|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
92-342 |
1.27e-146 |
|
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: 413.77 E-value: 1.27e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 92 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 171
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 FLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDVRKE 251
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 252 ISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPA 331
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
|
250
....*....|.
gi 1147372655 332 TLAYRSVIKRI 342
Cdd:pfam10609 235 AKAFLKIADKV 245
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
94-314 |
2.54e-130 |
|
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.
Pssm-ID: 349757 [Multi-domain] Cd Length: 213 Bit Score: 371.45 E-value: 2.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 173
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLaaaHIDGAVIITTPQEVSLQDVRKEIS 253
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147372655 254 FCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGK 314
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
89-355 |
5.22e-127 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 368.76 E-value: 5.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 89 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 168
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSSPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAAahiDGAVIITTPQEVSLQDV 248
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPD---AGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFPptTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250 260
....*....|....*....|....*..
gi 1147372655 329 SPATLAYRSVIKRIQEFCSAQQSNKEN 355
Cdd:NF041136 235 SPAAKALEKIVDPILELLENKKSLTEE 261
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
90-342 |
8.48e-60 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 196.80 E-value: 8.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 90 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 168
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 169 SVGFLLSsPDDAVIWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVQYLAaahIDGAVIITTPQEVSLQDV 248
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 249 RKEISFCHKVKLPIIGVVENMSGFVCPKCKKESQIFppTTGGAEIMCQDLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPG 328
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
|
250
....*....|....
gi 1147372655 329 SPATLAYRSVIKRI 342
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
71-276 |
1.51e-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: 162.66 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 71 ASGAGAAPDPAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-- 148
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 149 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVV 223
Cdd:COG0489 149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1147372655 224 QylaaAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENMsgfVCPK 276
Cdd:COG0489 222 A----SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
96-342 |
1.03e-22 |
|
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443989 [Multi-domain] Cd Length: 358 Bit Score: 97.49 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 171
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 F-LLSSPDDAVIWR--GPKKSGMIKQFLRDvdwgDVDYLIVDTPPGTSDEHLSVvqyLAAAHIdgaVIITTPQEV-SLQD 247
Cdd:COG4963 185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 248 VRKEISFCHKVKLPI--IGVVENmsgfvcpKCKKESQIfppttgGAEIMCQDLKVPLLAKVPLDP-HIGKSCDKGQSFFV 324
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321
|
250
....*....|....*...
gi 1147372655 325 EAPGSPATLAYRSVIKRI 342
Cdd:COG4963 322 VAPKSPLAKAIRKLAARL 339
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
96-335 |
1.11e-20 |
|
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.
Pssm-ID: 131024 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQV--HQSGSGWSPVyvEDNLGVMSVGFL 173
Cdd:TIGR01969 3 ITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDKPVtlHDVLAGEADI--KDAIYEGPFGVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 LSSPddAVIWRGPKKSGMIKqfLRDV---DWGDVDYLIVDTPPGTSdehLSVVQYLAAAhiDGAVIITTPQEVSLQDVRK 250
Cdd:TIGR01969 80 VIPA--GVSLEGLRKADPDK--LEDVlkeIIDDTDFLLIDAPAGLE---RDAVTALAAA--DELLLVVNPEISSITDALK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 251 EISFCHKVKLPIIGVVENMSGfvcpkckKESQIFPPTTggAEIMcqdLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSP 330
Cdd:TIGR01969 151 TKIVAEKLGTAILGVVLNRVT-------RDKTELGREE--IETI---LEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSP 218
|
....*
gi 1147372655 331 ATLAY 335
Cdd:TIGR01969 219 AAQAF 223
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
109-342 |
2.05e-19 |
|
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: 85.71 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 109 TFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VEDNLGVmsvgFLLSSPDDAVIWR 184
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 185 GPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEVSLQD---VRKEISFCHKVKlp 261
Cdd:COG0455 76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDayaLLKLLRRRLGVR-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 262 IIGVVENMSgfvcpkckKESQIFPPTTGGAEIMCQ---DLKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSV 338
Cdd:COG0455 148 RAGVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIREL 219
|
....
gi 1147372655 339 IKRI 342
Cdd:COG0455 220 AARL 223
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
96-322 |
5.58e-19 |
|
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: 84.70 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 166
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 167 VMSVGFLLSSPD---DAVIWRGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDehlSVVQYLAAAhiDGAVIITTPQEV 243
Cdd:pfam01656 79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 244 SLQDVRKEISFCHKVK-------LPIIGVVENMSGfvcPKCKKESQIfppttggaEIMCQDL-KVPLLAKVPLDPHIGKS 315
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221
|
....*..
