSGFINAIAPADE------AIIVT 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 161 TPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGfacPHCAEctnvfssgGGEELARLA-----GVPFLGSVPLDPQLTRS 235
Cdd:cd02036 141 NPEISSVRDADRVIGLLESKGIVNIGLIVNRYR---PEMVK--------SGDMLSVEDiqeilGIPLLGVIPEDPEVIVA 209

                       250       260
                ....*....|....*....|....*..
gi 58865352 236 LEEGRDFIQEFPKSTAYSALTSIAHKV 262
Cdd:cd02036 210 TNRGEPLVLYKPNSLAAKAFENIARRL 236
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 14-190 1.41e-11

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: 61.82  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  14 RHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHML---HAQGKA---VHQCDsgWVPVFVDQEQS- 86
Cdd:cd05387  19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLglpNEPGLSevlSGQAS--LEDVIQSTNIPn 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  87 ISLMSVGFLLENPDEAVvwRGPKKHALIKQFVsdvawGELDYLVVDTPP--GTSDEHM--ATVEalrpykplGALVVTTP 162
Cdd:cd05387  97 LDVLPAGTVPPNPSELL--SSPRFAELLEELK-----EQYDYVIIDTPPvlAVADALIlaPLVD--------GVLLVVRA 161

                       170       180
                ....*....|....*....|....*...
gi 58865352 163 QAVSIGDVRRELTFCKKTGLQVIGVIEN 190
Cdd:cd05387 162 GKTRRREVKEALERLEQAGAKVLGVVLN 189
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-262 4.97e-11

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 61.34  E-value: 4.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  17 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgpsiPHM-LHAQ-GkavhqcdsgwVPVFVDQEQSISLM---- 90
Cdd:COG3640   2 KIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDAD------PNAnLAEAlG----------LEVEADLIKPLGEMreli 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  91 -------SVGFLLENP------DEAVVWRG---------PKK---------HALIKQFVSDVAWGELDYLVVDTPPGTsd 139
Cdd:COG3640  66 kertgapGGGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI-- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 140 EHMA-----TVEALrpykplgaLVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfacphcaectnVFSSGGGEEL 214
Cdd:COG3640 144 EHLGrgtaeGVDLL--------LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNK-------------VREEEDEEFL 202

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 58865352 215 ARLAGVPFLGSVPLDPQLtRSLEEGRDFIQEFPKSTAYSALTSIAHKV 262
Cdd:COG3640 203 RELLGLELLGFIPYDEEV-READLEGKPLLDLPDSPAVAAVEEIAEKL 249
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 15-52 2.67e-10

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: 56.78  E-value: 2.67e-10
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 58865352  15 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 16-265 2.57e-09

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: 56.58  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQcdsgwvpvFVDqeqsislmsvgfL 95
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRIVYT--------LVD------------V 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    96 LE---NPDEAVVW--RGPKKHAL---------------IKQFVSDVAwGELDYLVVDTPPGT-SDEHMATVEALRpykpl 154
Cdd:TIGR01968  63 VEgecRLQQALIKdkRLKNLYLLpasqtrdkdavtpeqMKKLVNELK-EEFDYVIIDCPAGIeSGFRNAVAPADE----- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   155 gALVVTTPQAVSIGDVRReltfckktglqVIGVIENMSGFAC--------PHCAECTNVFSSgggEELARLAGVPFLGSV 226
Cdd:TIGR01968 137 -AIVVTTPEVSAVRDADR-----------VIGLLEAKGIEKIhlivnrlrPEMVKKGDMLSV---DDVLEILSIPLIGVI 201

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 58865352   227 PLDPQLTRSLEEGRDFIQEfPKSTAYSALTSIAHKVLHQ 265
Cdd:TIGR01968 202 PEDEAIIVSTNKGEPVVLN-DKSRAGKAFENIARRILGE 239
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 16-260 2.72e-09

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: 56.13  E-value: 2.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGK-KVGILDVDLCGPSIPHMLHAqgkavhQCDSGWVPVF-----VDQEQSISL 89
Cdd:cd03111   2 VVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNL------RPDYDLADVIqnldrLDRTLLDSA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  90 M---SVGF-LLENPDEAVvwRGPKKHALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATVEALRPykplgALVVTTPQAV 165
Cdd:cd03111  76 VtrhSSGLsLLPAPQELE--DLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADE-----ILLVTQQDLP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 166 SIGDVRRELTFCKKTGL---QVIGVIenmsgfacphcaectNVFSSGGG---EELARLAGVPFLGSVPLDPQL-TRSLEE 238
Cdd:cd03111 149 SLRNARRLLDSLRELEGssdRLRLVL---------------NRYDKKSEispKDIEEALGLEVFATLPNDYKAvSESANT 213

