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Conserved domains on  [gi|524969539|ref|XP_005084640|]
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cytosolic Fe-S cluster assembly factor NUBP1 [Mesocricetus auratus]

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 ...
53-303 2.00e-149

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: 419.55  E-value: 2.00e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   53 VKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 524969539  293 TAAYRSIIHRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
53-303 2.00e-149

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: 419.55  E-value: 2.00e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   53 VKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 524969539  293 TAAYRSIIHRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
55-275 3.60e-131

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 371.83  E-value: 3.60e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524969539 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
Mrp COG0489
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell ...
9-277 5.46e-74

Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223563 [Multi-domain]  Cd Length: 265  Bit Score: 228.84  E-value: 5.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   9 PGIDSAQAGRGASCQGCPNQrLCASGAGAAPDPAVEEIKEKM---KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDt 85
Cdd:COG0489   10 PFASSSEEIPELLAKALAAL-LPKSTASEALRALRTNLKFAKvlrKGVKNVIAVTSGKGGVGKSTVAVNLAAALAQLGK- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  86 QVALLDIDICGPSIPKIMGLEGEQVHQ---SGSGWSPVYVEDNLGVMSVGFLLSSPddaVIWRGPKKNGMIKQFLRDVDW 162
Cdd:COG0489   88 RVLLLDADLRGPSIPRMLGLENLPGLTellAGEALEPVIQHDGIKVLSILPLGPVP---VIPRGLLGSKAMLQLLEDVLW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 163 GDVDYLIIDTPPGTSDEHLSVVQYLAaahiDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKes 242
Cdd:COG0489  165 GEYDYVIIDTPPGTGDADATVLQRIP----DGVVIVTTPGKTALEDVKKAIDMLEKAGIPVLGVVENMSYFICPRCGE-- 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 524969539 243 qifppttGGAEAMCQDLKiPLLGRVPLDPLIGKSC 277
Cdd:COG0489  239 -------GGGEKYAERYG-PYLGSIPLDPSAREAS 265
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.04e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  51 KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
                        250
                 ....*....|....
gi 524969539 290 SPATAAYRSIIHRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
57-304 5.03e-15

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: 73.53  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGK-KVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDVDYLIIDTPPGtsdehLSVVQYLAAAHIDGAVILTTPQEVAL 206
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  207 QDVRKeisfchkvklpIIGVVENMS--------GFICPKCKKESQIFppttgGAEAMCQDLKIPLLGRVPLDPLIGKSCD 278
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKGiekihlivNRLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPEDEAIIVSTN 212
                         250       260
                  ....*....|....*....|....*.
gi 524969539  279 KGQSFFVEaPDSPATAAYRSIIHRIQ 304
Cdd:TIGR01968 213 KGEPVVLN-DKSRAGKAFENIARRIL 237
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
53-303 2.00e-149

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: 419.55  E-value: 2.00e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   53 VKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
                         250
                  ....*....|.
gi 524969539  293 TAAYRSIIHRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
55-275 3.60e-131

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 371.83  E-value: 3.60e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524969539 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
Mrp COG0489
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell ...
9-277 5.46e-74

Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223563 [Multi-domain]  Cd Length: 265  Bit Score: 228.84  E-value: 5.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   9 PGIDSAQAGRGASCQGCPNQrLCASGAGAAPDPAVEEIKEKM---KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDt 85
Cdd:COG0489   10 PFASSSEEIPELLAKALAAL-LPKSTASEALRALRTNLKFAKvlrKGVKNVIAVTSGKGGVGKSTVAVNLAAALAQLGK- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  86 QVALLDIDICGPSIPKIMGLEGEQVHQ---SGSGWSPVYVEDNLGVMSVGFLLSSPddaVIWRGPKKNGMIKQFLRDVDW 162
Cdd:COG0489   88 RVLLLDADLRGPSIPRMLGLENLPGLTellAGEALEPVIQHDGIKVLSILPLGPVP---VIPRGLLGSKAMLQLLEDVLW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 163 GDVDYLIIDTPPGTSDEHLSVVQYLAaahiDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKes 242
Cdd:COG0489  165 GEYDYVIIDTPPGTGDADATVLQRIP----DGVVIVTTPGKTALEDVKKAIDMLEKAGIPVLGVVENMSYFICPRCGE-- 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 524969539 243 qifppttGGAEAMCQDLKiPLLGRVPLDPLIGKSC 277
Cdd:COG0489  239 -------GGGEKYAERYG-PYLGSIPLDPSAREAS 265
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.04e-63

