|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
97-342 |
1.74e-139 |
|
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.
Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 396.05 E-value: 1.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 97 GVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKWfVPLEAHGVQVMSM 176
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGL-EGERPEQSDGGI-IPVEAHGIKVMSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 177 AFLTDD-NTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKKGVE 255
Cdd:pfam10609 79 GFLLPDeDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAID 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 256 MFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADPESQIAMIY 335
Cdd:pfam10609 159 MFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAF 238
|
....*..
gi 1252870960 336 QDLARKV 342
Cdd:pfam10609 239 LKIADKV 245
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
6-360 |
7.55e-133 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 384.01 E-value: 7.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 6 REAVEACLRQFTDPHLDQDPVSAGCLREVDIQGARVTVRLELGYAaglFKNGWAQM---LQMALENLDGVDSAQVKVDCV 82
Cdd:PRK11670 14 RAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFV---WNSAFEELkeqCSAELLRITGAKAIDWKLSHN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 83 IDSHQGQAQVPALAGVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGiAEGTRPQVKDQKW 162
Cdd:PRK11670 91 IATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLG-AEDQRPTSPDGTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 163 FVPLEAHGVQVMSMAFLTDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTP 242
Cdd:PRK11670 170 MAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 243 QDLALLDAKKGVEMFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPT 322
Cdd:PRK11670 250 QDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPT 329
|
330 340 350
....*....|....*....|....*....|....*...
gi 1252870960 323 TIADPESQIAMIYQDLARKVGARIAQAGKpAMPSiEIS 360
Cdd:PRK11670 330 VVSRPESEFTAIYRQLADRVAAQLYWQGE-VIPG-EIS 365
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
100-314 |
7.35e-111 |
|
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: 322.14 E-value: 7.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKWfVPLEAHGVQVMSMAFL 179
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGV-EGKPLHQSEEGI-VPVEVGGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 180 TDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKKGVEMFRK 259
Cdd:cd02037 79 LPEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1252870960 260 VHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRM 314
Cdd:cd02037 159 LNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
95-342 |
2.45e-89 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 272.85 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 95 LAGVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKwFVPLEAH-GVQV 173
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGL-EGKRLGSEDEG-ILPVEYSdNLKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 174 MSMAF-LTDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKK 252
Cdd:NF041136 79 MSIGFlLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 253 GVEMFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADPESQIA 332
Cdd:NF041136 159 SINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAA 238
|
250
....*....|
gi 1252870960 333 MIYQDLARKV 342
Cdd:NF041136 239 KALEKIVDPI 248
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
101-290 |
4.15e-48 |
|
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: 164.20 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIAEGT------RPQVKDQKWFVPLEAHGVQVM 174
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPglsdvlAGEASLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 175 SMAFLTDDNTpmvwrGPMVSGALLQLITQTAwNDLDYLVVDMPPGTGDIQLTLAQKVpVAGSVIVTTPQDLALLDAKKGV 254
Cdd:COG0489 174 PAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 1252870960 255 EMFRKVHIPVLGVVENMAvhicsnCGHAEHLFGEGG 290
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
101-342 |
8.80e-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: 73.23 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRP----------QVKDQKWFVPleaHG 170
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGM-EDKPVtlhdvlageaDIKDAIYEGP---FG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 171 VQVMSMAfltddntpMVWRGPMVSGA--LLQLITQTAwNDLDYLVVDMPPGtgdIQLTLAQKVPVA-GSVIVTTPQDLAL 247
Cdd:TIGR01969 78 VKVIPAG--------VSLEGLRKADPdkLEDVLKEII-DDTDFLLIDAPAG---LERDAVTALAAAdELLLVVNPEISSI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 248 LDAKKGVEMFRKVHIPVLGVVENmavhicsncgHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADP 327
Cdd:TIGR01969 146 TDALKTKIVAEKLGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNP 215
|
250
....*....|....*
gi 1252870960 328 ESQIAMIYQDLARKV 342
Cdd:TIGR01969 216 NSPAAQAFMELAAEL 230
|
|
| FeS_assembly_P |
pfam01883 |
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 ... |
6-79 |
1.73e-13 |
|
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF), PaaI (PhaG) and PaaK (PhaI), which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid. It also includes PaaD from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialized proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS). SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins. Given all this data, it is hypothesized that this domain might play a role in FeS cluster assembly.