gi 1147372655 316 CDKGQSF 322
Cdd:pfam01656 222 PARGLPV 228
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
96-342 |
2.82e-17 |
|
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: 79.94 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 159
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 160 yveDNLGVMSVGFllSSPDDAViwrGPKKsgmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSvvqylAAAHIDGAVIITT 239
Cdd:cd02036 79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 240 PQEVSLQDVRKEISFCHKVKLPIIGVVENMsgfVCPKCKKESQIFPPttggaEIMCQDLKVPLLAKVPLDPHIGKSCDKG 319
Cdd:cd02036 142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213
|
250 260
....*....|....*....|...
gi 1147372655 320 QSFFVEAPGSPATLAYRSVIKRI 342
Cdd:cd02036 214 EPLVLYKPNSLAAKAFENIARRL 236
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
96-332 |
4.73e-17 |
|
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: 79.15 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 165
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGfllSSPDDAVIWRGPKKSGMIKQFLRDVDwgDVDYLIVDTPPGTSDehlSVVQYLAAAHIdgAVIITTPQEVSL 245
Cdd:cd02038 78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QD---VRKEISfcHKVKLPIIGVVENMSgfvcpKCKKESQifpPTTGGAEIMCQ---DLKVPLLAKVPLDPHIGKSCDKG 319
Cdd:cd02038 148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQ 217
|
250
....*....|...
gi 1147372655 320 QSFFVEAPGSPAT 332
Cdd:cd02038 218 KPFVLLFPNSKAS 230
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
89-344 |
1.28e-16 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 78.36 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 89 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQVALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 161
Cdd:COG1192 1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 162 EDNLGVMSVgfLLSSPD----DAVIWRGPKKSGMIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVvqyLAAAhiDGAVII 237
Cdd:COG1192 75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 238 TTPQEVSL----------QDVRKEisfcHKVKLPIIGVVENMsgfvcpkckkesqiFPPTTGGAEIMCQDLK----VPLL 303
Cdd:COG1192 147 VQPEYLSLeglaqlletiEEVRED----LNPKLEILGILLTM--------------VDPRTRLSREVLEELReefgDKVL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1147372655 304 -AKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRIQE 344
Cdd:COG1192 209 dTVIPRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
96-338 |
9.46e-14 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 70.00 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 171
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 172 F-LLSSP---DDAVIWRGPKKSGMIkQFLRdvdwGDVDYLIVDTPPgtsdeHLSVVQYLAAAHIDGAVIITTPQEVSLQD 247
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 248 VRKEISFCHKVKLPI--IGVVENmsgfvcpKCKKESQIFPPTTGGAeimcqdLKVPLLAKVPLDPH-IGKSCDKGQSFFV 324
Cdd:cd03111 153 ARRLLDSLRELEGSSdrLRLVLN-------RYDKKSEISPKDIEEA------LGLEVFATLPNDYKaVSESANTGRPLVE 219
|
250
....*....|....
gi 1147372655 325 EAPGSPATLAYRSV 338
Cdd:cd03111 220 VAPRSALVRALQDL 233
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
95-344 |
7.12e-13 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 67.50 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 95 KILVlSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMGLEGEQvhqsgSGWSPV-----YVEDNLGVMS 169
Cdd:COG3640 2 KIAV-AGKGGVGKTTLSALLARYLAE-KGKPVLAVDADP-NANLAEALGLEVEA-----DLIKPLgemreLIKERTGAPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 170 VGFLLSSP------DDAVIWRG---------PKKSG---------MIKQFLRDVDWGDVDYLIVDTPPGTsdEHLSvvqY 225
Cdd:COG3640 74 GGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEGGsgcycpenaLLRALLNHLVLGNYEYVVVDMEAGI--EHLG---R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 226 LAAAHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENmsgfvcpKCKKESQIfppttggaEIMCQDLKVPLLAK 305
Cdd:COG3640 149 GTAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGF 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 1147372655 306 VPLDPHIGKSCDKGQSFFvEAPGSPAtlayRSVIKRIQE 344
Cdd:COG3640 214 IPYDEEVREADLEGKPLL-DLPDSPA----VAAVEEIAE 247
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
96-343 |
7.86e-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: 67.75 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 165
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGPKKsgMIKQFLRdvdwgDVDYLIVDTPPGtsdehLSVVQYLAAAHIDGAVIITTPQEVSL 245
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QDVRKeisfchkvklpIIGVVENMSgfvcpkCKKESQIF----PPTTGGAEIMCQD-----LKVPLLAKVPLDPHIGKSC 316
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKG------IEKIHLIVnrlrPEMVKKGDMLSVDdvleiLSIPLIGVIPEDEAIIVST 211
|
250 260
....*....|....*....|....*..
