|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
4-391 |
0e+00 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 837.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 4 MKLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRVEQRV 83
Cdd:PRK13705 1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 84 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 163
Cdd:PRK13705 81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 164 HIHAEDTLLPFYLGEKDDVTYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 243
Cdd:PRK13705 161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 244 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 323
Cdd:PRK13705 241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309400378 324 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 391
Cdd:PRK13705 321 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 388
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
33-357 |
3.53e-56 |
|
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: 189.03 E-value: 3.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 33 SPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRveqRVgYTIEQINHMRDVFGTRLRRAEDVFP--- 109
Cdd:TIGR03453 24 PPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGR---RS-YTLEQINELRRHLAQRGREARRYLPhrr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 110 -----PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTLLPF--YLGEKDDV 182
Cdd:TIGR03453 100 ggehlQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAID-LDPQASLSALFGYQPEFDVGENETLYGAirYDDERRPI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 183 TYAIKPTCWPGLDIIPSCLALHRIETE----LMGKFDEGKLPTdphLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVC 258
Cdd:TIGR03453 179 SEIIRKTYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIFF---ARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 259 AADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPD---VRILLTKYSNSNGSQSPwMEEQIRDAWGSMVLKN-V 334
Cdd:TIGR03453 256 AATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSydfMRYLVTRYEPNDGPQAQ-MVAFLRSLFGDHVLTNpM 334
|
330 340 350
....*....|....*....|....*....|....*
gi 309400378 335 VRETD------------EVGKGQIRmRTVFEQAID 357
Cdd:TIGR03453 335 LKSTAisdagltkqtlyEVERSQFT-RSTYDRAME 368
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
109-383 |
4.55e-55 |
|
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: 181.98 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 109 PPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDlhiHAEDTLLPFYLGEKDdVTYAIKP 188
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLID-LDPQGNLTSGLGLDPD---DLDPTLYDLLLDDAP-LEDAIVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 189 TCWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP 268
Cdd:COG1192 76 TEIPGLDLIPANIDLAGAEIELVSR-------PGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 269 AELFDYTSALQFFDMLRDLLK--NVDLKGfepdVRILLTKYSNSNGSQSPWMEEqIRDAWGSMVLKNVVRETDEVGKGQI 346
Cdd:COG1192 149 PEYLSLEGLAQLLETIEEVREdlNPKLEI----LGILLTMVDPRTRLSREVLEE-LREEFGDKVLDTVIPRSVALAEAPS 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 309400378 347 RMRTVFEQAidqRSSTGAwrnalSIWEPVCNEIFDRL 383
Cdd:COG1192 224 AGKPVFEYD---PKSKGA-----KAYRALAEELLERL 252
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
112-351 |
2.06e-48 |
|
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: 163.67 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 112 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHI--HAEDTLLPfYLGEKDDVTYAIKPT 189
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLID-LDPQSNNSSVEGLEGDIAPalQALAEGLK-GRVNLDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 190 CWpGLDIIPSCLALHRIETELMGKFDEGKLptdphlmlRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 269
Cdd:pfam01656 79 EG-GLDLIPGNIDLEKFEKELLGPRKEERL--------REALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 270 ELFDYTSALQFFDMLRDLLKNVDLKGFEPdVRILLTKYSNSNGSQS--PWMEEQIRdawGSMVLKnVVRETDEVGKGQIR 347
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGLKI-IGVVLNKVDGDNHGKLlkEALEELLR---GLPVLG-VIPRDEAVAEAPAR 224
|
....
gi 309400378 348 MRTV 351
Cdd:pfam01656 225 GLPV 228
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
110-320 |
5.85e-28 |
|
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: 106.47 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 110 PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHgwvpdlhihaedtllpfylgekddvtyaikpt 189
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 190 cwpgldiipsclalhrietelmgkfdegklptdphlmlrlaietvahdYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 269
Cdd:cd02042 48 ------------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 309400378 270 ELFDYTSALQFFDMLRDLLKNVDLKGfePDVRILLTKYSNSNGSQSPWMEE 320
Cdd:cd02042 80 SPFDLDGLAKLLDTLEELKKQLNPPL--LILGILLTRVDPRTKLAREVLEE 128
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
111-285 |
6.67e-18 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 81.44 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGWVPDlhihaeDTLLPFylgekddVTYAiKPTc 190
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA-DPQGSALDWAAARED------ERPFPV-------VGLA-RPT- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 191 wpgldiipsclaLHRietelmgkfdegklptdphlmlrlAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 270
Cdd:NF041546 65 ------------LHR------------------------ELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPS 108
|
170
....*....|....*
gi 309400378 271 LFDYTSALQFFDMLR 285
Cdd:NF041546 109 PYDLWASADTVDLIK 123
|
|
| HTH_MERR |
smart00422 |
helix_turn_helix, mercury resistance; |
43-71 |
1.88e-03 |
|
helix_turn_helix, mercury resistance;
Pssm-ID: 197716 Cd Length: 70 Bit Score: 36.73 E-value: 1.88e-03
10 20
....*....|....*....|....*....