Pssm-ID: 460370 Cd Length: 73 Bit Score: 64.96 E-value: 1.73e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252870960 6 REAVEACLRQFTDPHLDQDPVSAGCLREVDIQGARVTVRLELGYAAGLFKNGWAQMLQMALENLDGVDsAQVKV 79
Cdd:pfam01883 1 KAAVLAALRTVIDPETGVDLVSLGLVRNIDIEGGKVSVDITLTYPACPAAEAIRADAEAALRALPGEV-VEVSV 73
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
101-137 |
4.40e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 41.00 E-value: 4.40e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
|
|
| PaaD |
COG2151 |
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, ... |
2-80 |
7.08e-03 |
|
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441754 Cd Length: 102 Bit Score: 35.85 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 2 SAVTREAVEACLRQFTDPHLDQDPVSAGCLREVDI-QGARVTVRLELGY----AAGLFkngwAQMLQMALENLDGVDSAQ 76
Cdd:COG2151 5 AEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVdDDGRVKVTMTLTTpgcpAADVI----PDDVEEALEEVPGVEDVE 80
|
....
gi 1252870960 77 VKVD 80
Cdd:COG2151 81 VELV 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
pfam10609 |
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ... |
97-342 |
1.74e-139 |
|
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.
Pssm-ID: 431392 [Multi-domain] Cd Length: 246 Bit Score: 396.05 E-value: 1.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 97 GVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKWfVPLEAHGVQVMSM 176
Cdd:pfam10609 1 GVKHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDADIYGPSIPRMLGL-EGERPEQSDGGI-IPVEAHGIKVMSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 177 AFLTDD-NTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKKGVE 255
Cdd:pfam10609 79 GFLLPDeDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLPLTGAVIVTTPQDVALLDVRKAID 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 256 MFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADPESQIAMIY 335
Cdd:pfam10609 159 MFKKVNVPVLGVVENMSYFVCPHCGEETYIFGKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPAAKAF 238
|
....*..
gi 1252870960 336 QDLARKV 342
Cdd:pfam10609 239 LKIADKV 245
|
|
| PRK11670 |
PRK11670 |
iron-sulfur cluster carrier protein ApbC; |
6-360 |
7.55e-133 |
|
iron-sulfur cluster carrier protein ApbC;
Pssm-ID: 183270 [Multi-domain] Cd Length: 369 Bit Score: 384.01 E-value: 7.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 6 REAVEACLRQFTDPHLDQDPVSAGCLREVDIQGARVTVRLELGYAaglFKNGWAQM---LQMALENLDGVDSAQVKVDCV 82
Cdd:PRK11670 14 RAMVAGTLANFQHPTLKHNLTTLKALHHVALLDDTLHIELVMPFV---WNSAFEELkeqCSAELLRITGAKAIDWKLSHN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 83 IDSHQGQAQVPALAGVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGiAEGTRPQVKDQKW 162
Cdd:PRK11670 91 IATLKRVNNQPGVNGVKNIIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLG-AEDQRPTSPDGTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 163 FVPLEAHGVQVMSMAFLTDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTP 242
Cdd:PRK11670 170 MAPIMAHGLATNSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPVTGAVVVTTP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 243 QDLALLDAKKGVEMFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPT 322
Cdd:PRK11670 250 QDIALIDAKKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFGTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPT 329
|
330 340 350
....*....|....*....|....*....|....*...
