|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-303 |
1.17e-148 |
|
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: 417.62 E-value: 1.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 213 INFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
|
250
....*....|.
gi 562834429 293 TLAYRSIIQRI 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 |
2.18e-130 |
|
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: 369.91 E-value: 2.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLaaaHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 562834429 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
50-319 |
3.32e-127 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 367.61 E-value: 3.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDDNLGVM 129
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAAahiDGAVIITTPQEVSLQDV 209
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 210 RKEINFCHKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250 260 270
....*....|....*....|....*....|
gi 562834429 290 SPATLAYRSIIQRIQEFCGFQQSKEETLTS 319
Cdd:NF041136 235 SPAAKALEKIVDPILELLENKKSLTEEPGT 264
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-303 |
8.77e-58 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 190.25 E-value: 8.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 210 RKEINFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
|
250
....*....|....
gi 562834429 290 SPATLAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
32-237 |
2.67e-45 |
|
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: 155.73 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 32 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 110 --VHQSGSGWSPV---YVDDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDFLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 562834429 185 QylaaAHIDGAVIITTPQEVSLQDVRKEINFCHKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
57-303 |
4.95e-20 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQV--HQSGSGWS----PVYVDDNlGVMS 130
Cdd:TIGR01969 3 ITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDKPVtlHDVLAGEAdikdAIYEGPF-GVKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 131 VgfllsspDDAVIWRGPKKNGMIKqfLRDV---DWGEVDFLIVDTPPGTSdehLSVVQYLAAAhiDGAVIITTPQEVSLQ 207
Cdd:TIGR01969 81 I-------PAGVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSIT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 208 DVRKEINFCHKVKLPIIGVVENMSGficpkckKESQIFPPTtggAAAMCqdLKVPLLGRVPLDPHIGKSCDKGQSFFTEA 287
Cdd:TIGR01969 147 DALKTKIVAEKLGTAILGVVLNRVT-------RDKTELGRE---EIETI--LEVPVLGVVPEDPEVRRAAAFGEPVVIYN 214
|
250
....*....|....*.
gi 562834429 288 PDSPATLAYRSIIQRI 303
Cdd:TIGR01969 215 PNSPAAQAFMELAAEL 230
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
57-198 |
7.81e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 48.70 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYVDDNLgvmsvgFLLS 136
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAREDERP------FPVV 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562834429 137 SPDDAVIWRGpkkngmIKQFLRDvdwgeVDFLIVDTPPGTSDEHLSVVQylaAAHIdgaVII 198
Cdd:NF041546 59 GLARPTLHRE------LPSLARD-----YDFVVIDGPPRAEDLARSAIK---AADL---VLI 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-303 |
1.17e-148 |
|
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: 417.62 E-value: 1.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVG 132
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEAH-GIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 213 INFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
|
250
....*....|.
gi 562834429 293 TLAYRSIIQRI 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 |
2.18e-130 |
|
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: 369.91 E-value: 2.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDdNLGVMSVGFL 134
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEVG-GIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLaaaHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 562834429 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
50-319 |
3.32e-127 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 367.61 E-value: 3.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDDNLGVM 129
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAAahiDGAVIITTPQEVSLQDV 209
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 210 RKEINFCHKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250 260 270
....*....|....*....|....*....|
gi 562834429 290 SPATLAYRSIIQRIQEFCGFQQSKEETLTS 319
Cdd:NF041136 235 SPAAKALEKIVDPILELLENKKSLTEEPGT 264
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-303 |
8.77e-58 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 190.25 E-value: 8.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVDdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 210 RKEINFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAAAMCQDLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
|
250
....*....|....
