|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
53-303 |
2.00e-149 |
|
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: 419.55 E-value: 2.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 53 VKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609 2 VKHVIAVASGKGGVGKSTVAVNLALALARLGY-KVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDVRKE 212
Cdd:pfam10609 80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 213 ISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234
|
250
....*....|.
gi 524969539 293 TAAYRSIIHRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
55-275 |
3.60e-131 |
|
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: 371.83 E-value: 3.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKG-YKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLaaaHIDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02037 79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 524969539 215 FCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGK 275
Cdd:cd02037 155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| Mrp |
COG0489 |
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell ... |
9-277 |
5.46e-74 |
|
Chromosome partitioning ATPase, Mrp family, contains Fe-S cluster [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 223563 [Multi-domain] Cd Length: 265 Bit Score: 228.84 E-value: 5.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 9 PGIDSAQAGRGASCQGCPNQrLCASGAGAAPDPAVEEIKEKM---KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGDt 85
Cdd:COG0489 10 PFASSSEEIPELLAKALAAL-LPKSTASEALRALRTNLKFAKvlrKGVKNVIAVTSGKGGVGKSTVAVNLAAALAQLGK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 86 QVALLDIDICGPSIPKIMGLEGEQVHQ---SGSGWSPVYVEDNLGVMSVGFLLSSPddaVIWRGPKKNGMIKQFLRDVDW 162
Cdd:COG0489 88 RVLLLDADLRGPSIPRMLGLENLPGLTellAGEALEPVIQHDGIKVLSILPLGPVP---VIPRGLLGSKAMLQLLEDVLW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 163 GDVDYLIIDTPPGTSDEHLSVVQYLAaahiDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKes 242
Cdd:COG0489 165 GEYDYVIIDTPPGTGDADATVLQRIP----DGVVIVTTPGKTALEDVKKAIDMLEKAGIPVLGVVENMSYFICPRCGE-- 238
|
250 260 270
....*....|....*....|....*....|....*
gi 524969539 243 qifppttGGAEAMCQDLKiPLLGRVPLDPLIGKSC 277
Cdd:COG0489 239 -------GGGEKYAERYG-PYLGSIPLDPSAREAS 265
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
51-303 |
1.04e-63 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 205.66 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 51 KTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEG-AKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVQYLAaahIDGAVILTTPQEVALQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 210 RKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335
|
250
....*....|....
gi 524969539 290 SPATAAYRSIIHRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
57-283 |
1.53e-20 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 88.17 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 127
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRG-LRVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGDVDYLIIDTPPGTSDehlSVVQYLAAAhiDGAVILTTPQEV 204
Cdd:pfam01656 79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 205 ALQDVRKEISFCHKVK-------LPIIGVVENMSGficPKCKKESQIfppttggaEAMCQDL-KIPLLGRVPLDPLIGKS 276
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNKVD---GDNHGKLLK--------EALEELLrGLPVLGVIPRDEAVAEA 221
|
....*..
gi 524969539 277 CDKGQSF 283
Cdd:pfam01656 222 PARGLPV 228
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
57-303 |
1.35e-19 |
|
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: 85.72 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 120
Cdd:cd02036 3 IVITSGKGGVGKTTTTANLGVALAKLGK-KVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 121 yveDNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGDVDYLIIDTPPGTSDEHLSvvqylAAAHIDGAVILTT 200
Cdd:cd02036 79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 201 PQEVALQDVRKEISFCHKVKLPIIGVVENMsgfICPKCKKESQIFPPttggaEAMCQDLKIPLLGRVPLDPLIGKSCDKG 280
Cdd:cd02036 142 PEISSVRDADRVIGLLESKGIVNIGLIVNR---YRPEMVKSGDMLSV-----EDIQEILGIPLLGVIPEDPEVIVATNRG 213
|
250 260
....*....|....*....|...