gi 1252870960 323 TIADPESQIAMIYQDLARKVGARIAQAGKpAMPSiEIS 360
Cdd:PRK11670 330 VVSRPESEFTAIYRQLADRVAAQLYWQGE-VIPG-EIS 365
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
100-314 |
7.35e-111 |
|
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: 322.14 E-value: 7.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKWfVPLEAHGVQVMSMAFL 179
Cdd:cd02037 1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGPSIPRLLGV-EGKPLHQSEEGI-VPVEVGGIKVMSIGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 180 TDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKKGVEMFRK 259
Cdd:cd02037 79 LPEDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLIPIDGAVVVTTPQEVSLIDVRKAIDMCKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1252870960 260 VHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRM 314
Cdd:cd02037 159 LNIPVLGIVENMSGFVCPHCGKKIYIFGKGGGEKLAEELGVPFLGKIPLDPELAK 213
|
|
| MrpORP |
NF041136 |
iron-sulfur cluster carrier protein MrpORP; |
95-342 |
2.45e-89 |
|
iron-sulfur cluster carrier protein MrpORP;
Pssm-ID: 469059 [Multi-domain] Cd Length: 365 Bit Score: 272.85 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 95 LAGVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRPQVKDQKwFVPLEAH-GVQV 173
Cdd:NF041136 1 LSRIKHKILVMSGKGGVGKSTVAANLAVALARRGYKVGLLDVDIHGPSIPKLLGL-EGKRLGSEDEG-ILPVEYSdNLKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 174 MSMAF-LTDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVVDMPPGTGDIQLTLAQKVPVAGSVIVTTPQDLALLDAKK 252
Cdd:NF041136 79 MSIGFlLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIPDAGAVIVTTPQELALADVRK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 253 GVEMFRKVHIPVLGVVENMAVHICSNCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADPESQIA 332
Cdd:NF041136 159 SINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFKSGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAWSPAA 238
|
250
....*....|
gi 1252870960 333 MIYQDLARKV 342
Cdd:NF041136 239 KALEKIVDPI 248
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
101-290 |
4.15e-48 |
|
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: 164.20 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIAEGT------RPQVKDQKWFVPLEAHGVQVM 174
Cdd:COG0489 94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRPglsdvlAGEASLEDVIQPTEVEGLDVL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 175 SMAFLTDDNTpmvwrGPMVSGALLQLITQTAwNDLDYLVVDMPPGTGDIQLTLAQKVpVAGSVIVTTPQDLALLDAKKGV 254
Cdd:COG0489 174 PAGPLPPNPS-----ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLLASL-VDGVLLVVRPGKTALDDVRKAL 246
|
170 180 190
....*....|....*....|....*....|....*.
gi 1252870960 255 EMFRKVHIPVLGVVENMAvhicsnCGHAEHLFGEGG 290
Cdd:COG0489 247 EMLEKAGVPVLGVVLNMV------CPKGERYYGGGE 276
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
101-342 |
8.80e-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: 73.23 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIaEGTRP----------QVKDQKWFVPleaHG 170
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGM-EDKPVtlhdvlageaDIKDAIYEGP---FG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 171 VQVMSMAfltddntpMVWRGPMVSGA--LLQLITQTAwNDLDYLVVDMPPGtgdIQLTLAQKVPVA-GSVIVTTPQDLAL 247
Cdd:TIGR01969 78 VKVIPAG--------VSLEGLRKADPdkLEDVLKEII-DDTDFLLIDAPAG---LERDAVTALAAAdELLLVVNPEISSI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 248 LDAKKGVEMFRKVHIPVLGVVENmavhicsncgHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIADP 327
Cdd:TIGR01969 146 TDALKTKIVAEKLGTAILGVVLN----------RVTRDKTELGREEIETILEVPVLGVVPEDPEVRRAAAFGEPVVIYNP 215
|
250
....*....|....*
gi 1252870960 328 ESQIAMIYQDLARKV 342
Cdd:TIGR01969 216 NSPAAQAFMELAAEL 230
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
101-347 |
1.36e-13 |
|
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: 69.89 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADiygpSQG---IMFGIAEGTRPQ-----VKDQKWF----VPLEA 168
Cdd:COG1192 3 VIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLD----PQGnltSGLGLDPDDLDPtlydlLLDDAPLedaiVPTEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 169 HGVQVM----SMAFLTDDNTPMVWRGPMVSGALLQLitqtaWNDLDYLVVDMPPGTGDIQ---LTLAQKVpvagsVIVTT 241
Cdd:COG1192 79 PGLDLIpaniDLAGAEIELVSRPGRELRLKRALAPL-----ADDYDYILIDCPPSLGLLTlnaLAAADSV-----LIPVQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 242 PQDLALLDAKKGVEMFRKV------HIPVLGVVENMavHICSNCGHAEHLfgegggEKLAAQYGVELL-ASLPLSMAIRM 314
Cdd:COG1192 149 PEYLSLEGLAQLLETIEEVredlnpKLEILGILLTM--VDPRTRLSREVL------EELREEFGDKVLdTVIPRSVALAE 220
|
250 260 270
....*....|....*....|....*....|...
