|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
4-294 |
1.60e-49 |
|
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: 164.65 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTDLLLktfkennnallneimnsnnfesvLDEKENEil 83
Cdd:COG1192 3 VIAVANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG-----------------------LDPDDLD-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 84 dlllrkstdineNDLYHTLKEKKPIHEAIIELS-DNLSIIPSDFNMIGypylLEDLKLNRIDGAKYFNSFLEEVKKDYDY 162
Cdd:COG1192 57 ------------PTLYDLLLDDAPLEDAIVPTEiPGLDLIPANIDLAG----AEIELVSRPGRELRLKRALAPLADDYDY 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 163 ILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDVIGILPVMFKKQGKIDSFILSLLQ 242
Cdd:COG1192 121 ILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELR 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 517997210 243 HVYGSYVFKNKVFQRERVKFWDTTGIANEDMHDRNVLAM-YESITNELLEKMR 294
Cdd:COG1192 201 EEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKaYRALAEELLERLE 253
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
2-219 |
1.10e-29 |
|
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: 110.75 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 2 TEVVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTdlllktfkennnallneimnsnnfesvldekene 81
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNAT---------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 82 ildLLLRKSTDINENDLYHTLKEKKPIHEAIIELS-DNLSIIPSDFNMIGYPYLLEDLKLNRIdgakYFNSFLEEVKKDY 160
Cdd:pfam13614 46 ---SGLGIDKNNVEKTIYELLIGECNIEEAIIKTViENLDLIPSNIDLAGAEIELIGIENREN----ILKEALEPVKDNY 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517997210 161 DYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDV 219
Cdd:pfam13614 119 DYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLVKKRLNPSLEI 177
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
4-242 |
2.34e-24 |
|
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: 95.30 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTDLLlktfkennnallneimnsnnfesvldekeneil 83
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 84 dlllrkstdinendlyhtlkekkpiheaiielsdnlsiipsdfnmigypylledlklnridgakyfnsfleevkkdYDYI 163
Cdd:cd02042 48 ----------------------------------------------------------------------------YDYI 51
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517997210 164 LIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDVIGILPVMFKKQGKIDSFILSLLQ 242
Cdd:cd02042 52 LIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
3-260 |
5.24e-15 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 74.71 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSeIKQKNVLVVDLDPQADVTDLLlktfkennnallneimnsnnfeSVLDEkenei 82
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLA-LQGYRVLAVDLDPQASLSALL----------------------GVLPE----- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 83 ldlllrksTDINEND-LYHTLK---EKKPIHEAIIELS-DNLSIIPSDFNMIGY----PYLLED------LKLNRIDGAk 147
Cdd:PRK13869 174 --------TDVGANEtLYAAIRyddTRRPLRDVIRPTYfDGLHLVPGNLELMEFehttPKALSDkgtrdgLFFTRVAQA- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 148 yfnsfLEEVKKDYDYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDF----KELHGN-DFDVIGI 222
Cdd:PRK13869 245 -----FDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLlgvvKEAGGNlQYDFIRY 319
|
250 260 270
....*....|....*....|....*....|....*...
gi 517997210 223 LPVMFKKQGKIDSFILSLLQHVYGSYVFKNKVFQRERV 260
Cdd:PRK13869 320 LLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAV 357
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
3-189 |
8.75e-15 |
|
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: 73.86 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSeIKQKNVLVVDLDPQADVTDLLlktfkennnALLNEImnsnnfesvldekenei 82
Cdd:TIGR03453 105 QVIAVTNFKGGSGKTTTAAHLAQYLA-LRGYRVLAIDLDPQASLSALF---------GYQPEF----------------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 83 ldlllrkstDINEND-LYHTLK---EKKPIHEaIIELS--DNLSIIPSDFNMIGY----PYLL------EDLKLNRIDGA 146
Cdd:TIGR03453 158 ---------DVGENEtLYGAIRyddERRPISE-IIRKTyfPGLDLVPGNLELMEFehetPRALsrgqggDTIFFARVGEA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517997210 147 kyfnsfLEEVKKDYDYILIDTPPTLSDFANSGIYACDySLIVT 189
Cdd:TIGR03453 228 ------LAEVEDDYDVVVIDCPPQLGFLTLSALCAAT-GVLIT 263
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
153-190 |
7.59e-06 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 45.62 E-value: 7.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 517997210 153 LEEVKKDYDYILIDTPPTLSDFANSGIYACDYSLIVTQ 190