gi 309400378 43 WRIGEAADLVGVSSQAIRDAEKAGRLPHP 71
Cdd:smart00422 1 YTIGEVAKLAGVSVRTLRYYERIGLLPPP 29
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
4-391 |
0e+00 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 837.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 4 MKLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRVEQRV 83
Cdd:PRK13705 1 MDLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEMRGRVEQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 84 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 163
Cdd:PRK13705 81 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 164 HIHAEDTLLPFYLGEKDDVTYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 243
Cdd:PRK13705 161 HIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 244 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 323
Cdd:PRK13705 241 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309400378 324 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 391
Cdd:PRK13705 321 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWEIR 388
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
4-389 |
0e+00 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 704.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 4 MKLMETLNQCINAGHEMTKAIAIAQFNDDSPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRVEQRV 83
Cdd:PHA02519 1 MSLINLLNSCIERGQEMTQAIAIAQFGDDSPEARAITRRWGITEVADLIGVTPQAIRDAEKSGRLPPPDFETRGRVERRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 84 GYTIEQINHMRDVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDL 163
Cdd:PHA02519 81 GYTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQGTASMYHGYVPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 164 HIHAEDTLLPFYLGEKDDVTYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRLAIETVAHDYDVIVI 243
Cdd:PHA02519 161 HIHADDTLLPFYLGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYHDAGKLPHPPHLMLRAAIESVWDNYDIIVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 244 DSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPDVRILLTKYSNSNGSQSPWMEEQIR 323
Cdd:PHA02519 241 DSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDLGGFEPVVRLLLTKYSLTVGNQSRWMEEQIR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309400378 324 DAWGSMVLKNVVRETDEVGKGQIRMRTVFEQAIDQRSSTGAWRNALSIWEPVCNEIFDRLIKPRWE 389
Cdd:PHA02519 321 NTWGSMVLRQVVRVTDEVGKGQIKMRTVFEQAANQRSTLNAWRNAVAIWEPVCAEIFNDLIKPRWE 386
|
|
| partition_RepA |
TIGR03453 |
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ... |
33-357 |
3.53e-56 |
|
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: 189.03 E-value: 3.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 33 SPEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRveqRVgYTIEQINHMRDVFGTRLRRAEDVFP--- 109
Cdd:TIGR03453 24 PPNARKTLRKFTSGEVAKLLGVSDSYLRQLSLEGKGPEPETLSNGR---RS-YTLEQINELRRHLAQRGREARRYLPhrr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 110 -----PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTLLPF--YLGEKDDV 182
Cdd:TIGR03453 100 ggehlQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAID-LDPQASLSALFGYQPEFDVGENETLYGAirYDDERRPI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 183 TYAIKPTCWPGLDIIPSCLALHRIETE----LMGKFDEGKLPTdphLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVC 258
Cdd:TIGR03453 179 SEIIRKTYFPGLDLVPGNLELMEFEHEtpraLSRGQGGDTIFF---ARVGEALAEVEDDYDVVVIDCPPQLGFLTLSALC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 259 AADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKGFEPD---VRILLTKYSNSNGSQSPwMEEQIRDAWGSMVLKN-V 334
Cdd:TIGR03453 256 AATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVREAGGNLSydfMRYLVTRYEPNDGPQAQ-MVAFLRSLFGDHVLTNpM 334
|
330 340 350
....*....|....*....|....*....|....*
gi 309400378 335 VRETD------------EVGKGQIRmRTVFEQAID 357
Cdd:TIGR03453 335 LKSTAisdagltkqtlyEVERSQFT-RSTYDRAME 368
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
109-383 |
4.55e-55 |
