|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-292 |
4.96e-139 |
|
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: 392.59 E-value: 4.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-YVED---------NLGVMSVGF 122
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERpEQSDggiipveahGIKVMSIGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 123 LLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKEI 202
Cdd:pfam10609 81 LLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 203 NFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPAT 282
Cdd:pfam10609 158 DMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAA 235
|
250
....*....|
gi 511772980 283 LAYRSIIQRI 292
Cdd:pfam10609 236 KAFLKIADKV 245
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
50-304 |
1.53e-122 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 355.28 E-value: 1.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQY-----------VEDNLGVM 118
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLgsedegilpveYSDNLKVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 119 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 198
Cdd:NF041136 80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIP---DAGAVIVTTPQELALADV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 199 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPD 278
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234
|
250 260
....*....|....*....|....*.
gi 511772980 279 SPATLAYRSIIQRIQefcNLHQSKEE 304
Cdd:NF041136 235 SPAAKALEKIVDPIL---ELLENKKS 257
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
55-264 |
2.20e-121 |
|
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: 346.80 E-value: 2.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQYVE----------DNLGVMSVGFLL 124
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQseegivpvevGGIKVMSIGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 125 SsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLataHIDGAVIITTPQEVSLQDVRKEINF 204
Cdd:cd02037 80 P-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAIDM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 205 CRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGK 264
Cdd:cd02037 156 CKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-292 |
1.28e-59 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 194.88 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQYVE-DN----------LGVMS 119
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRPTSpDGthmapimahgLATNS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 120 VGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVR 199
Cdd:PRK11670 183 IGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 200 KEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDS 279
Cdd:PRK11670 259 KGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPES 336
|
250
....*....|...
gi 511772980 280 PATLAYRSIIQRI 292
Cdd:PRK11670 337 EFTAIYRQLADRV 349
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
32-226 |
2.51e-44 |
|
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: 152.65 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 32 ASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGE--- 108
Cdd:COG0489 70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRpgl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 109 ---------------QYVEDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVV 173
Cdd:COG0489 149 sdvlageasledviqPTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 511772980 174 rylaTAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMsgfICPK 226
Cdd:COG0489 222 ----ASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
57-292 |
7.16e-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: 94.03 E-value: 7.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQYVED---NLGVMSVGFL---------- 123
Cdd:COG4963 105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRGLADalrNPDRLDETLLdraltrhssg 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 124 ---LSSPDDAVIWR--GPKKNGMIKQFLRDvdwgEVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVIITTPQEV-SLQD 197
Cdd:COG4963 185 lsvLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 198 VRKEINFCRKVKLPI--IGVVENmsgficpKCKKESQIfppttgGAELMCQDLEVPLLGRVPLDP-LIGKNCDKGQSFFI 274
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321
|
250
....*....|....*...
gi 511772980 275 DAPDSPATLAYRSIIQRI 292
Cdd:COG4963 322 VAPKSPLAKAIRKLAARL 339
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
70-292 |
2.53e-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: 84.94 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 70 TFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLE----------GEQYVEDNLGVMSVGF-LLSSPDDAVIWRGPKK 138
Cdd:COG0455 1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEpkatladvlaGEADLEDAIVQGPGGLdVLPGGSGPAELAELDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 139 NGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCR-KVKLPIIGVVE 217
Cdd:COG0455 80 EERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDAYALLKLLRrRLGVRRAGVVV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511772980 218 NMSgficpkckKESQIFPPTTGGAELMCQ---DLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPATLAYRSIIQRI 292
Cdd:COG0455 154 NRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARL 223
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
57-292 |
1.57e-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: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLE------------GEQYVED---------NL 115
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLEnrivytlvdvleGECRLEQalikdkrweNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 116 GVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSvvrylATAHIDGAVIITTPQEVSL 195
Cdd:cd02036 82 YLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTNPEISSV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 196 QDVRKeinfcrkvklpIIGVVENMS----GFICPKCKKESqifppTTGGAELMCQD----LEVPLLGRVPLDPLIGKNCD 267
Cdd:cd02036 148 RDADR-----------VIGLLESKGivniGLIVNRYRPEM-----VKSGDMLSVEDiqeiLGIPLLGVIPEDPEVIVATN 211
|
250 260
....*....|....*....|....*
gi 511772980 268 KGQSFFIDAPDSPATLAYRSIIQRI 292
Cdd:cd02036 212 RGEPLVLYKPNSLAAKAFENIARRL 236
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
57-272 |
2.99e-17 |
|
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: 78.93 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDIcGPSIPKIMGLEG-------------------------EQYV 111
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGdiapalqalaeglkgrvnldpillkEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 112 EDNLGVMSVGFLLSspDDAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQ 191
Cdd:pfam01656 79 EGGLDLIPGNIDLE--KFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 192 EVSLQDVRKEINFCRKVK-------LPIIGVVENMsgficpkckkesqiFPPTTGGAELMcQDLE-----VPLLGRVPLD 259
Cdd:pfam01656 151 VILVEDAKRLGGVIAALVggyallgLKIIGVVLNK--------------VDGDNHGKLLK-EALEellrgLPVLGVIPRD 215
|
250
....*....|...