Cdd:NF041546 69 LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
4-294 |
1.60e-49 |
|
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: 164.65 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTDLLLktfkennnallneimnsnnfesvLDEKENEil 83
Cdd:COG1192 3 VIAVANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG-----------------------LDPDDLD-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 84 dlllrkstdineNDLYHTLKEKKPIHEAIIELS-DNLSIIPSDFNMIGypylLEDLKLNRIDGAKYFNSFLEEVKKDYDY 162
Cdd:COG1192 57 ------------PTLYDLLLDDAPLEDAIVPTEiPGLDLIPANIDLAG----AEIELVSRPGRELRLKRALAPLADDYDY 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 163 ILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDVIGILPVMFKKQGKIDSFILSLLQ 242
Cdd:COG1192 121 ILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELR 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 517997210 243 HVYGSYVFKNKVFQRERVKFWDTTGIANEDMHDRNVLAM-YESITNELLEKMR 294
Cdd:COG1192 201 EEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKaYRALAEELLERLE 253
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
2-219 |
1.10e-29 |
|
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: 110.75 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 2 TEVVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTdlllktfkennnallneimnsnnfesvldekene 81
Cdd:pfam13614 1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNAT---------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 82 ildLLLRKSTDINENDLYHTLKEKKPIHEAIIELS-DNLSIIPSDFNMIGYPYLLEDLKLNRIdgakYFNSFLEEVKKDY 160
Cdd:pfam13614 46 ---SGLGIDKNNVEKTIYELLIGECNIEEAIIKTViENLDLIPSNIDLAGAEIELIGIENREN----ILKEALEPVKDNY 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517997210 161 DYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDV 219
Cdd:pfam13614 119 DYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLNTIKLVKKRLNPSLEI 177
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-268 |
2.22e-24 |
|
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: 98.19 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 5 VSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQadvtdlllktfkennnallneimnSNNFESvldekeneild 84
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALAR-RGLRVLLIDLDPQ------------------------SNNSSV----------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 85 LLLRKSTDINENDLYHTLKEKKPIHEAII---ELSDNLSIIPSDFNMIGYPYLLE-DLKLNRIdgakyfNSFLEEVKKDY 160
Cdd:pfam01656 45 EGLEGDIAPALQALAEGLKGRVNLDPILLkekSDEGGLDLIPGNIDLEKFEKELLgPRKEERL------REALEALKEDY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 161 DYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDF-KELHGNDFDVIGILPVMFKKQGKIDSFILS 239
Cdd:pfam01656 119 DYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKRLGGVIAALvGGYALLGLKIIGVVLNKVDGDNHGKLLKEA 198
|
250 260
....*....|....*....|....*....
gi 517997210 240 LLQHVYGSYVFKnKVFQRERVKFWDTTGI 268
Cdd:pfam01656 199 LEELLRGLPVLG-VIPRDEAVAEAPARGL 226
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
4-242 |
2.34e-24 |
|
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: 95.30 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTDLLlktfkennnallneimnsnnfesvldekeneil 83
Cdd:cd02042 2 VIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 84 dlllrkstdinendlyhtlkekkpiheaiielsdnlsiipsdfnmigypylledlklnridgakyfnsfleevkkdYDYI 163
Cdd:cd02042 48 ----------------------------------------------------------------------------YDYI 51
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517997210 164 LIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDFKELHGNDFDVIGILPVMFKKQGKIDSFILSLLQ 242
Cdd:cd02042 52 LIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
3-260 |
5.24e-15 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 74.71 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSeIKQKNVLVVDLDPQADVTDLLlktfkennnallneimnsnnfeSVLDEkenei 82
Cdd:PRK13869 122 QVIAVTNFKGGSGKTTTSAHLAQYLA-LQGYRVLAVDLDPQASLSALL----------------------GVLPE----- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 83 ldlllrksTDINEND-LYHTLK---EKKPIHEAIIELS-DNLSIIPSDFNMIGY----PYLLED------LKLNRIDGAk 147
Cdd:PRK13869 174 --------TDVGANEtLYAAIRyddTRRPLRDVIRPTYfDGLHLVPGNLELMEFehttPKALSDkgtrdgLFFTRVAQA- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 148 yfnsfLEEVKKDYDYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLISHLSDF----KELHGN-DFDVIGI 222
Cdd:PRK13869 245 -----FDEVADDYDVVVIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLlgvvKEAGGNlQYDFIRY 319
|
250 260 270
....*....|....*....|....*....|....*...
