|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
7-248 |
8.78e-42 |
|
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: 143.46 E-value: 8.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 7 PLIFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIVSSDFLKQNIQSNEI-----KEN 81
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAivpteIPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 82 LDLITFGPSLYGFEPKVALQVIKP--LRAMLKSL--PYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQ 157
Cdd:COG1192 81 LDLIPANIDLAGAEIELVSRPGRElrLKRALAPLadDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 158 LDTIYRIQQQTDSQVQMAGILATM-RDRNNHNKRKLAEIQETYGASVFKTVVPARVVAQDWSEYGIS----EKGSDNSIL 232
Cdd:COG1192 161 LETIEEVREDLNPKLEILGILLTMvDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPvfeyDPKSKGAKA 240
|
250
....*....|....*.
gi 1196942936 233 lnvyYADAFKELMDRV 248
Cdd:COG1192 241 ----YRALAEELLERL 252
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
9-195 |
1.31e-20 |
|
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: 84.51 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQdqikdlllGTentedivSSDFLkqniqsneikenldlitfg 88
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQ--------GS-------LTSWL------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 89 pslygfepkvalqvikplramlkslpYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRIQQQT 168
Cdd:cd02042 48 --------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQL 101
|
170 180
....*....|....*....|....*..
gi 1196942936 169 DSQVQMAGILATMRDRNNHNKRKLAEI 195
Cdd:cd02042 102 NPPLLILGILLTRVDPRTKLAREVLEE 128
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
10-223 |
1.47e-19 |
|
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: 84.32 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 10 FSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQ--------DQIKDLLLGTENTEDIVSSDFLKQNIQSNEIKE- 80
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQsnnssvegLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 81 NLDLITFGPSLYGFEpKVALQVIKP--LRAMLKSL--PYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISE 156
Cdd:pfam01656 81 GLDLIPGNIDLEKFE-KELLGPRKEerLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196942936 157 QLDTIYRIQQ-QTDSQVQMAGILATMRDRNNHNKRKLAEIQET-YGASVFKtVVPARVVAQDWSEYGIS 223
Cdd:pfam01656 160 LGGVIAALVGgYALLGLKIIGVVLNKVDGDNHGKLLKEALEELlRGLPVLG-VIPRDEAVAEAPARGLP 227
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
9-158 |
1.69e-10 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 60.46 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKdLLLGTENTEDIVSSDFLKQNIQSNEIKEN------- 81
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS-ALLGVLPETDVGANETLYAAIRYDDTRRPlrdvirp 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 82 -----LDLITFGPSLYGFE---PKvALQVikplRAMLKSL--------------PYDIIFIDNPPGLQPASLAGIGVADY 139
Cdd:PRK13869 202 tyfdgLHLVPGNLELMEFEhttPK-ALSD----KGTRDGLfftrvaqafdevadDYDVVVIDCPPQLGFLTLSGLCAATS 276
|
170
....*....|....*....