gi 1147372655 317 DKGQSFFVEaPGSPATLAYRSVIKRIQ 343
Cdd:TIGR01968 212 NKGEPVVLN-DKSRAGKAFENIARRIL 237
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
94-268 |
2.29e-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: 64.90 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 166
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 167 VMSVGFLLSSPDDAViwRGPKKSGMIKQFLRDVDwgdvdYLIVDTPP--GTSDEHLsvvqylAAAHIDGAVIITTPQEVS 244
Cdd:cd05387 99 VLPAGTVPPNPSELL--SSPRFAELLEELKEQYD-----YVIIDTPPvlAVADALI------LAPLVDGVLLVVRAGKTR 165
|
170 180
....*....|....*....|....
gi 1147372655 245 LQDVRKEISFCHKVKLPIIGVVEN 268
Cdd:cd05387 166 RREVKEALERLEQAGAKVLGVVLN 189
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
96-342 |
4.18e-11 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 62.65 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 165
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGpkksgmIKQFLRDVDWGDVDYLIVDTPPGTSDEHLSVVqYLAaahiDGAVIITTPQEVSL 245
Cdd:PRK10818 84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 246 QDVRKeisfchkvklpIIGVVENMS--GFVCPKCKKESQIFPPTTGG---------AEIMCQDLKVPLLAKVPLDPHIGK 314
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219
|
250 260
....*....|....*....|....*...
gi 1147372655 315 SCDKGQSFFVEAPgSPATLAYRSVIKRI 342
Cdd:PRK10818 220 ASNQGEPVILDIE-ADAGKAYADTVDRL 246
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
96-343 |
1.68e-10 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 60.84 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDICGPSIPKIMGLE------------GE-QVHQSgsgwspvYVE 162
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 163 D----NLgvmsvgFLLssP-----D-DAViwrgpKKSGMIK--QFLRDvdwgDVDYLIVDTPPGTsdEHLSvvqYLAAAH 230
Cdd:COG2894 77 DkrfeNL------YLL--PasqtrDkDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 231 IDGAVIITTPQEVSLQDV-RkeisfchkvklpIIGVVENMSgfvcpkcKKESQI----FPPT---TGG---AEIMCQDLK 299
Cdd:COG2894 135 ADEAIVVTTPEVSSVRDAdR------------IIGLLEAKG-------IRKPHLiinrYRPAmvkRGDmlsVEDVLEILA 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1147372655 300 VPLLAKVPLDPHIGKSCDKGQSfFVEAPGSPATLAYRSVIKRIQ 343
Cdd:COG2894 196 IPLLGVVPEDEEVIVSSNRGEP-VVLDEKSKAGQAYRNIARRLL 238
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
95-307 |
6.32e-09 |
|
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: 55.85 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 95 KILVLSGKGGVGKSTFSAHLAHGLAEdentqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED----------- 163
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 164 -NLGVMSVGF----------------LLSSPDDAVIWR------------------------GPKKSGMIKQFLR---DV 199
Cdd:cd03110 76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLKdrdtgkifisssdggplvhgrlniGEENSGKLVTELRkkaLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 200 DWGDVDYLIVDTPPGTsdeHLSVVQYLAAAhiDGAVIITTPQEVSLQDVRKEISFCHKVKLPiIGVVENMSGfvcpkckk 279
Cdd:cd03110 156 RSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD-------- 221
|
250 260
....*....|....*....|....*...
gi 1147372655 280 esqIFPPTTGGAEIMCQDLKVPLLAKVP 307
Cdd:cd03110 222 ---INDEISEEIEDFADEEGIPLLGKIP 246
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
94-269 |
1.26e-08 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 52.93 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 94 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 173
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 174 lsspdDAVIWRgpkksgmikqflrdvdwgdVDYLIVDTPPGTSDEHLSVvqyLAAAHIdgaVII-TTPQEVSLQDVRKEI 252
Cdd:cd02042 42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLL 91
|
170 180
....*....|....*....|...
gi 1147372655 253 SFCHKVK------LPIIGVVENM 269
Cdd:cd02042 92 DTLEELKkqlnppLLILGILLTR 114
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
96-237 |
7.62e-08 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 52.17 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 96 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 175
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147372655 176 SPDdaviwrgpkksgmIKQFLRDVDwGDVDYLIVDTPPGTSDEHLSVVQylaAAHIdgaVII 237
Cdd:NF041546 62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK---AADL---VLI 103
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
95-323 |
1.72e-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: 51.54 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 95 KILVlSGKGGVGKSTFSAHLAHGLAEDENTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 170
Cdd:cd02034 2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 171 GFLLSSPDDAVIWRG--------------PKKSG---------MIKQFLRDVDWGDVDYLIVDTPPGTsdEHLS--VVQy 225
Cdd:cd02034 76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGGGsgcycpvnaLLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 226 laaaHIDGAVIITTPQEVSLQDVRKEISFCHKVKLPIIGVVENmsgfvcpKCKKESQIfppttggAEIMCQDLKVPLLAK 305
Cdd:cd02034 153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVN-------KVRNEEEQ-------ELIEELLIKLKLIGV 214
|
250
....*....|....*...
