|
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: 832.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVAWMDDTLHVELVMPFVWHSAFEELKEQCSAELLRITGA 80
Cdd:PRK11670 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFVWNSAFEELKEQCSAELLRITGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 81 KAIDWKLSHNIATLKRVKNQPGINGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQ 160
Cdd:PRK11670 81 KAIDWKLSHNIATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 161 RPTSPDGTHMAPIMSHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
Cdd:PRK11670 161 RPTSPDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
Cdd:PRK11670 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 90111388 321 EDLDKGTPTVISRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
Cdd:PRK11670 321 EDLDRGTPTVVSRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
105-350 |
3.22e-144 |
|
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: 408.38 E-value: 3.22e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSPDGThMAPIMSHGLATNSIG 184
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGG-IIPVEAHGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 185 YLVTDDN-AMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:pfam10609 80 FLLPDEDdAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 264 FEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYR 343
Cdd:pfam10609 160 FKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFL 239
|
....*..
gi 90111388 344 QLADRVA 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 |
1.51e-115 |
|
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: 334.47 E-value: 1.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSpDGTHMAPIMSHGLATNSIGYLV 187
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ-SEEGIVPVEVGGIKVMSIGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 188 TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKV 267
Cdd:cd02037 80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90111388 268 EVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLRE 321
Cdd:cd02037 160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
106-353 |
1.16e-93 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 284.02 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSpDGTHMAPIMSH-GLATNSIG 184
Cdd:NF041136 4 IKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGS-EDEGILPVEYSdNLKVMSIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 185 YLVTD-DNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:NF041136 83 FLLENrDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 264 FEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYR 343
Cdd:NF041136 163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALE 242
|
250
....*....|
gi 90111388 344 QLADRVAAQL 353
Cdd:NF041136 243 KIVDPILELL 252
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
109-303 |
3.23e-50 |
|
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: 169.98 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTS-------PDGTHMAPIMSHGLATN 181
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaSLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 182 SIGYLVTDDnamvwRGPMASKALMQMLQEtLWPDLDYLVLDMPPGTGDIQLTLAQNIpVTGAVVVTTPQDIALIDAKKGI 261
Cdd:COG0489 174 PAGPLPPNP-----SELLASKRLKQLLEE-LRGRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 90111388 262 VMFEKVEVPVLGIVENMSvhicsnCGHHEPIFGTGGAEKLAE 303
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGEEYGYRE 282
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
109-350 |
1.43e-15 |
|
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: 75.54 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSPDGTHMAPIMSHGLATNSIGYLVT 188
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFGVKVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 189 dDNAMVWRGPMASKA-LMQMLQETLWPDLDYLVLDMPPGtgdIQLTLAQNIPV-TGAVVVTTPQDIALIDAKKGIVMFEK 266
Cdd:TIGR01969 82 -PAGVSLEGLRKADPdKLEDVLKEIIDDTDFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALKTKIVAEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 267 VEVPVLGIVENmsvhicsNCGHHEPIFGTGGAEKLAEkyhTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYRQLA 346
Cdd:TIGR01969 158 LGTAILGVVLN-------RVTRDKTELGREEIETILE---VPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELA 227
|
....
gi 90111388 347 DRVA 350
Cdd:TIGR01969 228 AELA 231
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
109-145 |
4.19e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 41.00 E-value: 4.19e-04
10 20 30
....*....|....*....|....*....|....*..
gi 90111388 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: 832.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVAWMDDTLHVELVMPFVWHSAFEELKEQCSAELLRITGA 80
Cdd:PRK11670 1 MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFVWNSAFEELKEQCSAELLRITGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 81 KAIDWKLSHNIATLKRVKNQPGINGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQ 160
Cdd:PRK11670 81 KAIDWKLSHNIATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAEDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 161 RPTSPDGTHMAPIMSHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
Cdd:PRK11670 161 RPTSPDGTHMAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
Cdd:PRK11670 241 TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 90111388 321 EDLDKGTPTVISRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
Cdd:PRK11670 321 EDLDRGTPTVVSRPESEFTAIYRQLADRVAAQLYWQGEVIPGEISFRAV 369
|
|
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
105-350 |
3.22e-144 |
|
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: 408.38 E-value: 3.22e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSPDGThMAPIMSHGLATNSIG 184
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGG-IIPVEAHGIKVMSIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 185 YLVTDDN-AMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:pfam10609 80 FLLPDEDdAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAIDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 264 FEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYR 343
Cdd:pfam10609 160 FKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAFL 239
|
....*..
