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Conserved domains on  [gi|1907124568|ref|XP_036016517|]
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cytosolic Fe-S cluster assembly factor NUBP2 isoform X1 [Mus musculus]

Protein Classification

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

MRP (Multiple Resistance and pH adaptation)/NBP35 (Nucleotide-binding protein 35) family ATP-binding protein, similar to the yeast cytosolic iron-sulfur (Fe-S) assembly factors, NBP35 and CFD1 (also called NUBP1/NUBP2 in higher eukaryotes), which functions as a heterotetrameric complex to assemble nascent Fe-S clusters and transfer them to apoprotein targets

Gene Ontology:  GO:0005524|GO:0016887|GO:0046872
PubMed:  11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 44-256 3.63e-125

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: 355.99  E-value: 3.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  44 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDqeqSISLMS 123
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 124 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALrpyrPL-GALVVTTPQAVSIGDV 202
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907124568 203 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLG 207
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 44-256 3.63e-125

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: 355.99  E-value: 3.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  44 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDqeqSISLMS 123
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 124 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALrpyrPL-GALVVTTPQAVSIGDV 202
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907124568 203 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLG 207
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 47-256 7.06e-121

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: 344.10  E-value: 7.06e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGF 126
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 127 LLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPYrplGALVVTTPQAVSIGDVRREL 206
Cdd:cd02037    78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907124568 207 TFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:cd02037   154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLG 203
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
42-256 5.58e-104

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 306.74  E-value: 5.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  42 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDQeqSISL 121
Cdd:NF041136    1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSD--NLKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 122 MSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALrpyrPL-GALVVTTPQAVSIG 200
Cdd:NF041136   79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907124568 201 DVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:NF041136  155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLG 210
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
44-256 3.59e-55

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 181.78  E-value: 3.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  44 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWV-PVfvdQEQSISLM 122
Cdd:PRK11670  105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPI---MAHGLATN 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 123 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMaTMEALRPYRplGALVVTTPQAVSIGDV 202
Cdd:PRK11670  182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907124568 203 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:PRK11670  258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLG 311
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 41-230 2.53e-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: 2.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  41 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAvhqcdnGWVPVFVDQ----- 115
Cdd:COG0489    87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP------GLSDVLAGEasled 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 116 ------EQSISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGQLDYLVVDTPPGTSDEHMATMEALRPyrplGAL 189
Cdd:COG0489   161 viqpteVEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVL 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907124568 190 VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfTCPH 230
Cdd:COG0489   230 LVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
ParA_partition NF041546
ParA family partition ATPase;
48-84 3.43e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 52.55  E-value: 3.43e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 48-222 5.07e-08

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: 52.73  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCgpsiphmLRaQGKAVHQCDNGWVPVFVDqeqsislmsvgfL 127
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIG-------LR-NLDLLLGLENRIVYTLVD------------V 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 128 LE---NPDEAVVW--RGPKKHAL---------------IKQFVSDVAwGQLDYLVVDTPPGT-SDEHMATMEALRpyrpl 186
Cdd:TIGR01968  63 VEgecRLQQALIKdkRLKNLYLLpasqtrdkdavtpeqMKKLVNELK-EEFDYVIIDCPAGIeSGFRNAVAPADE----- 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907124568 187 gALVVTTPQAVSIGDVRReltfckktglqVIGVIEN 222
Cdd:TIGR01968 137 -AIVVTTPEVSAVRDADR-----------VIGLLEA 160
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 44-256 3.63e-125

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: 355.99  E-value: 3.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  44 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDqeqSISLMS 123
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH---GIKVMS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 124 VGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALrpyrPL-GALVVTTPQAVSIGDV 202
Cdd:pfam10609  78 IGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL----PLtGAVIVTTPQDVALLDV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907124568 203 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:pfam10609 154 RKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLG 207
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 47-256 7.06e-121

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: 344.10  E-value: 7.06e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGF 126
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 127 LLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPYrplGALVVTTPQAVSIGDVRREL 206
Cdd:cd02037    78 LLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPID---GAVVVTTPQEVSLIDVRKAI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907124568 207 TFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:cd02037   154 DMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLG 203
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
42-256 5.58e-104

