|
Name |
Accession |
Description |
Interval |
E-value |
| PrgP |
NF041283 |
ParA superfamily DNA segregation protein PrgP; |
1-297 |
0e+00 |
|
ParA superfamily DNA segregation protein PrgP;
Pssm-ID: 469180 [Multi-domain] Cd Length: 297 Bit Score: 532.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 1 MGYVIVNAQQKGGVGKTTDTVMEAVVASSFYNKKVLVIDTDLQGNATQFLAKTFQVLTFNQSFMSCIEDGSLEKGIVSLS 80
Cdd:NF041283 1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDGDLEKGIVHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 81 DNLDLIGSDYDTRKFGDFLDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAF 160
Cdd:NF041283 81 PNLDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQQFAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 161 DGSKRLVLTYLQTLADDFGDKVHFQVAGILPVLLQAKRPLHQRIVKETIEYFGKDNVFNNIVNNHARLEWYAAQGIQFED 240
Cdd:NF041283 161 EGSKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDNVFNNIIKNHARLEWYGEQGIQFED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 983062479 241 YHDKRVWGLFADIFSELELRIKSFENTGDIENFTYAHQFITGNKLTSKGKAMTVSGF 297
Cdd:NF041283 241 YHDRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYINQNKLTPKGKEITINGF 297
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
3-229 |
9.55e-44 |
|
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: 149.62 E-value: 9.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 3 YVIVNaqQKGGVGKTTDTVMEAVvASSFYNKKVLVIDTDLQGNATQFLAKT--------FQVLTFNQSFMSCIedgslek 74
Cdd:COG1192 4 IAVAN--QKGGVGKTTTAVNLAA-ALARRGKRVLLIDLDPQGNLTSGLGLDpddldptlYDLLLDDAPLEDAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 75 gIVSLSDNLDLIGSDYDTRKFgdflDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQE 154
Cdd:COG1192 74 -VPTEIPGLDLIPANIDLAGA----EIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983062479 155 TQQFAFDGSKRLvLTYLQTLADDFGDKVhfQVAGILPVLLQAKRPLHQRIVKETIEYFGkDNVFNNIVNNHARLE 229
Cdd:COG1192 149 PEYLSLEGLAQL-LETIEEVREDLNPKL--EILGILLTMVDPRTRLSREVLEELREEFG-DKVLDTVIPRSVALA 219
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
4-169 |
4.21e-33 |
|
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: 119.61 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAVvASSFYNKKVLVIDTDLQGNATQ--FLAKTFQVLTFNQSFmscIEDGSLEKGIVSLS- 80
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAA-ALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELL---IGECNIEEAIIKTVi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 81 DNLDLIGSDYDTRKFgdflDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAF 160
Cdd:pfam13614 79 ENLDLIPSNIDLAGA----EIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYAL 154
|
....*....
gi 983062479 161 DGSKRLVLT 169
Cdd:pfam13614 155 EGLSQLLNT 163
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
3-207 |
6.05e-22 |
|
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: 89.14 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 3 YVIVNAQQKGGVGKTTDTVMEAVVASSfYNKKVLVIDTDLQGNATQFLaktfqvltfnqsfmsciedgslekgivslsdn 82
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 83 ldligsdydtrkfgdfldnkfssisdrtfylsklvnkikdrYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAFDG 162
Cdd:cd02042 48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 983062479 163 SKRLvLTYLQTLADDFGDKvhFQVAGILPVLLQAKRPLHQRIVKE 207
Cdd:cd02042 87 LAKL-LDTLEELKKQLNPP--LLILGILLTRVDPRTKLAREVLEE 128
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
4-151 |
9.58e-10 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 57.18 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAVVASSfYNKKVLVIDTDLQGNATQFLAktfqvltfnqsfmsCIEDGSLekgivslsdnL 83