                       250       260
                ....*....|....*....|..
gi 58865352 239 GRDFIQEFPKSTAYSALTSIAH 260
Cdd:cd03111 214 GRPLVEVAPRSALVRALQDLAA 235
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 16-227 3.68e-09

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 55.85  E-value: 3.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALrhqgKKVGILDVDLCGPSIPHMLHAQGKAVHQCDSGWVPvFVDQEQSIS------- 88
Cdd:cd03110   1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKA-FIDQEKCIRcgncerv 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  89 -----LMSVG-------FLLEN--------PDEAVVWRgPKKHALIKQFVSD---VAWGEL------------------- 126
Cdd:cd03110  76 ckfgaILEFFqklivdeSLCEGcgacviicPRGAIYLK-DRDTGKIFISSSDggpLVHGRLnigeensgklvtelrkkal 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 127 ------DYLVVDTPPGTsdeHMATVEALRpykplGA---LVVTTPQAVSIGDVRRELTFCKKTGLQViGVIENMSGFacp 197
Cdd:cd03110 155 erskecDLAIIDGPPGT---GCPVVASIT-----GAdavLLVTEPTPSGLHDLKRAIELAKHFGIPT-GIVINRYDI--- 222

                       250       260       270
                ....*....|....*....|....*....|
gi 58865352 198 hcaectNVFSSGGGEELARLAGVPFLGSVP 227
Cdd:cd03110 223 ------NDEISEEIEDFADEEGIPLLGKIP 246
minD CHL00175
septum-site determining protein; Validated
 9-239 1.11e-08

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 54.78  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    9 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVH--------QC-------- 72
Cdd:CHL00175  10 KSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYtamdvlegECrldqalir 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   73 DSGWvpvfvdqeQSISLMSVGfllENPDEAVVWRGPkkhalIKQFVSDVAWGELDYLVVDTPPGTSdehMATVEALRPYK 152
Cdd:CHL00175  90 DKRW--------KNLSLLAIS---KNRQRYNVTRKN-----MNMLVDSLKNRGYDYILIDCPAGID---VGFINAIAPAQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  153 PlgALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfACPHCAECTNVFSSGGGEElarLAGVPFLGSVPLDPQL 232
Cdd:CHL00175 151 E--AIVVTTPEITAIRDADRVAGLLEANGIYNVKLLVNR---VRPDMIQANDMMSVRDVQE---MLGIPLLGAIPEDENV 222


                 ....*..
gi 58865352  233 TRSLEEG 239
Cdd:CHL00175 223 IISTNRG 229
ParA_partition NF041546
ParA family partition ATPase;
16-147 1.84e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 53.32  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPsiphmlhaQGKAvhqcdSGWvpvfvdQEQSislmsvgfl 95
Cdd:NF041546   1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD---P--------QGSA-----LDW------AAAR--------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 58865352   96 LENPDEAVV-WRGPKKHALIKQFVSDVawgelDYLVVDTPPGTSDEHMATVEA 147
Cdd:NF041546  50 EDERPFPVVgLARPTLHRELPSLARDY-----DFVVIDGPPRAEDLARSAIKA 97
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 15-263 2.91e-08

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: 53.32  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  15 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGpSIPHMLhaqGKAVHQCDSGWVPVFVDQ---EQSISLMS 91
Cdd:COG1192   2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGL---GLDPDDLDPTLYDLLLDDaplEDAIVPTE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  92 VG---FLLENPD----EAVVWRGPKKHALIKQFVSDVAwGELDYLVVDTPPGTSdehMATVEALRpykplgA----LVVT 160
Cdd:COG1192  78 IPgldLIPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLG---LLTLNALA------AadsvLIPV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 161 TPQAVS----------IGDVRRELtfckKTGLQVIGVIENMsgfacphcAECTNVFSSGGGEELARLAGVPFLGS-VPLD 229
Cdd:COG1192 148 QPEYLSleglaqlletIEEVREDL----NPKLEILGILLTM--------VDPRTRLSREVLEELREEFGDKVLDTvIPRS 215

                       250       260       270
                ....*....|....*....|....*....|....
gi 58865352 230 PQLTRSLEEGRDFIQEFPKSTAYSALTSIAHKVL 263
Cdd:COG1192 216 VALAEAPSAGKPVFEYDPKSKGAKAYRALAEELL 249
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 16-191 3.54e-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: 50.51  E-value: 3.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgpsiphmlhaqgkavhqcdsgwvpvfvdqeqsislmsvgfl 95
Cdd:cd01983   2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------- 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  96 lenpdeavvwrgpkkhalikqfvsdvawgelDYLVVDTPPGTSDE--HMATVEALRPYKPLGALVVTTPQAVSIGDVRRE 173
Cdd:cd01983  39 -------------------------------DYVLIDGGGGLETGllLGTIVALLALKKADEVIVVVDPELGSLLEAVKL 87