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 306.74  E-value: 5.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  42 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPVFVDQeqSISL 121
Cdd:NF041136    1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSD--NLKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 122 MSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALrpyrPL-GALVVTTPQAVSIG 200
Cdd:NF041136   79 MSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI----PDaGAVIVTTPQELALA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907124568 201 DVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:NF041136  155 DVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLG 210
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
44-256 3.59e-55

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 181.78  E-value: 3.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  44 GVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWV-PVfvdQEQSISLM 122
Cdd:PRK11670  105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQRPTSPDGTHMaPI---MAHGLATN 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 123 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMaTMEALRPYRplGALVVTTPQAVSIGDV 202
Cdd:PRK11670  182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907124568 203 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLG 256
Cdd:PRK11670  258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLG 311
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 41-230 2.53e-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: 2.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  41 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAvhqcdnGWVPVFVDQ----- 115
Cdd:COG0489    87 LLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP------GLSDVLAGEasled 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 116 ------EQSISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGQLDYLVVDTPPGTSDEHMATMEALRPyrplGAL 189
Cdd:COG0489   161 viqpteVEGLDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVL 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907124568 190 VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgfTCPH 230
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) ...
 48-201 5.25e-16

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 74.91  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGK-AVHQCDNGWVPVF---VDQEQSISLMS 123
Cdd:cd02038     2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKkTLGDVLKGRVSLEdiiVEGPEGLDIIP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907124568 124 VGFLLEnpdEAVVWRGPKKHALIKQFVSDVAwgQLDYLVVDTPPGTSDEhmaTMEALRPYRPLgaLVVTTPQAVSIGD 201
Cdd:cd02038    82 GGSGME---ELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN---VLDFLLAADEV--IVVTTPEPTSITD 149
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 49-223 4.05e-14

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: 69.68  E-value: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  49 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQ-------CDNGWV-PVFVD---QEQ 117
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqalaeglKGRVNLdPILLKeksDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 118 SISLMSVGFLLENPDEavVWRGPKKHALIKQFVSDVAwGQLDYLVVDTPPGTsdeHMATMEALRPyrPLGALVVTTPQAV 197
Cdd:pfam01656  81 GLDLIPGNIDLEKFEK--ELLGPRKEERLREALEALK-EDYDYVIIDGAPGL---GELLRNALIA--ADYVIIPLEPEVI 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907124568 198 SIGDVRRELTFCKKTG-------LQVIGVIENM 223
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK 185
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 47-214 2.23e-12

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 66.29  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALAL-RHQGKKVGILDVDLCGPSIPHMLraqgkavhqcdngwvpvfvDQEQSISLMSVG 125
Cdd:COG4963   103 RVIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDLDLQFGDVALYL-------------------DLEPRRGLADAL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 126 FLLENPDEAVVWRGPKKH-------ALIKQF-----VSDVAWGQL--------DYLVVDTPPGTSDEHMATMEAlrpyrp 185
Cdd:COG4963   164 RNPDRLDETLLDRALTRHssglsvlAAPADLeraeeVSPEAVERLldllrrhfDYVVVDLPRGLNPWTLAALEA------ 237

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907124568 186 lgA---LVVTTPQAVSIGDVRRELTFCKKTGL 214
Cdd:COG4963   238 --AdevVLVTEPDLPSLRNAKRLLDLLRELGL 267
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 46-222 3.86e-12

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: 63.36  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  46 RHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKA------VHQCDngWVPVFVDQEQS- 118
Cdd:cd05387    19 PKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPglsevlSGQAS--LEDVIQSTNIPn 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 119 ISLMSVGFLLENPDEAVvwRGPKKHALIKQFVsdvawGQLDYLVVDTPP--GTSDEHM-ATMEAlrpyrplGALVVTTPQ 195
Cdd:cd05387    97 LDVLPAGTVPPNPSELL--SSPRFAELLEELK-----EQYDYVIIDTPPvlAVADALIlAPLVD-------GVLLVVRAG 162

