|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
56-307 |
6.75e-155 |
|
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: 433.42 E-value: 6.75e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 56 SVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLAVMSI 135
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALA-RLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 136 GFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDVRK 215
Cdd:pfam10609 79 GFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 216 EIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSP 295
Cdd:pfam10609 156 AIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233
|
250
....*....|..
gi 62955037 296 AAAAYQSIVQKI 307
Cdd:pfam10609 234 AAKAFLKIADKV 245
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
54-307 |
2.08e-133 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 383.40 E-value: 2.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 54 MTSVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLAVM 133
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 134 SIGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDV 213
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 214 RKEIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFPptTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPD 293
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250
....*....|....
gi 62955037 294 SPAAAAYQSIVQKI 307
Cdd:NF041136 235 SPAAKALEKIVDPI 248
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
59-279 |
5.53e-132 |
|
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: 374.15 E-value: 5.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 59 HKILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLAVMSIGFL 138
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAK-KGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 139 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDVRKEIR 218
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62955037 219 FCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGK 279
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
57-307 |
4.22e-64 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 206.82 E-value: 4.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 57 VKHKILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLAVMSI 135
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK-VGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 136 GFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLSgagIDGAVIITTPQEVSLQDVRK 215
Cdd:PRK11670 184 GYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAKK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 216 EIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSP 295
Cdd:PRK11670 260 GIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337
|
250
....*....|..
gi 62955037 296 AAAAYQSIVQKI 307
Cdd:PRK11670 338 FTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
36-241 |
2.78e-47 |
|
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: 160.74 E-value: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 36 ASGATKAPDPAIEEIKQKMTSVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQ-- 113
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALA-QSGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 114 --VHQSGSGWSPV---YVEDNLAVMSIGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSIV 188
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 62955037 189 QYLsgagIDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIENMsgfVCPK 241
Cdd:COG0489 222 ASL----VDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
61-308 |
3.64e-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: 68.13 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 130
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGT-SDEHLSIvqylsgAGIDGAVIITTPQEVS 209
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAGIeSGFRNAV------APADEAIVVTTPEVSA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 210 LQDVRKeirfckkvnlpILGVIENMSgfVCPKCKNTSQIFPPTTGGAQRMC-----EELNLPLLGRIPLDPRIGKSCDEG 284
Cdd:TIGR01968 148 VRDADR-----------VIGLLEAKG--IEKIHLIVNRLRPEMVKKGDMLSvddvlEILSIPLIGVIPEDEAIIVSTNKG 214
|
250 260
....*....|....*....|....
gi 62955037 285 KSFLTEvPDSPAAAAYQSIVQKIR 308
Cdd:TIGR01968 215 EPVVLN-DKSRAGKAFENIARRIL 237
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
61-97 |
2.84e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 50.24 E-value: 2.84e-07
10 20 30
....*....|....*....|....*....|....*..
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVD 97
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
56-307 |
6.75e-155 |
|
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: 433.42 E-value: 6.75e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 56 SVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLAVMSI 135
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALA-RLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 136 GFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDVRK 215
Cdd:pfam10609 79 GFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 216 EIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSP 295
Cdd:pfam10609 156 AIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233
|
250
....*....|..
gi 62955037 296 AAAAYQSIVQKI 307
Cdd:pfam10609 234 AAKAFLKIADKV 245
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
54-307 |
2.08e-133 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 383.40 E-value: 2.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 54 MTSVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLAVM 133
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 134 SIGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDV 213
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLI---PDAGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 214 RKEIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFPptTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPD 293
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250
....*....|....
