|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
1-369 |
0e+00 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 808.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 1 MSSQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVAWLDDTLHIELQMPFVWTSAFDALKEQTSSELLRITGA 80
Cdd:PRK11670 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFVWNSAFEELKEQCSAELLRITGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 81 KAIDWKLSHSIATLKRVKNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQ 160
Cdd:PRK11670 81 KAIDWKLSHNIATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 161 RPTSPDGTHMAPIVAHGLATNSIGYLVTDDNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
Cdd:PRK11670 161 RPTSPDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLR 320
Cdd:PRK11670 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 515952784 321 EDLDSGKPTVVSRPDSEFTEIYRQLAGRVAAQLYWQGEVIPGEIAFRAV 369
Cdd:PRK11670 321 EDLDRGTPTVVSRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
105-350 |
4.35e-143 |
|
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: 405.30 E-value: 4.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSPDGThMAPIVAHGLATNSIG 184
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGG-IIPVEAHGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 185 YLVTDDN-AMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:pfam10609 80 FLLPDEDdAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 264 FEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYR 343
Cdd:pfam10609 160 FKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFL 239
|
....*..
gi 515952784 344 QLAGRVA 350
Cdd:pfam10609 240 KIADKVA 246
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
108-321 |
3.84e-114 |
|
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: 330.62 E-value: 3.84e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSpDGTHMAPIVAHGLATNSIGYLV 187
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ-SEEGIVPVEVGGIKVMSIGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 188 TDDNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKV 267
Cdd:cd02037 80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515952784 268 EVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLRE 321
Cdd:cd02037 160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
106-353 |
3.21e-91 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 277.85 E-value: 3.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSpDGTHMAPIVAH-GLATNSIG 184
Cdd:NF041136 4 IKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGS-EDEGILPVEYSdNLKVMSIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 185 YLVTD-DNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:NF041136 83 FLLENrDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 264 FEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYR 343
Cdd:NF041136 163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALE 242
|
250
....*....|
gi 515952784 344 QLAGRVAAQL 353
Cdd:NF041136 243 KIVDPILELL 252
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
109-297 |
4.01e-49 |
|
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: 166.90 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTS-------PDGTHMAPIVAHGLATN 181
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaSLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 182 SIGYLVTDDnamvwRGPMASKALLQMLQETmWPDLDYLVLDMPPGTGDIQLTLAQNIpVTGAVVVTTPQDIALIDAKKGI 261
Cdd:COG0489 174 PAGPLPPNP-----SELLASKRLKQLLEEL-RGRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 515952784 262 VMFEKVEVPVLGIVENMSmhicsnCGHHEPIFGTGG 297
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
109-350 |
1.56e-14 |
|
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: 72.46 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSPDGTHMAPIVAHGLATNSIGYLVT 188
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFGVKVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 189 dDNAMVWRGPMASKA-LLQMLQETMWPDLDYLVLDMPPGtgdIQLTLAQNIPV-TGAVVVTTPQDIALIDAKKGIVMFEK 266
Cdd:TIGR01969 82 -PAGVSLEGLRKADPdKLEDVLKEIIDDTDFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALKTKIVAEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 267 VEVPVLGIVENmsmhicsncgHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYRQLA 346
Cdd:TIGR01969 158 LGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELA 227
|
....
gi 515952784 347 GRVA 350
Cdd:TIGR01969 228 AELA 231
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
109-145 |
5.24e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 40.61 E-value: 5.24e-04
10 20 30
....*....|....*....|....*....|....*..
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
1-369 |
0e+00 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 808.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 1 MSSQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVAWLDDTLHIELQMPFVWTSAFDALKEQTSSELLRITGA 80
Cdd:PRK11670 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFVWNSAFEELKEQCSAELLRITGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 81 KAIDWKLSHSIATLKRVKNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQ 160
Cdd:PRK11670 81 KAIDWKLSHNIATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 161 RPTSPDGTHMAPIVAHGLATNSIGYLVTDDNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
Cdd:PRK11670 161 RPTSPDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLR 320
Cdd:PRK11670 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 515952784 321 EDLDSGKPTVVSRPDSEFTEIYRQLAGRVAAQLYWQGEVIPGEIAFRAV 369
Cdd:PRK11670 321 EDLDRGTPTVVSRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
105-350 |
4.35e-143 |
|
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: 405.30 E-value: 4.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSPDGThMAPIVAHGLATNSIG 184
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGG-IIPVEAHGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 185 YLVTDDN-AMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:pfam10609 80 FLLPDEDdAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 264 FEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYR 343
Cdd:pfam10609 160 FKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFL 239
|
....*..