gi 524969539 281 QSFFVEAPDSPATAAYRSIIHRI 303
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) ... |
57-293 |
1.37e-19 |
|
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: 85.70 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 126
Cdd:cd02038 3 IAVTSGKGGVGKTNVSANLALALSKLGKR-VLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgDVDYLIIDTPPGTSDehlSVVQYLAAAHIdgAVILTTPQEVAL 206
Cdd:cd02038 78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISR---NVLDFLLAADE--VIVVTTPEPTSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 207 QD---VRKEISfcHKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAEAMCQ---DLKIPLLGRVPLDPLIGKSCDKG 280
Cdd:cd02038 148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQ 217
|
250
....*....|...
gi 524969539 281 QSFFVEAPDSPAT 293
Cdd:cd02038 218 KPFVLLFPNSKAS 230
|
|
| FlhG |
COG0455 |
MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, ... |
55-321 |
2.73e-19 |
|
MinD-like ATPase involved in chromosome partitioning or flagellar assembly [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 223531 [Multi-domain] Cd Length: 262 Bit Score: 85.40 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGE--QVHQSGSGWSP------VYVEDNL 126
Cdd:COG0455 3 KVIAVVSGKGGVGKTTITANLGAALAALGGKVVLLIDADLGLGNLSLLLGVESKptTLHDVLAGEASiediiyETPQDGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVG-----FLLSSPDDaviwrgpkKNGMIKQFLRDVDwgdvdYLIIDTPPGTSDEhlsVVQYLAAAhiDGAVILTTP 201
Cdd:COG0455 83 YVLPGGsgledLAKLDPED--------LEDVIKELEELYD-----YILIDTGAGLSRD---TLSFILSS--DELVIVTTP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 202 QEVALQDVRK--EISFCHKVKLPIIGVVENMSgficpkckkeSQIFPPTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDK 279
Cdd:COG0455 145 EPTSITDAYKtiKILSKLGLDLLGRRVVLNRV----------RSTKEGVDVAALLIQVVKQVPVLQVIPFDPEVRRALAE 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 524969539 280 GQSFFVEAPDSPATAAYRSIIHRIQEFCSSHPSLKGTEPSAT 321
Cdd:COG0455 215 GKPIVLYSPNSKASQAIKELAAKLAGLPEPKAPRRGFISKIK 256
|
|
| MinD |
COG2894 |
Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, ... |
57-304 |
9.47e-17 |
|
Septum formation inhibitor-activating ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225447 [Multi-domain] Cd Length: 272 Bit Score: 78.43 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:COG2894 5 IVVTSGKGGVGKTTTTANIGTALAQLGK-KVVLIDFDIGLRNLDLIMGLENRIVYdlvdviEGEATLNQALIKDkrleNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 gvmsvgFLL----SSPDDAViwrgpKKNGMIKqFLRDVDWGDVDYLIIDTPPGTSDEHLsvvqyLAAAHIDGAVILTTPQ 202
Cdd:COG2894 84 ------FLLpasqTRDKDAL-----TPEGVKK-VVNELKAMDFDYIIIDSPAGIEQGFK-----NAVYFADEAIVVTNPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 203 EVALQDVRKeisfchkvklpIIGVVENMSgficPKCKKESQIFPP-----------TTG---GAEAMCQDLKIPLLGRVP 268
Cdd:COG2894 147 VSSVRDSDR-----------IIGLLESKS----RRAEIGEEPKEHlllnryrpemvKRGemlSVEDVLEILSIPLIGVIP 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 524969539 269 LDPLIGKSCDKGQSfFVEAPDSPATAAYRSIIHRIQ 304
Cdd:COG2894 212 EDQDVLRASNKGEP-VILDDNSDAGKAYRDIARRLL 246
|
|
| BcsQ |
COG1192 |
Cellulose biosynthesis protein BcsQ [Cell motility]; |
49-307 |
1.03e-16 |
|
Cellulose biosynthesis protein BcsQ [Cell motility];
Pssm-ID: 224113 [Multi-domain] Cd Length: 259 Bit Score: 78.33 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 49 KMKTvkhrILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDicgPSIPKIMGLeGEQVHQSGSGWS---------- 118