gi 62955037 294 SPAAAAYQSIVQKI 307
Cdd:NF041136 235 SPAAKALEKIVDPI 248
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
59-279 |
5.53e-132 |
|
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: 374.15 E-value: 5.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 59 HKILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLAVMSIGFL 138
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAK-KGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 139 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLsgaGIDGAVIITTPQEVSLQDVRKEIR 218
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62955037 219 FCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGK 279
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
57-307 |
4.22e-64 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 206.82 E-value: 4.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 57 VKHKILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLAVMSI 135
Cdd:PRK11670 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAK-VGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATNSI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 136 GFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSIVQYLSgagIDGAVIITTPQEVSLQDVRK 215
Cdd:PRK11670 184 GYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAKK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 216 EIRFCKKVNLPILGVIENMSGFVCPKCKNTSQIFppTTGGAQRMCEELNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSP 295
Cdd:PRK11670 260 GIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337
|
250
....*....|..
gi 62955037 296 AAAAYQSIVQKI 307
Cdd:PRK11670 338 FTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
36-241 |
2.78e-47 |
|
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: 160.74 E-value: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 36 ASGATKAPDPAIEEIKQKMTSVKHKILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEGEQ-- 113
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALA-QSGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 114 --VHQSGSGWSPV---YVEDNLAVMSIGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSIV 188
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 62955037 189 QYLsgagIDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIENMsgfVCPK 241
Cdd:COG0489 222 ASL----VDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
61-307 |
7.21e-24 |
|
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: 99.80 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKEVALLDVDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLAVMSIG 136
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 137 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgEVDYLIVDTPPGTSDEHLSIvqyLSGAGIdgaVIITTPQEV-SLQD 212
Cdd:COG4963 185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 213 VRKEIRFCKKVNLPI--LGVIENMsgfvcpkckntsqiFPPTTG-GAQRMCEELNLPLLGRIPLDPR-IGKSCDEGKSFL 288
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLNR--------------VPKRGEiSAKDIEEALGLPVAAVLPNDPKaVAEAANQGRPLA 320
|
250
....*....|....*....
gi 62955037 289 TEVPDSPAAAAYQSIVQKI 307
Cdd:COG4963 321 EVAPKSPLAKAIRKLAARL 339
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
61-287 |
2.71e-20 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 87.79 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDIcGPSIPKIMGLEGE--QVHQS------GSGW------SPVYV 126
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALA-RRGLRVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNldpillKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 127 EDNLAVMSIGFLLSspDDAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSivqYLSGAgiDGAVIITTPQ 206
Cdd:pfam01656 79 EGGLDLIPGNIDLE--KFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGELLRN---ALIAA--DYVIIPLEPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 207 EVSLQDVRKEIRFCKKV-------NLPILGVIENMSGfvcpkckntsqifPPTTGGAQR--MCEEL-NLPLLGRIPLDPR 276
Cdd:pfam01656 151 VILVEDAKRLGGVIAALvggyallGLKIIGVVLNKVD-------------GDNHGKLLKeaLEELLrGLPVLGVIPRDEA 217
|
250
....*....|.
gi 62955037 277 IGKSCDEGKSF 287
Cdd:pfam01656 218 VAEAPARGLPV 228
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
61-307 |
3.46e-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: 87.64 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 124
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALA-KLGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 125 yveDNLAVMSIGFllSSPDDAViwrGPKKngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSIVqylsgAGIDGAVIITT 204
Cdd:cd02036 79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFINAI-----APADEAIIVTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 205 PQEVSLQDVRKEIRFCKKVNLPILGVIENMsgfVCPKCKNTSQIFPPttggaQRMCEELNLPLLGRIPLDPRIGKSCDEG 284
Cdd:cd02036 142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213
|
250 260
....*....|....*....|...