gi 90111388 344 QLADRVA 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 |
1.51e-115 |
|
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: 334.47 E-value: 1.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSpDGTHMAPIMSHGLATNSIGYLV 187
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQ-SEEGIVPVEVGGIKVMSIGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 188 TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVMFEKV 267
Cdd:cd02037 80 PEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKKL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90111388 268 EVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLRE 321
Cdd:cd02037 160 NIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
106-353 |
1.16e-93 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 284.02 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 106 VKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSpDGTHMAPIMSH-GLATNSIG 184
Cdd:NF041136 4 IKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGS-EDEGILPVEYSdNLKVMSIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 185 YLVTD-DNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTPQDIALIDAKKGIVM 263
Cdd:NF041136 83 FLLENrDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRKSINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 264 FEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYR 343
Cdd:NF041136 163 CRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAAKALE 242
|
250
....*....|
gi 90111388 344 QLADRVAAQL 353
Cdd:NF041136 243 KIVDPILELL 252
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
109-303 |
3.23e-50 |
|
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: 169.98 E-value: 3.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTS-------PDGTHMAPIMSHGLATN 181
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPGLSdvlageaSLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 182 SIGYLVTDDnamvwRGPMASKALMQMLQEtLWPDLDYLVLDMPPGTGDIQLTLAQNIpVTGAVVVTTPQDIALIDAKKGI 261
Cdd:COG0489 174 PAGPLPPNP-----SELLASKRLKQLLEE-LRGRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 90111388 262 VMFEKVEVPVLGIVENMSvhicsnCGHHEPIFGTGGAEKLAE 303
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGEEYGYRE 282
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
108-339 |
1.58e-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: 77.99 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGaenqrpTSPDGThmapiMSHGLATNsigylV 187
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLG------LAPKKT-----LGDVLKGR-----V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 188 TDDNAMVwRGP--------------MASKALMQMLQ-----ETLWPDLDYLVLDMPPGTGDIQLTLAqnIPVTGAVVVTT 248
Cdd:cd02038 65 SLEDIIV-EGPegldiipggsgmeeLANLDPEQKAKlieelSSLESNYDYLLIDTGAGISRNVLDFL--LAADEVIVVTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 249 PQDIALIDAKKGI-VMFEKVEVPVLGIVENMSvhicsncghHEPIFGTGGAEKL---AEKYHT---QLLGQMPLHISLRE 321
Cdd:cd02038 142 PEPTSITDAYALIkVLSRRGGKKNFRLIVNMA---------RSPKEGRATFERLkkvAKRFLDinlDFVGFIPYDQSVRR 212
|
250
....*....|....*...
gi 90111388 322 DLDKGTPTVISRPESEFT 339
Cdd:cd02038 213 AVRSQKPFVLLFPNSKAS 230
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
109-350 |
1.43e-15 |
|
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: 75.54 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSPDGTHMAPIMSHGLATNSIGYLVT 188
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIKDAIYEGPFGVKVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 189 dDNAMVWRGPMASKA-LMQMLQETLWPDLDYLVLDMPPGtgdIQLTLAQNIPV-TGAVVVTTPQDIALIDAKKGIVMFEK 266
Cdd:TIGR01969 82 -PAGVSLEGLRKADPdKLEDVLKEIIDDTDFLLIDAPAG---LERDAVTALAAaDELLLVVNPEISSITDALKTKIVAEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 267 VEVPVLGIVENmsvhicsNCGHHEPIFGTGGAEKLAEkyhTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYRQLA 346
Cdd:TIGR01969 158 LGTAILGVVLN-------RVTRDKTELGREEIETILE---VPVLGVVPEDPEVRRAAAFGEPVVIYNPNSPAAQAFMELA 227
|
....
gi 90111388 347 DRVA 350
Cdd:TIGR01969 228 AELA 231
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
110-328 |
2.01e-14 |
|
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: 71.61 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTS-------PDGTHMAPIM--SHGLAT 180
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALqalaeglKGRVNLDPILlkEKSDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 181 NS---IGYLVTDDNAMVWRGPMASKALMQMLQEtLWPDLDYLVLDMPPGTGDiqLTLAQNIPVTGAVVVTTPQDIALIDA 257
Cdd:pfam01656 81 GLdliPGNIDLEKFEKELLGPRKEERLREALEA-LKEDYDYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILVEDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 258 KKGIVMFEKV-------EVPVLGIVENMsvhicsncghhepiFGTGGAEKL------AEKYHTQLLGQMPLHISLREDLD 324
Cdd:pfam01656 158 KRLGGVIAALvggyallGLKIIGVVLNK--------------VDGDNHGKLlkealeELLRGLPVLGVIPRDEAVAEAPA 223
|
....