gi 515952784 344 QLAGRVA 350
Cdd:pfam10609 240 KIADKVA 246
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
108-321 |
3.84e-114 |
|
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: 330.62 E-value: 3.84e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSpDGTHMAPIVAHGLATNSIGYLV 187
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ-SEEGIVPVEVGGIKVMSIGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 188 TDDNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKV 267
Cdd:cd02037 80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515952784 268 EVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLRE 321
Cdd:cd02037 160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
106-353 |
3.21e-91 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 277.85 E-value: 3.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSpDGTHMAPIVAH-GLATNSIG 184
Cdd:NF041136 4 IKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGS-EDEGILPVEYSdNLKVMSIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 185 YLVTD-DNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:NF041136 83 FLLENrDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 264 FEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYR 343
Cdd:NF041136 163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALE 242
|
250
....*....|
gi 515952784 344 QLAGRVAAQL 353
Cdd:NF041136 243 KIVDPILELL 252
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
109-297 |
4.01e-49 |
|
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: 166.90 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTS-------PDGTHMAPIVAHGLATN 181
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaSLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 182 SIGYLVTDDnamvwRGPMASKALLQMLQETmWPDLDYLVLDMPPGTGDIQLTLAQNIpVTGAVVVTTPQDIALIDAKKGI 261
Cdd:COG0489 174 PAGPLPPNP-----SELLASKRLKQLLEEL-RGRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 515952784 262 VMFEKVEVPVLGIVENMSmhicsnCGHHEPIFGTGG 297
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
108-280 |
4.67e-15 |
|
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: 73.76 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGaenqrpTSPDGThmapiVAHGLATN-SIGYL 186
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLG------LAPKKT-----LGDVLKGRvSLEDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 187 V-------------TDDNAMVWRGPMASKALLQMLQEtMWPDLDYLVLDMPPGTGDIQLTLAqnIPVTGAVVVTTPQDIA 253
Cdd:cd02038 70 IvegpegldiipggSGMEELANLDPEQKAKLIEELSS-LESNYDYLLIDTGAGISRNVLDFL--LAADEVIVVTTPEPTS 146
|
170 180
....*....|....*....|....*...
gi 515952784 254 LIDAKKGI-VMFEKVEVPVLGIVENMSM 280
Cdd:cd02038 147 ITDAYALIkVLSRRGGKKNFRLIVNMAR 174
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
109-350 |
1.56e-14 |
|
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: 72.46 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTSPDGTHMAPIVAHGLATNSIGYLVT 188
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFGVKVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 189 dDNAMVWRGPMASKA-LLQMLQETMWPDLDYLVLDMPPGtgdIQLTLAQNIPV-TGAVVVTTPQDIALIDAKKGIVMFEK 266
Cdd:TIGR01969 82 -PAGVSLEGLRKADPdKLEDVLKEIIDDTDFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALKTKIVAEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 267 VEVPVLGIVENmsmhicsncgHHEPIFGTGGAEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYRQLA 346
Cdd:TIGR01969 158 LGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELA 227
|
....