gi 62955037 285 KSFLTEVPDSPAAAAYQSIVQKI 307
Cdd:cd02036 214 EPLVLYKPNSLAAKAFENIARRL 236
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
74-309 |
6.80e-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: 86.48 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 74 TFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLEGEQ-VHQSGSGWSPVyvEDNLAVMSIGF-LLSSPDDAVIWRGP 151
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADL--EDAIVQGPGGLdVLPGGSGPAELAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 152 KKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSIVQyLSgagiDGAVIITTPQEVSLQD---VRKEIRfcKKVNLPIL 228
Cdd:COG0455 78 DPEERLIRVLEELE-RFYDVVLVDTGAGISDSVLLFLA-AA----DEVVVVTTPEPTSITDayaLLKLLR--RRLGVRRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 229 GVIENMSGfvcpkcknTSQIFPPTTGGAQRMCEE---LNLPLLGRIPLDPRIGKSCDEGKSFLTEVPDSPAAAAYQSIVQ 305
Cdd:COG0455 150 GVVVNRVR--------SEAEARDVFERLEQVAERflgVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAA 221
|
....
gi 62955037 306 KIRD 309
Cdd:COG0455 222 RLAG 225
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
61-297 |
2.08e-18 |
|
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: 82.62 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALaSDSSKEVALLD-------VDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 130
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALAL-SKLGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgEVDYLIVDTPPGTSDEhlsiVQYLSGAgIDGAVIITTPQEVSL 210
Cdd:cd02038 78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN----VLDFLLA-ADEVIVVTTPEPTSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 211 QDVRKEIRFC-KKVNLPILGVIENMsgfvcpkCKNTSQifppttggAQRMCEEL----------NLPLLGRIPLDPRIGK 279
Cdd:cd02038 148 TDAYALIKVLsRRGGKKNFRLIVNM-------ARSPKE--------GRATFERLkkvakrfldiNLDFVGFIPYDQSVRR 212
|
250
....*....|....*...
gi 62955037 280 SCDEGKSFLTEVPDSPAA 297
Cdd:cd02038 213 AVRSQKPFVLLFPNSKAS 230
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
60-307 |
6.75e-17 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 78.67 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 60 KILVlSGKGGVGKSTFSAHLSHALASDsSKEVALLDVDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----YVEDNLAVMS 134
Cdd:COG3640 2 KIAV-AGKGGVGKTTLSALLARYLAEK-GKPVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 135 IGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLSivqy 190
Cdd:COG3640 74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 191 lSG--AGIDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIENmsgfvcpKCKNTSQIFppttggaqRMCEELNLPLL 268
Cdd:COG3640 148 -RGtaEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDEE--------FLRELLGLELL 211
|
250 260 270
....*....|....*....|....*....|....*....
gi 62955037 269 GRIPLDPRIGKSCDEGKSfLTEVPDSPAAAAYQSIVQKI 307
Cdd:COG3640 212 GFIPYDEEVREADLEGKP-LLDLPDSPAVAAVEEIAEKL 249
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
61-307 |
1.80e-15 |
|
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: 74.51 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALAsDSSKEVALLDVDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYVEDNLAVM 133
Cdd:COG1192 4 IAVANQKGGVGKTTTAVNLAAALA-RRGKRVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIVPTEIPGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 134 SIgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSIvqyLSGAgiDGAVIITTPQEVS 209
Cdd:COG1192 82 DL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIPVQPEYLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 210 LQDVRKEIRFCKKV------NLPILGVIENMsgfvcpkckntsqiFPPTTGGAQRMCEEL----NLPLLG-RIPLDPRIG 278
Cdd:COG1192 154 LEGLAQLLETIEEVredlnpKLEILGILLTM--------------VDPRTRLSREVLEELreefGDKVLDtVIPRSVALA 219
|
250 260
....*....|....*....|....*....
gi 62955037 279 KSCDEGKSFLTEVPDSPAAAAYQSIVQKI 307
Cdd:COG1192 220 EAPSAGKPVFEYDPKSKGAKAYRALAEEL 248
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
61-304 |
1.90e-15 |
|
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: 74.24 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKEVALLDVDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLAVMSIG 136
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 137 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGEVDYLIVDTPPGtsDEHLSiVQYLSGAgiDGAVIITTPQEVSLQD 212
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGHF--LDEVT-LAVLEAA--DEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 213 VRKEIRFCKKvnlpiLGVIENMSGFVCPKCKNTSQIFPPTTGgaqrmcEELNLPLLGRIPLDPR-IGKSCDEGKSFLTEV 291
Cdd:cd03111 153 ARRLLDSLRE-----LEGSSDRLRLVLNRYDKKSEISPKDIE------EALGLEVFATLPNDYKaVSESANTGRPLVEVA 221
|
250
....*....|...