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALAR-RGYRVLLVDADPQGSALDWAA--------------AREDERP----------F 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983062479 84 DLIGSDYDTrkfgdfldnkfssisdrtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIV 151
Cdd:NF041546 56 PVVGLARPT--------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI 103
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
4-152 |
1.66e-04 |
|
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: 42.41 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAvVASSFYNKKVLVIDTDLQgnatqfLAKTFQVLtfnqsfmsciedgSLEKGIVSLSDNL 83
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLG-VALAKLGKKVLALDADIT------MANLELIL-------------GMEDKPVTLHDVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 84 ----DLIGSDYDTrKFGDF-------LDNKFSSISDRtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVI 152
Cdd:TIGR01969 62 ageaDIKDAIYEG-PFGVKvipagvsLEGLRKADPDK---LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PrgP |
NF041283 |
ParA superfamily DNA segregation protein PrgP; |
1-297 |
0e+00 |
|
ParA superfamily DNA segregation protein PrgP;
Pssm-ID: 469180 [Multi-domain] Cd Length: 297 Bit Score: 532.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 1 MGYVIVNAQQKGGVGKTTDTVMEAVVASSFYNKKVLVIDTDLQGNATQFLAKTFQVLTFNQSFMSCIEDGSLEKGIVSLS 80
Cdd:NF041283 1 MGYVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDGDLEKGIVHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 81 DNLDLIGSDYDTRKFGDFLDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAF 160
Cdd:NF041283 81 PNLDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQQFAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 161 DGSKRLVLTYLQTLADDFGDKVHFQVAGILPVLLQAKRPLHQRIVKETIEYFGKDNVFNNIVNNHARLEWYAAQGIQFED 240
Cdd:NF041283 161 EGSKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDNVFNNIIKNHARLEWYGEQGIQFED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 983062479 241 YHDKRVWGLFADIFSELELRIKSFENTGDIENFTYAHQFITGNKLTSKGKAMTVSGF 297
Cdd:NF041283 241 YHDRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYINQNKLTPKGKEITINGF 297
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
3-229 |
9.55e-44 |
|
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: 149.62 E-value: 9.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 3 YVIVNaqQKGGVGKTTDTVMEAVvASSFYNKKVLVIDTDLQGNATQFLAKT--------FQVLTFNQSFMSCIedgslek 74
Cdd:COG1192 4 IAVAN--QKGGVGKTTTAVNLAA-ALARRGKRVLLIDLDPQGNLTSGLGLDpddldptlYDLLLDDAPLEDAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 75 gIVSLSDNLDLIGSDYDTRKFgdflDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQE 154
Cdd:COG1192 74 -VPTEIPGLDLIPANIDLAGA----EIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983062479 155 TQQFAFDGSKRLvLTYLQTLADDFGDKVhfQVAGILPVLLQAKRPLHQRIVKETIEYFGkDNVFNNIVNNHARLE 229
Cdd:COG1192 149 PEYLSLEGLAQL-LETIEEVREDLNPKL--EILGILLTMVDPRTRLSREVLEELREEFG-DKVLDTVIPRSVALA 219
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
4-169 |
4.21e-33 |
|
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: 119.61 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAVvASSFYNKKVLVIDTDLQGNATQ--FLAKTFQVLTFNQSFmscIEDGSLEKGIVSLS- 80
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAA-ALAKKGKKVLLIDLDPQGNATSglGIDKNNVEKTIYELL---IGECNIEEAIIKTVi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 81 DNLDLIGSDYDTRKFgdflDNKFSSISDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAF 160
Cdd:pfam13614 79 ENLDLIPSNIDLAGA----EIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYAL 154
|
....*....