Cdd:COG1192 1 MMKI----IAVANQKGGVGKTTTAVNLAAALAKRGGKKVLLIDLD---PQGSLTSWL-GLRPDLEGDLYNllsglkerpd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 119 ---PVYVEDNLGVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVdWGDVDYLIIDTPPGTSDEHLSVvqyLAAAhiDGA 195
Cdd:COG1192 73 ildYTVVIEGLDLIPSNIDLAEGAEIELNAVAKEL-LLKRLLDPV-KDDYDYIIIDTPPSLGVLTLNA---LAAA--DHV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 196 VILTTPQEVAL-------QDVRKEISFcHKVKLPIIGVVENMsgfICPKCKKESQIFppttggaEAMCQDLKIPLLG-RV 267
Cdd:COG1192 146 LIPVQPEFLDLegleqllNTLEDLLKL-RRNKLIVVGILITR---FDSRTKLADEVL-------QELKQLLGDPVLKtKI 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 524969539 268 PLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQEFC 307
Cdd:COG1192 215 PRRVAYREAAAEGKPLYEYDPKSKAAEEYYELAKELLEEL 254
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
56-306 |
2.26e-16 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 224071 [Multi-domain] Cd Length: 284 Bit Score: 77.78 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDgdTQVALLDIDICGPSIPKIMGLEGEQVH---------------------QSG 114
Cdd:COG1149 3 QVAVASGKGGTGKTTVAANLAVLLGDK--YKLVLADCDVEAPNLHLLLGVEVLEEEevirgeipeidpekcircgkcAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 115 SGWSPVYVEDNLGVMSVGFL--------LSSPDDAvIWRGPKKNGMIKQFLrdVDWGD---------------------- 164
Cdd:COG1149 81 CRFGAIVVLPGGKPVLNPDLcegcgacsIVCPEPA-IEEEPVVIGKIYESK--TDYGFplisgrlnvgeeesgklvtalk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 165 ------VDYLIIDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkc 238
Cdd:COG1149 158 khakelADLLIIDSAAGT---GCPVIASLKGA--DLAILVTEPTPFGLHDLKRALELVEHFGIP-TGIVINRYN------ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524969539 239 kkesqifpPTTGGAEAMCQDLKIPLLGRVPLDPLIGKSCDKGQSFFVeaPDSPATAAYRSIIHRIQEF 306
Cdd:COG1149 226 --------LGDSEIEEYCEEEGIPILGEIPYDKDIPEAYVNGEPFVE--PDSKEAEAILEEAEKLKEF 283
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
57-304 |
5.03e-15 |
|
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: 73.53 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968 4 IVITSGKGGVGKTTTTANLGTALARLGK-KVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRdvdwgDVDYLIIDTPPGtsdehLSVVQYLAAAHIDGAVILTTPQEVAL 206
Cdd:TIGR01968 83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKE-----EFDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 207 QDVRKeisfchkvklpIIGVVENMS--------GFICPKCKKESQIFppttgGAEAMCQDLKIPLLGRVPLDPLIGKSCD 278
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKGiekihlivNRLRPEMVKKGDML-----SVDDVLEILSIPLIGVIPEDEAIIVSTN 212
|
250 260
....*....|....*....|....*.
gi 524969539 279 KGQSFFVEaPDSPATAAYRSIIHRIQ 304
Cdd:TIGR01968 213 KGEPVVLN-DKSRAGKAFENIARRIL 237
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
57-301 |
1.09e-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: 72.31 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:cd03111 3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGDVDYLIIDTPPgtsdeHLSVVQYLAAAHIDGAVILTTPQEVALQD 208
Cdd:cd03111 83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGH-----FLDEVTLAVLEAADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 209 VRKEISFC-------HKVKLpIIGVVENMSGfICPKckkesQIfppttggAEAmcqdLKIPLLGRVPLDP-LIGKSCDKG 280
Cdd:cd03111 153 ARRLLDSLrelegssDRLRL-VLNRYDKKSE-ISPK-----DI-------EEA----LGLEVFATLPNDYkAVSESANTG 214
|
250 260
....*....|....*....|.