gi 90111388 325 KGTP 328
Cdd:pfam01656 224 RGLP 227
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
136-352 |
8.86e-14 |
|
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: 69.92 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 136 GAKVGILDADIYGPSIPTMLGAENQRPTS---PDGTHMAPIMSHGlaTNSIGYLVTDDNAMVWRGPMASKALMQMLQEtL 212
Cdd:COG0455 14 GKRVLLVDADLGLANLDVLLGLEPKATLAdvlAGEADLEDAIVQG--PGGLDVLPGGSGPAELAELDPEERLIRVLEE-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 213 WPDLDYLVLDMPPGTGDI---QLTLAQNIpvtgaVVVTTPQDIALIDAKKGI-VMFEKVEVPVLGIVENMSVHicsncgH 288
Cdd:COG0455 91 ERFYDVVLVDTGAGISDSvllFLAAADEV-----VVVTTPEPTSITDAYALLkLLRRRLGVRRAGVVVNRVRS------E 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111388 289 HEPIFGTGGAEKLAEKY---HTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYRQLADRVAAQ 352
Cdd:COG0455 160 AEARDVFERLEQVAERFlgvRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARLAGW 226
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
91-350 |
1.33e-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: 71.30 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 91 IATLKRVKNqPGINGVKNIIAVSSGKGGVGKSSTAVNL-ALALAAEGAKVGILDADIYGPSIPTMLGAENQR-------- 161
Cdd:COG4963 87 RAALARLLD-PGAARRGRVIAVVGAKGGVGATTLAVNLaWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladalrn 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 162 PTSPDGTHMAPIMSH---GL----ATNSIG--YLVTDDnamvwrgpmASKALMQMLQETlwpdLDYLVLDMPPGTGDIQL 232
Cdd:COG4963 166 PDRLDETLLDRALTRhssGLsvlaAPADLEraEEVSPE---------AVERLLDLLRRH----FDYVVVDLPRGLNPWTL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 233 TLAQNipvTGAVVVTTPQDIA-LIDAKKGIVMFEKVEVPV--LGIVENMSvhicsncghhePIFGTGGAEKLAEKYHTQL 309
Cdd:COG4963 233 AALEA---ADEVVLVTEPDLPsLRNAKRLLDLLRELGLPDdkVRLVLNRV-----------PKRGEISAKDIEEALGLPV 298
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 90111388 310 LGQMPL-HISLREDLDKGTPTVISRPESEFTAIYRQLADRVA 350
Cdd:COG4963 299 AAVLPNdPKAVAEAANQGRPLAEVAPKSPLAKAIRKLAARLT 340
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
109-353 |
5.59e-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: 62.18 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGpSIPTMLGAENQ--------------------RPTSPDGT 168
Cdd:COG1192 3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQG-NLTSGLGLDPDdldptlydlllddapledaiVPTEIPGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 169 HMAPimshglATNSIGYLVTDDNAMVWRGPMASKALmqmlqETLWPDLDYLVLDMPPGTGDIQ---LTLAQNIpvtgaVV 245
Cdd:COG1192 82 DLIP------ANIDLAGAEIELVSRPGRELRLKRAL-----APLADDYDYILIDCPPSLGLLTlnaLAAADSV-----LI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 246 VTTPQDIALIDAKKGIVMFEKVE------VPVLGIVENMsvHICSNCGHHEPIfgtggaEKLAEKYHTQLLGQM-PLHIS 318
Cdd:COG1192 146 PVQPEYLSLEGLAQLLETIEEVRedlnpkLEILGILLTM--VDPRTRLSREVL------EELREEFGDKVLDTViPRSVA 217
|
250 260 270
....*....|....*....|....*....|....*
gi 90111388 319 LREDLDKGTPTVISRPESEFTAIYRQLADRVAAQL 353
Cdd:COG1192 218 LAEAPSAGKPVFEYDPKSKGAKAYRALAEELLERL 252
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
108-349 |
3.92e-10 |
|
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: 59.52 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSpdgthmapiMSHGLATNsigylV 187
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYT---------LVDVLEGE-----C 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 188 TDDNAMV----------------WRGPMASKALMQMLQETLWPDLDYLVLDMPPGtgdIQLTLAQNI-PVTGAVVVTTPQ 250
Cdd:cd02036 67 RLEQALIkdkrwenlyllpasqtRDKDALTPEKLEELVKELKDSFDFILIDSPAG---IESGFINAIaPADEAIIVTNPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 251 DIALIDAKKgivmfekvevpVLGIVENMS---VHICSNcgHHEPIFGTGGA----EKLAEKYHTQLLGQMPLHISLREDL 323
Cdd:cd02036 144 ISSVRDADR-----------VIGLLESKGivnIGLIVN--RYRPEMVKSGDmlsvEDIQEILGIPLLGVIPEDPEVIVAT 210
|
250 260
....*....|....*....|....*.