gi 562834429 290 SPATLAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
32-237 |
2.67e-45 |
|
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: 155.73 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 32 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 110 --VHQSGSGWSPV---YVDDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDFLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 562834429 185 QylaaAHIDGAVIITTPQEVSLQDVRKEINFCHKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
57-303 |
4.12e-23 |
|
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: 97.88 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVDDNLGVMSVG 132
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 133 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgEVDFLIVDTPPGTSDEHLSVvqyLAAAHIdgaVIITTPQEV-SLQD 208
Cdd:COG4963 185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 209 VRKEINFCHKVKLPI--IGVVENmsgficpKCKKESQIfppttgGAAAMCQDLKVPLLGRVPLDP-HIGKSCDKGQSFFT 285
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321
|
250
....*....|....*...
gi 562834429 286 EAPDSPATLAYRSIIQRI 303
Cdd:COG4963 322 VAPKSPLAKAIRKLAARL 339
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
57-303 |
3.65e-20 |
|
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: 87.26 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQV-------------HQSgsgwspVYVD 123
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENRIVytlvdvlegecrlEQA------LIKD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 124 ---DNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGEVDFLIVDTPPGTSDEHLSvvqylAAAHIDGAVIITT 200
Cdd:cd02036 76 krwENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 201 PQEVSLQDVRKEINFCHKVKLPIIGVVENMsgfICPKCKKESQIFPPttggaAAMCQDLKVPLLGRVPLDPHIGKSCDKG 280
Cdd:cd02036 142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213
|
250 260
....*....|....*....|...
gi 562834429 281 QSFFTEAPDSPATLAYRSIIQRI 303
Cdd:cd02036 214 EPLVLYKPNSLAAKAFENIARRL 236
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
70-303 |
4.34e-20 |
|
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: 86.87 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 70 TFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VDDNLGVmsvgFLLSSPDDAVIWR 145
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 146 GPKKNGMIKQFLRDVDwGEVDFLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEVSLQD---VRKEINFCHKVKlp 222
Cdd:COG0455 76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDayaLLKLLRRRLGVR-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 223 IIGVVENMSgficpkckKESQIFPPTTGGAAAMCQ---DLKVPLLGRVPLDPHIGKSCDKGQSFFTEAPDSPATLAYRSI 299
Cdd:COG0455 148 RAGVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIREL 219
|
....
gi 562834429 300 IQRI 303
Cdd:COG0455 220 AARL 223
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
57-303 |
4.95e-20 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQV--HQSGSGWS----PVYVDDNlGVMS 130
Cdd:TIGR01969 3 ITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDKPVtlHDVLAGEAdikdAIYEGPF-GVKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 131 VgfllsspDDAVIWRGPKKNGMIKqfLRDV---DWGEVDFLIVDTPPGTSdehLSVVQYLAAAhiDGAVIITTPQEVSLQ 207
Cdd:TIGR01969 81 I-------PAGVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSIT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 208 DVRKEINFCHKVKLPIIGVVENMSGficpkckKESQIFPPTtggAAAMCqdLKVPLLGRVPLDPHIGKSCDKGQSFFTEA 287
Cdd:TIGR01969 147 DALKTKIVAEKLGTAILGVVLNRVT-------RDKTELGRE---EIETI--LEVPVLGVVPEDPEVRRAAAFGEPVVIYN 214
|
250
....*....|....*.
gi 562834429 288 PDSPATLAYRSIIQRI 303
Cdd:TIGR01969 215 PNSPAAQAFMELAAEL 230
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
57-283 |
3.20e-18 |
|
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: 82.01 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVDDNLG 127
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGEVDFLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEV 204
Cdd:pfam01656 79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 205 SLQDVRKEINFCHKVK-------LPIIGVVENMSGficPKCKKESQIfppttggaAAMCQDL-KVPLLGRVPLDPHIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221
|
....*..