gi 524969539 281 QSFFVEAPDSPATAAYRSIIH 301
Cdd:cd03111 215 RPLVEVAPRSALVRALQDLAA 235
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
57-303 |
2.92e-13 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 68.81 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVaLLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:PRK10818 5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTV-VIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGDVDYLIIDTPPGTSDEHLSVVqYLAaahiDGAVILTTPQEVAL 206
Cdd:PRK10818 84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 207 QDVRKeisfchkvklpIIGVVENMS--GFICPKCKKESQIFPPTTGG---------AEAMCQDLKIPLLGRVPLDPLIGK 275
Cdd:PRK10818 151 RDSDR-----------ILGILASKSrrAENGEEPIKEHLLLTRYNPGrvsrgdmlsMEDVLEILRIKLVGVIPEDQSVLR 219
|
250 260
....*....|....*....|....*...
gi 524969539 276 SCDKGQSFFVEApDSPATAAYRSIIHRI 303
Cdd:PRK10818 220 ASNQGEPVILDI-EADAGKAYADTVDRL 246
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
55-229 |
3.75e-12 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 64.13 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 127
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSG-KRVLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 128 VMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgDVDYLIIDTPP--GTSDEHlsvvqyLAAAHIDGAVILTTPQEVA 205
Cdd:cd05387 99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADAL------ILAPLVDGVLLVVRAGKTR 165
|
170 180
....*....|....*....|....
gi 524969539 206 LQDVRKEISFCHKVKLPIIGVVEN 229
Cdd:cd05387 166 RREVKEALERLEQAGAKVLGVVLN 189
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
57-268 |
5.97e-10 |
|
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: 58.55 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEdgdtqVALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED------------ 124
Cdd:cd03110 2 IAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncervc 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 125 NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD----------------------------V 160
Cdd:cd03110 77 KFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkalE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 161 DWGDVDYLIIDTPPGTsdeHLSVVQYLAAAhiDGAVILTTPQEVALQDVRKEISFCHKVKLPiIGVVENMSGficpkckk 240
Cdd:cd03110 156 RSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD-------- 221
|
250 260
....*....|....*....|....*...
gi 524969539 241 esqIFPPTTGGAEAMCQDLKIPLLGRVP 268
Cdd:cd03110 222 ---INDEISEEIEDFADEEGIPLLGKIP 246
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
55-230 |
1.21e-09 |
|
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: 55.62 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 134
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 135 lsspdDAVIWRgpkkngmikqflrdvdwgdVDYLIIDTPPGTSDEHLSVvqyLAAAhiDGAVILTTPQEVALQDVRKEIS 214
Cdd:cd02042 42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAA--DLVLIPVQPSPFDLDGLAKLLD 92
|
170 180
....*....|....*....|..
gi 524969539 215 FCHKVK------LPIIGVVENM 230
Cdd:cd02042 93 TLEELKkqlnppLLILGILLTR 114
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
57-308 |
6.97e-09 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 226166 [Multi-domain] Cd Length: 255 Bit Score: 55.73 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDiCGPSIPKIMGLEGEQVHQSG------------SGWSPVYV-E 123
Cdd:COG3640 2 KIAITGKGGVGKTTIAALLLKRLLSKGGYNVLVVDAD-PDSNLPEALGVEEPMKYLGGkrellkkrtgaePGGPPGEMfK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DNLGVMSVgfllssPDDAVIWRGPKK------------------NGMIKQFLRDVDWGDVDYLIIDTPPGTsdEHLS--V 183
Cdd:COG3640 81 ENPLVSDL------PDEYLVENGDIDllvmgkieeggegcacpmNALLRRLLRHLILNRYEVVIVDTEAGI--EHFGrgT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 184 VQylaaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENmsgficpKCKKESQIFppttggaEAMCQDLKIPL 263
Cdd:COG3640 153 IE-----GVDLVIVVVDPSYKSLRTAERIKELAEELGIKRIFVVLN-------KVDEEEELL-------RELAEELGLEV 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 524969539 264 LGRVPLDPLIGKSCDKGQSFFVEAPDSPATaayRSIIHRIQEFCS 308
Cdd:COG3640 214 LGVIPYDPEVVEADLKGEPLNEEPEVLKEI---EEIAERLIKLVE 255
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
44-281 |
4.29e-08 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 53.62 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 44 EEIKEKMKTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 123
Cdd:CHL00175 5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 dnLGVMSVGFLLsspDDAVI----WRG---------------PKKNgmIKQFLRDVDWGDVDYLIIDTPPGtsdehLSVV 184
Cdd:CHL00175 74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKN--MNMLVDSLKNRGYDYILIDCPAG-----IDVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 185 QYLAAAHIDGAVILTTPQEVALQDVRK-----EISFCHKVKLPIIGVVENMsgficpkCKKESQIfppTTGGAEAMcqdL 259
Cdd:CHL00175 142 FINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMM---SVRDVQEM---L 208
|
250 260
....*....|....*....|..