gi 515952784 347 GRVA 350
Cdd:TIGR01969 228 AELA 231
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
110-328 |
1.52e-13 |
|
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: 69.30 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTS-------PDGTHMAPIV------AH 176
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqalaeglKGRVNLDPILlkeksdEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 177 GLATNsIGYLVTDDNAMVWRGPMASKALLQMLQEtMWPDLDYLVLDMPPGTGDiqLTLAQNIPVTGAVVVTTPQDIALID 256
Cdd:pfam01656 81 GLDLI-PGNIDLEKFEKELLGPRKEERLREALEA-LKEDYDYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 257 AKKGIVMFEKV-------EVPVLGIVENMsmhicsncghhepiFGTGGAEKL------AAQYHTQLLGQLPLHITLREDL 323
Cdd:pfam01656 157 AKRLGGVIAALvggyallGLKIIGVVLNK--------------VDGDNHGKLlkealeELLRGLPVLGVIPRDEAVAEAP 222
|
....*
gi 515952784 324 DSGKP 328
Cdd:pfam01656 223 ARGLP 227
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
91-350 |
1.82e-13 |
|
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: 70.91 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 91 IATLKRVKNqPGVNGVKNIIAVSSGKGGVGKSSTAVNL-ALALAAEGAKVGILDADIYGPSIPNMLGAENQR-------- 161
Cdd:COG4963 87 RAALARLLD-PGAARRGRVIAVVGAKGGVGATTLAVNLaWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladalrn 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 162 PTSPDGTHMAPIVAHglATNSIGYL--VTDDNAMVWRGPMASKALLQMLQETMwpdlDYLVLDMPPGTGDIQLTLAQNip 239
Cdd:COG4963 166 PDRLDETLLDRALTR--HSSGLSVLaaPADLERAEEVSPEAVERLLDLLRRHF----DYVVVDLPRGLNPWTLAALEA-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 240 vTGAVVVTTPQDIA-LIDAKKGIVMFEKVEVPV--LGIVENMSmhicsncghhePIFGTGGAEKLAAQYHTQLLGQLPL- 315
Cdd:COG4963 238 -ADEVVLVTEPDLPsLRNAKRLLDLLRELGLPDdkVRLVLNRV-----------PKRGEISAKDIEEALGLPVAAVLPNd 305
|
250 260 270
....*....|....*....|....*....|....*
gi 515952784 316 HITLREDLDSGKPTVVSRPDSEFTEIYRQLAGRVA 350
Cdd:COG4963 306 PKAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLT 340
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
136-352 |
4.27e-13 |
|
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440223 [Multi-domain] Cd Length: 230 Bit Score: 67.99 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 136 GAKVGILDADIYGPSIPNMLGAENQRPTS---PDGTHMAPIVAHGlaTNSIGYLVTDDNAMVWRGPMASKALLQMLQETM 212
Cdd:COG0455 14 GKRVLLVDADLGLANLDVLLGLEPKATLAdvlAGEADLEDAIVQG--PGGLDVLPGGSGPAELAELDPEERLIRVLEELE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 213 wPDLDYLVLDMPPGTGDI---QLTLAQNIpvtgaVVVTTPQDIALIDAKKGI-VMFEKVEVPVLGIVENMSmhicsncgh 288
Cdd:COG0455 92 -RFYDVVLVDTGAGISDSvllFLAAADEV-----VVVTTPEPTSITDAYALLkLLRRRLGVRRAGVVVNRV--------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 289 HEPIFGTGGAEKLAA------QYHTQLLGQLPLHITLREDLDSGKPTVVSRPDSEFTEIYRQLAGRVAAQ 352
Cdd:COG0455 157 RSEAEARDVFERLEQvaerflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
109-353 |
9.84e-10 |
|
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: 58.33 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGpSIPNMLGAENQ--------------------RPTSPDGT 168
Cdd:COG1192 3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLDPDdldptlydlllddapledaiVPTEIPGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 169 HMAPivahglATNSIGYLVTDDNAMVWRGPMASKALlqmlqETMWPDLDYLVLDMPPGTGDIQ---LTLAQNIpvtgaVV 245
Cdd:COG1192 82 DLIP------ANIDLAGAEIELVSRPGRELRLKRAL-----APLADDYDYILIDCPPSLGLLTlnaLAAADSV-----LI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 246 VTTPQDIALIDAKKGIVMFEKVE------VPVLGIVenMSMHICSNCGHHEPIfgtggaEKLAAQYHTQLLGQ-LPLHIT 318