gi 511772980 260 PLIGKNCDKGQSF 272
Cdd:pfam01656 216 EAVAEAPARGLPV 228
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
57-282 |
1.80e-16 |
|
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: 76.84 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLD-------IDIC-GPSIPKIMG--LEGEQYVEDNLGVMSVGFLL-- 124
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGRVSLEDIIVEGPEGLDIip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 125 --SSPDDAVIWRGPKKNGMIKQFLRDVDwgEVDYLIVDTPPGTSDEhlsvVRYLATAhIDGAVIITTPQEVSLQD---VR 199
Cdd:cd02038 82 ggSGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN----VLDFLLA-ADEVIVVTTPEPTSITDayaLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 200 KEINfcRKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAELMCQ---DLEVPLLGRVPLDPLIGKNCDKGQSFFIDA 276
Cdd:cd02038 155 KVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQKPFVLLF 224
|
....*.
gi 511772980 277 PDSPAT 282
Cdd:cd02038 225 PNSKAS 230
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
56-292 |
7.28e-16 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 75.59 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDIcGPSIPKIMGLEGE-----------QYVEDNLGVMSVGFLL 124
Cdd:COG3640 2 KIAV-AGKGGVGKTTLSALLARYLAEKGKPVLA-VDADP-NANLAEALGLEVEadlikplgemrELIKERTGAPGGGMFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 125 SSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLSvvRYLATaH 180
Cdd:COG3640 79 LNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG--RGTAE-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 181 IDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENmsgficpKCKKESQIfppttggaELMCQDLEVPLLGRVPLDP 260
Cdd:COG3640 154 VDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLGFIPYDE 218
|
250 260 270
....*....|....*....|....*....|..
gi 511772980 261 LIGKNCDKGQSFFiDAPDSPATLAYRSIIQRI 292
Cdd:COG3640 219 EVREADLEGKPLL-DLPDSPAVAAVEEIAEKL 249
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
57-293 |
1.40e-12 |
|
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: 66.59 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEgEQYVEDNLGVMS----------------- 119
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLE-NRIVYTLVDVVEgecrlqqalikdkrlkn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 120 VGFLLSSPD---DAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSLQ 196
Cdd:TIGR01968 82 LYLLPASQTrdkDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 197 DVRKeinfcrkvklpIIGVVENMSgfICPKCKKESQIFPPTTGGAELMCQD-----LEVPLLGRVPLDPLIGKNCDKGQS 271
Cdd:TIGR01968 150 DADR-----------VIGLLEAKG--IEKIHLIVNRLRPEMVKKGDMLSVDdvleiLSIPLIGVIPEDEAIIVSTNKGEP 216
|
250 260
....*....|....*....|..
gi 511772980 272 FFIDaPDSPATLAYRSIIQRIQ 293
Cdd:TIGR01968 217 VVLN-DKSRAGKAFENIARRIL 237
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
55-218 |
2.18e-11 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 61.82 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDICGPSIPKIMGLEGEQYVED------------------NLG 116
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPGLSEvlsgqasledviqstnipNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 117 VMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgEVDYLIVDTPP--GTSDEHLsvvryLATaHIDGAVIITTPQEVS 194
Cdd:cd05387 99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADALI-----LAP-LVDGVLLVVRAGKTR 165
|
170 180
....*....|....*....|....