gi 517997210 223 LPVMFKKQGKIDSFILSLLQHVYGSYVFKNKVFQRERV 260
Cdd:PRK13869 320 LLTRYEPQDAPQTKVAALLRNMFEDHVLTNPMVKSAAV 357
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
3-189 |
8.75e-15 |
|
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: 73.86 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSeIKQKNVLVVDLDPQADVTDLLlktfkennnALLNEImnsnnfesvldekenei 82
Cdd:TIGR03453 105 QVIAVTNFKGGSGKTTTAAHLAQYLA-LRGYRVLAIDLDPQASLSALF---------GYQPEF----------------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 83 ldlllrkstDINEND-LYHTLK---EKKPIHEaIIELS--DNLSIIPSDFNMIGY----PYLL------EDLKLNRIDGA 146
Cdd:TIGR03453 158 ---------DVGENEtLYGAIRyddERRPISE-IIRKTyfPGLDLVPGNLELMEFehetPRALsrgqggDTIFFARVGEA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517997210 147 kyfnsfLEEVKKDYDYILIDTPPTLSDFANSGIYACDySLIVT 189
Cdd:TIGR03453 228 ------LAEVEDDYDVVVIDCPPQLGFLTLSALCAAT-GVLIT 263
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
20-220 |
5.56e-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: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 20 TAGIAYVLSEiKQKNVLVVDLDPQAdvtdlllktfkennnallneimnSNnfesvldekeneiLDLLLRKSTdinENDLY 99
Cdd:COG0455 3 AVNLAAALAR-LGKRVLLVDADLGL-----------------------AN-------------LDVLLGLEP---KATLA 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 100 HTLKEKKPIHEAIIELSDNLSIIPSDFNMIGYPYLLEDLKLNRIdgakyfnsfLEEVKKDYDYILIDTPPTLSDFANSGI 179
Cdd:COG0455 43 DVLAGEADLEDAIVQGPGGLDVLPGGSGPAELAELDPEERLIRV---------LEELERFYDVVLVDTGAGISDSVLLFL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517997210 180 YACDYSLIVTQTHVRSFNAIEKLISHLSdfKELHGNDFDVI 220
Cdd:COG0455 114 AAADEVVVVTTPEPTSITDAYALLKLLR--RRLGVRRAGVV 152
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
4-189 |
1.67e-12 |
|
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: 65.67 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDpqadvtdlllktfkennnallneIMNSNnfesvldekeneiL 83
Cdd:cd02038 2 IIAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDAD-----------------------LGLAN-------------L 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 84 DLLLrksTDINENDLYHTLKEKKPIHEAIIELSDNLSIIPSDfnmIGYPYLLEdlkLNRIDGAKYFNSFlEEVKKDYDYI 163
Cdd:cd02038 45 DILL---GLAPKKTLGDVLKGRVSLEDIIVEGPEGLDIIPGG---SGMEELAN---LDPEQKAKLIEEL-SSLESNYDYL 114
|
170 180
....*....|....*....|....*.
gi 517997210 164 LIDTPPTLSDFANSGIYACDYSLIVT 189
Cdd:cd02038 115 LIDTGAGISRNVLDFLLAADEVIVVT 140
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
11-232 |
5.94e-10 |
|
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: 59.04 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 11 KGGVSKTSSTAGIAYVLSEIKQKnVLVVDLD---PQadvtdlLLKTFKENNNALLNEImnsnnfesvldekeneildlll 87
Cdd:COG0489 101 KGGEGKSTVAANLALALAQSGKR-VLLIDADlrgPS------LHRMLGLENRPGLSDV---------------------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 88 rkstdinendlyhtLKEKKPIHEAIIEL-SDNLSIIPSDFNMigyPYLLEDLKLNRidgakyFNSFLEEVKKDYDYILID 166
Cdd:COG0489 152 --------------LAGEASLEDVIQPTeVEGLDVLPAGPLP---PNPSELLASKR------LKQLLEELRGRYDYVIID 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517997210 167 TPPTLSDfANSGIYA--CDYSLIVTQTHVRSFNAIEKLIshlsdfKELHGNDFDVIGILPVMFKKQGK 232
Cdd:COG0489 209 TPPGLGV-ADATLLAslVDGVLLVVRPGKTALDDVRKAL------EMLEKAGVPVLGVVLNMVCPKGE 269
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
3-189 |
3.75e-09 |
|
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: 56.06 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSEiKQKNVLVVDldpqADVTdlllktfkennnaLLNeimnsnnfesvldekenei 82
Cdd:cd02036 1 RVIVITSGKGGVGKTTTTANLGVALAK-LGKKVLLID----ADIG-------------LRN------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 83 LDLLLRKSTDINEnDLYHTLKEKKPIHEAIIE--LSDNLSIIPSDFNmigypylLEDLKLNRidgaKYFNSFLEEVKKDY 160
Cdd:cd02036 44 LDLILGLENRIVY-TLVDVLEGECRLEQALIKdkRWENLYLLPASQT-------RDKDALTP----EKLEELVKELKDSF 111
|
170 180
....*....|....*....|....*....
