|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-273 |
3.00e-134 |
|
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: 379.88 E-value: 3.00e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021312262 213 INFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLI 273
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDI 215
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
55-274 |
1.50e-129 |
|
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: 366.83 E-value: 1.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLataHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 215 FCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIG 274
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
50-273 |
1.59e-114 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 334.48 E-value: 1.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 129
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIP---DAGAVIVTTPQELALADV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021312262 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAELMCQDLEVPLLGRVPLDPLI 273
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEI 218
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-269 |
2.35e-54 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 180.62 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPL 269
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPL 315
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
32-237 |
4.49e-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: 154.19 E-value: 4.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 32 ASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 110 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1021312262 185 rylaTAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 ----ASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
57-208 |
1.74e-08 |
|
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]
Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSL 206
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
|
..
gi 1021312262 207 QD 208
Cdd:TIGR01968 149 RD 150
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
57-185 |
8.82e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 48.32 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 136
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1021312262 137 SPDdaviwrgpkkngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVVR 185
Cdd:NF041546 62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-273 |
3.00e-134 |
|
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: 379.88 E-value: 3.00e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021312262 213 INFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLI 273
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDI 215
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
55-274 |
1.50e-129 |
|
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: 366.83 E-value: 1.50e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLataHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 215 FCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIG 274
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
50-273 |
1.59e-114 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 334.48 E-value: 1.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 129
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIP---DAGAVIVTTPQELALADV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021312262 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAELMCQDLEVPLLGRVPLDPLI 273
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEI 218
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-269 |
2.35e-54 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 180.62 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPL 269
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPL 315
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
32-237 |
4.49e-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: 154.19 E-value: 4.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 32 ASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 110 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1021312262 185 rylaTAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489 222 ----ASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
57-273 |
9.83e-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: 80.08 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 127
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQEV 204
Cdd:pfam01656 79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 205 SLQDVRKEINFCRKVK-------LPIIGVVENMsgficpkckkesqiFPPTTGGAELMcQDLE-----VPLLGRVPLDPL 272
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK--------------VDGDNHGKLLK-EALEellrgLPVLGVIPRDEA 217
|
.
gi 1021312262 273 I 273
Cdd:pfam01656 218 V 218
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
57-271 |
1.22e-17 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 81.70 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 133 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgEVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVIITTPQEV-SLQD 208
Cdd:COG4963 185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021312262 209 VRKEINFCRKVKLPI--IGVVENmsgficpKCKKESQIfppttgGAELMCQDLEVPLLGRVPLDP 271
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDP 306
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
57-273 |
1.57e-13 |
|
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: 68.36 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 126
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgEVDYLIVDTPPGTSDEhlsvVRYLATAhIDGAVIITTPQEVSL 206
Cdd:cd02038 78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN----VLDFLLA-ADEVIVVTTPEPTSI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021312262 207 QD---VRKEINfcRKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAELMCQ---DLEVPLLGRVPLDPLI 273
Cdd:cd02038 148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSV 210
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
50-230 |
1.92e-11 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 62.95 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 50 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 122
Cdd:COG1192 1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 123 EDNLGVMSVgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVvryLATAhiDGAVII 198
Cdd:COG1192 75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1021312262 199 TTPQEVSL----------QDVRKEINfcrkVKLPIIGVVENM 230
Cdd:COG1192 147 VQPEYLSLeglaqlletiEEVREDLN----PKLEILGILLTM 184
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
55-229 |
1.97e-11 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 61.82 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 127
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 128 VMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgEVDYLIVDTPP--GTSDEHLsvvryLATaHIDGAVIITTPQEVS 205
Cdd:cd05387 99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADALI-----LAP-LVDGVLLVVRAGKTR 165
|
170 180
....*....|....*....|....
gi 1021312262 206 LQDVRKEINFCRKVKLPIIGVVEN 229
Cdd:cd05387 166 RREVKEALERLEQAGAKVLGVVLN 189
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
56-273 |
2.13e-11 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 62.49 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----YVEDNLGVMS 130
Cdd:COG3640 2 KIAV-AGKGGVGKTTLSALLARYLAEKGKPVLA-VDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 131 VGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLSvvRY 186
Cdd:COG3640 74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG--RG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 187 LATaHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENmsgficpKCKKESQIfppttggaELMCQDLEVPLLGR 266
Cdd:COG3640 150 TAE-GVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGF 213
|
....*..
gi 1021312262 267 VPLDPLI 273
Cdd:COG3640 214 IPYDEEV 220
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
57-273 |
5.78e-11 |
|
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: 61.06 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 120
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 121 yveDNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSvvrylATAHIDGAVIITT 200
Cdd:cd02036 79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 201 PQEVSLQDVRKeinfcrkvklpIIGVVENMS----GFICPKCKKESqifppTTGGAELMCQD----LEVPLLGRVPLDPL 272
Cdd:cd02036 142 PEISSVRDADR-----------VIGLLESKGivniGLIVNRYRPEM-----VKSGDMLSVEDiqeiLGIPLLGVIPEDPE 205
|
.