gi 1196942936 140 ALISTQTHHLSVKGISEQL 158
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFL 295
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
9-213 |
3.50e-08 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 52.17 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQdqikdlllGTentedivSSDFlkqniqsNEIKENLDLITF- 87
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQ--------GS-------ALDW-------AAAREDERPFPVv 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 88 ---GPSLYGFEPKVAlqvikplramlksLPYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRI 164
Cdd:NF041546 59 glaRPTLHRELPSLA-------------RDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEA 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196942936 165 QQQTD--------SQVQMAGILAtmrdrnnhnkRKLAEIQETYGASVFKTVVPARVV 213
Cdd:NF041546 126 REYTPglkaafvlNRAIARTALG----------REVAEALAEYGLPVLKTRIGQRVA 172
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
9-158 |
5.64e-07 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 49.98 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKdLLLGTENTEDIVSSDFLKQNIQSNE----IKE---- 80
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-ALFGYQPEFDVGENETLYGAIRYDDerrpISEiirk 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 81 ----NLDLITFGPSLYGFE---PKvALQVIKPLRAM--------LKSLP--YDIIFIDNPPGLQPASLAGIGVADYALIS 143
Cdd:TIGR03453 185 tyfpGLDLVPGNLELMEFEhetPR-ALSRGQGGDTIffarvgeaLAEVEddYDVVVIDCPPQLGFLTLSALCAATGVLIT 263
|
170
....*....|....*
gi 1196942936 144 TQTHHLSVKGISEQL 158
Cdd:TIGR03453 264 VHPQMLDVMSMSQFL 278
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
7-248 |
8.78e-42 |
|
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: 143.46 E-value: 8.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 7 PLIFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIVSSDFLKQNIQSNEI-----KEN 81
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAivpteIPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 82 LDLITFGPSLYGFEPKVALQVIKP--LRAMLKSL--PYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQ 157
Cdd:COG1192 81 LDLIPANIDLAGAEIELVSRPGRElrLKRALAPLadDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 158 LDTIYRIQQQTDSQVQMAGILATM-RDRNNHNKRKLAEIQETYGASVFKTVVPARVVAQDWSEYGIS----EKGSDNSIL 232
Cdd:COG1192 161 LETIEEVREDLNPKLEILGILLTMvDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPvfeyDPKSKGAKA 240
|
250
....*....|....*.
gi 1196942936 233 lnvyYADAFKELMDRV 248
Cdd:COG1192 241 ----YRALAEELLERL 252
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
9-195 |
1.31e-20 |
|
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: 84.51 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQdqikdlllGTentedivSSDFLkqniqsneikenldlitfg 88
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQ--------GS-------LTSWL------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 89 pslygfepkvalqvikplramlkslpYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRIQQQT 168
Cdd:cd02042 48 --------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQL 101
|
170 180
....*....|....*....|....*..
gi 1196942936 169 DSQVQMAGILATMRDRNNHNKRKLAEI 195
Cdd:cd02042 102 NPPLLILGILLTRVDPRTKLAREVLEE 128
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
10-223 |
1.47e-19 |
|
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: 84.32 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 10 FSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQ--------DQIKDLLLGTENTEDIVSSDFLKQNIQSNEIKE- 80
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQsnnssvegLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 81 NLDLITFGPSLYGFEpKVALQVIKP--LRAMLKSL--PYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISE 156
Cdd:pfam01656 81 GLDLIPGNIDLEKFE-KELLGPRKEerLREALEALkeDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196942936 157 QLDTIYRIQQ-QTDSQVQMAGILATMRDRNNHNKRKLAEIQET-YGASVFKtVVPARVVAQDWSEYGIS 223
Cdd:pfam01656 160 LGGVIAALVGgYALLGLKIIGVVLNKVDGDNHGKLLKEALEELlRGLPVLG-VIPRDEAVAEAPARGLP 227
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
9-174 |
1.19e-16 |
|
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: 75.31 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQ---------------DQIKDLLLGTENTEDIVssdflkqni 73
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgnatsglgidknnveKTIYELLIGECNIEEAI--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 74 qSNEIKENLDLITFGPSLYGFEPKVaLQVIKPLRAMLKSLP-----YDIIFIDNPPGLQPASLAGIGVADYALISTQTHH 148
Cdd:pfam13614 74 -IKTVIENLDLIPSNIDLAGAEIEL-IGIENRENILKEALEpvkdnYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEY 151
|
170 180
....*....|....*....|....*.