gi 562834429 277 CDKGQSF 283
Cdd:pfam01656 222 PARGLPV 228
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
57-293 |
1.52e-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: 77.22 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVDDNL 126
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgEVDFLIVDTPPGTSDehlSVVQYLAAAHIdgAVIITTPQEVSL 206
Cdd:cd02038 78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 207 QDVRKEINFCHKVKLPI-IGVVENMSgficpKCKKESQifpPTTGGAAAMCQ---DLKVPLLGRVPLDPHIGKSCDKGQS 282
Cdd:cd02038 148 TDAYALIKVLSRRGGKKnFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQKP 219
|
250
....*....|.
gi 562834429 283 FFTEAPDSPAT 293
Cdd:cd02038 220 FVLLFPNSKAS 230
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
50-305 |
7.23e-16 |
|
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: 75.66 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 50 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 122
Cdd:COG1192 1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 123 DDNLGVMSVgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGEVDFLIVDTPPGTSDEHLSVvqyLAAAhiDGAVII 198
Cdd:COG1192 75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 199 TTPQEVSL----------QDVRKEINfchkVKLPIIGVVENMsgficpkckkesqiFPPTTGGAAAMCQDLK----VPLL 264
Cdd:COG1192 147 VQPEYLSLeglaqlletiEEVREDLN----PKLEILGILLTM--------------VDPRTRLSREVLEELReefgDKVL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 562834429 265 G-RVPLDPHIGKSCDKGQSFFTEAPDSPATLAYRSIIQRIQE 305
Cdd:COG1192 209 DtVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
57-299 |
1.33e-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: 71.93 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVDDNLGVMSVG 132
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGEVDFLIVDTPPgtsdeHLSVVQYLAAAHIDGAVIITTPQEVSLQD 208
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 209 VRKEINFCHKVKLPI--IGVVENmsgficpKCKKESQIFPPTTGGAaamcqdLKVPLLGRVPLDPH-IGKSCDKGQSFFT 285
Cdd:cd03111 153 ARRLLDSLRELEGSSdrLRLVLN-------RYDKKSEISPKDIEEA------LGLEVFATLPNDYKaVSESANTGRPLVE 219
|
250
....*....|....
gi 562834429 286 EAPDSPATLAYRSI 299
Cdd:cd03111 220 VAPRSALVRALQDL 233
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
57-304 |
1.74e-13 |
|
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]
Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 69.29 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQsgsgwspvYVD------------- 123
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYT--------LVDvvegecrlqqali 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 124 -----DNLGVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDFLIVDTPPGtsdehLSVVQYLAAAHIDGAVII 198
Cdd:TIGR01968 75 kdkrlKNLYLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 199 TTPQEVSLQDVRKeinfchkvklpIIGVVENMS--------GFICPKCKKESQIFppttgGAAAMCQDLKVPLLGRVPLD 270
Cdd:TIGR01968 141 TTPEVSAVRDADR-----------VIGLLEAKGiekihlivNRLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPED 204
|
250 260 270
....*....|....*....|....*....|....
gi 562834429 271 PHIGKSCDKGQSFFTEaPDSPATLAYRSIIQRIQ 304
Cdd:TIGR01968 205 EAIIVSTNKGEPVVLN-DKSRAGKAFENIARRIL 237
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
56-303 |
4.62e-13 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 67.88 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAL-LDIDicgPSIPKIMGLEGEQvhqsgSGWSPV-----YVDDNLGVM 129
Cdd:COG3640 2 KIAV-AGKGGVGKTTLSALLARYLAEKGKPVLAVdADPN---ANLAEALGLEVEA-----DLIKPLgemreLIKERTGAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 130 SVGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGEVDFLIVDTPPGTsdEHLSvvq 185
Cdd:COG3640 73 GGGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 186 YLAAAHIDGAVIITTPQEVSLQDVRKEINFCHKVKLPIIGVVENmsgficpKCKKESQIfppttggaAAMCQDLKVPLLG 265
Cdd:COG3640 148 RGTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLG 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 562834429 266 RVPLDPHIGKSCDKGQSFFtEAPDSPATLAYRSIIQRI 303
Cdd:COG3640 213 FIPYDEEVREADLEGKPLL-DLPDSPAVAAVEEIAEKL 249