Cdd:COG1192 146 PVQPEYLSLEGLAQLLETIEEVRedlnpkLEILGIL--LTMVDPRTRLSREVL------EELREEFGDKVLDTvIPRSVA 217
|
250 260 270
....*....|....*....|....*....|....*
gi 515952784 319 LREDLDSGKPTVVSRPDSEFTEIYRQLAGRVAAQL 353
Cdd:COG1192 218 LAEAPSAGKPVFEYDPKSKGAKAYRALAEELLERL 252
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
108-349 |
3.02e-08 |
|
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: 53.75 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRP-TSPDgthmapiVAHGLATNSIGyL 186
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVyTLVD-------VLEGECRLEQA-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 187 VTDDN---------AMVWRGPMAS-KALLQMLQETMwPDLDYLVLDMPPGtgdIQLTLAQNI-PVTGAVVVTTPQDIALI 255
Cdd:cd02036 73 IKDKRwenlyllpaSQTRDKDALTpEKLEELVKELK-DSFDFILIDSPAG---IESGFINAIaPADEAIIVTNPEISSVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 256 DAKKGIVMFEKVEVPVLGIVEN-MSMHICSNcGHHEPIfgtggaEKLAAQYHTQLLGQLPLHITLREDLDSGKPTVVSRP 334
Cdd:cd02036 149 DADRVIGLLESKGIVNIGLIVNrYRPEMVKS-GDMLSV------EDIQEILGIPLLGVIPEDPEVIVATNRGEPLVLYKP 221
|
250
....*....|....*
gi 515952784 335 DSEFTEIYRQLAGRV 349
Cdd:cd02036 222 NSLAAKAFENIARRL 236
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
90-277 |
4.99e-08 |
|
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: 52.57 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 90 SIATLKRVKNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRPTS---PD 166
Cdd:cd05387 2 AFRTLRTNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSevlSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 167 GTHMAPIVAHglaTNSIGYLV-----TDDNAMVWRGPMASKALLQMLQEtmwpDLDYLVLDMPP--GTGDIQLtLAQNip 239
Cdd:cd05387 82 QASLEDVIQS---TNIPNLDVlpagtVPPNPSELLSSPRFAELLEELKE----QYDYVIIDTPPvlAVADALI-LAPL-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515952784 240 VTGAVVVT----TPQDialiDAKKGIVMFEKVEVPVLGIVEN 277
Cdd:cd05387 152 VDGVLLVVragkTRRR----EVKEALERLEQAGAKVLGVVLN 189
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
104-265 |
1.07e-07 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 52.85 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQ--------------------RPT 163
Cdd:CHL00175 12 ATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRvlytamdvlegecrldqaliRDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 164 SPDGTHMAPIvahglATNSIGYLVTDDNAMVwrgpmaskaLLQMLQETmwpDLDYLVLDMPPGtgdIQLTLAQNI-PVTG 242
Cdd:CHL00175 92 RWKNLSLLAI-----SKNRQRYNVTRKNMNM---------LVDSLKNR---GYDYILIDCPAG---IDVGFINAIaPAQE 151
|
170 180
....*....|....*....|...
gi 515952784 243 AVVVTTPQDIALIDAKKGIVMFE 265
Cdd:CHL00175 152 AIVVTTPEITAIRDADRVAGLLE 174
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
108-277 |
5.40e-07 |
|
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: 50.41 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRptspdgTHMAPIVAHGLATNSIGyLV 187
Cdd:TIGR01968 2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRI------VYTLVDVVEGECRLQQA-LI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 188 TD---------------DNAMVWRGPMasKALLQMLQEtmwpDLDYLVLDMPPG--TGdiqltlAQN--IPVTGAVVVTT 248
Cdd:TIGR01968 75 KDkrlknlyllpasqtrDKDAVTPEQM--KKLVNELKE----EFDYVIIDCPAGieSG------FRNavAPADEAIVVTT 142
|
170 180
....*....|....*....|....*....
gi 515952784 249 PQDIALIDAKKgivmfekvevpVLGIVEN 277
Cdd:TIGR01968 143 PEVSAVRDADR-----------VIGLLEA 160
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
109-145 |
6.61e-07 |
|
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: 47.92 E-value: 6.61e-07
10 20 30
....*....|....*....|....*....|....*..