gi 511772980 195 LQDVRKEINFCRKVKLPIIGVVEN 218
Cdd:cd05387 166 RREVKEALERLEQAGAKVLGVVLN 189
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
57-292 |
4.32e-11 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 62.26 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEgEQYVEDNLGVMSVGFLLSSP--------- 127
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCE-RRVVYDFVNVIQGDATLNQAlikdkrten 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 128 -----------DDAVIWRGpkkngmIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVrYLAtahiDGAVIITTPQEVSLQ 196
Cdd:PRK10818 83 lyilpasqtrdKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 197 DVRKeinfcrkvklpIIGVVENmsgficpKCKKESQIFPP--------------TTGGAELMCQD----LEVPLLGRVPL 258
Cdd:PRK10818 152 DSDR-----------ILGILAS-------KSRRAENGEEPikehllltrynpgrVSRGDMLSMEDvleiLRIKLVGVIPE 213
|
250 260 270
....*....|....*....|....*....|....
gi 511772980 259 DPLIGKNCDKGQSFFIDApDSPATLAYRSIIQRI 292
Cdd:PRK10818 214 DQSVLRASNQGEPVILDI-EADAGKAYADTVDRL 246
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
50-294 |
6.08e-11 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 61.41 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 50 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDID-------ICGPSIPKIMG-----LEGEQYVEDNLGV 117
Cdd:COG1192 1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDpqgnltsGLGLDPDDLDPtlydlLLDDAPLEDAIVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 118 MSVG---FLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVvryLATAhiDGAVIITTP 190
Cdd:COG1192 76 TEIPgldLIPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIPVQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 191 QEVSL----------QDVRKEINfcrkVKLPIIGVVENMSGficPKCKKESQIfppttggAELMCQDLEVPLLG-RVPLD 259
Cdd:COG1192 150 EYLSLeglaqlletiEEVREDLN----PKLEILGILLTMVD---PRTRLSREV-------LEELREEFGDKVLDtVIPRS 215
|
250 260 270
....*....|....*....|....*....|....*
gi 511772980 260 PLIGKNCDKGQSFFIDAPDSPATLAYRSIIQRIQE 294
Cdd:COG1192 216 VALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
57-293 |
8.31e-11 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 61.23 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLE------------GEQYVE---------DNL 115
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGECRLKqalikdkrfENL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 116 gvmsvgFLL----SSPDDAViwrgpKKNGMIK--QFLRDvdwgEVDYLIVDTPPGTsdEHLSvvrYLATAHIDGAVIITT 189
Cdd:COG2894 84 ------YLLpasqTRDKDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIAGADEAIVVTT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 190 PQEVSLQDV-RkeinfcrkvklpIIGVVENMSgficpkcKKESQI----FPPT---TGG---AELMCQDLEVPLLGRVPL 258
Cdd:COG2894 144 PEVSSVRDAdR------------IIGLLEAKG-------IRKPHLiinrYRPAmvkRGDmlsVEDVLEILAIPLLGVVPE 204
|
250 260 270
....*....|....*....|....*....|....*
gi 511772980 259 DPLIGKNCDKGQSFFIDaPDSPATLAYRSIIQRIQ 293
Cdd:COG2894 205 DEEVIVSSNRGEPVVLD-EKSKAGQAYRNIARRLL 238
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
57-288 |
5.14e-10 |
|
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: 58.44 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQYVEDNLGVM---------------SVG 121
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYDLADVIQNLdrldrtlldsavtrhSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 122 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGEVDYLIVDTPPGTSDEHLSVVRylataHIDGAVIITTPQEVSLQD 197
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGHFLDEVTLAVLE-----AADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 198 VRKEINFCRKVKLPI--IGVVENmsgficpKCKKESQIFPPTTGGAelmcqdLEVPLLGRVPLDP-LIGKNCDKGQSFFI 274
Cdd:cd03111 153 ARRLLDSLRELEGSSdrLRLVLN-------RYDKKSEISPKDIEEA------LGLEVFATLPNDYkAVSESANTGRPLVE 219
|
250
....*....|....