                         170       180
                  ....*....|....*....|....*..
gi 1907124568 196 AVSIGDVRRELTFCKKTGLQVIGVIEN 222
Cdd:cd05387   163 KTRRREVKEALERLEQAGAKVLGVVLN 189
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 47-84 2.72e-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: 2.72e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 48-222 3.91e-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: 58.37  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAV---HQCDNGWVP----VFVDQEQ-SI 119
Cdd:cd02036     2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVytlVDVLEGECRleqaLIKDKRWeNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 120 SLMSVGFLLENpDEAvvwrGPKKhalIKQFVSDVAwGQLDYLVVDTPPGT-SDEHMATMEALRpyrplgALVVTTPQAVS 198
Cdd:cd02036    82 YLLPASQTRDK-DAL----TPEK---LEELVKELK-DSFDFILIDSPAGIeSGFINAIAPADE------AIIVTNPEISS 146

                         170       180
                  ....*....|....*....|....
gi 1907124568 199 IGDVRRELTFCKKTGLQVIGVIEN 222
Cdd:cd02036   147 VRDADRVIGLLESKGIVNIGLIVN 170
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 62-223 3.16e-09

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: 55.67  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  62 TISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGK---------------AVHQCDNGwvpvfvdqeqsISLMSVGf 126
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKatladvlageadledAIVQGPGG-----------LDVLPGG- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 127 llenPDEAVVWRGPKKHALIKQFvsDVAWGQLDYLVVDTPPGTSDEHMATMEAlrpyrplgA---LVVTTPQAVSIGDVR 203
Cdd:COG0455    69 ----SGPAELAELDPEERLIRVL--EELERFYDVVLVDTGAGISDSVLLFLAA--------AdevVVVTTPEPTSITDAY 134

                         170       180
                  ....*....|....*....|....
gi 1907124568 204 ReltFCK----KTGLQVIGVIENM 223
Cdd:COG0455   135 A---LLKllrrRLGVRRAGVVVNR 155
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 47-223 2.75e-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: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGpSIPHMLraqGKAVHQCDNGWVPVFVDQ---EQSISLMS 123
Cdd:COG1192     2 KVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGL---GLDPDDLDPTLYDLLLDDaplEDAIVPTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 124 VG---FLLENPD----EAVVWRGPKKHALIKQFVSDVAwGQLDYLVVDTPPGTSdehMATMEALRpyrplgA----LVVT 192
Cdd:COG1192    78 IPgldLIPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLG---LLTLNALA------AadsvLIPV 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907124568 193 TPQAVS----------IGDVRRELtfckKTGLQVIGVIENM 223
Cdd:COG1192   148 QPEYLSleglaqlletIEEVREDL----NPKLEILGILLTM 184
ParA_partition NF041546
ParA family partition ATPase;
48-84 3.43e-08

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 52.55  E-value: 3.43e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:NF041546    1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 48-256 4.63e-08

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: 52.77  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALrhqgKKVGILDVDLCGPSIPHMLRAQGKAVHQCDNGWVPvFVDQEQSIS------- 120
Cdd:cd03110     1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKA-FIDQEKCIRcgncerv 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 121 -----LMSVG-------FLLEN--------PDEAVVWRgPKKHALIKQFVSD---VAWGQL------------------- 158
Cdd:cd03110    76 ckfgaILEFFqklivdeSLCEGcgacviicPRGAIYLK-DRDTGKIFISSSDggpLVHGRLnigeensgklvtelrkkal 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 159 ------DYLVVDTPPGTsdeHMATMEALRpyrplGA---LVVTTPQAVSIGDVRRELTFCKKTGLQViGVIENMSGFtcp 229
Cdd:cd03110   155 erskecDLAIIDGPPGT---GCPVVASIT-----GAdavLLVTEPTPSGLHDLKRAIELAKHFGIPT-GIVINRYDI--- 222

                         250       260
                  ....*....|....*....|....*..
gi 1907124568 230 hcaectNVFSSGSGEELARLAGVPFLG 256
Cdd:cd03110   223 ------NDEISEEIEDFADEEGIPLLG 243
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 48-222 5.07e-08