gi 517997210 161 DYILIDTPPTLSDFANSGIYACDYSLIVT 189
Cdd:cd02036 112 DFILIDSPAGIESGFINAIAPADEAIIVT 140
|
|
| CooC1 |
cd02034 |
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ... |
11-224 |
2.12e-08 |
|
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: 53.85 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 11 KGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPqadvtdlllktfkennNALLNEIMNSnnfesvldekENEILDLLLRKS 90
Cdd:cd02034 8 KGGVGKTTIAALLIRYLAK-KGGKVLAVDADP----------------NSNLAETLGV----------EVEKLPLIKTIG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 91 tDINENdlyhtLKEKKPIHEAIIELSDNLSIIPSDFNMIGYPYLLedLKLNRIDGAK-----YFNSFLEEV-----KKDY 160
Cdd:cd02034 61 -DIRER-----TGAKKGEPPEGMSLNPYVDDIIKEIIVEPDGIDL--LVMGRPEGGGsgcycPVNALLRELlrhlaLKNY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 161 DYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNA---IEKLISHL-----------------SDFKELHGNDFDVI 220
Cdd:cd02034 133 EYVVIDMEAGIEHLSRGTIRAVDLLIIVIEPSKRSIQTakrIKELAEELgikkiylivnkvrneeeQELIEELLIKLKLI 212
|
....
gi 517997210 221 GILP 224
Cdd:cd02034 213 GVIP 216
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
11-216 |
3.38e-08 |
|
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: 53.96 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 11 KGGVSKTSSTAGIAYVLSEIKQKNVLVVDLDPQADVTDLLLKtfkennnallneimnsnnfesvLDEKENeILDLLLrks 90
Cdd:COG4963 111 KGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLD----------------------LEPRRG-LADALR--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 91 tDINENDlyHTLkekkpIHEAIIELSDNLSIIPSdfnmigyPYLLEDLklNRIDgAKYFNSFLEEVKKDYDYILIDTPPT 170
Cdd:COG4963 165 -NPDRLD--ETL-----LDRALTRHSSGLSVLAA-------PADLERA--EEVS-PEAVERLLDLLRRHFDYVVVDLPRG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517997210 171 LSDFANSGIYACDYSLIVTQTHVRSfnaIEKLISHLSDFKELHGND 216
Cdd:COG4963 227 LNPWTLAALEAADEVVLVTEPDLPS---LRNAKRLLDLLRELGLPD 269
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
16-222 |
4.06e-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: 49.49 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 16 KTSSTAGIAYVLSEIKQKnVLVVDLD---PQadvtdlLLKTFKENNnallneimnsnnfesvldekeneildlllrkstd 92
Cdd:cd05387 33 KSTVAANLAVALAQSGKR-VLLIDADlrrPS------LHRLLGLPN---------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 93 inENDLYHTLKEKKPIHEAIIEL-SDNLSIIPSDFNMigyPYLLEDLKLNRidgakyFNSFLEEVKKDYDYILIDTPPTL 171
Cdd:cd05387 72 --EPGLSEVLSGQASLEDVIQSTnIPNLDVLPAGTVP---PNPSELLSSPR------FAELLEELKEQYDYVIIDTPPVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517997210 172 SdFANSGIYA--CDYSLIVTQTHVRSFNAIEKLISHLsdfkELHGNdfDVIGI 222
Cdd:cd05387 141 A-VADALILAplVDGVLLVVRAGKTRRREVKEALERL----EQAGA--KVLGV 186
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
3-216 |
2.59e-06 |
|
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.