                       170       180
                ....*....|....*....|
gi 58865352 174 LTFCK--KTGLQVIGVIENM 191
Cdd:cd01983  88 LLALLllGIGIRPDGIVLNK 107
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 16-52 7.27e-08

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 51.98  E-value: 7.27e-08
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:COG2894   4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 16-261 1.40e-07

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 51.16  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD-------LCGPSIPHMLHAQGKAVhqcdsgwvpVFVDQEQSIS 88
Cdd:cd02034   1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADpnsnlaeTLGVEVEKLPLIKTIGD---------IRERTGAKKG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  89 LMSVGFLLENPDEAVVWRG--------------PKK---------HALIKQFVSDVAWGELDYLVVDTPPGTsdEHMA-- 143
Cdd:cd02034  72 EPPEGMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrg 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 144 ---TVEALrpykplgaLVVTTPQAVSIGDVRR--ELTfcKKTGLQVIGVIENMsgfacphcaectnVFSSGGGEELARLA 218
Cdd:cd02034 150 tirAVDLL--------IIVIEPSKRSIQTAKRikELA--EELGIKKIYLIVNK-------------VRNEEEQELIEELL 206

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 58865352 219 -GVPFLGSVPLDPQLTRSLEEGRDFIQEFPKstAYSALTSIAHK 261
Cdd:cd02034 207 iKLKLIGVIPYDEEIMEADLKGKPLFDLDSA--AVKAIEKIVEK 248
PHA02518 PHA02518
ParA-like protein; Provisional
 16-175 1.55e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 50.62  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgpsiphmlhAQGKAvhqcdSGWVPVFVDQEQSISLMSVGFL 95
Cdd:PHA02518   2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD-----------PQGSS-----TDWAEAREEGEPLIPVVRMGKS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   96 LENPDEAVVwrgpkkhalikqfvsdvawGELDYLVVDTPPGTSDEHMATVEA----LRPYKPLGALVVTTPQAVSIGDVR 171
Cdd:PHA02518  66 IRADLPKVA-------------------SGYDYVVVDGAPQDSELARAALRIadmvLIPVQPSPFDIWAAPDLVELIKAR 126


                 ....
gi 58865352  172 RELT 175
Cdd:PHA02518 127 QEVT 130
PRK10818 PRK10818
septum site-determining protein MinD;
16-243 2.97e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 50.32  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVH------QCDSGWVPVFVDQEQSISL 89
Cdd:PRK10818   4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDKRTENL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352   90 MSVGFLLENPDEAVVWRGpkkhalIKQFVSDVAWGELDYLVVDTPPGtsdehMATVEALRPYKPLGALVVTTPQAVSIGD 169
Cdd:PRK10818  84 YILPASQTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAG-----IETGALMALYFADEAIITTNPEVSSVRD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  170 VRReltfckktglqVIGVIENMSGFA----------------CPHCAECTNVFSSgggEELARLAGVPFLGSVPLDPQLT 233
Cdd:PRK10818 153 SDR-----------ILGILASKSRRAengeepikehllltryNPGRVSRGDMLSM---EDVLEILRIKLVGVIPEDQSVL 218

                        250
                 ....*....|
gi 58865352  234 RSLEEGRDFI 243
Cdd:PRK10818 219 RASNQGEPVI 228
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 15-53 7.21e-07

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: 49.37  E-value: 7.21e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 58865352    15 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDL 53
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDL 39
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
17-52 1.68e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 48.28  E-value: 1.68e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 58865352  17 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:COG0003   5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTD 40
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 16-52 2.01e-06

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: 46.81  E-value: 2.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 58865352    16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 16-190 6.51e-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: 46.35  E-value: 6.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLsGKGGVGKSTISTELALALRHQGKKV------------GILDVDLcGPSIP---------------HMLHAQGKA 68
Cdd:cd02035   2 IIFFG-GKGGVGKTTIAAATAVRLAEQGKRVllvstdpahslsDAFGQKL-GGETPvkgapnlwameidpeEALEEYWEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352  69 VHQCDSGWVPVFVDQEQSISLMSVGfllenP--DEAVvwrgpkkhAL--IKQFVSDvawGELDYLVVDTPPgtsdehmaT 144
Cdd:cd02035  80 VKELLAQYLRLPGLDEVYAEELLSL-----PgmDEAA--------AFdeLREYVES---GEYDVIVFDTAP--------T 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352 145 VEALR----PYKPLGAL----------VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIEN 190
Cdd:cd02035 136 GHTLRllslPLEQVRELlrdperttfvLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 16-190 8.89e-06