|
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: 181.98 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 109 PPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDlhiHAEDTLLPFYLGEKDdVTYAIKP 188
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLID-LDPQGNLTSGLGLDPD---DLDPTLYDLLLDDAP-LEDAIVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 189 TCWPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTP 268
Cdd:COG1192 76 TEIPGLDLIPANIDLAGAEIELVSR-------PGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 269 AELFDYTSALQFFDMLRDLLK--NVDLKGfepdVRILLTKYSNSNGSQSPWMEEqIRDAWGSMVLKNVVRETDEVGKGQI 346
Cdd:COG1192 149 PEYLSLEGLAQLLETIEEVREdlNPKLEI----LGILLTMVDPRTRLSREVLEE-LREEFGDKVLDTVIPRSVALAEAPS 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 309400378 347 RMRTVFEQAidqRSSTGAwrnalSIWEPVCNEIFDRL 383
Cdd:COG1192 224 AGKPVFEYD---PKSKGA-----KAYRALAEELLERL 252
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
34-388 |
8.15e-49 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 170.24 E-value: 8.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 34 PEARKITRRWRIGEAADLVGVSSQAIRDAEKAGRLPHPDMEIRGRveqRVgYTIEQINHMRDVFG--TRLRRAEDVFP-- 109
Cdd:PRK13869 40 PTSHKSLRKFTSGEAARLMKISDSTLRKMTLAGEGPQPELASNGR---RF-YTLGQINEIRQMLAgsTRGRESIDFVPhr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 110 ------PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHIHAEDTLLPF--YLGEKDD 181
Cdd:PRK13869 116 rgsehlQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVD-LDPQASLSALLGVLPETDVGANETLYAAirYDDTRRP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 182 VTYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLpTDPHLMLRLA--IETVAHDYDVIVIDSAPNLGIGTINVVCA 259
Cdd:PRK13869 195 LRDVIRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGT-RDGLFFTRVAqaFDEVADDYDVVVIDCPPQLGFLTLSGLCA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 260 ADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKG--FEPD-VRILLTKYSNSNGSQSPwMEEQIRDAWGSMVLKNVVR 336
Cdd:PRK13869 274 ATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAGgnLQYDfIRYLLTRYEPQDAPQTK-VAALLRNMFEDHVLTNPMV 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 309400378 337 ETDEVGKGQIRMRTVFEqaIDQRSST-GAWRNALSIWEPVCNEIfDRLIKPRW 388
Cdd:PRK13869 353 KSAAVSDAGLTKQTLYE--IGRENLTrSTYDRAMESLDAVNSEI-EALIKMAW 402
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
112-351 |
2.06e-48 |
|
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: 163.67 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 112 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDPQGTASMYHGWVPDLHI--HAEDTLLPfYLGEKDDVTYAIKPT 189
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLID-LDPQSNNSSVEGLEGDIAPalQALAEGLK-GRVNLDPILLKEKSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 190 CWpGLDIIPSCLALHRIETELMGKFDEGKLptdphlmlRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 269
Cdd:pfam01656 79 EG-GLDLIPGNIDLEKFEKELLGPRKEERL--------REALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 270 ELFDYTSALQFFDMLRDLLKNVDLKGFEPdVRILLTKYSNSNGSQS--PWMEEQIRdawGSMVLKnVVRETDEVGKGQIR 347
Cdd:pfam01656 150 EVILVEDAKRLGGVIAALVGGYALLGLKI-IGVVLNKVDGDNHGKLlkEALEELLR---GLPVLG-VIPRDEAVAEAPAR 224
|
....
gi 309400378 348 MRTV 351
Cdd:pfam01656 225 GLPV 228
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
111-302 |
1.11e-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: 112.68 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGWVPDlhiHAEDTLLPFYLGEKDdVTYAIKPTC 190
Cdd:pfam13614 3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDL-DPQGNATSGLGIDKN---NVEKTIYELLIGECN-IEEAIIKTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 191 WPGLDIIPSCLALHRIETELMGKfdegklpTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 270
Cdd:pfam13614 78 IENLDLIPSNIDLAGAEIELIGI-------ENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCE 150
|
170 180 190
....*....|....*....|....*....|....