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 205.66  E-value: 1.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  51 KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
                        250
                 ....*....|....
gi 524969539 290 SPATAAYRSIIHRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
57-283 1.53e-20

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: 88.17  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   57 ILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 127
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRG-LRVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGDVDYLIIDTPPGTSDehlSVVQYLAAAhiDGAVILTTPQEV 204
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  205 ALQDVRKEISFCHKVK-------LPIIGVVENMSGficPKCKKESQIfppttggaEAMCQDL-KIPLLGRVPLDPLIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221

                  ....*..
gi 524969539  277 CDKGQSF 283
Cdd:pfam01656 222 PARGLPV 228
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
57-303 1.35e-19

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: 85.72  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 120
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVALAKLGK-KVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 121 yveDNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGDVDYLIIDTPPGTSDEHLSvvqylAAAHIDGAVILTT 200
Cdd:cd02036   79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 201 PQEVALQDVRKEISFCHKVKLPIIGVVENMsgfICPKCKKESQIFPPttggaEAMCQDLKIPLLGRVPLDPLIGKSCDKG 280
Cdd:cd02036  142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213
                        250       260
                 ....*....|....*....|...
gi 524969539 281 QSFFVEAPDSPATAAYRSIIHRI 303
Cdd:cd02036  214 EPLVLYKPNSLAAKAFENIARRL 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
57-293 1.37e-19

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: 85.70  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 126
Cdd:cd02038    3 IAVTSGKGGVGKTNVSANLALALSKLGKR-VLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgDVDYLIIDTPPGTSDehlSVVQYLAAAHIdgAVILTTPQEVAL 206
Cdd:cd02038   78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 207 QD---VRKEISfcHKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAEAMCQ---DLKIPLLGRVPLDPLIGKSCDKG 280
Cdd:cd02038  148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQ 217
                        250
                 ....*....|...
gi 524969539 281 QSFFVEAPDSPAT 293
Cdd:cd02038  218 KPFVLLFPNSKAS 230
FlhG COG0455
MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, ...
55-321 2.73e-19

MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 223531 [Multi-domain]  Cd Length: 262  Bit Score: 85.40  E-value: 2.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGE--QVHQSGSGWSP------VYVEDNL 126
Cdd:COG0455    3 KVIAVVSGKGGVGKTTITANLGAALAALGGKVVLLIDADLGLGNLSLLLGVESKptTLHDVLAGEASiediiyETPQDGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVG-----FLLSSPDDaviwrgpkKNGMIKQFLRDVDwgdvdYLIIDTPPGTSDEhlsVVQYLAAAhiDGAVILTTP 201
Cdd:COG0455   83 YVLPGGsgledLAKLDPED--------LEDVIKELEELYD-----YILIDTGAGLSRD---TLSFILSS--DELVIVTTP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 202 QEVALQDVRK--EISFCHKVKLPIIGVVENMSgficpkckkeSQIFPPTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDK 279
Cdd:COG0455  145 EPTSITDAYKtiKILSKLGLDLLGRRVVLNRV----------RSTKEGVDVAALLIQVVKQVPVLQVIPFDPEVRRALAE 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 524969539 280 GQSFFVEAPDSPATAAYRSIIHRIQEFCSSHPSLKGTEPSAT 321
Cdd:COG0455  215 GKPIVLYSPNSKASQAIKELAAKLAGLPEPKAPRRGFISKIK 256
MinD COG2894
Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, ...
57-304 9.47e-17

Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225447 [Multi-domain]  Cd Length: 272  Bit Score: 78.43  E-value: 9.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:COG2894    5 IVVTSGKGGVGKTTTTANIGTALAQLGK-KVVLIDFDIGLRNLDLIMGLENRIVYdlvdviEGEATLNQALIKDkrleNL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 gvmsvgFLL----SSPDDAViwrgpKKNGMIKqFLRDVDWGDVDYLIIDTPPGTSDEHLsvvqyLAAAHIDGAVILTTPQ 202
Cdd:COG2894   84 ------FLLpasqTRDKDAL-----TPEGVKK-VVNELKAMDFDYIIIDSPAGIEQGFK-----NAVYFADEAIVVTNPE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 203 EVALQDVRKeisfchkvklpIIGVVENMSgficPKCKKESQIFPP-----------TTG---GAEAMCQDLKIPLLGRVP 268
Cdd:COG2894  147 VSSVRDSDR-----------IIGLLESKS----RRAEIGEEPKEHlllnryrpemvKRGemlSVEDVLEILSIPLIGVIP 211
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 524969539 269 LDPLIGKSCDKGQSfFVEAPDSPATAAYRSIIHRIQ 304
Cdd:COG2894  212 EDQDVLRASNKGEP-VILDDNSDAGKAYRDIARRLL 246
BcsQ COG1192
Cellulose biosynthesis protein BcsQ [Cell motility];
49-307 1.03e-16