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: 52.73  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCgpsiphmLRaQGKAVHQCDNGWVPVFVDqeqsislmsvgfL 127
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIG-------LR-NLDLLLGLENRIVYTLVD------------V 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 128 LE---NPDEAVVW--RGPKKHAL---------------IKQFVSDVAwGQLDYLVVDTPPGT-SDEHMATMEALRpyrpl 186
Cdd:TIGR01968  63 VEgecRLQQALIKdkRLKNLYLLpasqtrdkdavtpeqMKKLVNELK-EEFDYVIIDCPAGIeSGFRNAVAPADE----- 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907124568 187 gALVVTTPQAVSIGDVRReltfckktglqVIGVIEN 222
Cdd:TIGR01968 137 -AIVVTTPEVSAVRDADR-----------VIGLLEA 160
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 48-84 7.90e-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: 7.90e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:COG2894     4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
PHA02518 PHA02518
ParA-like protein; Provisional
 48-207 1.00e-07

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 51.39  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgpsiphmlrAQGKAVHqcdngWVPVFVDQEQSISLMSVGFL 127
Cdd:PHA02518    2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD-----------PQGSSTD-----WAEAREEGEPLIPVVRMGKS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 128 LENPDEAVVwrgpkkhalikqfvsdvawGQLDYLVVDTPPGTSDEHMATMEA----LRPYRPLGALVVTTPQAVSIGDVR 203
Cdd:PHA02518   66 IRADLPKVA-------------------SGYDYVVVDGAPQDSELARAALRIadmvLIPVQPSPFDIWAAPDLVELIKAR 126


                  ....
gi 1907124568 204 RELT 207
Cdd:PHA02518  127 QEVT 130
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 48-84 1.02e-07

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: 49.35  E-value: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:cd01983     2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 48-213 1.89e-07

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: 50.74  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGK-KVGILDVDLCGPSIPHMLRAqgkavhQCDNGWVPVfVDQ-----EQSISL 121
Cdd:cd03111     2 VVAVVGAKGGVGASTLAVNLAQELAQRAKdKVLLIDLDLPFGDLGLYLNL------RPDYDLADV-IQNldrldRTLLDS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 122 MSV----GF-LLENPDEAVvwRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMATMEALRPyrplgALVVTTPQA 196
Cdd:cd03111    75 AVTrhssGLsLLPAPQELE--DLEALGAEQVDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADE-----ILLVTQQDL 147

                         170
                  ....*....|....*..
gi 1907124568 197 VSIGDVRRELTFCKKTG 213
Cdd:cd03111   148 PSLRNARRLLDSLRELE 164
PRK10818 PRK10818
septum site-determining protein MinD;
48-206 3.63e-07

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 50.32  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVHQcdngwvpvFVDQEQSISLMSVGFL 127
Cdd:PRK10818    4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYD--------FVNVIQGDATLNQALI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 128 LENPDEAV----VWRGPKKHAL----IKQFVSDVAWGQLDYLVVDTPPGTsdEHMATMeALrpYRPLGALVVTTPQAVSI 199
Cdd:PRK10818   76 KDKRTENLyilpASQTRDKDALtregVAKVLDDLKAMDFEFIVCDSPAGI--ETGALM-AL--YFADEAIITTNPEVSSV 150


                  ....*..
gi 1907124568 200 GDVRREL 206
Cdd:PRK10818  151 RDSDRIL 157
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 47-85 7.33e-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: 7.33e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907124568  47 HIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDL 85
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDL 39
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 42-222 1.20e-06

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


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 49.33  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  42 LAGVRHIILVLSGK-GGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHML---RAQGKAVHQCDNGWVP--VFVDQ 115
Cdd:TIGR01005 548 LADAENNLIAIAGAlPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFgkaPKPGLLDLLAGEASIEagIHRDQ 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 116 EQSISLMSVGFLL---ENPDEAVVwrGPKKHALIKQFVSdvawgQLDYLVVDTPPGTSdehMATMEALRPyRPLGALVVT 192
Cdd:TIGR01005 628 RPGLAFIAAGGAShfpHNPNELLA--NPAMAELIDNARN-----AFDLVLVDLAALAA---VADAAAFAA-LADGILFVT 696