gi 524969539 260 KIPLLGRVPLDPLIGKSCDKGQ 281
Cdd:CHL00175 209 GIPLLGAIPEDENVIISTNRGE 230
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
56-284 |
1.22e-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: 51.93 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 131
Cdd:cd02034 1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGK-VLAVDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 132 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGDVDYLIIDTPPGTsdEHLS--VVQy 186
Cdd:cd02034 76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 187 laaaHIDGAVILTTPQEVALQDVRKEISFCHKVKLPIIGVVENMSGFICPKCKKESQIfppttggaeamcqdLKIPLLGR 266
Cdd:cd02034 153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELL--------------IKLKLIGV 214
|
250
....*....|....*...
gi 524969539 267 VPLDPLIGKSCDKGQSFF 284
Cdd:cd02034 215 IPYDEEIMEADLKGKPLF 232
|
|
| CpaE |
COG4963 |
Flp pilus assembly protein, ATPase CpaE [Intracellular trafficking, secretion, and vesicular ... |
54-303 |
1.65e-07 |
|
Flp pilus assembly protein, ATPase CpaE [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 227298 [Multi-domain] Cd Length: 366 Bit Score: 52.03 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 54 KHRIL-VLSGKGGVGKSTFSAHLAHGLAEDGDTQVALLDIDICGPSIPKIMGLEGEQvHQSGSGWSPVYVED-NLGVM-- 129
Cdd:COG4963 103 QGRELaFLGAKGGVGTSTLAHNLAKGLAILSGAAVLLVDLDLQGGTAALYLDQDPAF-GIAEAVKQPERLDQvLLDSLlt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 130 ------SVGFLLSSPDDAviwrGPKKNGMIKQFLrDVDWGDVDYLIIDTPPGTSDEHlsvVQYLAAAhiDGAVILTTPQE 203
Cdd:COG4963 182 rlasglKLLAAPTELAKN----YDLKTGAVERLL-DLLRGSFDFVVVDLPNIWTDWT---RQVLSGS--DEIVIVAEPSL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 204 VALQDVRKEISFCHKVKL---PIIGVVEnmsgficpkckkesQIFPPTTGGAEAMCQDLKIPLLGRVPLDPLI-GKSCDK 279
Cdd:COG4963 252 ASLRNAKELLDELKRLRPndpKPILVLN--------------RVGVPKRPEPSDLEEILGIESLLVLPFDPALfGDAANN 317
|
250 260
....*....|....*....|....
gi 524969539 280 GQSFFVEAPDSPATAAYRSIIHRI 303
Cdd:COG4963 318 GRMLSEVDPGSPAAKALAQLAQSL 341
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
56-93 |
5.68e-07 |
|
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: 47.43 E-value: 5.68e-07
10 20 30
....*....|....*....|....*....|....*...