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
109-346 |
5.91e-06 |
|
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: 46.89 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAE-GAKVGILDADIYGPSIPNMLGAEN--------QRPTSPDGTHMAPIVAH--- 176
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPdydladviQNLDRLDRTLLDSAVTRhss 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 177 GLATNSIGYLVTDDNAMvwrGPMASKALLQMLQETmwpdLDYLVLDMPPGTGDIQLTLAQniPVTGAVVVTTPQDIALID 256
Cdd:cd03111 82 GLSLLPAPQELEDLEAL---GAEQVDKLLQVLRAF----YDHIIVDLGHFLDEVTLAVLE--AADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 257 AKKGIVMFEKVEVPvlgiveNMSMHICSNCghhepiFGTGGAekLAAQYHTQLLGQLPLHiTLRED-------LDSGKPT 329
Cdd:cd03111 153 ARRLLDSLRELEGS------SDRLRLVLNR------YDKKSE--ISPKDIEEALGLEVFA-TLPNDykavsesANTGRPL 217
|
250
....*....|....*..
gi 515952784 330 VVSRPDSEFTEIYRQLA 346
Cdd:cd03111 218 VEVAPRSALVRALQDLA 234
|
|
| PRK13230 |
PRK13230 |
nitrogenase reductase-like protein; Reviewed |
115-346 |
2.63e-05 |
|
nitrogenase reductase-like protein; Reviewed
Pssm-ID: 183903 Cd Length: 279 Bit Score: 45.53 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 115 GKGGVGKSSTAVNLALALAAEGAKVGILDAD--------IYGPSIPNMLGAenQRPTSPDGTHMAPIVAHGLatNSIgYL 186
Cdd:PRK13230 8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVLDV--LREKGIDNLGLEDIIYEGF--NGI-YC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 187 VTDDN-----AMVWRGPMASKALLQMLQ--ETMWPDLD-YLVLD--------MPpgtgdIQLTLAQNIpvtgaVVVTTPQ 250
Cdd:PRK13230 83 VESGGpepgyGCAGRGVITAIDLLKKLGvfEELGPDVViYDILGdvvcggfaMP-----LQKGLADDV-----YIVTTCD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 251 DIALIDAK---KGIVMF-EKVEVPVLGIVENMSMHIcsncghHEPIFgtggAEKLAAQYHTQLLGQLPLHITLREDLDSG 326
Cdd:PRK13230 153 PMAIYAANnicKGIKRFaKRGKSALGGIIYNGRSVI------DAPDI----VEEFAKKIGTNVIGKIPMSNIITEAEIYG 222
|
250 260
....*....|....*....|
gi 515952784 327 KPTVVSRPDSEFTEIYRQLA 346
Cdd:PRK13230 223 KTVIEYAPDSEISNIFRELA 242
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
109-277 |
2.87e-05 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 44.74 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQRptspdgTHMAPIVAHglaTNSIGYLVT 188
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKI------TGLTNFLSG---TTDLSDAIC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 189 DDNA----MVWRGP--------MASKALLQMLqETMWPDLDYLVLDMPP-GT-GDIQLtLAQNipVTGAVVVTTPQDIAL 254
Cdd:TIGR01007 90 DTNIenldVITAGPvppnptelLQSSNFKTLI-ETLRKRFDYIIIDTPPiGTvTDAAI-IARA--CDASILVTDAGKIKK 165
|
170 180
....*....|....*....|...
gi 515952784 255 IDAKKGIVMFEKVEVPVLGIVEN 277
Cdd:TIGR01007 166 REVKKAKEQLEQAGSNFLGVVLN 188
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
109-252 |
3.59e-05 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 45.39 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILD-------ADIYGPSIPNM------------LGAENQ-----RPTS 164
Cdd:PHA02519 108 VLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgndpqgtASMYHGYVPDLhihaddtllpfyLGERDNaeyaiKPTC 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 165 PDGTHMAP--IVAHGLATNSIGYLVTDdnamvwRGPMASKALLQMLQETMWPDLDYLVLDMPP--GTGDIQLTLAQNIpv 240
Cdd:PHA02519 188 WPGLDIIPscLALHRIETDLMQYHDAG------KLPHPPHLMLRAAIESVWDNYDIIVIDSAPnlGTGTINVVCAADV-- 259
|
170
....*....|..