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907124568 193 TPQAVSIGDVRRELTFCKKTGLQVIGVIEN 222
Cdd:TIGR01005 697 EFERSPLGEIRDLIHQEPHANSDVLGVIFN 726
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
49-84 1.52e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 48.28  E-value: 1.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907124568  49 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:COG0003     5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTD 40
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 48-84 2.03e-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: 2.03e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
minD CHL00175
septum-site determining protein; Validated
 41-221 2.28e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 47.84  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  41 NLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKAVH--------QC-------- 104
Cdd:CHL00175   10 KSATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRVLYtamdvlegECrldqalir 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 105 DNGWvpvfvdqeQSISLMSVGfllENPDEAVVWRGPkkhalIKQFVSDVAWGQLDYLVVDTPPGTSdehMATMEALRPYR 184
Cdd:CHL00175   90 DKRW--------KNLSLLAIS---KNRQRYNVTRKN-----MNMLVDSLKNRGYDYILIDCPAGID---VGFINAIAPAQ 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907124568 185 PlgALVVTTPQAVSIGDVRReltfckktglqVIGVIE 221
Cdd:CHL00175  151 E--AIVVTTPEITAIRDADR-----------VAGLLE 174
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 48-222 2.90e-06

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


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 47.12  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLsGKGGVGKSTISTELALALRHQGKKV------------GILDVDLcGPSIP---------------HMLRAQGKA 100
Cdd:cd02035     2 IIFFG-GKGGVGKTTIAAATAVRLAEQGKRVllvstdpahslsDAFGQKL-GGETPvkgapnlwameidpeEALEEYWEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 101 VHQCDNGWVPVFVDQEQSISLMSVGfllenP--DEAVvwrgpkkhAL--IKQFVSDvawGQLDYLVVDTPPgtsdehmaT 176
Cdd:cd02035    80 VKELLAQYLRLPGLDEVYAEELLSL-----PgmDEAA--------AFdeLREYVES---GEYDVIVFDTAP--------T 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 177 MEALR----PYRPLGAL----------VVTTPQAVSIGDVRRELTFCKKTGLQVIGVIEN 222
Cdd:cd02035   136 GHTLRllslPLEQVRELlrdperttfvLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 49-256 3.86e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.08  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  49 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPSiPHMLRAQGkavhqcdngwVPVFVDQEQSISLM------ 122
Cdd:COG3640     2 KIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDAD---PN-ANLAEALG----------LEVEADLIKPLGEMrelike 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 123 -----SVGFLLENP------DEAVVWRG---------PKK---------HALIKQFVSDVAWGQLDYLVVDTPPGTsdEH 173
Cdd:COG3640    68 rtgapGGGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EH 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 174 MA--TME---ALrpyrplgaLVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMsgftcphcaectnVFSSGSGEELAR 248
Cdd:COG3640   146 LGrgTAEgvdLL--------LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNK-------------VREEEDEEFLRE 204


                  ....*...
gi 1907124568 249 LAGVPFLG 256
Cdd:COG3640   205 LLGLELLG 212
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 48-222 6.61e-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: 45.89  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCGPSIPHMLRAQGKavhqcdNGWVPVFVDQEQSISLMSVGFL 127
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNK------ITGLTNFLSGTTDLSDAICDTN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 128 LENPDeaVVWRG---PKKHALI--KQFVS--DVAWGQLDYLVVDTPPgtsdEHMATMEALRPYRPLGALVVTTPQAVSIG 200
Cdd:TIGR01007  93 IENLD--VITAGpvpPNPTELLqsSNFKTliETLRKRFDYIIIDTPP----IGTVTDAAIIARACDASILVTDAGKIKKR 166

                         170       180
                  ....*....|....*....|..
gi 1907124568 201 DVRRELTFCKKTGLQVIGVIEN 222
Cdd:TIGR01007 167 EVKKAKEQLEQAGSNFLGVVLN 188
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 48-223 2.37e-05