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 45.51  E-value: 8.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKAVHQCDsgwvpvFVDQEQSISLMSVGFL 95
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTN------FLSGTTDLSDAICDTN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    96 LENPDeaVVWRG---PKKHALI--KQFVS--DVAWGELDYLVVDTPPgtsdEHMATVEALRPYKPLGALVVTTPQAVSIG 168
Cdd:TIGR01007  93 IENLD--VITAGpvpPNPTELLqsSNFKTliETLRKRFDYIIIDTPP----IGTVTDAAIIARACDASILVTDAGKIKKR 166

                         170       180
                  ....*....|....*....|..
gi 58865352   169 DVRRELTFCKKTGLQVIGVIEN 190
Cdd:TIGR01007 167 EVKKAKEQLEQAGSNFLGVVLN 188
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 10-190 1.29e-05

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: 46.25  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    10 LAGVRHIILVLSGK-GGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLHAQGKA----VHQCDSGWVPVF-VDQ 83
Cdd:TIGR01005 548 LADAENNLIAIAGAlPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPKPglldLLAGEASIEAGIhRDQ 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865352    84 EQSISLMSVGFLL---ENPDEAVVwrGPKKHALIKQFVSdvawgELDYLVVDTPPgtsdehMATVEALRPYKPL--GALV 158
Cdd:TIGR01005 628 RPGLAFIAAGGAShfpHNPNELLA--NPAMAELIDNARN-----AFDLVLVDLAA------LAAVADAAAFAALadGILF 694

                         170       180       190
                  ....*....|....*....|....*....|..
gi 58865352   159 VTTPQAVSIGDVRRELTFCKKTGLQVIGVIEN 190
Cdd:TIGR01005 695 VTEFERSPLGEIRDLIHQEPHANSDVLGVIFN 726
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 16-59 3.60e-05

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 44.10  E-value: 3.60e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPSIP 59
Cdd:cd03114  47 FRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVD---PSSP 87
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 16-52 6.80e-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: 43.49  E-value: 6.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 58865352    16 IILVlSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:pfam02374   3 WIFF-GGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 18-52 1.43e-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: 1.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 58865352    18 LVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:TIGR04291   6 LFFTGKGGVGKTSIACATAINLADQGKRVLLVSTD 40
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 16-52 2.12e-04

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 40.79  E-value: 2.12e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:cd05386   2 IHFVLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTD 38
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 17-46 2.30e-04

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: 41.51  E-value: 2.30e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 58865352  17 ILVLSGKGGVGKSTISTELALALRHQGKKV 46
Cdd:cd02032   2 VIAVYGKGGIGKSTTSSNLSAAFAKRGKKV 31
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 22-46 3.80e-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: 40.96  E-value: 3.80e-04
                        10        20
                ....*....|....*....|....*
gi 58865352  22 GKGGVGKSTISTELALALRHQGKKV 46
Cdd:cd02040   7 GKGGIGKSTTASNLSAALAEMGKKV 31
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 10-46 4.17e-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: 41.61  E-value: 4.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 58865352    10 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKV 46
Cdd:TIGR04291 316 IAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDV 352
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 17-60 4.83e-04

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: 40.81  E-value: 4.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 58865352  17 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD--------LCGPSIPH 60
Cdd:cd02117   2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDpkhdstllLTGGKVPP 53
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 18-46 1.18e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.56  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 58865352   18 LVLS--GKGGVGKSTISTELALALRHQGKKV 46
Cdd:PRK13185   3 LVLAvyGKGGIGKSTTSSNLSAAFAKLGKKV 33
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 22-62 1.87e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.98  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 58865352   22 GKGGVGKSTISTELALALRHQGKKVGILDVD--------LCGPSIPHML 62
Cdd:PRK13230   8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVL 56
chlL CHL00072
photochlorophyllide reductase subunit L
 18-46 1.97e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.95  E-value: 1.97e-03
                         10        20
                 ....*....|....*....|....*....
gi 58865352   18 LVLSGKGGVGKSTISTELALALRHQGKKV 46
Cdd:CHL00072   3 LAVYGKGGIGKSTTSCNISIALARRGKKV 31
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 16-55 2.19e-03

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 38.29  E-value: 2.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 58865352  16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCG 55
Cdd:cd17869   5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQ 44
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 14-53 5.24e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 36.92  E-value: 5.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 58865352   14 RHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDL 53
Cdd:PRK00889   3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDA 42
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 14-59 8.33e-03

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 37.03  E-value: 8.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 58865352    14 RHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPSIP 59
Cdd:pfam03308  32 RAHRVGVTGVPGAGKSTLIEALGMELRRRGHRVAVLAVD---PSSP 74
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
 16-52 9.63e-03

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 36.63  E-value: 9.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 58865352   16 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 52
Cdd:PRK13886   4 IHMVLQGKGGVGKSFIAATIAQYKASKGQKPLCIDTD 40
 
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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