gi 515952784 241 tgaVVVTTPQDI 252
Cdd:PHA02519 260 ---IVVATPAEL 268
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
109-352 |
9.62e-05 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 43.59 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSsGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQrptspdgthmaPIVAHGLA-TNSIGYLV 187
Cdd:pfam00142 2 QIAIY-GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQ-----------PTVLDTAReKGYVEDVE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 188 TDD---------NAMVWRGPMASKAL--------LQMLQET-MWPDLDYLVLDMppgTGD---------IQLTLAQNIpv 240
Cdd:pfam00142 70 VEDvvykgyggvKCVESGGPEPGVGCagrgvitaINLLEELgAYDDLDFVLYDV---LGDvvcggfampIREGKAQEI-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 241 tgaVVVTTPQDIALIDAK---KGIVMFEKV-EVPVLGIVenmsmhicsnCGHHEPIFGTGGAEKLAAQYHTQLLGQLPLH 316
Cdd:pfam00142 145 ---YIVTSNEMMALYAANniaKGIQKYAKSgGVRLGGII----------CNSRKVDDERELIDAFAEELGTQVLHFVPRD 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 515952784 317 ITLREDLDSGKPTVVSRPDSEFTEIYRQLAGRVAAQ 352
Cdd:pfam00142 212 NIVRKAELRKQTVIEYAPDSEQAQEYRELARKILEN 247
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
109-146 |
1.13e-04 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 43.12 E-value: 1.13e-04
10 20 30
....*....|....*....|....*....|....*...
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
Cdd:COG2894 4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI 41
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
109-145 |
1.61e-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: 41.80 E-value: 1.61e-04
10 20 30
....*....|....*....|....*....|....*..
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
109-150 |
3.48e-04 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 41.37 E-value: 3.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPS 150
Cdd:PHA02518 2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
109-145 |
5.24e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 40.61 E-value: 5.24e-04
10 20 30
....*....|....*....|....*....|....*..
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
108-225 |
9.18e-04 |
|
exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273391 [Multi-domain] Cd Length: 764 Bit Score: 41.24 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGaENQRPTSPD---GTHMAPIVAHGLATNSIG 184
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFG-KAPKPGLLDllaGEASIEAGIHRDQRPGLA 632
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 515952784 185 YLVTDDNAMVWRGP---MASKALLQMLqETMWPDLDYLVLDMPP 225
Cdd:TIGR01005 633 FIAAGGASHFPHNPnelLANPAMAELI-DNARNAFDLVLVDLAA 675
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
108-145 |
4.69e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 36.25 E-value: 4.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 515952784 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
109-224 |
5.64e-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: 38.20 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLgaENQRPTSpDGTHMApivahgLATNSIGYLVT 188
Cdd:pfam09140 2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYF--ENRSATA-DRTGLS------LPTPEHLNLPD 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 515952784 189 DDNAMVWRGPMASKALLQMLQETMWPDLDYLVLDMP 224
Cdd:pfam09140 73 NDVAEVPDGENIDDARLEEAFADLEARCDFIVIDTP 108
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
115-361 |
8.17e-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: 37.49 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 115 GKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPNMLGAENQrPTspdgthmapiVAHGLATNsiGYLVTDDNAM- 193
Cdd:cd02040 7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAI-PT----------VLDTLREK--GEVEELEDVIk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 194 -----VW---------------RGPMASkalLQMLQET--MWPDLDYLVLD-----------MPpgtgdIQLTLAQNIpv 240
Cdd:cd02040 74 egfngIKcvesggpepgvgcagRGIITA---INLLEELgaYEEDLDVVFYDvlgdvvcggfaMP-----IREGYADEV-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515952784 241 tgaVVVTTPQDIALIDAK---KGIVMF-EKVEVPVLGIVENMsmhicSNCGHHEPIfgtggAEKLAAQYHTQLLGQLPLH 316
Cdd:cd02040 144 ---YIVTSGEMMALYAANniaKGIVKYaERGGVRLGGLICNS-----RNVDREEEL-----VEEFAERLGTQIIHFVPRS 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515952784 317 ITLREDLDSGKpTVVSR-PDSEFTEIYRQLAGRVAAQlywQGEVIP 361
Cdd:cd02040 211 NEVQEAELRGK-TVIEYdPDSEQADEYRELAKKILEN---KKLVIP 252
|
|
| |