gi 511772980 275 DAPDSPATLAYRSI 288
Cdd:cd03111 220 VAPRSALVRALQDL 233
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
56-292 |
4.73e-09 |
|
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: 55.78 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDiCGPSIPKIMGLEGEQY--------VEDNLG----VMSVGFL 123
Cdd:cd02034 2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLA-VDAD-PNSNLAETLGVEVEKLpliktigdIRERTGakkgEPPEGMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 124 LSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLS--VVRylat 178
Cdd:cd02034 79 LNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 179 aHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSgficPKCKKESQIfppttggAELMCQDlevPLLGRVPL 258
Cdd:cd02034 153 -AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----RNEEEQELI-------EELLIKL---KLIGVIPY 217
|
250 260 270
....*....|....*....|....*....|....
gi 511772980 259 DPLIGKNCDKGQSFFIDapDSPATLAYRSIIQRI 292
Cdd:cd02034 218 DEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
55-219 |
2.85e-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: 51.39 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsipkimglegEQYvednlgvmsvgfllsspdDAVIWR 134
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD--------------PQG------------------SLTSWL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 135 gpkkngmikqflrdvdwgeVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVII-TTPQEVSLQDVRKEINFCRKVK---- 209
Cdd:cd02042 48 -------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLLDTLEELKkqln 102
|
170
....*....|..
gi 511772980 210 --LPIIGVVENM 219
Cdd:cd02042 103 ppLLILGILLTR 114
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
56-257 |
4.84e-08 |
|
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: 52.77 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVLSGKGGVGKSTFSAHLAHGLAEdentqIALLDIDICGPSIPKIMGLEGEQyVEDNLGVM----------SVG---- 121
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEE-EEDFVGGKkafidqekciRCGncer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 122 ------------------FL--------LSSPDDAVIWRgPKKNGMIKQFLRD--------------------------- 148
Cdd:cd03110 75 vckfgaileffqklivdeSLcegcgacvIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkka 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 149 -VDWGEVDYLIVDTPPGTsdeHLSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCRKVKLPiIGVVENMSGficpkc 227
Cdd:cd03110 154 lERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------ 221
|
250 260 270
....*....|....*....|....*....|
gi 511772980 228 kkesqIFPPTTGGAELMCQDLEVPLLGRVP 257
Cdd:cd03110 222 -----INDEISEEIEDFADEEGIPLLGKIP 246
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
44-295 |
7.13e-08 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 52.85 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 44 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQIALLDIDICGPSIPKIMGLEgEQYVEDNLGVMSVGFL 123
Cdd:CHL00175 5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLE-NRVLYTAMDVLEGECR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 124 LsspDDAVI----WRG---------------PKKN-GMIKQFLRDVDWgevDYLIVDTPPGtsdehLSVVRYLATAHIDG 183
Cdd:CHL00175 83 L---DQALIrdkrWKNlsllaisknrqrynvTRKNmNMLVDSLKNRGY---DYILIDCPAG-----IDVGFINAIAPAQE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 184 AVIITTPQEVSLQDVRK-----EINFCRKVKLPIIGVVENMsgficpkCKKESQIFPPTTGGAelmcqdLEVPLLGRVPL 258
Cdd:CHL00175 152 AIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMMSVRDVQEM------LGIPLLGAIPE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511772980 259 DPLIGKNCDKG--------------------------QSFFIDApDSPatlaYRSIIQRIQEF 295
Cdd:CHL00175 219 DENVIISTNRGeplvlnkkltlsgiafenaarrlvgkQDYFIDL-DSP----SKGPLKRLQKF 276
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
57-93 |
1.34e-06 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 47.93 E-value: 1.34e-06
10 20 30
....*....|....*....|....*....|....*..