Cellulose biosynthesis protein BcsQ [Cell motility];


Pssm-ID: 224113 [Multi-domain]  Cd Length: 259  Bit Score: 78.33  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  49 KMKTvkhrILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDicgPSIPKIMGLeGEQVHQSGSGWS---------- 118
Cdd:COG1192    1 MMKI----IAVANQKGGVGKTTTAVNLAAALAKRGGKKVLLIDLD---PQGSLTSWL-GLRPDLEGDLYNllsglkerpd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 119 ---PVYVEDNLGVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVdWGDVDYLIIDTPPGTSDEHLSVvqyLAAAhiDGA 195
Cdd:COG1192   73 ildYTVVIEGLDLIPSNIDLAEGAEIELNAVAKEL-LLKRLLDPV-KDDYDYIIIDTPPSLGVLTLNA---LAAA--DHV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 196 VILTTPQEVAL-------QDVRKEISFcHKVKLPIIGVVENMsgfICPKCKKESQIFppttggaEAMCQDLKIPLLG-RV 267
Cdd:COG1192  146 LIPVQPEFLDLegleqllNTLEDLLKL-RRNKLIVVGILITR---FDSRTKLADEVL-------QELKQLLGDPVLKtKI 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 524969539 268 PLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQEFC 307
Cdd:COG1192  215 PRRVAYREAAAEGKPLYEYDPKSKAAEEYYELAKELLEEL 254
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
56-306 2.26e-16

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 224071 [Multi-domain]  Cd Length: 284  Bit Score: 77.78  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDgdTQVALLDIDICGPSIPKIMGLEGEQVH---------------------QSG 114
Cdd:COG1149    3 QVAVASGKGGTGKTTVAANLAVLLGDK--YKLVLADCDVEAPNLHLLLGVEVLEEEevirgeipeidpekcircgkcAEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 115 SGWSPVYVEDNLGVMSVGFL--------LSSPDDAvIWRGPKKNGMIKQFLrdVDWGD---------------------- 164
Cdd:COG1149   81 CRFGAIVVLPGGKPVLNPDLcegcgacsIVCPEPA-IEEEPVVIGKIYESK--TDYGFplisgrlnvgeeesgklvtalk 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 165 ------VDYLIIDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkc 238
Cdd:COG1149  158 khakelADLLIIDSAAGT---GCPVIASLKGA--DLAILVTEPTPFGLHDLKRALELVEHFGIP-TGIVINRYN------ 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524969539 239 kkesqifpPTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVeaPDSPATAAYRSIIHRIQEF 306
Cdd:COG1149  226 --------LGDSEIEEYCEEEGIPILGEIPYDKDIPEAYVNGEPFVE--PDSKEAEAILEEAEKLKEF 283
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
57-304 5.03e-15

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: 73.53  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGK-KVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDVDYLIIDTPPGtsdehLSVVQYLAAAHIDGAVILTTPQEVAL 206
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  207 QDVRKeisfchkvklpIIGVVENMS--------GFICPKCKKESQIFppttgGAEAMCQDLKIPLLGRVPLDPLIGKSCD 278
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKGiekihlivNRLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPEDEAIIVSTN 212
                         250       260
                  ....*....|....*....|....*.
gi 524969539  279 KGQSFFVEaPDSPATAAYRSIIHRIQ 304
Cdd:TIGR01968 213 KGEPVVLN-DKSRAGKAFENIARRIL 237
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
57-301 1.09e-14

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: 72.31  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGDVDYLIIDTPPgtsdeHLSVVQYLAAAHIDGAVILTTPQEVALQD 208
Cdd:cd03111   83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 209 VRKEISFC-------HKVKLpIIGVVENMSGfICPKckkesQIfppttggAEAmcqdLKIPLLGRVPLDP-LIGKSCDKG 280
Cdd:cd03111  153 ARRLLDSLrelegssDRLRL-VLNRYDKKSE-ISPK-----DI-------EEA----LGLEVFATLPNDYkAVSESANTG 214
                        250       260
                 ....*....|....*....|.
gi 524969539 281 QSFFVEAPDSPATAAYRSIIH 301
Cdd:cd03111  215 RPLVEVAPRSALVRALQDLAA 235
PRK10818 PRK10818
septum site-determining protein MinD;
57-303 2.92e-13