gi 1196942936 149 LSVKGISEQLDTIYRIQQQTDSQVQM 174
Cdd:pfam13614 152 YALEGLSQLLNTIKLVKKRLNPSLEI 177
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
9-144 |
3.54e-14 |
|
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: 69.54 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIVSSDFLKQNIQSNE--IK----ENL 82
Cdd:cd02036 2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGLRNLDLILGLENRIVYTLVDVLEGECRLEQalIKdkrwENL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196942936 83 DLITFGPSL--YGFEPKVALQVIKPLRAMlkslpYDIIFIDNPPGLQPASLAGIGVADYALIST 144
Cdd:cd02036 82 YLLPASQTRdkDALTPEKLEELVKELKDS-----FDFILIDSPAGIESGFINAIAPADEAIIVT 140
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
4-187 |
2.73e-11 |
|
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: 62.13 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 4 FVEPLIFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLD----QQDQikdlLLGTENTEDIvsSDFLKQNIQSNEI- 78
Cdd:COG0489 89 RLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgpSLHR----MLGLENRPGL--SDVLAGEASLEDVi 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 79 ----KENLDLITFGPSLygfEPKVALQVIKPLRAMLKSL--PYDIIFIDNPPGLQPASLAGIG-VADYALIST---QTHH 148
Cdd:COG0489 163 qpteVEGLDVLPAGPLP---PNPSELLASKRLKQLLEELrgRYDYVIIDTPPGLGVADATLLAsLVDGVLLVVrpgKTAL 239
|
170 180 190
....*....|....*....|....*....|....*....
gi 1196942936 149 LSVKGISEQLDtiyriqqqtDSQVQMAGILATMRDRNNH 187
Cdd:COG0489 240 DDVRKALEMLE---------KAGVPVLGVVLNMVCPKGE 269
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
9-158 |
1.69e-10 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 60.46 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKdLLLGTENTEDIVSSDFLKQNIQSNEIKEN------- 81
Cdd:PRK13869 123 VIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLS-ALLGVLPETDVGANETLYAAIRYDDTRRPlrdvirp 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 82 -----LDLITFGPSLYGFE---PKvALQVikplRAMLKSL--------------PYDIIFIDNPPGLQPASLAGIGVADY 139
Cdd:PRK13869 202 tyfdgLHLVPGNLELMEFEhttPK-ALSD----KGTRDGLfftrvaqafdevadDYDVVVIDCPPQLGFLTLSGLCAATS 276
|
170
....*....|....*....
gi 1196942936 140 ALISTQTHHLSVKGISEQL 158
Cdd:PRK13869 277 MVITVHPQMLDIASMSQFL 295
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
9-145 |
1.03e-09 |
|
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: 57.82 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALS-TISAKRNYETCAMDLDQQ--DQikDLLLGTENTEDIVS---------SDFLKQNIQsn 76
Cdd:COG4963 104 VIAVVGAKGGVGATTLAVNLAwALARESGRRVLLVDLDLQfgDV--ALYLDLEPRRGLADalrnpdrldETLLDRALT-- 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196942936 77 EIKENLDLITFGPSL---YGFEPKVALQVIKPLRAMlkslpYDIIFIDNPPGLQPASLAGIGVADYALISTQ 145
Cdd:COG4963 180 RHSSGLSVLAAPADLeraEEVSPEAVERLLDLLRRH-----FDYVVVDLPRGLNPWTLAALEAADEVVLVTE 246
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
9-223 |
1.81e-09 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 56.01 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIVSsdflkqniqsneikenldLITFG 88
Cdd:PHA02518 2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGEPLIP------------------VVRMG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 89 PSLYGFEPKVALQvikplramlkslpYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRIQQQT 168
Cdd:PHA02518 64 KSIRADLPKVASG-------------YDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVT 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196942936 169 DSQVQMAGILAtmRD-RNNHNKRKLAEIQETYGASVFKTVVPARVVAQDWSEYGIS 223
Cdd:PHA02518 131 DGLPKFAFIIS--RAiKNTQLYREARKALAGYGLPILRNGTTQRVAYADAAEAGGS 184
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
9-144 |
6.34e-09 |
|
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: 54.88 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIvsSDFLKQNIQSNEI----KENLDL 84