gi 511772980 57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDID 93
Cdd:NF041546 2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD 37
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
56-219 |
2.98e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 42.42 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQIALLDIDicgpsipkimglegeqyvednlgvmsvgfllsspddaviwrg 135
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 136 pkkngmikqflrdvdwgevDYLIVDTPPGTSDE--HLSVVRYLATAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPI- 212
Cdd:cd01983 39 -------------------DYVLIDGGGGLETGllLGTIVALLALKKADEVIVVVDPELGSLLEAVKLLLALLLLGIGIr 99
|
....*...
gi 511772980 213 -IGVVENM 219
Cdd:cd01983 100 pDGIVLNK 107
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
55-163 |
1.19e-04 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 43.11 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 55 HKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDIcGPSIPKIMGLE---GEQYVEDNLGVMSVG---------- 121
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSE-LGKKVLLISTDP-AHSLSDSFNQKfghEPTKVKENLSAMEIDpnmeleeywq 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511772980 122 ---------------------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGEVDYLIVDTPP 163
Cdd:pfam02374 79 evqkymnallglrmlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
56-163 |
4.23e-04 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 41.34 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVLSGKGGVGKSTFSAHLAHGLAEDEN------TQIA-----LLDIDIcGPSIPKI-----------MGLEGEQYVED 113
Cdd:COG0003 4 RIIFFTGKGGVGKTTVAAATALALAERGKrtllvsTDPAhslgdVLGTEL-GNEPTEVavpnlyaleidPEAELEEYWER 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 511772980 114 NLGVMSvGFLLSSPDDAVIWRGPkknGM--------IKQFLRDVDWgevDYLIVDTPP 163
Cdd:COG0003 83 VRAPLR-GLLPSAGVDELAESLP---GTeelaaldeLLELLEEGEY---DVIVVDTAP 133
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
56-245 |
1.20e-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: 39.80 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 56 KILVLSGKGGVGKSTFSAHLAHGLAEDEN------TQIA-----LLDIDIcGPSIP-----------------------K 101
Cdd:cd02035 1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKrvllvsTDPAhslsdAFGQKL-GGETPvkgapnlwameidpeealeeyweE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 102 IMGLEGEQYVEDNLGVMSVGFLLSSP--DDAViwrgpkkngMIKQFLRDVDWGEVDYLIVDTPPgtsDEH----LS---- 171
Cdd:cd02035 80 VKELLAQYLRLPGLDEVYAEELLSLPgmDEAA---------AFDELREYVESGEYDVIVFDTAP---TGHtlrlLSlple 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511772980 172 -VVRYLATAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENmsgficpkckkesQIFPPTTGGAELMC 245
Cdd:cd02035 148 qVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN-------------QVLPEEADDSFFLR 209
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
43-81 |
1.56e-03 |
|
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).
Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 40.07 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*....
gi 511772980 43 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
54-83 |
2.28e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.79 E-value: 2.28e-03
10 20 30
....*....|....*....|....*....|
gi 511772980 54 KHKILVLSGKGGVGKSTFSAHLAHGLAEDE 83
Cdd:COG5635 179 KKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
56-81 |
2.53e-03 |
|
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction
Pssm-ID: 349761 Cd Length: 266 Bit Score: 38.89 E-value: 2.53e-03
10 20
....*....|....*....|....*.
gi 511772980 56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02117 1 ESIVVYGKGGIGKSTTASNLSAALAE 26
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
63-212 |
3.26e-03 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 37.95 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 63 KGGVGKSTFSAHLAHGLAE------------DENTQIAL-LDIDICGPSIPKIMGLEGE------QYVEDNLGVMSVGFL 123
Cdd:pfam13614 10 KGGVGKTTTSVNLAAALAKkgkkvllidldpQGNATSGLgIDKNNVEKTIYELLIGECNieeaiiKTVIENLDLIPSNID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511772980 124 LSSPDDAVIWRGPKKNgMIKQFLRDVDwGEVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSLQDVRKEIN 203
Cdd:pfam13614 90 LAGAEIELIGIENREN-ILKEALEPVK-DNYDYIIIDCPPS-----LGLLTINALTASDSVLIPVQCEYYALEGLSQLLN 162
|
....*....
gi 511772980 204 FCRKVKLPI 212
Cdd:pfam13614 163 TIKLVKKRL 171
|
|
| |