gi 90111388 324 DKGTPTVISRPESEFTAIYRQLADRV 349
Cdd:cd02036 211 NRGEPLVLYKPNSLAAKAFENIARRL 236
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
104-265 |
3.15e-09 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 57.47 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQ--------------------RPT 163
Cdd:CHL00175 12 ATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIGLRNLDLLLGLENRvlytamdvlegecrldqaliRDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 164 SPDGTHMAPImshglATNSIGYLVTDDNamvwrgpmaskalMQMLQETLWP-DLDYLVLDMPPGtgdIQLTLAQNI-PVT 241
Cdd:CHL00175 92 RWKNLSLLAI-----SKNRQRYNVTRKN-------------MNMLVDSLKNrGYDYILIDCPAG---IDVGFINAIaPAQ 150
|
170 180
....*....|....*....|....
gi 90111388 242 GAVVVTTPQDIALIDAKKGIVMFE 265
Cdd:CHL00175 151 EAIVVTTPEITAIRDADRVAGLLE 174
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
108-280 |
4.83e-08 |
|
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: 53.50 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQ--------------------RPTSPDG 167
Cdd:TIGR01968 2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIGLRNLDLLLGLENRivytlvdvvegecrlqqaliKDKRLKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 168 THMAPImshglATNSIGYLVTDDNamvwrgpmaskalMQMLQETLWPDLDYLVLDMPPG--TGdiqltlAQN--IPVTGA 243
Cdd:TIGR01968 82 LYLLPA-----SQTRDKDAVTPEQ-------------MKKLVNELKEEFDYVIIDCPAGieSG------FRNavAPADEA 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111388 244 VVVTTPQDIALIDAKKgivmfekvevpVLGIVENMSV 280
Cdd:TIGR01968 138 IVVTTPEVSAVRDADR-----------VIGLLEAKGI 163
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
108-277 |
1.13e-07 |
|
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: 51.42 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTS---PDGTHMAPIMSHglaTNSIG 184
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSevlSGQASLEDVIQS---TNIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 185 YLV-----TDDNAMVwrgPMASKALMQMLqETLWPDLDYLVLDMPP--GTGDIQLtLAQNipVTGAVVVT----TPQDia 253
Cdd:cd05387 97 LDVlpagtVPPNPSE---LLSSPRFAELL-EELKEQYDYVIIDTPPvlAVADALI-LAPL--VDGVLLVVragkTRRR-- 167
|
170 180
....*....|....*....|....
gi 90111388 254 liDAKKGIVMFEKVEVPVLGIVEN 277
Cdd:cd05387 168 --EVKEALERLEQAGAKVLGVVLN 189
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
109-145 |
5.24e-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: 48.31 E-value: 5.24e-07
10 20 30
....*....|....*....|....*....|....*..
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
109-277 |
2.01e-06 |
|
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: 47.82 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRptspdgTHMAPIMSHglaTNSIGYLVT 188
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKI------TGLTNFLSG---TTDLSDAIC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 189 DDNA----MVWRGP--------MASKALMQMLqETLWPDLDYLVLDMPP-GT-GDIQLtLAQNipVTGAVVVTTPQDIAL 254
Cdd:TIGR01007 90 DTNIenldVITAGPvppnptelLQSSNFKTLI-ETLRKRFDYIIIDTPPiGTvTDAAI-IARA--CDASILVTDAGKIKK 165
|
170 180
....*....|....*....|...
