|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
1-203 |
6.85e-105 |
|
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: 302.06 E-value: 6.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:pfam10609 50 MLGLEGERPEQSDGGIIPVEAH---GIKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALrpyqPL-GALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAG 159
Cdd:pfam10609 127 QLTLAQLL----PLtGAVIVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530407428 160 VPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKIL 203
Cdd:pfam10609 203 VPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
1-173 |
3.41e-92 |
|
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: 268.60 E-value: 3.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:cd02037 47 LLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGFLLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALRPYqplGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGV 160
Cdd:cd02037 123 HLSLVQLIPID---GAVVVTTPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGV 199
|
170
....*....|...
gi 530407428 161 PFLGSVPLDPALM 173
Cdd:cd02037 200 PFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
1-206 |
4.45e-86 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 258.59 E-value: 4.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:NF041136 52 LLGLEGKRLGSEDEGILPVEYS--DNLKVMSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALrpyqPL-GALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAG 159
Cdd:NF041136 130 PLSVAQLI----PDaGAVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMG 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530407428 160 VPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDAT 206
Cdd:NF041136 206 VPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPILELL 252
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
31-179 |
6.61e-32 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 118.61 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 31 SVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMaTIEALRPYQplGALVVTTPQAVSVGDV 110
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407428 111 RRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEG 179
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRG 326
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
27-138 |
3.53e-18 |
|
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: 80.62 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 27 ISLMSVGFLLEKPDEAVVwrgpkkNALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATIealrpyQPL--GALVVTTPQA 104
Cdd:COG0489 170 LDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL------ASLvdGVLLVVRPGK 236
|
90 100 110
....*....|....*....|....*....|....
gi 530407428 105 VSVGDVRRELTFCRKTGLRVMGIVENMsgfTCPH 138
Cdd:COG0489 237 TALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
1-203 |
6.85e-105 |
|
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: 302.06 E-value: 6.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:pfam10609 50 MLGLEGERPEQSDGGIIPVEAH---GIKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALrpyqPL-GALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAG 159
Cdd:pfam10609 127 QLTLAQLL----PLtGAVIVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530407428 160 VPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKIL 203
Cdd:pfam10609 203 VPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFLKIADKVA 246
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
1-173 |
3.41e-92 |
|
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: 268.60 E-value: 3.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreqSISLMSVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:cd02037 47 LLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGFLLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALRPYqplGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGV 160
Cdd:cd02037 123 HLSLVQLIPID---GAVVVTTPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGV 199
|
170
....*....|...
gi 530407428 161 PFLGSVPLDPALM 173
Cdd:cd02037 200 PFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
1-206 |
4.45e-86 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 258.59 E-value: 4.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 1 MLGAQGRAVHQCDRGWAPVFLDreQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDE 80
Cdd:NF041136 52 LLGLEGKRLGSEDEGILPVEYS--DNLKVMSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 81 HMATIEALrpyqPL-GALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAG 159
Cdd:NF041136 130 PLSVAQLI----PDaGAVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMG 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530407428 160 VPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDAT 206
Cdd:NF041136 206 VPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPILELL 252
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
31-179 |
6.61e-32 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 118.61 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 31 SVGFLLEkPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMaTIEALRPYQplGALVVTTPQAVSVGDV 110
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407428 111 RRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEG 179
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRG 326
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
27-138 |
3.53e-18 |
|
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: 80.62 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 27 ISLMSVGFLLEKPDEAVVwrgpkkNALIKQFVSDVAwGELDYLVVDTPPGTSDEHMATIealrpyQPL--GALVVTTPQA 104
Cdd:COG0489 170 LDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL------ASLvdGVLLVVRPGK 236
|
90 100 110
....*....|....*....|....*....|....