Cdd:cd02038 2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLANLDILLGLAPKKTL--GDVLKGRVSLEDIivegPEGLDI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196942936 85 I---TFGPSLYGFEPKVALQVIKPLRAMLksLPYDIIFIDNPPGLQPASLAGIGVADYALIST 144
Cdd:cd02038 80 IpggSGMEELANLDPEQKAKLIEELSSLE--SNYDYLLIDTGAGISRNVLDFLLAADEVIVVT 140
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
9-213 |
3.50e-08 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 52.17 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQdqikdlllGTentedivSSDFlkqniqsNEIKENLDLITF- 87
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQ--------GS-------ALDW-------AAAREDERPFPVv 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 88 ---GPSLYGFEPKVAlqvikplramlksLPYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRI 164
Cdd:NF041546 59 glaRPTLHRELPSLA-------------RDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEA 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196942936 165 QQQTD--------SQVQMAGILAtmrdrnnhnkRKLAEIQETYGASVFKTVVPARVV 213
Cdd:NF041546 126 REYTPglkaafvlNRAIARTALG----------REVAEALAEYGLPVLKTRIGQRVA 172
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
9-158 |
5.64e-07 |
|
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 274585 [Multi-domain] Cd Length: 387 Bit Score: 49.98 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKdLLLGTENTEDIVSSDFLKQNIQSNE----IKE---- 80
Cdd:TIGR03453 106 VIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-ALFGYQPEFDVGENETLYGAIRYDDerrpISEiirk 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 81 ----NLDLITFGPSLYGFE---PKvALQVIKPLRAM--------LKSLP--YDIIFIDNPPGLQPASLAGIGVADYALIS 143
Cdd:TIGR03453 185 tyfpGLDLVPGNLELMEFEhetPR-ALSRGQGGDTIffarvgeaLAEVEddYDVVVIDCPPQLGFLTLSALCAATGVLIT 263
|
170
....*....|....*
gi 1196942936 144 TQTHHLSVKGISEQL 158
Cdd:TIGR03453 264 VHPQMLDVMSMSQFL 278
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
6-146 |
7.09e-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: 48.34 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 6 EPLIFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTENTEDIvsSDFLK------QNIQSNEIk 79
Cdd:cd05387 18 GPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGL--SEVLSgqasleDVIQSTNI- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196942936 80 ENLDLITFGPSLygFEPKVALQvIKPLRAMLKSL--PYDIIFIDNPPGLqpaslagiGVADYALISTQT 146
Cdd:cd05387 95 PNLDVLPAGTVP--PNPSELLS-SPRFAELLEELkeQYDYVIIDTPPVL--------AVADALILAPLV 152
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
9-124 |
1.55e-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: 47.43 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLLGTEN-----TEDIVSSDFLKQNIQSNEIkENLD 83
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNkitglTNFLSGTTDLSDAICDTNI-ENLD 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1196942936 84 LITFGPslygFEPK-VALQVIKPLRAMLKSLP--YDIIFIDNPP 124
Cdd:TIGR01007 98 VITAGP----VPPNpTELLQSSNFKTLIETLRkrFDYIIIDTPP 137
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
23-198 |
2.16e-06 |
|
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: 47.19 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 23 TTVAALSTISAKRNYETCAMDLD-QQDQIkDLLLGTENTEDIvsSDFLKQNIQSNEI----KENLDLITFGPSLYGFEpk 97
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADlGLANL-DVLLGLEPKATL--ADVLAGEADLEDAivqgPGGLDVLPGGSGPAELA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 98 vALQVIKPLRAMLKSL--PYDIIFIDNPPGLQPASLAGIGVADYALISTQTHHLSVKGISEQLDTIYRiqqqtDSQVQMA 175
Cdd:COG0455 76 -ELDPEERLIRVLEELerFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRR-----RLGVRRA 149
|
170 180
....*....|....*....|...