gi 983062479 161 DGSKRLVLT 169
Cdd:pfam13614 155 EGLSQLLNT 163
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
3-207 |
6.05e-22 |
|
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: 89.14 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 3 YVIVNAQQKGGVGKTTDTVMEAVVASSfYNKKVLVIDTDLQGNATQFLaktfqvltfnqsfmsciedgslekgivslsdn 82
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALAL-RGKRVLLIDLDPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 83 ldligsdydtrkfgdfldnkfssisdrtfylsklvnkikdrYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAFDG 162
Cdd:cd02042 48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 983062479 163 SKRLvLTYLQTLADDFGDKvhFQVAGILPVLLQAKRPLHQRIVKE 207
Cdd:cd02042 87 LAKL-LDTLEELKKQLNPP--LLILGILLTRVDPRTKLAREVLEE 128
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-218 |
1.14e-16 |
|
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: 77.39 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 5 IVNAQQKGGVGKTTDTVMEAVVASSFyNKKVLVIDTDLQGNAT------QFLAKTFQVL--------TFNQSFMSCIEDg 70
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARR-GLRVLLIDLDPQSNNSsvegleGDIAPALQALaeglkgrvNLDPILLKEKSD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 71 slEKGIVSLSDNLDLIGSDYDTRKFGDFLDnkfssisdrtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYII 150
Cdd:pfam01656 79 --EGGLDLIPGNIDLEKFEKELLGPRKEER------------LREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 151 VIQETQQFAFDGSKRLVltylqTLADDFGDKVHFQVAGILPVLLQ--AKRPLHQRIVKETIEYFGKDNVF 218
Cdd:pfam01656 145 IPLEPEVILVEDAKRLG-----GVIAALVGGYALLGLKIIGVVLNkvDGDNHGKLLKEALEELLRGLPVL 209
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
4-151 |
9.58e-10 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 57.18 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAVVASSfYNKKVLVIDTDLQGNATQFLAktfqvltfnqsfmsCIEDGSLekgivslsdnL 83
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALAR-RGYRVLLVDADPQGSALDWAA--------------AREDERP----------F 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983062479 84 DLIGSDYDTrkfgdfldnkfssisdrtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIV 151
Cdd:NF041546 56 PVVGLARPT--------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLI 103
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
11-152 |
7.24e-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: 55.89 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 11 KGGVGKTTDTVMEAVVASSFYNKKVLVIDTDLQ-GNATQFLAktfqvLTFNQSFMSCIEDGS------LEKGIVSLSDNL 83
Cdd:COG4963 111 KGGVGATTLAVNLAWALARESGRRVLLVDLDLQfGDVALYLD-----LEPRRGLADALRNPDrldetlLDRALTRHSSGL 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983062479 84 DLIGSDYDtrkfgdflDNKFSSISDRTFylSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVI 152
Cdd:COG4963 186 SVLAAPAD--------LERAEEVSPEAV--ERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLV 244
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
11-152 |
1.86e-08 |
|
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: 54.42 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 11 KGGVGKTTDTVMEAVVASSfYNKKVLVIDTDLQGNAtqfLAKTFQvLTFNQSFMSCIEDG-SLEKGIVSL-SDNLDLIGS 88
Cdd:COG0489 101 KGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPS---LHRMLG-LENRPGLSDVLAGEaSLEDVIQPTeVEGLDVLPA 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983062479 89 dydtrkfGDFLDNKFSSISDRTFylSKLVNKIKDRYDYIFIDVPPSTDikVDNAMVCADY----IIVI 152
Cdd:COG0489 176 -------GPLPPNPSELLASKRL--KQLLEELRGRYDYVIIDTPPGLG--VADATLLASLvdgvLLVV 232
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
31-152 |
5.27e-07 |
|
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: 49.50 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 31 YNKKVLVIDTDLQ-GNATQFL----AKTF-QVLTfnqsfmsciEDGSLEKGIVSLSDNLDLIGSDYDTRKFGDFldnkfs 104
Cdd:COG0455 13 LGKRVLLVDADLGlANLDVLLglepKATLaDVLA---------GEADLEDAIVQGPGGLDVLPGGSGPAELAEL------ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 983062479 105 sisDRTFYLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVI 152
Cdd:COG0455 78 ---DPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVV 122
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
4-152 |
7.34e-06 |
|
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: 46.04 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAvVASSFYNKKVLVIDTD-----------------------LQGNAtqflaktfqvlTFN 60
Cdd:cd02036 2 VIVITSGKGGVGKTTTTANLG-VALAKLGKKVLLIDADiglrnldlilglenrivytlvdvLEGEC-----------RLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 61 QSFmscIEDGSLEkgivslsdNLDLIGSDYDTRKFGdfLDNKfssisdrtfYLSKLVNKIKDRYDYIFIDVPPSTDIKVD 140
Cdd:cd02036 70 QAL---IKDKRWE--------NLYLLPASQTRDKDA--LTPE---------KLEELVKELKDSFDFILIDSPAGIESGFI 127
|
170
....*....|..