gi 1147372655 306 VPLDPHIGKSCDKGQSFF 323
Cdd:cd02034 215 IPYDEEIMEADLKGKPLF 232
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
83-342 |
3.75e-07 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 50.92 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 83 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 162
Cdd:CHL00175 5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 163 dnLGVMSVGFLLsspDDAVI----WRG----------------PKKSGMIKQFLRDVDWgdvDYLIVDTPPGtsdehLSV 222
Cdd:CHL00175 74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvtRKNMNMLVDSLKNRGY---DYILIDCPAG-----IDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 223 VQYLAAAHIDGAVIITTPQEVSLQDVRK-----EISFCHKVKLPIIGVVENMsgfvcpkCKKESQIfpPTTGGAEImcqd 297
Cdd:CHL00175 141 GFINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM--SVRDVQEM---- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1147372655 298 LKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRI 342
Cdd:CHL00175 208 LGIPLLGAIPEDENVIISTNRGEPLVLNKKLTLSGIAFENAARRL 252
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
95-132 |
1.11e-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: 43.96 E-value: 1.11e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1147372655 95 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDID 132
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
94-213 |
4.02e-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: 44.65 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 94 HKILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDIDIcGPSIPKIMGLEgeqvhqsgSGWSPVYVEDNLGVMSV--- 170
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSE-LGKKVLLISTDP-AHSLSDSFNQK--------FGHEPTKVKENLSAMEIdpn 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1147372655 171 ----------------GFLLSSPDDAV-----IWRGPKKSGMIKQFLRDVDWGDVDYLIVDTPP 213
Cdd:pfam02374 71 meleeywqevqkymnaLLGLRMLEGILaeelaSLPGIDEAASFDEFKKYMDEGEYDVVVFDTAP 134
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
95-213 |
4.52e-04 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 41.73 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 95 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQVALLDIDIcGPSIPKIMGLEGeqvhqsgsGWSPVYVE-DNLGVMSVgfl 173
Cdd:COG0003 4 RIIFFTGKGGVGKTTVAAATALALAER-GKRTLLVSTDP-AHSLGDVLGTEL--------GNEPTEVAvPNLYALEI--- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147372655 174 lsSPDDAV--IWRGPKK------------------SGM--------IKQFLRDVDWgdvDYLIVDTPP 213
Cdd:COG0003 71 --DPEAELeeYWERVRAplrgllpsagvdelaeslPGTeelaaldeLLELLEEGEY---DVIVVDTAP 133
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
95-343 |
1.74e-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: 39.66 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 95 KILVLSGKGGVGKSTFSAHLAHGLAEdENTQVALLDID--------ICGPSIPK-IMGLEGEQVHQSGSGWSPVYVEDNL 165
Cdd:cd02117 1 ESIVVYGKGGIGKSTTASNLSAALAE-GGKKVLHVGCDpkhdstllLTGGKVPPtIDEMLTEDGTAEELRREDLLFSGFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 166 GVMSVGflLSSPDDAVIWRGPKKSGMIKqFLRDV---DW----------GDV---------------DYLIVdtppgTSD 217
Cdd:cd02117 80 GVDCVE--AGGPEPGVGCGGRGIGTMLE-LLEEHgllDDdydvvifdvlGDVvcggfaaplrrgfaqKVVIV-----VSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147372655 218 EHLSVvqyLAAAHIDGAViittpQEVSLQDVRkeisfchkvklpIIGVVENMSGfvcpkckkesqifPPTTGGAEIMCQD 297
Cdd:cd02117 152 ELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAFAAA 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1147372655 298 LKVPLLAKVPLDPHIGKSCDKGQSFFVEAPGSPATLAYRSVIKRIQ 343
Cdd:cd02117 199 VGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFARLAAKIA 244
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
82-120 |
2.04e-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: 2.04e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1147372655 82 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 120
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
93-131 |
2.71e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.79 E-value: 2.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1147372655 93 KHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQVALLDI 131
Cdd:COG5635 179 KKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPI 217
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
95-120 |
3.46e-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: 3.46e-03
10 20
....*....|....*....|....*.
gi 1147372655 95 KILVLSGKGGVGKSTFSAHLAHGLAE 120
Cdd:cd02035 1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
94-132 |
7.21e-03 |
|
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.
Pssm-ID: 401181 [Multi-domain] Cd Length: 262 Bit Score: 37.82 E-value: 7.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1147372655 94 HKILVLSGKGGVGKSTFSAHLAHGLAeDENTQVALLDID 132
Cdd:pfam09140 1 HVIVVGNEKGGSGKSTTAVHVAVALL-YKGARVAAIDLD 38
|
|
|