|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
1-203 |
5.55e-102 |
|
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: 294.75 E-value: 5.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:pfam10609 50 MLGLEGERPEQSDGGIIPVEAH---GIKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALrpyrPL-GALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAG 159
Cdd:pfam10609 127 QLTLAQLL----PLtGAVIVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822188060 160 VPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVV 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 |
3.11e-91 |
|
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: 266.29 E-value: 3.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:cd02037 47 LLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGFLLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALRPYrplGALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGV 160
Cdd:cd02037 123 HLSLVQLIPID---GAVVVTTPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGV 199
|
170
....*....|...
gi 1822188060 161 PFLGSVPLDSQLT 173
Cdd:cd02037 200 PFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
1-203 |
1.03e-84 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 255.13 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDQeqSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:NF041136 52 LLGLEGKRLGSEDEGILPVEYSD--NLKVMSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALrpyrPL-GALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAG 159
Cdd:NF041136 130 PLSVAQLI----PDaGAVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMG 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822188060 160 VPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVV 203
Cdd:NF041136 206 VPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPIL 249
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
31-206 |
9.28e-31 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 115.53 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 31 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMaTMEALRPYRplGALVVTTPQAVSIGDV 110
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 111 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLGSVPLDSQLTRSLEEGRDFIQEFPKST 190
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337
|
170
....*....|....*.
gi 1822188060 191 AYSALTSIAQRVVHRM 206
Cdd:PRK11670 338 FTAIYRQLADRVAAQL 353
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
27-138 |
1.45e-19 |
|
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: 84.08 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 27 ISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGQLDYLVVDTPPGTSDEHMATMEALRPyrplGALVVTTPQAVS 106
Cdd:COG0489 170 LDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVLLVVRPGKTA 238
|
90 100 110
....*....|....*....|....*....|..
gi 1822188060 107 IGDVRRELTFCKKTGLQVIGVIENMsgfTCPH 138
Cdd:COG0489 239 LDDVRKALEMLEKAGVPVLGVVLNM---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 |
5.55e-102 |
|
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: 294.75 E-value: 5.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:pfam10609 50 MLGLEGERPEQSDGGIIPVEAH---GIKVMSIGFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALrpyrPL-GALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAG 159
Cdd:pfam10609 127 QLTLAQLL----PLtGAVIVTTPQDVALLDVRKAIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822188060 160 VPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVV 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 |
3.11e-91 |
|
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: 266.29 E-value: 3.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDqeqSISLMSVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:cd02037 47 LLGVEGKPLHQSEEGIVPVEVG---GIKVMSIGFLLP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALRPYrplGALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGV 160
Cdd:cd02037 123 HLSLVQLIPID---GAVVVTTPQEVSLIDVRKAIDMCKKLNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGV 199
|
170
....*....|...
gi 1822188060 161 PFLGSVPLDSQLT 173
Cdd:cd02037 200 PFLGKIPLDPELA 212
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
1-203 |
1.03e-84 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 255.13 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 1 MLRAQGKAVHQCDNGWVPVFVDQeqSISLMSVGFLLENPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDE 80
Cdd:NF041136 52 LLGLEGKRLGSEDEGILPVEYSD--NLKVMSIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 81 HMATMEALrpyrPL-GALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAG 159
Cdd:NF041136 130 PLSVAQLI----PDaGAVIVTTPQELALADVRKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMG 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822188060 160 VPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVV 203
Cdd:NF041136 206 VPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALEKIVDPIL 249
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
31-206 |
9.28e-31 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 115.53 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 31 SVGFLLEnPDEAVVWRGPKKHALIKQFVSDVAWGQLDYLVVDTPPGTSDEHMaTMEALRPYRplGALVVTTPQAVSIGDV 110
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQL-TLAQNIPVT--GAVVVTTPQDIALIDA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 111 RRELTFCKKTGLQVIGVIENMSGFTCPHCAECTNVFSSGSGEELARLAGVPFLGSVPLDSQLTRSLEEGRDFIQEFPKST 190
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPESE 337
|
170
....*....|....*.
gi 1822188060 191 AYSALTSIAQRVVHRM 206
Cdd:PRK11670 338 FTAIYRQLADRVAAQL 353
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
27-138 |
1.45e-19 |
|
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: 84.08 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 27 ISLMSVGFLLENPDEAVVwrgpkkHALIKQFVSDVAwGQLDYLVVDTPPGTSDEHMATMEALRPyrplGALVVTTPQAVS 106
Cdd:COG0489 170 LDVLPAGPLPPNPSELLA------SKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASLVD----GVLLVVRPGKTA 238
|
90 100 110
....*....|....*....|....*....|..