gi 983062479 141 NAMVCADYIIVI 152
Cdd:cd02036 128 NAIAPADEAIIV 139
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
5-157 |
3.03e-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: 44.19 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 5 IVNAqqKGGVGKTTDTVMEAVVASSFYNKKVLVIDTDLQ-GNATQFL--AKTFQVLTFNQSFmSCIEDGSLEKGIVSLSD 81
Cdd:cd03111 5 VVGA--KGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPfGDLGLYLnlRPDYDLADVIQNL-DRLDRTLLDSAVTRHSS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983062479 82 NLDLIGSdydTRKFGDFldNKFSSISdrtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIqeTQQ 157
Cdd:cd03111 82 GLSLLPA---PQELEDL--EALGAEQ-----VDKLLQVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLV--TQQ 145
|
|
| minD_arch |
TIGR01969 |
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ... |
4-152 |
1.66e-04 |
|
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: 42.41 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 4 VIVNAQQKGGVGKTTDTVMEAvVASSFYNKKVLVIDTDLQgnatqfLAKTFQVLtfnqsfmsciedgSLEKGIVSLSDNL 83
Cdd:TIGR01969 2 IITIASGKGGTGKTTITANLG-VALAKLGKKVLALDADIT------MANLELIL-------------GMEDKPVTLHDVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 84 ----DLIGSDYDTrKFGDF-------LDNKFSSISDRtfyLSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVI 152
Cdd:TIGR01969 62 ageaDIKDAIYEG-PFGVKvipagvsLEGLRKADPDK---LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137
|
|
| MinD |
COG2894 |
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ... |
1-152 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 1 MGYVIVNAQQKGGVGKTTDTvmeAVVASSF--YNKKVLVIDTD-----------------------LQGNAtqflaktfq 55
Cdd:COG2894 1 MGKVIVVTSGKGGVGKTTTT---ANLGTALalLGKKVVLIDADiglrnldlvmglenrivydlvdvIEGEC--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 56 vlTFNQSFmscIEDGSLEkgivslsdNLDLIGSdydtrkfgdfldnkfSSISDRTfYLS-----KLVNKIKDRYDYIFID 130
Cdd:COG2894 69 --RLKQAL---IKDKRFE--------NLYLLPA---------------SQTRDKD-ALTpeqmkKLVEELKEEFDYILID 119
|
170 180
....*....|....*....|..
gi 983062479 131 VPPSTDIKVDNAMVCADYIIVI 152
Cdd:COG2894 120 SPAGIEQGFKNAIAGADEAIVV 141
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
13-133 |
3.55e-04 |
|
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: 40.63 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 13 GVGKTTDTV-MEAVVASSfyNKKVLVIDTDL-QGNATQFL--AKTFQVLTFNqsfmscIEDGSLEKGI-VSLSDNLDLIG 87
Cdd:cd05387 30 GEGKSTVAAnLAVALAQS--GKRVLLIDADLrRPSLHRLLglPNEPGLSEVL------SGQASLEDVIqSTNIPNLDVLP 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 983062479 88 SdydtrkfGDFLDNKFSSISDRTFylSKLVNKIKDRYDYIFIDVPP 133
Cdd:cd05387 102 A-------GTVPPNPSELLSSPRF--AELLEELKEQYDYVIIDTPP 138
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
113-167 |
1.05e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 39.68 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 983062479 113 LSKLVNKIKDRYDYIFIDVPPSTDIKVDNAMVCADYIIVIQETQQFAFDGSKRLV 167
Cdd:cd03110 149 LRKKALERSKECDLAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAI 203
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
11-153 |
1.38e-03 |
|
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: 38.96 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983062479 11 KGGVGKTTdTVMEAVVASSFYNKKVLVIDTDLQgNATQflAKTFQVLTFNQSFMSCIE-DGSLEKGIVSLS-DNLDLIGS 88
Cdd:TIGR01007 26 KPGEGKST-TSANIAIAFAQAGYKTLLIDGDMR-NSVM--SGTFKSQNKITGLTNFLSgTTDLSDAICDTNiENLDVITA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983062479 89 dydtrkfGDFLDNKFSSISDRTFylSKLVNKIKDRYDYIFIDVPPsTDIKVDNAMV---CADYIIVIQ 153
Cdd:TIGR01007 102 -------GPVPPNPTELLQSSNF--KTLIETLRKRFDYIIIDTPP-IGTVTDAAIIaraCDASILVTD 159
|
|
| |