gi 1252870960 315 QADDGKPTTIADPESQIAMIYQDLARKVGARIA 347
Cdd:COG1192 221 APSAGKPVFEYDPKSKGAKAYRALAEELLERLE 253
|
|
| FeS_assembly_P |
pfam01883 |
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 ... |
6-79 |
1.73e-13 |
|
Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF), PaaI (PhaG) and PaaK (PhaI), which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid. It also includes PaaD from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialized proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS). SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins. Given all this data, it is hypothesized that this domain might play a role in FeS cluster assembly.
Pssm-ID: 460370 Cd Length: 73 Bit Score: 64.96 E-value: 1.73e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252870960 6 REAVEACLRQFTDPHLDQDPVSAGCLREVDIQGARVTVRLELGYAAGLFKNGWAQMLQMALENLDGVDsAQVKV 79
Cdd:pfam01883 1 KAAVLAALRTVIDPETGVDLVSLGLVRNIDIEGGKVSVDITLTYPACPAAEAIRADAEAALRALPGEV-VEVSV 73
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
100-250 |
4.53e-13 |
|
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: 67.98 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIA---------EGtrpQVKDQKWFVPLEAH- 169
Cdd:cd02038 1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLApkktlgdvlKG---RVSLEDIIVEGPEGl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 170 -----GVQVMSMAFLTddntpmvwrgpmvSGALLQLIT--QTAWNDLDYLVVDMPPGTGD--IQLTLAQKVPvagsVIVT 240
Cdd:cd02038 78 diipgGSGMEELANLD-------------PEQKAKLIEelSSLESNYDYLLIDTGAGISRnvLDFLLAADEV----IVVT 140
|
170
....*....|
gi 1252870960 241 TPQDLALLDA 250
Cdd:cd02038 141 TPEPTSITDA 150
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
89-356 |
1.67e-12 |
|
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: 67.83 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 89 QAQVPALAGVKNVIAVASGKGGVGKSTTAANLALALARE-GARVGILDADIYGPSQGIMFG------IAEGTR-PQVKDQ 160
Cdd:COG4963 92 RLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQFGDVALYLDleprrgLADALRnPDRLDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 161 KWF---VPLEAHGVQVMSMaflTDDNTPMVWRGPMVSGALLQLITQTAwndlDYLVVDMPPGTGDIQLTLAQKvpvAGSV 237
Cdd:COG4963 172 TLLdraLTRHSSGLSVLAA---PADLERAEEVSPEAVERLLDLLRRHF----DYVVVDLPRGLNPWTLAALEA---ADEV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 238 IVTTPQDLA-LLDAKKGVEMFRKVHIPV--LGVVENMAvhicsncghaeHLFGEGGGEKLAAQYGVELLASLPLSMAIRM 314
Cdd:COG4963 242 VLVTEPDLPsLRNAKRLLDLLRELGLPDdkVRLVLNRV-----------PKRGEISAKDIEEALGLPVAAVLPNDPKAVA 310
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1252870960 315 QA-DDGKPTTIADPESQIAMIYQDLARKVGARIAQAGKPAMPS 356
Cdd:COG4963 311 EAaNQGRPLAEVAPKSPLAKAIRKLAARLTGRPAAAAAKAGGK 353
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
126-342 |
2.06e-12 |
|
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: 66.07 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 126 REGARVGILDADIYGPSQGIMFGIAEGT--------RPQVKDqkwFVPLEAHGVQVMSMafltdDNTPMVWRGPMVSGAL 197