gi 1021312262 273 I 273
Cdd:cd02036 206 V 206
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
57-218 |
6.26e-11 |
|
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: 61.14 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGEVDYLIVDTPPGTSDEHLSVVRylataHIDGAVIITTPQEVSLQD 208
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGHFLDEVTLAVLE-----AADEILLVTQQDLPSLRN 152
|
170
....*....|
gi 1021312262 209 VRKEINFCRK 218
Cdd:cd03111 153 ARRLLDSLRE 162
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
70-273 |
1.94e-10 |
|
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: 59.52 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 70 TFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VEDNLGVmsvgFLLSSPDDAVIWR 145
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 146 GPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCR-KVKLPII 224
Cdd:COG0455 76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDAYALLKLLRrRLGVRRA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1021312262 225 GVVENMSgficpkckKESQIFPPTTGGAELMCQ---DLEVPLLGRVPLDPLI 273
Cdd:COG0455 150 GVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAV 193
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
56-268 |
2.85e-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: 59.32 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 56 KILVLSGKGGVGKSTFSAHLAHGLAEdentqIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED----------- 124
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 159
Cdd:cd03110 76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 160 VDWGEVDYLIVDTPPGTsdeHLSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCRKVKLPiIGVVENMSGficpkck 239
Cdd:cd03110 155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------- 221
|
250 260
....*....|....*....|....*....
gi 1021312262 240 kesqIFPPTTGGAELMCQDLEVPLLGRVP 268
Cdd:cd03110 222 ----INDEISEEIEDFADEEGIPLLGKIP 246
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
57-208 |
1.45e-09 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 57.64 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVrYLAtahiDGAVIITTPQEVSL 206
Cdd:PRK10818 84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
|
..
gi 1021312262 207 QD 208
Cdd:PRK10818 151 RD 152
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
57-208 |
1.74e-08 |
|
septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]
Pssm-ID: 131023 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSL 206
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
|
..
gi 1021312262 207 QD 208
Cdd:TIGR01968 149 RD 150
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
56-273 |
1.03e-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: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 131
Cdd:cd02034 2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLA-VDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 132 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLS--VVRy 186
Cdd:cd02034 76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 187 lataHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSgficPKCKKESQIfppttggAELMCQDlevPLLGR 266
Cdd:cd02034 153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----RNEEEQELI-------EELLIKL---KLIGV 214
|
....*..
gi 1021312262 267 VPLDPLI 273
Cdd:cd02034 215 IPYDEEI 221
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
55-230 |
1.50e-07 |
|
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: 49.46 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 134
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 135 lsspdDAVIWRgpkkngmikqflrdvdwgeVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVII-TTPQEVSLQDVRKEI 213
Cdd:cd02042 42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLL 91
|
170 180
....*....|....*....|...
gi 1021312262 214 NFCRKVK------LPIIGVVENM 230
Cdd:cd02042 92 DTLEELKkqlnppLLILGILLTR 114
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
57-185 |
8.82e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 48.32 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 136
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1021312262 137 SPDdaviwrgpkkngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVVR 185
Cdd:NF041546 62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK 96
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
57-205 |
1.45e-06 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 48.51 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLE------------GE-QVHQSgsgwspvYVE 123
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 124 D----NLgvmsvgFLL----SSPDDAViwrgpKKNGMIK--QFLRDvdwgEVDYLIVDTPPGTsdEHLSvvrYLATAHID 193
Cdd:COG2894 77 DkrfeNL------YLLpasqTRDKDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIAGAD 136
|
170
....*....|..
gi 1021312262 194 GAVIITTPqEVS 205
Cdd:COG2894 137 EAIVVTTP-EVS 147
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
44-271 |
9.85e-06 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 45.92 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 44 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQIALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 123
Cdd:CHL00175 5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 124 dnLGVMSVGFLLsspDDAVI----WRG---------------PKKN-GMIKQFLRDVDWgevDYLIVDTPPGtsdehLSV 183
Cdd:CHL00175 74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKNmNMLVDSLKNRGY---DYILIDCPAG-----IDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 184 VRYLATAHIDGAVIITTPQEVSLQDVRK-----EINFCRKVKLPIIGVVENMsgficpkCKKESQIFPPTTGGAelmcqd 258
Cdd:CHL00175 141 GFINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMMSVRDVQEM------ 207
|
250
....*....|...
gi 1021312262 259 LEVPLLGRVPLDP 271
Cdd:CHL00175 208 LGIPLLGAIPEDE 220
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
56-93 |
3.76e-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: 42.03 E-value: 3.76e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1021312262 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 |
6.15e-05 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 43.88 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 55 HKILVLSGKGGVGKSTFSAHLAHGLAE-------------------------------DENTQIALLDIDicgpsipkiM 103
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSElgkkvllistdpahslsdsfnqkfgheptkvKENLSAMEIDPN---------M 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312262 104 GLEGEqvhqsgsgWSPVYVEDNLGVMSVG-------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGEVDYLIVDTPP 174
Cdd:pfam02374 72 ELEEY--------WQEVQKYMNALLGLRMlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
56-82 |
1.08e-03 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 39.80 E-value: 1.08e-03
10 20
....*....|....*....|....*..
gi 1021312262 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 |
1.40e-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: 1.40e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1021312262 43 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
54-83 |
2.05e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.79 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|
gi 1021312262 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 |
2.30e-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: 2.30e-03
10 20
....*....|....*....|....*.
gi 1021312262 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 |
2.50e-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: 2.50e-03
10 20
....*....|....*....|....*.
gi 1021312262 56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02035 1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
|
|
| |