gi 62955037 292 PDSPAAAAYQSIV 304
Cdd:cd03111 222 PRSALVRALQDLA 234
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
61-308 |
3.64e-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: 68.13 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 130
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGT-SDEHLSIvqylsgAGIDGAVIITTPQEVS 209
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAGIeSGFRNAV------APADEAIVVTTPEVSA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 210 LQDVRKeirfckkvnlpILGVIENMSgfVCPKCKNTSQIFPPTTGGAQRMC-----EELNLPLLGRIPLDPRIGKSCDEG 284
Cdd:TIGR01968 148 VRDADR-----------VIGLLEAKG--IEKIHLIVNRLRPEMVKKGDMLSvddvlEILSIPLIGVIPEDEAIIVSTNKG 214
|
250 260
....*....|....*....|....
gi 62955037 285 KSFLTEvPDSPAAAAYQSIVQKIR 308
Cdd:TIGR01968 215 EPVVLN-DKSRAGKAFENIARRIL 237
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
61-307 |
2.28e-12 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 65.85 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIPKIMGLE------------GE-QVHQSgsgwspvYVE 127
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 128 D----NLavmsigFLLssP-----D-DAViwrgpKKNGMIK--QFLRDvdwgEVDYLIVDTPPGTsdEH---LSIvqyls 192
Cdd:COG2894 77 DkrfeNL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQgfkNAI----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 193 gAGIDGAVIITTPqEVSlqDVRKEIRfckkvnlpILGVIENMSgfvcpkckntsqIFPP------------TTGG---AQ 257
Cdd:COG2894 133 -AGADEAIVVTTP-EVS--SVRDADR--------IIGLLEAKG------------IRKPhliinryrpamvKRGDmlsVE 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62955037 258 RMCEELNLPLLGRIPLDPRIGKSCDEGKSfLTEVPDSPAAAAYQSIVQKI 307
Cdd:COG2894 189 DVLEILAIPLLGVVPEDEEVIVSSNRGEP-VVLDEKSKAGQAYRNIARRL 237
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
60-272 |
3.24e-12 |
|
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: 65.10 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 60 KILVLSGKGGVGKSTFSAHLSHALasdssKEVALLDVDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED----------- 128
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLL-----YNVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 129 -------NLAVMSIGF----------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 163
Cdd:cd03110 76 ckfgailEFFQKLIVDeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 164 VDWGEVDYLIVDTPPGTsdeHLSIVQYLSGAgiDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIenmsgfvcpkck 243
Cdd:cd03110 155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIPTGIVI------------ 217
|
250 260
....*....|....*....|....*....
gi 62955037 244 NTSQIFPPTTGGAQRMCEELNLPLLGRIP 272
Cdd:cd03110 218 NRYDINDEISEEIEDFADEEGIPLLGKIP 246
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
59-233 |
4.04e-12 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 64.13 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 59 HKILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLA 131
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 132 VMSIGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgEVDYLIVDTPP-GTSDEHLSIVQYLsgagiDGAVIITTPQEVSL 210
Cdd:cd05387 99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvLAVADALILAPLV-----DGVLLVVRAGKTRR 166
|
170 180
....*....|....*....|...