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 68.81  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVaLLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVqYLAaahiDGAVILTTPQEVAL 206
Cdd:PRK10818  84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 207 QDVRKeisfchkvklpIIGVVENMS--GFICPKCKKESQIFPPTTGG---------AEAMCQDLKIPLLGRVPLDPLIGK 275
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219
                        250       260
                 ....*....|....*....|....*...
gi 524969539 276 SCDKGQSFFVEApDSPATAAYRSIIHRI 303
Cdd:PRK10818 220 ASNQGEPVILDI-EADAGKAYADTVDRL 246
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
55-229 3.75e-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: 64.13  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 127
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSG-KRVLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 128 VMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgDVDYLIIDTPP--GTSDEHlsvvqyLAAAHIDGAVILTTPQEVA 205
Cdd:cd05387   99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADAL------ILAPLVDGVLLVVRAGKTR 165
                        170       180
                 ....*....|....*....|....
gi 524969539 206 LQDVRKEISFCHKVKLPIIGVVEN 229
Cdd:cd05387  166 RREVKEALERLEQAGAKVLGVVLN 189
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
57-268 5.97e-10

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 58.55  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEdgdtqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED------------ 124
Cdd:cd03110    2 IAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncervc 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 125 NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD----------------------------V 160
Cdd:cd03110   77 KFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkalE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 161 DWGDVDYLIIDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkckk 240
Cdd:cd03110  156 RSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD-------- 221
                        250       260
                 ....*....|....*....|....*...
gi 524969539 241 esqIFPPTTGGAEAMCQDLKIPLLGRVP 268
Cdd:cd03110  222 ---INDEISEEIEDFADEEGIPLLGKIP 246
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
55-230 1.21e-09

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: 55.62  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 134
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 135 lsspdDAVIWRgpkkngmikqflrdvdwgdVDYLIIDTPPGTSDEHLSVvqyLAAAhiDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02042   42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAA--DLVLIPVQPSPFDLDGLAKLLD 92
                        170       180
                 ....*....|....*....|..
gi 524969539 215 FCHKVK------LPIIGVVENM 230
Cdd:cd02042   93 TLEELKkqlnppLLILGILLTR 114
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
57-308 6.97e-09

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


Pssm-ID: 226166 [Multi-domain]  Cd Length: 255  Bit Score: 55.73  E-value: 6.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDiCGPSIPKIMGLEGEQVHQSG------------SGWSPVYV-E 123
Cdd:COG3640    2 KIAITGKGGVGKTTIAALLLKRLLSKGGYNVLVVDAD-PDSNLPEALGVEEPMKYLGGkrellkkrtgaePGGPPGEMfK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DNLGVMSVgfllssPDDAVIWRGPKK------------------NGMIKQFLRDVDWGDVDYLIIDTPPGTsdEHLS--V 183
Cdd:COG3640   81 ENPLVSDL------PDEYLVENGDIDllvmgkieeggegcacpmNALLRRLLRHLILNRYEVVIVDTEAGI--EHFGrgT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 184 VQylaaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENmsgficpKCKKESQIFppttggaEAMCQDLKIPL 263
Cdd:COG3640  153 IE-----GVDLVIVVVDPSYKSLRTAERIKELAEELGIKRIFVVLN-------KVDEEEELL-------RELAEELGLEV 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 524969539 264 LGRVPLDPLIGKSCDKGQSFFVEAPDSPATaayRSIIHRIQEFCS 308
Cdd:COG3640  214 LGVIPYDPEVVEADLKGEPLNEEPEVLKEI---EEIAERLIKLVE 255
minD CHL00175
septum-site determining protein; Validated
44-281 4.29e-08