Cdd:COG0455 12 RLGKRVLLVDADLGLANLDVLLGLEPKAtladvlagEADLED---AIVQGPGGLDVLPG-----GSGPAELAELDPEERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 198 LQLITQTAwNDLDYLVVDMPPGTGDI---QLTLAQKVpvagsVIVTTPQDLALLDAKKGVEMFRKVH-IPVLGVVENMAV 273
Cdd:COG0455 84 IRVLEELE-RFYDVVLVDTGAGISDSvllFLAAADEV-----VVVTTPEPTSITDAYALLKLLRRRLgVRRAGVVVNRVR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252870960 274 HIcsncGHAEHLFgegggEKLAA------QYGVELLASLPLSMAIRMQADDGKPTTIADPESQIAMIYQDLARKV 342
Cdd:COG0455 158 SE----AEARDVF-----ERLEQvaerflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAARL 223
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
102-271 |
1.26e-11 |
|
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: 63.52 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 102 IAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGP---SQGIMFGI-------AEGTRPQVKDQKWFV--PLEAH 169
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNnssVEGLEGDIapalqalAEGLKGRVNLDPILLkeKSDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 170 GVQVMSMAFL--TDDNTPMVWRGPMVSGALLQLITQTAwndlDYLVVDMPPGTGDiqLTLAQKVPVAGSVIVTTPQDLAL 247
Cdd:pfam01656 81 GLDLIPGNIDleKFEKELLGPRKEERLREALEALKEDY----DYVIIDGAPGLGE--LLRNALIAADYVIIPLEPEVILV 154
|
170 180 190
....*....|....*....|....*....|.
gi 1252870960 248 LDAKKGVEMFRKV-------HIPVLGVVENM 271
Cdd:pfam01656 155 EDAKRLGGVIAALvggyallGLKIIGVVLNK 185
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
100-342 |
1.69e-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: 54.52 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFG------------IAEGTRPQ---VKDQKWfv 164
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGlenrivytlvdvLEGECRLEqalIKDKRW-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 165 pleaHGVQVMSMAFLTDDNtpmvwrgpMVSGALLQLITQTAWNDLDYLVVDMPPGtgdIQLTLAQKV-PVAGSVIVTTPQ 243
Cdd:cd02036 79 ----ENLYLLPASQTRDKD--------ALTPEKLEELVKELKDSFDFILIDSPAG---IESGFINAIaPADEAIIVTNPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 244 DLALLDAKKgvemfrkvhipVLGVVENMAVHIcsncghaEHL----FGEG---GGEKLAAQ-----YGVELLASLPLSMA 311
Cdd:cd02036 144 ISSVRDADR-----------VIGLLESKGIVN-------IGLivnrYRPEmvkSGDMLSVEdiqeiLGIPLLGVIPEDPE 205
|
250 260 270
....*....|....*....|....*....|.
gi 1252870960 312 IRMQADDGKPTTIADPESQIAMIYQDLARKV 342
Cdd:cd02036 206 VIVATNRGEPLVLYKPNSLAAKAFENIARRL 236
|
|
| minD |
CHL00175 |
septum-site determining protein; Validated |
95-252 |
5.48e-07 |
|
septum-site determining protein; Validated
Pssm-ID: 214385 [Multi-domain] Cd Length: 281 Bit Score: 50.54 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 95 LAGVKNVIAVASGKGGVGKSTTAANLALALAREGARVGILDADI--------YGPSQGIMFG---IAEG----TRPQVKD 159
Cdd:CHL00175 11 SATMSRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIglrnldllLGLENRVLYTamdVLEGecrlDQALIRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 160 QKWfvpleahgvqvMSMAFLTDDNTPMvwRGPMVSGALLQLITQTAWNDLDYLVVDMPPGtgdIQLTLAQKV-PVAGSVI 238
Cdd:CHL00175 91 KRW-----------KNLSLLAISKNRQ--RYNVTRKNMNMLVDSLKNRGYDYILIDCPAG---IDVGFINAIaPAQEAIV 154
|
170
....*....|....