gi 530407428 105 VSVGDVRRELTFCRKTGLRVMGIVENMsgfTCPH 138
Cdd:COG0489 237 TALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
64-205 |
1.15e-13 |
|
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: 67.22 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 64 GELDYLVVDTPPGTSDEHMATIEAlrpyqplgA---LVVTTPQAVSVGDVRRELTFCRKT-GLRVMGIVENMsgftcphc 139
Cdd:COG0455 92 RFYDVVLVDTGAGISDSVLLFLAA--------AdevVVVTTPEPTSITDAYALLKLLRRRlGVRRAGVVVNR-------- 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530407428 140 tectsVFSRGGGEELA-QLAGV---------PFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDA 205
Cdd:COG0455 156 -----VRSEAEARDVFeRLEQVaerflgvrlRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
42-182 |
1.88e-08 |
|
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: 52.73 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 42 AVVWRGPKKNALIKQFVSDVAwGELDYLVVDTPPGTsdeHMATIEALRPYQplGALVVTTPQAVSVGDVRRELTFCRKTG 121
Cdd:pfam01656 95 EKELLGPRKEERLREALEALK-EDYDYVIIDGAPGL---GELLRNALIAAD--YVIIPLEPEVILVEDAKRLGGVIAALV 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530407428 122 -------LRVMGIVENMSGftcphctectsvfSRGGGEELAQ-----LAGVPFLGSVPLDPALMRTLEEGHDF 182
Cdd:pfam01656 169 ggyallgLKIIGVVLNKVD-------------GDNHGKLLKEaleelLRGLPVLGVIPRDEAVAEAPARGLPV 228
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
49-191 |
3.55e-06 |
|
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: 46.02 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 49 KKNALIKQFVSDVAwgELDYLVVDTPPGTSDEhmaTIEALRPYQPLgaLVVTTPQAVSVGD--------VRRELtfcrKT 120
Cdd:cd02038 96 QKAKLIEELSSLES--NYDYLLIDTGAGISRN---VLDFLLAADEV--IVVTTPEPTSITDayalikvlSRRGG----KK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 121 GLRVmgiVENMsgftcphctectsVFSRGGGEELAQ-LAGV---------PFLGSVPLDPALMRTLEEGHDFIQEFPGSP 190
Cdd:cd02038 165 NFRL---IVNM-------------ARSPKEGRATFErLKKVakrfldinlDFVGFIPYDQSVRRAVRSQKPFVLLFPNSK 228
|
.
gi 530407428 191 A 191
Cdd:cd02038 229 A 229
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
51-202 |
1.31e-05 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 44.39 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 51 NALIKQFVSDVAWGELDYLVVDTPPGTsdEHMA--TIE---ALrpyqplgaLVVTTPQAVSVGDVRRELTFCRKTGLRVM 125
Cdd:COG3640 117 NALLRALLNHLVLGNYEYVVVDMEAGI--EHLGrgTAEgvdLL--------LVVSEPSRRSIETARRIKELAEELGIKKI 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530407428 126 GIVENMsgftcphctectsVFSRGGGEELAQLAGVPFLGSVPLDPALMRtLEEGHDFIQEFPGSPAFAALTSIAQKI 202
Cdd:COG3640 187 YLVGNK-------------VREEEDEEFLRELLGLELLGFIPYDEEVRE-ADLEGKPLLDLPDSPAVAAVEEIAEKL 249
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
23-202 |
1.02e-04 |
|
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: 41.80 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 23 REQSISLMSVGFLLEKpDEAvvwrGPKKnalIKQFVSDVAwGELDYLVVDTPPGT-SDEHMATIEALRpyqplgALVVTT 101
Cdd:cd02036 77 RWENLYLLPASQTRDK-DAL----TPEK---LEELVKELK-DSFDFILIDSPAGIeSGFINAIAPADE------AIIVTN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407428 102 PQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVfsrgggEELAQLAGVPFLGSVPLDPALMRTLEEGHD 181
Cdd:cd02036 142 PEISSVRDADRVIGLLESKGIVNIGLIVNRYRPEMVKSGDMLSV------EDIQEILGIPLLGVIPEDPEVIVATNRGEP 215
|
170 180
....*....|....*....|.
gi 530407428 182 FIQEFPGSPAFAALTSIAQKI 202
Cdd:cd02036 216 LVLYKPNSLAAKAFENIARRL 236
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
67-131 |
1.62e-03 |
|
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: 36.64 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407428 67 DYLVVDTPPGTSDE--HMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCR--KTGLRVMGIVENM 131
Cdd:cd01983 39 DYVLIDGGGGLETGllLGTIVALLALKKADEVIVVVDPELGSLLEAVKLLLALLllGIGIRPDGIVLNK 107
|
|
|