gi 90111388 255 IDAKKGIVMFEKVEVPVLGIVEN 277
Cdd:TIGR01007 166 REVKKAKEQLEQAGSNFLGVVLN 188
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
109-347 |
1.27e-05 |
|
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: 46.12 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAE-GAKVGILDADIYGPSIPTMLGAEN--------QRPTSPDGTHMAPIMSH--- 176
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPFGDLGLYLNLRPdydladviQNLDRLDRTLLDSAVTRhss 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 177 GLATNSIGYLVTDDNAMvwrGPMASKALMQMLQETlwpdLDYLVLDMPPGTGDIQLTLAQniPVTGAVVVTTPQDIALID 256
Cdd:cd03111 82 GLSLLPAPQELEDLEAL---GAEQVDKLLQVLRAF----YDHIIVDLGHFLDEVTLAVLE--AADEILLVTQQDLPSLRN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 257 AKKGIVMFEKVEVPvlgiveNMSVHICSNCghhepiFGTGGAEKLAEKyhTQLLGQMPLHiSLRED-------LDKGTPT 329
Cdd:cd03111 153 ARRLLDSLRELEGS------SDRLRLVLNR------YDKKSEISPKDI--EEALGLEVFA-TLPNDykavsesANTGRPL 217
|
250
....*....|....*...
gi 90111388 330 VISRPESEFTAIYRQLAD 347
Cdd:cd03111 218 VEVAPRSALVRALQDLAA 235
|
|
| PRK13230 |
PRK13230 |
nitrogenase reductase-like protein; Reviewed |
115-349 |
3.24e-05 |
|
nitrogenase reductase-like protein; Reviewed
Pssm-ID: 183903 Cd Length: 279 Bit Score: 45.15 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 115 GKGGVGKSSTAVNLALALAAEGAKVGILDAD--------IYGPSIPTMLGAenQRPTSPDGTHMAPIMSHGLatNSIgYL 186
Cdd:PRK13230 8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDpkadctrnLVGEKIPTVLDV--LREKGIDNLGLEDIIYEGF--NGI-YC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 187 VTDDN-----AMVWRGPMASKALMQMLQ--ETLWPDLD-YLVLD--------MPpgtgdIQLTLAQNIpvtgaVVVTTPQ 250
Cdd:PRK13230 83 VESGGpepgyGCAGRGVITAIDLLKKLGvfEELGPDVViYDILGdvvcggfaMP-----LQKGLADDV-----YIVTTCD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 251 DIALIDAK---KGIVMF-EKVEVPVLGIVENMSVHIcsncghHEPIFgtggAEKLAEKYHTQLLGQMPL-HISLREDLDK 325
Cdd:PRK13230 153 PMAIYAANnicKGIKRFaKRGKSALGGIIYNGRSVI------DAPDI----VEEFAKKIGTNVIGKIPMsNIITEAEIYG 222
|
250 260
....*....|....*....|....
gi 90111388 326 GTpTVISRPESEFTAIYRQLADRV 349
Cdd:PRK13230 223 KT-VIEYAPDSEISNIFRELAEAI 245
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
109-146 |
1.28e-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: 1.28e-04
10 20 30
....*....|....*....|....*....|....*...
gi 90111388 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 |
1.68e-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: 1.68e-04
10 20 30
....*....|....*....|....*....|....*..
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
115-349 |
1.97e-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: 42.74 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 115 GKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQrPTspdgthmapIMSHGLATNSIGYLVTDD---- 190
Cdd:cd02117 7 GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVP-PT---------IDEMLTEDGTAEELRREDllfs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 191 -----NAMVWRGP-----MASKALMQMLQ------ETLWpDLDYLVLDMppgTGD---------IQLTLAQNipvtgaVV 245
Cdd:cd02117 77 gfngvDCVEAGGPepgvgCGGRGIGTMLElleehgLLDD-DYDVVIFDV---LGDvvcggfaapLRRGFAQK------VV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 246 VTTPQDIALIDAKKGIVM----FEKVEVPVLGIVENMsvhicSNCGhhepifGTGGAEKLAEKYHTQLLGQMPLHISLRE 321
Cdd:cd02117 147 IVVSEELMSLYAANNIVKavenYSKNGVRLAGLVANL-----RDPA------GTEEIQAFAAAVGTKILAVIPRDPAVRR 215
|
250 260 270
....*....|....*....|....*....|...