gi 1252870960 239 VTTPQDLALLDAKK 252
Cdd:CHL00175 155 VTTPEITAIRDADR 168
|
|
| minD_bact |
TIGR01968 |
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ... |
100-342 |
8.89e-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: 49.64 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADI--------YGPSQGIMF---GIAEGT-RPQ---VKDQKWfv 164
Cdd:TIGR01968 2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIglrnldllLGLENRIVYtlvDVVEGEcRLQqalIKDKRL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 165 pleaHGVQVMSMAFLTDDNtpmvwrgpMVSGALLQLITQTAWNDLDYLVVDMPPGtgdIQLTLAQKV-PVAGSVIVTTPQ 243
Cdd:TIGR01968 80 ----KNLYLLPASQTRDKD--------AVTPEQMKKLVNELKEEFDYVIIDCPAG---IESGFRNAVaPADEAIVVTTPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 244 DLALLDAKKgvemfrkvhipVLGVVENMA---VHICSNCGHAEHLfgeGGGEKLAAQ-----YGVELLASLPLSMAIRMQ 315
Cdd:TIGR01968 145 VSAVRDADR-----------VIGLLEAKGiekIHLIVNRLRPEMV---KKGDMLSVDdvleiLSIPLIGVIPEDEAIIVS 210
|
250 260
....*....|....*....|....*..
gi 1252870960 316 ADDGKPtTIADPESQIAMIYQDLARKV 342
Cdd:TIGR01968 211 TNKGEP-VVLNDKSRAGKAFENIARRI 236
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
100-270 |
6.41e-06 |
|
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: 46.41 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIA--EGTRPQVKDQkwfvPLEAHGVQVMS-- 175
Cdd:cd05387 20 KVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPnePGLSEVLSGQ----ASLEDVIQSTNip 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 176 -MAFLTddntpmvwRGPmVSGALLQLITQTAWNDL--------DYLVVDMPP--GTGDIQLtLAQKvpVAGSVIVT---- 240
Cdd:cd05387 96 nLDVLP--------AGT-VPPNPSELLSSPRFAELleelkeqyDYVIIDTPPvlAVADALI-LAPL--VDGVLLVVragk 163
|
170 180 190
....*....|....*....|....*....|
gi 1252870960 241 TPQDlallDAKKGVEMFRKVHIPVLGVVEN 270
Cdd:cd05387 164 TRRR----EVKEALERLEQAGAKVLGVVLN 189
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
96-270 |
1.16e-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: 45.51 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 96 AGVKnVIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFgiaegtrpqvKDQKWFVPLEAH--GVQV 173
Cdd:TIGR01007 15 AEIK-VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTF----------KSQNKITGLTNFlsGTTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 174 MSMAfLTDDNTP---MVWRGPMVSG--ALLQ-----LITQTAWNDLDYLVVDMPP-GT-GDIQLtLAQKvpVAGSVIVTT 241
Cdd:TIGR01007 84 LSDA-ICDTNIEnldVITAGPVPPNptELLQssnfkTLIETLRKRFDYIIIDTPPiGTvTDAAI-IARA--CDASILVTD 159
|
170 180
....*....|....*....|....*....
gi 1252870960 242 PQDLALLDAKKGVEMFRKVHIPVLGVVEN 270
Cdd:TIGR01007 160 AGKIKKREVKKAKEQLEQAGSNFLGVVLN 188
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
101-137 |
1.19e-05 |
|
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: 44.45 E-value: 1.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLD 38
|
|
| eps_transp_fam |
TIGR01005 |
exopolysaccharide transport protein family; The model describes the exopolysaccharide ... |
94-270 |
5.17e-05 |
|
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: 45.10 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 94 ALAGVKN-VIAVASGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGIAEgtRPQVKD-----QKWfvPLE 167
Cdd:TIGR01005 547 ALADAENnLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAP--KPGLLDllageASI--EAG 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 168 AHGVQVMSMAFLTDDNTPMVWRGP---MVSGALLQLItQTAWNDLDYLVVDMPPgtgdiqltlaqKVPVAGSVIVTTPQD 244
Cdd:TIGR01005 623 IHRDQRPGLAFIAAGGASHFPHNPnelLANPAMAELI-DNARNAFDLVLVDLAA-----------LAAVADAAAFAALAD 690
|
170 180 190
....*....|....*....|....*....|....*.