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
57-303 |
3.53e-12 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 65.35 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVDD----NL 126
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGEVDFLIVDTPPGTSDEHLSVVqYLAaahiDGAVIITTPQEVSL 206
Cdd:PRK10818 84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 207 QDVRKeinfchkvklpIIGVVENmsgficpKCKKESQIFPP---------------TTGGAAAM---CQDLKVPLLGRVP 268
Cdd:PRK10818 151 RDSDR-----------ILGILAS-------KSRRAENGEEPikehllltrynpgrvSRGDMLSMedvLEILRIKLVGVIP 212
|
250 260 270
....*....|....*....|....*....|....*
gi 562834429 269 LDPHIGKSCDKGQSFFTEApDSPATLAYRSIIQRI 303
Cdd:PRK10818 213 EDQSVLRASNQGEPVILDI-EADAGKAYADTVDRL 246
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
55-229 |
3.75e-11 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 61.05 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDICGPSIPKIMGLEGEQ------VHQSgSGWSPVYVDD--NL 126
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglsevlSGQA-SLEDVIQSTNipNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 127 GVMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgEVDFLIVDTPP--GTSDEHLsvvqylAAAHIDGAVIITTPQEV 204
Cdd:cd05387 98 DVLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADALI------LAPLVDGVLLVVRAGKT 164
|
170 180
....*....|....*....|....*
gi 562834429 205 SLQDVRKEINFCHKVKLPIIGVVEN 229
Cdd:cd05387 165 RRREVKEALERLEQAGAKVLGVVLN 189
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
57-304 |
4.74e-11 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 62.00 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEgEQVhqsgsgwspVY--VD----------- 123
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLE-NRI---------VYdlVDviegecrlkqa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 124 -------DNLgvmsvgFLLssP-----D-DAViwrgpKKNGMIK--QFLRDvdwgEVDFLIVDTPPGTsdEHLSvvqYLA 188
Cdd:COG2894 74 likdkrfENL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 189 AAHIDGAVIITTPQEVSLQDV-RkeinfchkvklpIIGVVENMSgficpkCKKESQIFpptTGGAAAMCQD--------- 258
Cdd:COG2894 132 IAGADEAIVVTTPEVSSVRDAdR------------IIGLLEAKG------IRKPHLII---NRYRPAMVKRgdmlsvedv 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 562834429 259 ---LKVPLLGRVPLDPHIGKSCDKGqsfftE----APDSPATLAYRSIIQRIQ 304
Cdd:COG2894 191 leiLAIPLLGVVPEDEEVIVSSNRG-----EpvvlDEKSKAGQAYRNIARRLL 238
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
44-311 |
2.53e-08 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 54.01 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 44 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQIALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyvd 123
Cdd:CHL00175 5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 124 dnLGVMSVGFLLsspDDAVI----WRG---------------PKKN-GMIKQFLRDVDWgevDFLIVDTPPGtsdehLSV 183
Cdd:CHL00175 74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKNmNMLVDSLKNRGY---DYILIDCPAG-----IDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 184 VQYLAAAHIDGAVIITTPQEVSLQDVRK-----EINFCHKVKLPIIGVVENMsgficpkCKKESQIfppttggAAAMCQD 258
Cdd:CHL00175 141 GFINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM-------SVRDVQE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 562834429 259 -LKVPLLGRVPLDPHIGKSCDKGQSFFTEAPDSPATLAY----RSIIQRIQEFCGFQQ 311
Cdd:CHL00175 207 mLGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFenaaRRLVGKQDYFIDLDS 264
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
56-268 |
3.17e-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: 53.54 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 56 KILVLSGKGGVGKSTFSAHLAHGLAEdentqIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVDD----------- 124
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 159
Cdd:cd03110 76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 160 VDWGEVDFLIVDTPPGTsdeHLSVVQYLAAAhiDGAVIITTPQEVSLQDVRKEINFCHKVKLPiIGVVENMSGfICPKCK 239
Cdd:cd03110 155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD-INDEIS 227
|
250 260
....*....|....*....|....*....