gi 1196942936 176 GILATMRDRNNHNKRKLAEIQET 198
Cdd:COG0455 150 GVVVNRVRSEAEARDVFERLEQV 172
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
9-145 |
1.24e-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: 44.96 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYE-TCAMDLDQQDQIKDLLLGTENTEDIVS---------SDFLKQNIQSneI 78
Cdd:cd03111 2 VVAVVGAKGGVGASTLAVNLAQELAQRAKDkVLLIDLDLPFGDLGLYLNLRPDYDLADviqnldrldRTLLDSAVTR--H 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196942936 79 KENLDLITFGPSLYGFEPKVALQVIKPLRAMLKSlpYDIIFIDNPPGLQPASLAGIGVADYALISTQ 145
Cdd:cd03111 80 SSGLSLLPAPQELEDLEALGAEQVDKLLQVLRAF--YDHIIVDLGHFLDEVTLAVLEAADEILLVTQ 144
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
15-126 |
1.49e-04 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 42.08 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 15 GKGGSGKSTTVAALSTISAKRNYETCAMDLD-------------QQDQIKDLllgTENTEDI------VSSDFLKQNIQS 75
Cdd:COG3640 7 GKGGVGKTTLSALLARYLAEKGKPVLAVDADpnanlaealglevEADLIKPL---GEMRELIkertgaPGGGMFKLNPKV 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196942936 76 NEI-------KENLDLIT------FGPSLYGFEPKValqvikpLRAMLKSL---PYDIIFIDNPPGL 126
Cdd:COG3640 84 DDIpeeylveGDGVDLLVmgtieeGGSGCYCPENAL-------LRALLNHLvlgNYEYVVVDMEAGI 143
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
9-46 |
2.79e-04 |
|
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: 39.34 E-value: 2.79e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDQ 46
Cdd:cd01983 2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
|
|
| Mrp_NBP35 |
cd02037 |
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ... |
9-125 |
5.05e-04 |
|
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: 40.18 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 9 IFSVTNGKGGSGKSTTVAALSTISAKRNYETCAMDLDqqdqikdL-------LLGTENtEDIVSSDFLKQNIQSNEIK-- 79
Cdd:cd02037 2 IIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD-------IygpsiprLLGVEG-KPLHQSEEGIVPVEVGGIKvm 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196942936 80 -------ENLDLITFGPSLYGFepkvalqvikpLRAMLKSLPY---DIIFIDNPPG 125
Cdd:cd02037 74 sigfllpEDDAVIWRGPMKSGA-----------IKQFLKDVDWgelDYLIIDLPPG 118
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
15-127 |
2.36e-03 |
|
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.
Pssm-ID: 349754 [Multi-domain] Cd Length: 249 Bit Score: 38.45 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 15 GKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIkDLLLGTENTEDIVSS------------------DFLKQ---NI 73
Cdd:cd02034 7 GKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNL-AETLGVEVEKLPLIKtigdirertgakkgeppeGMSLNpyvDD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 74 QSNEI---KENLDLITFGPSlYGFEPKVALQVIKPLRAMLKSL---PYDIIFIDNPPGLQ 127
Cdd:cd02034 86 IIKEIivePDGIDLLVMGRP-EGGGSGCYCPVNALLRELLRHLalkNYEYVVIDMEAGIE 144
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
15-127 |
2.95e-03 |
|
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.
Pssm-ID: 349755 [Multi-domain] Cd Length: 250 Bit Score: 38.26 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 15 GKGGSGKSTTVAALSTISAKRNYETCAMDLDQQDQIKDLLlgtenteDIVSSDFLKQNIQSNeikenldlitfgpsLYGF 94
Cdd:cd02035 7 GKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAF-------GQKLGGETPVKGAPN--------------LWAM 65
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1196942936 95 E--PKVAL-----QVIKPLRAMLKSLPYDIIFID---NPPGLQ 127
Cdd:cd02035 66 EidPEEALeeyweEVKELLAQYLRLPGLDEVYAEellSLPGMD 108
|
|
| ArsA |
COG0003 |
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism]; |
1-127 |
5.70e-03 |
|
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
Pssm-ID: 439774 Cd Length: 299 Bit Score: 37.49 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196942936 1 MPKFVeplIFSvtnGKGGSGKSTTVAALSTISAKRNYETcamdldqqdqikdLLLGTenteDIVSS--DFLKQNIqSNEI 78
Cdd:COG0003 2 MTRII---FFT---GKGGVGKTTVAAATALALAERGKRT-------------LLVST----DPAHSlgDVLGTEL-GNEP 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196942936 79 KEnldlITfGPSLYGFE--PKVALQ-----VIKPLRAMLKSLPYDIIfIDNPPGLQ 127
Cdd:COG0003 58 TE----VA-VPNLYALEidPEAELEeywerVRAPLRGLLPSAGVDEL-AESLPGTE 107
|
|
| |