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 53.62  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  44 EEIKEKMKTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 123
Cdd:CHL00175   5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 dnLGVMSVGFLLsspDDAVI----WRG---------------PKKNgmIKQFLRDVDWGDVDYLIIDTPPGtsdehLSVV 184
Cdd:CHL00175  74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKN--MNMLVDSLKNRGYDYILIDCPAG-----IDVG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 185 QYLAAAHIDGAVILTTPQEVALQDVRK-----EISFCHKVKLPIIGVVENMsgficpkCKKESQIfppTTGGAEAMcqdL 259
Cdd:CHL00175 142 FINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM---SVRDVQEM---L 208
                        250       260
                 ....*....|....*....|..
gi 524969539 260 KIPLLGRVPLDPLIGKSCDKGQ 281
Cdd:CHL00175 209 GIPLLGAIPEDENVIISTNRGE 230
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
56-284 1.22e-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: 51.93  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 131
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 132 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGDVDYLIIDTPPGTsdEHLS--VVQy 186
Cdd:cd02034   76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 187 laaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIfppttggaeamcqdLKIPLLGR 266
Cdd:cd02034  153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELL--------------IKLKLIGV 214
                        250
                 ....*....|....*...
gi 524969539 267 VPLDPLIGKSCDKGQSFF 284
Cdd:cd02034  215 IPYDEEIMEADLKGKPLF 232
CpaE COG4963
Flp pilus assembly protein, ATPase CpaE [Intracellular trafficking, secretion, and vesicular ...
54-303 1.65e-07

Flp pilus assembly protein, ATPase CpaE [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 227298 [Multi-domain]  Cd Length: 366  Bit Score: 52.03  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  54 KHRIL-VLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQvHQSGSGWSPVYVED-NLGVM-- 129
Cdd:COG4963  103 QGRELaFLGAKGGVGTSTLAHNLAKGLAILSGAAVLLVDLDLQGGTAALYLDQDPAF-GIAEAVKQPERLDQvLLDSLlt 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 130 ------SVGFLLSSPDDAviwrGPKKNGMIKQFLrDVDWGDVDYLIIDTPPGTSDEHlsvVQYLAAAhiDGAVILTTPQE 203
Cdd:COG4963  182 rlasglKLLAAPTELAKN----YDLKTGAVERLL-DLLRGSFDFVVVDLPNIWTDWT---RQVLSGS--DEIVIVAEPSL 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 204 VALQDVRKEISFCHKVKL---PIIGVVEnmsgficpkckkesQIFPPTTGGAEAMCQDLKIPLLGRVPLDPLI-GKSCDK 279
Cdd:COG4963  252 ASLRNAKELLDELKRLRPndpKPILVLN--------------RVGVPKRPEPSDLEEILGIESLLVLPFDPALfGDAANN 317
                        250       260
                 ....*....|....*....|....
gi 524969539 280 GQSFFVEAPDSPATAAYRSIIHRI 303
Cdd:COG4963  318 GRMLSEVDPGSPAAKALAQLAQSL 341
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
56-93 5.68e-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: 47.43  E-value: 5.68e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD 38
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
54-174 7.31e-07

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


Pssm-ID: 223082  Cd Length: 322  Bit Score: 50.05  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  54 KHRILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVAL-----------LDIDIcGPSIPKIMG-LEGEQVHQSGS---GWS 118
Cdd:COG0003    1 MTRIVFFTGKGGVGKTTIAAATAVKLAESGKKVLLVstdpahslgdvFDLEL-GHDPRKVGPnLDALELDPEKAleeYWD 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 524969539 119 PVY--VEDNLGVMSVGFLLssPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPP 174
Cdd:COG0003   80 EVKdyLARLLRTRGLGGIY--ADELATLPGIDEALALLKILEYYVSGEYDVIVVDTAP 135
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
55-174 8.56e-06

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


Pssm-ID: 396792  Cd Length: 302  Bit Score: 46.57  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDIcGPSIPKIMG-------------LEGEQVHQSGS---GWS 118
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGK-KVLLISTDP-AHSLSDSFNqkfgheptkvkenLSAMEIDPNMEleeYWQ 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524969539  119 PVYVEDNLGVMSVG-------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGDVDYLIIDTPP 174
Cdd:pfam02374  79 EVQKYMNALLGLRMlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
56-298 1.68e-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: 42.35  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGSGWSPVYVE 123
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGkkvlhvgcdpkhDSTLLLTG----GKVPPTIDEMLTEDGTAEELRREDLLFS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DNLGVMSVGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DWgDVDYLIID-----------TPPG----------TS 177
Cdd:cd02117   77 GFNGVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDD-DYDVVIFDvlgdvvcggfaAPLRrgfaqkvvivVS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 178 DEHLSVvqyLAAAHIDGAVilttpQEVALQDVRkeisfchkvklpIIGVVENMSGficpkckkesqifPPTTGGAEAMCQ 257
Cdd:cd02117  151 EELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAFAA 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 524969539 258 DLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRS 298
Cdd:cd02117  198 AVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFAR 238
NifH COG1348
Nitrogenase subunit NifH, an ATPase [Inorganic ion transport and metabolism];
56-305 2.47e-04