Pssm-ID: 349765 [Multi-domain] Cd Length: 235 Bit Score: 47.66 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 3 EVVSINNFKGGVSKTSSTAGIAYVLSEIKQKNVLVVDLD-PQADVTDLLlktfkennnallneimNSNNFESVLDEKEN- 80
Cdd:cd03111 1 RVVAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDlPFGDLGLYL----------------NLRPDYDLADVIQNl 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 81 EILD-LLLRKStdinendLYHTlkekkpiheaiielSDNLSIIPS-----DFNMIGYPYLLEDLKLnridgAKYFnsfle 154
Cdd:cd03111 65 DRLDrTLLDSA-------VTRH--------------SSGLSLLPApqeleDLEALGAEQVDKLLQV-----LRAF----- 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517997210 155 evkkdYDYILIDTPPTLSDFANSGIYACDYSLIVTQTHVRSFNAIEKLIshlSDFKELHGND 216
Cdd:cd03111 114 -----YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSLRNARRLL---DSLRELEGSS 167
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
4-201 |
3.06e-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: 47.05 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 4 VVSINNFKGGVSKTSSTAGIAYVLSEIKQKnVLVVDLDPQADVtdlLLKTFKENN--NALLNEIMNSNNFESVLDEKENE 81
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQAGYK-TLLIDGDMRNSV---MSGTFKSQNkiTGLTNFLSGTTDLSDAICDTNIE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 82 ILDLLLRKSTDINENDLYhtlkekkpiheaiielsdnlsiipsdfnmigypylledlklnridGAKYFNSFLEEVKKDYD 161
Cdd:TIGR01007 95 NLDVITAGPVPPNPTELL---------------------------------------------QSSNFKTLIETLRKRFD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517997210 162 YILIDTPPtLSDFANSGIYA--CDYSLIVTQTHVRSFNAIEK 201
Cdd:TIGR01007 130 YIIIDTPP-IGTVTDAAIIAraCDASILVTDAGKIKKREVKK 170
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
153-190 |
7.59e-06 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 45.62 E-value: 7.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 517997210 153 LEEVKKDYDYILIDTPPTLSDFANSGIYACDYSLIVTQ 190
Cdd:NF041546 69 LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
|
|
| ArsA_ATPase |
pfam02374 |
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ... |
11-170 |
8.33e-06 |
|
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Pssm-ID: 396792 Cd Length: 302 Bit Score: 46.57 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 11 KGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQADVTDLLLKTF-----KENNNALLNEImnsnnfESVLDEKENeildl 85
Cdd:pfam02374 9 KGGVGKTTVSAATAVQLSE-LGKKVLLISTDPAHSLSDSFNQKFgheptKVKENLSAMEI------DPNMELEEY----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517997210 86 llRKSTDINENDLYHTLKEKKPIHEAiielsdnLSIIPSdfnmigypylledlklnrIDGAKYFNSFLEEVKK-DYDYIL 164
Cdd:pfam02374 77 --WQEVQKYMNALLGLRMLEGILAEE-------LASLPG------------------IDEAASFDEFKKYMDEgEYDVVV 129
|
....*.
gi 517997210 165 IDTPPT 170
Cdd:pfam02374 130 FDTAPT 135
|
|
| NifH |
cd02040 |
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ... |
11-66 |
1.15e-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: 1.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517997210 11 KGGVSKTSSTAGIAYVLSEIKQKnVLVVDLDPQADVTDLLL-----KTF-----KENNNALLNEIM 66
Cdd:cd02040 8 KGGIGKSTTASNLSAALAEMGKK-VLHVGCDPKADSTRLLLggkaiPTVldtlrEKGEVEELEDVI 72
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
11-44 |
1.64e-03 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 38.99 E-value: 1.64e-03
10 20 30
....*....|....*....|....*....|....
gi 517997210 11 KGGVSKTSSTAGIAYVLSEiKQKNVLVVDLDPQA 44
Cdd:COG3640 8 KGGVGKTTLSALLARYLAE-KGKPVLAVDADPNA 40
|
|
| PRK13230 |
PRK13230 |
nitrogenase reductase-like protein; Reviewed |
11-66 |
7.60e-03 |
|
nitrogenase reductase-like protein; Reviewed
Pssm-ID: 183903 Cd Length: 279 Bit Score: 37.44 E-value: 7.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517997210 11 KGGVSKTSSTAGIAYVLSEIKQKnVLVVDLDPQADVTDLL--------LKTFKEN--NNALLNEIM 66
Cdd:PRK13230 9 KGGIGKSTTVCNIAAALAESGKK-VLVVGCDPKADCTRNLvgekiptvLDVLREKgiDNLGLEDII 73
|
|
| |