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAKGYK-VLLIDLD 38
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
54-174 |
7.31e-07 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 223082 Cd Length: 322 Bit Score: 50.05 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 54 KHRILVLSGKGGVGKSTFSAHLAHGLAEDGDTQVAL-----------LDIDIcGPSIPKIMG-LEGEQVHQSGS---GWS 118
Cdd:COG0003 1 MTRIVFFTGKGGVGKTTIAAATAVKLAESGKKVLLVstdpahslgdvFDLEL-GHDPRKVGPnLDALELDPEKAleeYWD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 524969539 119 PVY--VEDNLGVMSVGFLLssPDDAVIWRGPKKNGMIKQFLRDVDWGDVDYLIIDTPP 174
Cdd:COG0003 80 EVKdyLARLLRTRGLGGIY--ADELATLPGIDEALALLKILEYYVSGEYDVIVVDTAP 135
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
55-174 |
8.56e-06 |
|
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: 46.57 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGDtQVALLDIDIcGPSIPKIMG-------------LEGEQVHQSGS---GWS 118
Cdd:pfam02374 1 MRWIFFGGKGGVGKTTVSAATAVQLSELGK-KVLLISTDP-AHSLSDSFNqkfgheptkvkenLSAMEIDPNMEleeYWQ 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524969539 119 PVYVEDNLGVMSVG-------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGDVDYLIIDTPP 174
Cdd:pfam02374 79 EVQKYMNALLGLRMlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
56-298 |
1.68e-04 |
|
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: 42.35 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGSGWSPVYVE 123
Cdd:cd02117 1 ESIVVYGKGGIGKSTTASNLSAALAEGGkkvlhvgcdpkhDSTLLLTG----GKVPPTIDEMLTEDGTAEELRREDLLFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DNLGVMSVGflLSSPDDAViwrGPKKNGMIK--QFLRDV---DWgDVDYLIID-----------TPPG----------TS 177
Cdd:cd02117 77 GFNGVDCVE--AGGPEPGV---GCGGRGIGTmlELLEEHgllDD-DYDVVIFDvlgdvvcggfaAPLRrgfaqkvvivVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 178 DEHLSVvqyLAAAHIDGAVilttpQEVALQDVRkeisfchkvklpIIGVVENMSGficpkckkesqifPPTTGGAEAMCQ 257
Cdd:cd02117 151 EELMSL---YAANNIVKAV-----ENYSKNGVR------------LAGLVANLRD-------------PAGTEEIQAFAA 197
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 524969539 258 DLKIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRS 298
Cdd:cd02117 198 AVGTKILAVIPRDPAVRRAELARVTVFEHDPVSPAASEFAR 238
|
|
| NifH |
COG1348 |
Nitrogenase subunit NifH, an ATPase [Inorganic ion transport and metabolism]; |
56-305 |
2.47e-04 |
|
Nitrogenase subunit NifH, an ATPase [Inorganic ion transport and metabolism];
Pssm-ID: 224267 [Multi-domain] Cd Length: 278 Bit Score: 41.93 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDidicGPSIPKIMGLEGEQVHQSGsgwspVYVE 123
Cdd:COG1348 2 RQIAIYGKGGIGKSTTSQNLAAALAELGkkvlivgcdpkaDSTRLLLG----GKAIPTVLDTLREKGEVED-----LELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DnlgVMSVGFllsSPDDAVIWRGPKKN------GMIK--QFLRD--VDWGDVDYLIIDTPpgtSDehlsVVQYLAAAHI- 192
Cdd:COG1348 73 D---VIFTGF---GGVKCVESGGPEPGvgcagrGVITaiNLLEElgAFEEDLDVVIYDVL---GD----VVCGGFAMPIr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 193 ----DGAVILTTPQEVAL-------QDVRKeISFCHKVKLpiigvvenmSGFIC--PKCKKESQIfppttggAEAMCQDL 259
Cdd:COG1348 140 egyaDEIYIVTSGEMMALyaanniaKGIRK-YAKTGGVRL---------GGIICnsRSVDREREL-------VEAFAERL 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 524969539 260 KIPLLGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQE 305
Cdd:COG1348 203 GTQLIHFVPRDNIVQKAELNGKTVIEYAPDSNQAEEYRELAKKILE 248
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
56-83 |
2.97e-04 |
|
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: 41.72 E-value: 2.97e-04
10 20
....*....|....*....|....*...