gi 1252870960 245 LALLDAKKGVEMFRKV----------HIPVLGVVEN 270
Cdd:TIGR01005 691 GILFVTEFERSPLGEIrdlihqephaNSDVLGVIFN 726
|
|
| NifH-like |
cd02117 |
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ... |
107-361 |
7.15e-05 |
|
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: 43.89 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 107 GKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFG------IAEGTRPQVKDQ----KWFVPLEAHGVQVMSm 176
Cdd:cd02117 7 GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGgkvpptIDEMLTEDGTAEelrrEDLLFSGFNGVDCVE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 177 aflTDDNTPMVWRGPMVSGALLQLITQTAWNDLDYLVV--DMppgTGD---------IQLTLAQKVpvagsVIVTTPQDL 245
Cdd:cd02117 86 ---AGGPEPGVGCGGRGIGTMLELLEEHGLLDDDYDVVifDV---LGDvvcggfaapLRRGFAQKV-----VIVVSEELM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 246 ALLDAK---KGVEMFRKVHIPVLGVVENMavhicSNCGHAEHLfgegggEKLAAQYGVELLASLPLSMAIRMQADDGKPT 322
Cdd:cd02117 155 SLYAANnivKAVENYSKNGVRLAGLVANL-----RDPAGTEEI------QAFAAAVGTKILAVIPRDPAVRRAELARVTV 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1252870960 323 TIADPESQIAMIYQDLARKV-GARIAQAGKPAMPSIEISE 361
Cdd:cd02117 224 FEHDPVSPAASEFARLAAKIaDAVPPVPGPRPLSDRELFA 263
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
101-138 |
2.69e-04 |
|
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442139 [Multi-domain] Cd Length: 258 Bit Score: 41.97 E-value: 2.69e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADI 138
Cdd:COG2894 4 VIVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDADI 41
|
|
| Fer4_NifH |
pfam00142 |
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family; |
107-362 |
2.86e-04 |
|
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
Pssm-ID: 395090 Cd Length: 271 Bit Score: 42.05 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 107 GKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMF-GIAEGT---RPQVKDQKWFVPLEAHGVQVMSMAFLTDD 182
Cdd:pfam00142 7 GKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKADSTRLLLgGKLQPTvldTAREKGYVEDVEVEDVVYKGYGGVKCVES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 183 NTPMVWRGPMVSG---ALLQLITQTAWNDLDYLVVDMppgTGD---------IQLTLAQKVpvagsVIVTTPQDLALLDA 250
Cdd:pfam00142 87 GGPEPGVGCAGRGvitAINLLEELGAYDDLDFVLYDV---LGDvvcggfampIREGKAQEI-----YIVTSNEMMALYAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 251 K---KGVEMFRKVH-IPVLGVVenmavhicsnCGHAEHLFGEGGGEKLAAQYGVELLASLPLSMAIRMQADDGKPTTIAD 326
Cdd:pfam00142 159 NniaKGIQKYAKSGgVRLGGII----------CNSRKVDDERELIDAFAEELGTQVLHFVPRDNIVRKAELRKQTVIEYA 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 1252870960 327 PESQIAMIYQDLARKvgarIAQAGKPAMPSiEISED 362
Cdd:pfam00142 229 PDSEQAQEYRELARK----ILENPKGTIPT-PLSMD 259
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
101-137 |
4.40e-04 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 41.00 E-value: 4.40e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDAD 37
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
101-340 |
5.96e-04 |
|
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: 40.72 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAA-NLALALAREGARVGILDADIY----------GPSQGIMFGIAEGTRpqVKDQKWFVPLEAH 169
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVnLAQELAQRAKDKVLLIDLDLPfgdlglylnlRPDYDLADVIQNLDR--LDRTLLDSAVTRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 170 --GVQVMSMAFLTDDNTPMvwRGPMVSgALLQLITQTawndLDYLVVDMPPGTGDIQLTLAQKvpvAGSVIVTTPQDL-A 246
Cdd:cd03111 80 ssGLSLLPAPQELEDLEAL--GAEQVD-KLLQVLRAF----YDHIIVDLGHFLDEVTLAVLEA---ADEILLVTQQDLpS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 247 LLDAKKGVEMFRKVHIPvlgvveNMAVHICSNCghaehlFGEGGG---EKLAAQYGVELLASLPLSMAIRMQA-DDGKPT 322
Cdd:cd03111 150 LRNARRLLDSLRELEGS------SDRLRLVLNR------YDKKSEispKDIEEALGLEVFATLPNDYKAVSESaNTGRPL 217
|
250
....*....|....*...