gi 1822188060 107 IGDVRRELTFCKKTGLQVIGVIENMsgfTCPH 138
Cdd:COG0489 239 LDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
64-205 |
4.03e-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: 65.68 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 64 GQLDYLVVDTPPGTSDEHMATMEAlrpyrplgA---LVVTTPQAVSIGDVRReltFCK----KTGLQVIGVIENMsgftc 136
Cdd:COG0455 92 RFYDVVLVDTGAGISDSVLLFLAA--------AdevVVVTTPEPTSITDAYA---LLKllrrRLGVRRAGVVVNR----- 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822188060 137 phcaectnVFSSGSGEEL-ARLAGV---------PFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRVVHR 205
Cdd:COG0455 156 --------VRSEAEARDVfERLEQVaerflgvrlRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
42-182 |
1.26e-06 |
|
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: 47.34 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 42 AVVWRGPKKHALIKQFVSDVAwGQLDYLVVDTPPGTsdeHMATMEALRPyrPLGALVVTTPQAVSIGDVRRELTFCKKTG 121
Cdd:pfam01656 95 EKELLGPRKEERLREALEALK-EDYDYVIIDGAPGL---GELLRNALIA--ADYVIIPLEPEVILVEDAKRLGGVIAALV 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822188060 122 -------LQVIGVIENMSGftcphcaectnvfSSGSGEELA-----RLAGVPFLGSVPLDSQLTRSLEEGRDF 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) ... |
53-191 |
1.69e-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: 47.18 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 53 LIKQFVSDVAwgQLDYLVVDTPPGTSDEhmaTMEALRPYRPLgaLVVTTPQAVSIGD--------VRRELTFckktglqV 124
Cdd:cd02038 100 LIEELSSLES--NYDYLLIDTGAGISRN---VLDFLLAADEV--IVVTTPEPTSITDayalikvlSRRGGKK-------N 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822188060 125 IGVIENMsgftcphcaectnVFSSGSGEELA-RLAGV---------PFLGSVPLDSQLTRSLEEGRDFIQEFPKSTA 191
Cdd:cd02038 166 FRLIVNM-------------ARSPKEGRATFeRLKKVakrfldinlDFVGFIPYDQSVRRAVRSQKPFVLLFPNSKA 229
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
67-202 |
1.85e-06 |
|
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: 46.81 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 67 DYLVVDTPPGT-SDEHMATMEALRpyrplgALVVTTPQAVSIGDVRRELTFCKKTGLQVIGVIENMSGftcPHCAEctnv 145
Cdd:cd02036 112 DFILIDSPAGIeSGFINAIAPADE------AIIVTNPEISSVRDADRVIGLLESKGIVNIGLIVNRYR---PEMVK---- 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822188060 146 fssgSGEELARLA-----GVPFLGSVPLDSQLTRSLEEGRDFIQEFPKSTAYSALTSIAQRV 202
Cdd:cd02036 179 ----SGDMLSVEDiqeilGIPLLGVIPEDPEVIVATNRGEPLVLYKPNSLAAKAFENIARRL 236
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
67-131 |
1.47e-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: 37.03 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822188060 67 DYLVVDTPPGTSDE--HMATMEALRPYRPLGALVVTTPQAVSIGDVRRELTFCK--KTGLQVIGVIENM 131
Cdd:cd01983 39 DYVLIDGGGGLETGllLGTIVALLALKKADEVIVVVDPELGSLLEAVKLLLALLllGIGIRPDGIVLNK 107
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
49-167 |
3.04e-03 |
|
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: 37.36 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822188060 49 KKHALIKQFVSDVAwgqldylVVDTPPGTsdeHMATMEALRpyrplGA---LVVTTPQAVSIGDVRRELTFCKKTGLQVi 125
Cdd:cd03110 150 RKKALERSKECDLA-------IIDGPPGT---GCPVVASIT-----GAdavLLVTEPTPSGLHDLKRAIELAKHFGIPT- 213
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1822188060 126 GVIENMSGFtcphcaectNVFSSGSGEELARLAGVPFLGSVP 167
Cdd:cd03110 214 GIVINRYDI---------NDEISEEIEDFADEEGIPLLGKIP 246
|
|
|