Nitrogenase subunit NifH, an ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 224267 [Multi-domain]  Cd Length: 278  Bit Score: 41.93  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGsgwspVYVE 123
Cdd:COG1348    2 RQIAIYGKGGIGKSTTSQNLAAALAELGkkvlivgcdpkaDSTRLLLG----GKAIPTVLDTLREKGEVED-----LELE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DnlgVMSVGFllsSPDDAVIWRGPKKN------GMIK--QFLRD--VDWGDVDYLIIDTPpgtSDehlsVVQYLAAAHI- 192
Cdd:COG1348   73 D---VIFTGF---GGVKCVESGGPEPGvgcagrGVITaiNLLEElgAFEEDLDVVIYDVL---GD----VVCGGFAMPIr 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 193 ----DGAVILTTPQEVAL-------QDVRKeISFCHKVKLpiigvvenmSGFIC--PKCKKESQIfppttggAEAMCQDL 259
Cdd:COG1348  140 egyaDEIYIVTSGEMMALyaanniaKGIRK-YAKTGGVRL---------GGIICnsRSVDREREL-------VEAFAERL 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 524969539 260 KIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQE 305
Cdd:COG1348  203 GTQLIHFVPRDNIVQKAELNGKTVIEYAPDSNQAEEYRELAKKILE 248
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
56-83 2.97e-04

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


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 41.72  E-value: 2.97e-04
                         10        20
                 ....*....|....*....|....*...
gi 524969539  56 RILVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQG 28
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
63-174 3.65e-04

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: 40.65  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   63 KGGVGKSTFSAHLAHGLAE--------DGDTQVAL-----LDIDICGPSIPKIMGLEG---EQVHQSgsgwspvyVEDNL 126
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKkgkkvlliDLDPQGNAtsglgIDKNNVEKTIYELLIGECnieEAIIKT--------VIENL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 524969539  127 GVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVDwGDVDYLIIDTPP 174
Cdd:pfam13614  82 DLIPSNIDLAGAEIELIGIENREN-ILKEALEPVK-DNYDYIIIDCPP 127
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
55-93 4.83e-04

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  Cd Length: 262  Bit Score: 40.90  E-value: 4.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 524969539   55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDID 93
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKG-ARVAAIDLD 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
56-305 9.74e-04

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 40.12  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539   56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDIDICgPSIPKIMGLEGeqvhqsgsgwspvYVE 123
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGkkvlvvgcdpkaDSTRLLLGGKLQ-PTVLDTAREKG-------------YVE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  124 DnLGVMSVGFLLSSPDDAVIWRGPKKN------GMIK--QFLRDVD-WGDVDYLIIDTppgTSDehlsVV-----QYLAA 189
Cdd:pfam00142  67 D-VEVEDVVYKGYGGVKCVESGGPEPGvgcagrGVITaiNLLEELGaYDDLDFVLYDV---LGD----VVcggfaMPIRE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539  190 AHIDGAVILTTPQEVAL---QDVRKEISF---CHKVKLpiigvvenmSGFICPKCKKESQifpptTGGAEAMCQDLKIPL 263
Cdd:pfam00142 139 GKAQEIYIVTSNEMMALyaaNNIAKGIQKyakSGGVRL---------GGIICNSRKVDDE-----RELIDAFAEELGTQV 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 524969539  264 LGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQE 305
Cdd:pfam00142 205 LHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRELARKILE 246
PHA02518 PHA02518
ParA-like protein; Provisional
57-93 1.10e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.45  E-value: 1.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 524969539  57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHK-VLLVDLD 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
41-83 1.43e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.07  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 524969539   41 PAVEEIKEKMKTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:TIGR04291 307 PSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKG 349
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
47-93 2.54e-03

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 39.19  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 524969539   47 KEKMKTVKHR--------ILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDID 93
Cdd:TIGR03453  89 REARRYLPHRrggehlqvIAVTNFKGGSGKTTTAAHLAQYLALRG-YRVLAIDLD 142
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
62-83 4.23e-03

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: 38.26  E-value: 4.23e-03
                         10        20
                 ....*....|....*....|..
gi 524969539  62 GKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMG 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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