gi 562834429 240 KESQIFppttggaaamCQDLKVPLLGRVP 268
Cdd:cd03110 228 EEIEDF----------ADEEGIPLLGKIP 246
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
56-303 |
6.88e-08 |
|
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: 52.70 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDiCGPSIPKIMGLEGEQVHQSGSgwspvyVDD-------NLGV 128
Cdd:cd02034 2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLA-VDAD-PNSNLAETLGVEVEKLPLIKT------IGDirertgaKKGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 129 MSVGFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGEVDFLIVDTPPGTsdEHLS--V 183
Cdd:cd02034 73 PPEGMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 184 VQylaaaHIDGAVIITTPQEVSLQDVRKEINFCHKVKLPIIGVVENMSGficpkcKKESQIFPPTTGgaaamcqdLKVPL 263
Cdd:cd02034 151 IR-----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVR------NEEEQELIEELL--------IKLKL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 562834429 264 LGRVPLDPHIGKSCDKGQSFFTEapDSPATLAYRSIIQRI 303
Cdd:cd02034 212 IGVIPYDEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
55-230 |
9.58e-08 |
|
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: 50.23 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsipkimglegeqvHQSgsgwspvyvddnlgvmsvgfl 134
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 135 lsspdDAVIWRgpkkngmikqflrdvdwgeVDFLIVDTPPGTSDEHLSVvqyLAAAHIdgaVII-TTPQEVSLQDVRKEI 213
Cdd:cd02042 42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLL 91
|
170 180
....*....|....*....|...
gi 562834429 214 NFCHKVK------LPIIGVVENM 230
Cdd:cd02042 92 DTLEELKkqlnppLLILGILLTR 114
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
57-198 |
7.81e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 48.70 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYVDDNLgvmsvgFLLS 136
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAREDERP------FPVV 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562834429 137 SPDDAVIWRGpkkngmIKQFLRDvdwgeVDFLIVDTPPGTSDEHLSVVQylaAAHIdgaVII 198
Cdd:NF041546 59 GLARPTLHRE------LPSLARD-----YDFVVIDGPPRAEDLARSAIK---AADL---VLI 103
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
56-93 |
2.74e-05 |
|
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: 42.42 E-value: 2.74e-05
10 20 30
....*....|....*....|....*....|....*...
gi 562834429 56 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQIALLDID 93
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
55-174 |
5.62e-04 |
|
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: 41.18 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562834429 55 HKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVDDNLGVMSVG-- 132
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSE-LGKKVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIDpn 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 562834429 133 -----------------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGEVDFLIVDTPP 174
Cdd:pfam02374 71 meleeywqevqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
56-82 |
1.26e-03 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 39.80 E-value: 1.26e-03
10 20
....*....|....*....|....*..
gi 562834429 56 KILVLSGKGGVGKSTFSAHLAHGLAED 82
Cdd:COG0003 4 RIIFFTGKGGVGKTTVAAATALALAER 30
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
43-81 |
1.67e-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: 1.67e-03
10 20 30
....*....|....*....|....*....|....*....
gi 562834429 43 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
54-83 |
2.43e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.79 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|
gi 562834429 54 KHKILVLSGKGGVGKSTFSAHLAHGLAEDE 83
Cdd:COG5635 179 KKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
56-81 |
2.75e-03 |
|
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: 38.89 E-value: 2.75e-03
10 20
....*....|....*....|....*.
gi 562834429 56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02117 1 ESIVVYGKGGIGKSTTASNLSAALAE 26
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
56-81 |
2.90e-03 |
|
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: 38.64 E-value: 2.90e-03
10 20
....*....|....*....|....*.
gi 562834429 56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02035 1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
|
|
| |