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: 44.61  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD-------LCGPSIPHMLRAQGKAVhqcdngwvpVFVDQEQSIS 120
Cdd:cd02034     1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADpnsnlaeTLGVEVEKLPLIKTIGD---------IRERTGAKKG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907124568 121 LMSVGFLLENPDEAVVWRG--------------PKK---------HALIKQFVSDVAWGQLDYLVVDTPPGTsdEHMA-- 175
Cdd:cd02034    72 EPPEGMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrg 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907124568 176 ---TMEALrpyrplgaLVVTTPQAVSIGDVRR--ELTfcKKTGLQVIGVIENM 223
Cdd:cd02034   150 tirAVDLL--------IIVIEPSKRSIQTAKRikELA--EELGIKKIYLIVNK 192
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 48-91 5.13e-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: 43.72  E-value: 5.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPSIP 91
Cdd:cd03114    47 FRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVD---PSSP 87
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 48-84 6.91e-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: 6.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVlSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:pfam02374   3 WIFF-GGKGGVGKTTVSAATAVQLSELGKKVLLISTD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 50-84 1.45e-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: 1.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907124568  50 LVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
Cdd:TIGR04291   6 LFFTGKGGVGKTSIACATAINLADQGKRVLLVSTD 40
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 48-105 1.86e-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: 1.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDlcgPSIPHMLRAQGKAVHQCD 105
Cdd:cd05386     2 IHFVLQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTD---PVNKTFAGYKALNVQRIN 56
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 49-78 2.07e-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: 41.90  E-value: 2.07e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907124568  49 ILVLSGKGGVGKSTISTELALALRHQGKKV 78
Cdd:cd02032     2 VIAVYGKGGIGKSTTSSNLSAAFAKRGKKV 31
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 54-78 4.22e-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: 4.22e-04
                          10        20
                  ....*....|....*....|....*
gi 1907124568  54 GKGGVGKSTISTELALALRHQGKKV 78
Cdd:cd02040     7 GKGGIGKSTTASNLSAALAEMGKKV 31
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 42-78 4.24e-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: 4.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  42 LAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKV 78
Cdd:TIGR04291 316 IAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDV 352
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 49-92 6.21e-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: 40.43  E-value: 6.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907124568  49 ILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD--------LCGPSIPH 92
Cdd:cd02117     2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDpkhdstllLTGGKVPP 53
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 50-78 1.04e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 39.56  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907124568  50 LVLS--GKGGVGKSTISTELALALRHQGKKV 78
Cdd:PRK13185    3 LVLAvyGKGGIGKSTTSSNLSAAFAKLGKKV 33
chlL CHL00072
photochlorophyllide reductase subunit L
 50-78 1.79e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 38.95  E-value: 1.79e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907124568  50 LVLSGKGGVGKSTISTELALALRHQGKKV 78
Cdd:CHL00072    3 LAVYGKGGIGKSTTSCNISIALARRGKKV 31
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 54-94 1.90e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.98  E-value: 1.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907124568  54 GKGGVGKSTISTELALALRHQGKKVGILDVD--------LCGPSIPHML 94
Cdd:PRK13230    8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVL 56
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 48-87 2.22e-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: 2.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDLCG 87
Cdd:cd17869     5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQ 44
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 46-85 5.30e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 36.92  E-value: 5.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907124568  46 RHIILVLSGKGGVGKSTISTELALALRHQGKKVGILDVDL 85
Cdd:PRK00889    3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDA 42
PRK13029 PRK13029
indolepyruvate ferredoxin oxidoreductase family protein;
6-82 6.14e-03

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237278 [Multi-domain]  Cd Length: 1186  Bit Score: 37.84  E-value: 6.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907124568    6 ALVTIgsKAAKVWRGSGREPRKATSSGMEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHQGKKVGILD 82
Cdd:PRK13029   705 SFVTV--EGAQLKKPSDAALGRAALAAVAALPLPTLALLDRPYGILVTGIGGTGVVTIGGVLGMAAHLEGKGVSVLD 779
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
 48-84 9.40e-03

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 36.63  E-value: 9.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907124568  48 IILVLSGKGGVGKSTISTELALALRHQGKKVGILDVD 84
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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