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:cd02035 1 RIIFFGGKGGVGKTTIAAATAVRLAEQG 28
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
63-174 |
3.65e-04 |
|
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: 40.65 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 63 KGGVGKSTFSAHLAHGLAE--------DGDTQVAL-----LDIDICGPSIPKIMGLEG---EQVHQSgsgwspvyVEDNL 126
Cdd:pfam13614 10 KGGVGKTTTSVNLAAALAKkgkkvlliDLDPQGNAtsglgIDKNNVEKTIYELLIGECnieEAIIKT--------VIENL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 524969539 127 GVMSVGFLLSSPDDAVIWRGPKKNgMIKQFLRDVDwGDVDYLIIDTPP 174
Cdd:pfam13614 82 DLIPSNIDLAGAEIELIGIENREN-ILKEALEPVK-DNYDYIIIDCPP 127
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
55-93 |
4.83e-04 |
|
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 Cd Length: 262 Bit Score: 40.90 E-value: 4.83e-04
10 20 30
....*....|....*....|....*....|....*....
gi 524969539 55 HRILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDID 93
Cdd:pfam09140 1 HVIVVGNEKGGSGKSTTAVHVAVALLYKG-ARVAAIDLD 38
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
56-305 |
9.74e-04 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 40.12 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 56 RILVLSGKGGVGKSTFSAHLAHGLAEDG------------DTQVALLDIDICgPSIPKIMGLEGeqvhqsgsgwspvYVE 123
Cdd:pfam00142 1 RQIAIYGKGGIGKSTTSQNLSAALAEMGkkvlvvgcdpkaDSTRLLLGGKLQ-PTVLDTAREKG-------------YVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 124 DnLGVMSVGFLLSSPDDAVIWRGPKKN------GMIK--QFLRDVD-WGDVDYLIIDTppgTSDehlsVV-----QYLAA 189
Cdd:pfam00142 67 D-VEVEDVVYKGYGGVKCVESGGPEPGvgcagrGVITaiNLLEELGaYDDLDFVLYDV---LGD----VVcggfaMPIRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524969539 190 AHIDGAVILTTPQEVAL---QDVRKEISF---CHKVKLpiigvvenmSGFICPKCKKESQifpptTGGAEAMCQDLKIPL 263
Cdd:pfam00142 139 GKAQEIYIVTSNEMMALyaaNNIAKGIQKyakSGGVRL---------GGIICNSRKVDDE-----RELIDAFAEELGTQV 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 524969539 264 LGRVPLDPLIGKSCDKGQSFFVEAPDSPATAAYRSIIHRIQE 305
Cdd:pfam00142 205 LHFVPRDNIVRKAELRKQTVIEYAPDSEQAQEYRELARKILE 246
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
57-93 |
1.10e-03 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 39.45 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*..
gi 524969539 57 ILVLSGKGGVGKSTFSAHLAHGLAEDGDTqVALLDID 93
Cdd:PHA02518 3 IAVLNQKGGAGKTTVATNLASWLHADGHK-VLLVDLD 38
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
41-83 |
1.43e-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: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 524969539 41 PAVEEIKEKMKTVKHRILVLSGKGGVGKSTFSAHLAHGLAEDG 83
Cdd:TIGR04291 307 PSLSRLIDEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKG 349
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
47-93 |
2.54e-03 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 39.19 E-value: 2.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 524969539 47 KEKMKTVKHR--------ILVLSGKGGVGKSTFSAHLAHGLAEDGdTQVALLDID 93
Cdd:TIGR03453 89 REARRYLPHRrggehlqvIAVTNFKGGSGKTTTAAHLAQYLALRG-YRVLAIDLD 142
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
62-83 |
4.23e-03 |
|
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.
Pssm-ID: 349759 Cd Length: 265 Bit Score: 38.26 E-value: 4.23e-03
|
|