gi 62955037 211 QDVRKEIRFCKKVNLPILGVIEN 233
Cdd:cd05387 167 REVKEALERLEQAGAKVLGVVLN 189
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
61-307 |
1.68e-11 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 63.42 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKEVaLLDVDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 130
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGEVDYLIVDTPPGTSDEHLsIVQYLSgagiDGAVIITTPQEVSL 210
Cdd:PRK10818 84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGAL-MALYFA----DEAIITTNPEVSSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 211 QDVRKeirfckkvnlpILGVIENmsgfvcpKCKNTSQIFPP----------TTGGAQR--------MCEELNLPLLGRIP 272
Cdd:PRK10818 151 RDSDR-----------ILGILAS-------KSRRAENGEEPikehllltryNPGRVSRgdmlsmedVLEILRIKLVGVIP 212
|
250 260 270
....*....|....*....|....*....|....*
gi 62955037 273 LDPRIGKSCDEGKSFLTEVpDSPAAAAYQSIVQKI 307
Cdd:PRK10818 213 EDQSVLRASNQGEPVILDI-EADAGKAYADTVDRL 246
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
60-307 |
5.26e-10 |
|
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: 58.86 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 60 KILVlSGKGGVGKSTFSAHLSHALASDSsKEVALLDVDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNL----AVMSI 135
Cdd:cd02034 2 KIAV-AGKGGVGKTTIAALLIRYLAKKG-GKVLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTgakkGEPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 136 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLS--IVQy 190
Cdd:cd02034 76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 191 lsgaGIDGAVIITTPQEVSLQDVRKEIRFCKKVNLPILGVIENMSgfvcpkckntsqifppTTGGAQRMCEELN--LPLL 268
Cdd:cd02034 153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----------------RNEEEQELIEELLikLKLI 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 62955037 269 GRIPLDPRIGKSCDEGKSFLTEvpDSPAAAAYQSIVQKI 307
Cdd:cd02034 213 GVIPYDEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
61-97 |
2.84e-07 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 50.24 E-value: 2.84e-07
10 20 30
....*....|....*....|....*....|....*..
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVD 97
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
59-97 |
4.33e-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: 48.31 E-value: 4.33e-07
10 20 30
....*....|....*....|....*....|....*....
gi 62955037 59 HKILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVD 97
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD 38
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
61-233 |
2.54e-06 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 47.43 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVDICGPSIP-------KIMGLEGEQVHQS--GSGWSPVYVEdNLA 131
Cdd:TIGR01007 20 LLITSVKPGEGKSTTSANIAIAFAQ-AGYKTLLIDGDMRNSVMSgtfksqnKITGLTNFLSGTTdlSDAICDTNIE-NLD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 132 VMSIGFLlsSPDDAVIWRGPKKNGMIKQFLRdvdwgEVDYLIVDTPP-GTSDEHLSIVQYlsgagIDGAVIITTPQEVSL 210
Cdd:TIGR01007 98 VITAGPV--PPNPTELLQSSNFKTLIETLRK-----RFDYIIIDTPPiGTVTDAAIIARA-----CDASILVTDAGKIKK 165
|
170 180
....*....|....*....|...