gi 90111388 322 DLDKGtPTVI-----SRPESEFTAIYRQLADRV 349
Cdd:cd02117 216 AELAR-VTVFehdpvSPAASEFARLAAKIADAV 247
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
109-150 |
3.17e-04 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 41.37 E-value: 3.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPS 150
Cdd:PHA02518 2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSS 43
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
109-368 |
3.96e-04 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 41.66 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSsGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQrPTspdgthmapIMSHGLATNSIGYLVT 188
Cdd:pfam00142 2 QIAIY-GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLGGKLQ-PT---------VLDTAREKGYVEDVEV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 189 DD---------NAMVWRGPMASKAL--------MQMLQET-LWPDLDYLVLDMppgTGD---------IQLTLAQNIpvt 241
Cdd:pfam00142 71 EDvvykgyggvKCVESGGPEPGVGCagrgvitaINLLEELgAYDDLDFVLYDV---LGDvvcggfampIREGKAQEI--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 242 gaVVVTTPQDIALIDAK---KGIVMFEKV-EVPVLGIVenmsvhicsnCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHI 317
Cdd:pfam00142 145 --YIVTSNEMMALYAANniaKGIQKYAKSgGVRLGGII----------CNSRKVDDERELIDAFAEELGTQVLHFVPRDN 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90111388 318 SLREDLDKGTPTVISRPESEFTAIYRQLADRVAAQlywQGEVIPGEISFRA 368
Cdd:pfam00142 213 IVRKAELRKQTVIEYAPDSEQAQEYRELARKILEN---PKGTIPTPLSMDE 260
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
109-145 |
4.19e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 41.00 E-value: 4.19e-04
10 20 30
....*....|....*....|....*....|....*..
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
115-365 |
1.39e-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: 39.80 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 115 GKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQrptspdgthmaPIMSHGLATNsiGYLVTDDNAM- 193
Cdd:cd02040 7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKAI-----------PTVLDTLREK--GEVEELEDVIk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 194 -----VW---------------RGPMASkalMQMLQET--LWPDLDYLVLD-----------MPpgtgdIQLTLAQNIpv 240
Cdd:cd02040 74 egfngIKcvesggpepgvgcagRGIITA---INLLEELgaYEEDLDVVFYDvlgdvvcggfaMP-----IREGYADEV-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 241 tgaVVVTTPQDIALIDAK---KGIVMF-EKVEVPVLGIVENMsvhicSNCGHHEPIfgtggAEKLAEKYHTQLLGQMPLH 316
Cdd:cd02040 144 ---YIVTSGEMMALYAANniaKGIVKYaERGGVRLGGLICNS-----RNVDREEEL-----VEEFAERLGTQIIHFVPRS 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 90111388 317 ISLREDLDKGTpTVISR-PESEFTAIYRQLADRVAAQlywQGEVIPGEIS 365
Cdd:cd02040 211 NEVQEAELRGK-TVIEYdPDSEQADEYRELAKKILEN---KKLVIPKPLT 256
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
108-225 |
3.35e-03 |
|
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: 39.32 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGaENQRPTSPD---GTHMAPIMSHGLATNSIG 184
Cdd:TIGR01005 554 NLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFG-KAPKPGLLDllaGEASIEAGIHRDQRPGLA 632
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 90111388 185 YLVTDDNAMVWRGP---MASKALMQMLqETLWPDLDYLVLDMPP 225
Cdd:TIGR01005 633 FIAAGGASHFPHNPnelLANPAMAELI-DNARNAFDLVLVDLAA 675
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
109-224 |
3.70e-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: 38.59 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLgaENQRPTSpDGTHMApimshgLATNSIGYLVT 188
Cdd:pfam09140 2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYF--ENRSATA-DRTGLS------LPTPEHLNLPD 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 90111388 189 DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMP 224
Cdd:pfam09140 73 NDVAEVPDGENIDDARLEEAFADLEARCDFIVIDTP 108
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
108-145 |
4.17e-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: 36.64 E-value: 4.17e-03
10 20 30
....*....|....*....|....*....|....*...
gi 90111388 108 NIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| PRK10818 |
PRK10818 |
septum site-determining protein MinD; |
109-160 |
6.30e-03 |
|
septum site-determining protein MinD;
Pssm-ID: 182756 [Multi-domain] Cd Length: 270 Bit Score: 38.00 E-value: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQ 160
Cdd:PRK10818 4 IIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERR 55
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
109-158 |
8.55e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 37.36 E-value: 8.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 90111388 109 IIAVSSGKGGVGKSSTAVNLALALaaegAKVGILDADIYGPSIPTMLGAE 158
Cdd:cd03110 1 IIAVLSGKGGTGKTTITANLAVLL----YNVILVDCDVDAPNLHLLLGPE 46
|
|
| |