gi 1252870960 323 TIADPESQIAMIYQDLAR 340
Cdd:cd03111 218 VEVAPRSALVRALQDLAA 235
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
101-306 |
1.23e-03 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 39.83 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDADiygpsqgimfgiaegtrPQVKDQKWFVPLEAhgvqvmsmaflT 180
Cdd:PHA02518 2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLD-----------------PQGSSTDWAEAREE-----------G 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 181 DDNTPMVWRGPMVSGALLQLITQtawndLDYLVVDmppGTGDIQLTLAQKVPVAGSVIVTT---PQDL-ALLDAKKGVEM 256
Cdd:PHA02518 54 EPLIPVVRMGKSIRADLPKVASG-----YDYVVVD---GAPQDSELARAALRIADMVLIPVqpsPFDIwAAPDLVELIKA 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1252870960 257 FRKVH--IPVLGVVENMAVhicsncgHAEHLFGEggGEKLAAQYGVELLASL 306
Cdd:PHA02518 126 RQEVTdgLPKFAFIISRAI-------KNTQLYRE--ARKALAGYGLPILRNG 168
|
|
| BchX |
cd02033 |
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ... |
75-343 |
2.06e-03 |
|
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.
Pssm-ID: 349753 Cd Length: 329 Bit Score: 39.81 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 75 AQVKVDCVIDSHQGQAQVPAlAGVKNVIAVaSGKGGVGKSTTAANLALALAREGARVGILDADIYGPSQGIMFGiaEGTR 154
Cdd:cd02033 8 ARLRDEAAIEPSLEIPTGPP-TKETQIIAI-YGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSDTTSLLFG--GKAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 155 PQVKDQKWFVPLEAHGVQVMSMAFLTDDNTPMVWRGPMVSGA-----------LLQLITQTAWnDLDYLVVDMppgTGD- 222
Cdd:cd02033 84 PTIIETSTRKKLAGEEVKIGDVCFKRGGVFAMELGGPEVGRGcggrgiihgfeLLEKLGFHDW-GFDYVLLDF---LGDv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 223 --------IQLTLAQKVPVAGSvivttpQDLALL----DAKKGVEMFRKV--HIPVLGVVENMAVhicsncghaehlfGE 288
Cdd:cd02033 160 vcggfglpIARDMCQKVIVVGS------NDLQSLyvanNVCSAVEYFRKLggNVGVAGIVINKDD-------------GT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1252870960 289 GGGEKLAAQYGVELLASLPLSMAIRMQADDGKptTIADPESQIAMIYQDLARKVG 343
Cdd:cd02033 221 GEAQAFAKAAGIPVLAAIPADEDIRRKSANYQ--IVGRPETQWGPLFAELATNVA 273
|
|
| MipZ |
pfam09140 |
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ... |
101-137 |
2.65e-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: 38.97 E-value: 2.65e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:pfam09140 2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
101-137 |
4.32e-03 |
|
AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.
Pssm-ID: 433350 [Multi-domain] Cd Length: 177 Bit Score: 37.56 E-value: 4.32e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1252870960 101 VIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLD 39
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
100-137 |
4.41e-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: 4.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1252870960 100 NVIAVASGKGGVGKSTTAANLALALAREGARVGILDAD 137
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| PaaD |
COG2151 |
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, ... |
2-80 |
7.08e-03 |
|
Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441754 Cd Length: 102 Bit Score: 35.85 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252870960 2 SAVTREAVEACLRQFTDPHLDQDPVSAGCLREVDI-QGARVTVRLELGY----AAGLFkngwAQMLQMALENLDGVDSAQ 76
Cdd:COG2151 5 AEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVdDDGRVKVTMTLTTpgcpAADVI----PDDVEEALEEVPGVEDVE 80
|
....
gi 1252870960 77 VKVD 80
Cdd:COG2151 81 VELV 84
|
|
| |