gi 62955037 211 QDVRKEIRFCKKVNLPILGVIEN 233
Cdd:TIGR01007 166 REVKKAKEQLEQAGSNFLGVVLN 188
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
60-309 |
2.76e-06 |
|
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: 47.75 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 60 KILVLSGKGGVGKSTFSAHLSHALASdSSKEVALLDVD--------ICGPSIPK-IMGLEGEQVHQSGSGWSPVYVEDNL 130
Cdd:cd02117 1 ESIVVYGKGGIGKSTTASNLSAALAE-GGKKVLHVGCDpkhdstllLTGGKVPPtIDEMLTEDGTAEELRREDLLFSGFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DWGeVDYLIVDTppgtsdehLSIVqyLSGA-------GIDG 198
Cdd:cd02117 80 GVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDDD-YDVVIFDV--------LGDV--VCGGfaaplrrGFAQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 199 AVIITTPQEV-SL---QDVRKEIRFCKKVNLPILGVIENMSGfvcpkckntsqifPPTTGGAQRMCEELNLPLLGRIPLD 274
Cdd:cd02117 144 KVVIVVSEELmSLyaaNNIVKAVENYSKNGVRLAGLVANLRD-------------PAGTEEIQAFAAAVGTKILAVIPRD 210
|
250 260 270
....*....|....*....|....*....|....*
gi 62955037 275 PRIGKSCDEGKSFLTEVPDSPAAAAYQSIVQKIRD 309
Cdd:cd02117 211 PAVRRAELARVTVFEHDPVSPAASEFARLAAKIAD 245
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
61-285 |
1.33e-05 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 45.92 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 61 ILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVDICGPSIPKIMGLE------GEQVHQSGSGWSPVYVED----NL 130
Cdd:CHL00175 18 IVITSGKGGVGKTTTTANLGMSIARLGYR-VALIDADIGLRNLDLLLGLEnrvlytAMDVLEGECRLDQALIRDkrwkNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 131 AVMSIGfllSSPDDAVIWRgpKKNGMIKQFLRDVDWgevDYLIVDTPPGTSdehLSIVQYLSGAgiDGAVIITTPQEVSL 210
Cdd:CHL00175 97 SLLAIS---KNRQRYNVTR--KNMNMLVDSLKNRGY---DYILIDCPAGID---VGFINAIAPA--QEAIVVTTPEITAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 211 QDVRKeirfckkvnlpILGVIEnMSGFvcpkcKNTSQI---FPPTTGGAQRMC------EELNLPLLGRIPLDPRIGKSC 281
Cdd:CHL00175 164 RDADR-----------VAGLLE-ANGI-----YNVKLLvnrVRPDMIQANDMMsvrdvqEMLGIPLLGAIPEDENVIIST 226
|
....
gi 62955037 282 DEGK 285
Cdd:CHL00175 227 NRGE 230
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
60-97 |
1.71e-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: 43.19 E-value: 1.71e-05
10 20 30
....*....|....*....|....*....|....*...
gi 62955037 60 KILVLSGKGGVGKSTFSAHLSHALASDSSKeVALLDVD 97
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD 38
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
59-178 |
2.22e-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: 45.42 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 59 HKILVLSGKGGVGKSTFSAHLSHALaSDSSKEVALLDVDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVEDNLAVMSIG-- 136
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQL-SELGKKVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIDpn 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62955037 137 -----------------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGEVDYLIVDTPP 178
Cdd:pfam02374 71 meleeywqevqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
60-178 |
2.63e-05 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 45.20 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955037 60 KILVLSGKGGVGKSTFSAhlSHAL-ASDSSKEVALLDVDIcGPSIPKIMGLEGeqvhqsgsGWSPVYVE-DNLAVMSIgf 137
Cdd:COG0003 4 RIIFFTGKGGVGKTTVAA--ATALaLAERGKRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVAvPNLYALEI-- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62955037 138 llsSPDDAV--IWRGPKKN------------------GM--------IKQFLRDVDWgevDYLIVDTPP 178
Cdd:COG0003 71 ---DPEAELeeYWERVRAPlrgllpsagvdelaeslpGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
66-89 |
2.41e-03 |
|
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.
Pssm-ID: 349759 Cd Length: 265 Bit Score: 39.03 E-value: 2.41e-03
10 20
....*....|....*....|....
gi 62955037 66 GKGGVGKSTFSAHLSHALASDSSK 89
Cdd:cd02040 7 GKGGIGKSTTASNLSAALAEMGKK 30
|
|
| chlL |
PRK13185 |
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional |
60-84 |
6.84e-03 |
|
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
Pssm-ID: 237293 Cd Length: 270 Bit Score: 37.63 E-value: 6.84e-03
10 20
....*....|....*....|....*
gi 62955037 60 KILVLSGKGGVGKSTFSAHLSHALA 84
Cdd:PRK13185 3 LVLAVYGKGGIGKSTTSSNLSAAFA 27
|
|
| |