gi 309400378 271 LFdytsALQffdMLRDLLKNVDL--KGFEPDVRI 302
Cdd:pfam13614 151 YY----ALE---GLSQLLNTIKLvkKRLNPSLEI 177
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
110-320 |
5.85e-28 |
|
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: 106.47 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 110 PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHgwvpdlhihaedtllpfylgekddvtyaikpt 189
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDL-DPQGSLTSWL-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 190 cwpgldiipsclalhrietelmgkfdegklptdphlmlrlaietvahdYDVIVIDSAPNLGIGTINVVCAADVLIVPTPA 269
Cdd:cd02042 48 ------------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQP 79
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 309400378 270 ELFDYTSALQFFDMLRDLLKNVDLKGfePDVRILLTKYSNSNGSQSPWMEE 320
Cdd:cd02042 80 SPFDLDGLAKLLDTLEELKKQLNPPL--LILGILLTRVDPRTKLAREVLEE 128
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
111-285 |
6.67e-18 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 81.44 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASMYHGWVPDlhihaeDTLLPFylgekddVTYAiKPTc 190
Cdd:NF041546 1 IIAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDA-DPQGSALDWAAARED------ERPFPV-------VGLA-RPT- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 191 wpgldiipsclaLHRietelmgkfdegklptdphlmlrlAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 270
Cdd:NF041546 65 ------------LHR------------------------ELPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPS 108
|
170
....*....|....*
gi 309400378 271 LFDYTSALQFFDMLR 285
Cdd:NF041546 109 PYDLWASADTVDLIK 123
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
95-285 |
3.80e-15 |
|
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: 75.22 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 95 DVFGTRLRRAEDVFPPVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNdpqgtasMYHGWVPD-LHIHAEDTLLP 173
Cdd:COG0489 78 ALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDAD-------LRGPSLHRmLGLENRPGLSD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 174 fYLGEKDDVTYAIKPTCWPGLDIIPSclalhrietelmgkfdeGKLPTDP-----HLMLRLAIETVAHDYDVIVIDSAPN 248
Cdd:COG0489 151 -VLAGEASLEDVIQPTEVEGLDVLPA-----------------GPLPPNPsellaSKRLKQLLEELRGRYDYVIIDTPPG 212
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 309400378 249 LGIGTINVVCA-AD-VLIVPTP--AELFDYTSALQFFDMLR 285
Cdd:COG0489 213 LGVADATLLASlVDgVLLVVRPgkTALDDVRKALEMLEKAG 253
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
125-368 |
1.11e-12 |
|
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440223 [Multi-domain] Cd Length: 230 Bit Score: 66.84 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 125 SVSVHLAQDLALKGLRVLLVEGNDPQGTASMYHGWVPDLHIHAedtllpfYLGEKDDVTYAIKPTcwP-GLDIIPSCLAL 203
Cdd:COG0455 1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKATLAD-------VLAGEADLEDAIVQG--PgGLDVLPGGSGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 204 HRIEtELmgkfdegklptDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDM 283
Cdd:COG0455 72 AELA-EL-----------DPEERLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 284 LRDLLKnvdlkgfEPDVRILLTKYSNSNGSQSPWmeEQIRDAWGSMVLKNV-----VRETDEVGKGQIRMRTVFEQAIDQ 358
Cdd:COG0455 140 LRRRLG-------VRRAGVVVNRVRSEAEARDVF--ERLEQVAERFLGVRLrvlgvIPEDPAVREAVRRGRPLVLAAPDS 210
|
250
....*....|
gi 309400378 359 RSSTgAWRNA 368
Cdd:COG0455 211 PAAR-AIREL 219
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
111-268 |
7.32e-10 |
|
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: 58.73 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNdpQGTASMyhgwvpD--LHIHAEDTLLPFYLGEKDDVTYAIKP 188
Cdd:cd02038 2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDAD--LGLANL------DilLGLAPKKTLGDVLKGRVSLEDIIVEG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 189 TcwPGLDIIPSclalhriETELMGKFDegkLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAAD-VLIVPT 267
Cdd:cd02038 74 P--EGLDIIPG-------GSGMEELAN---LDPEQKAKLIEELSSLESNYDYLLIDTGAGISRNVLDFLLAADeVIVVTT 141
|
.
gi 309400378 268 P 268
Cdd:cd02038 142 P 142
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
88-265 |
1.81e-08 |
|
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: 53.73 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 88 EQINHMRdvfgTRLRRAEDVFPP-VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwvpdLHIH 166
Cdd:cd05387 1 EAFRTLR----TNLLFAGSDAGPkVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRL------LGLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 167 AEDTLLPfYLGEKDDVTYAIKPTCWPGLDIIPSclalhrietelmgkfdeGKLPTDPHLML---RLA--IETVAHDYDVI 241
Cdd:cd05387 71 NEPGLSE-VLSGQASLEDVIQSTNIPNLDVLPA-----------------GTVPPNPSELLsspRFAelLEELKEQYDYV 132
|
170 180
....*....|....*....|....
gi 309400378 242 VIDSAPNLGIgtinvvcaADVLIV 265
Cdd:cd05387 133 IIDTPPVLAV--------ADALIL 148
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
111-284 |
1.87e-08 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 54.09 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGnDPQGTASmyhGWVPDlhihaedtllpfylGEKDDvtyaikptc 190
Cdd:PHA02518 2 IIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDL-DPQGSST---DWAEA--------------REEGE--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 191 wpgldiiPSCLALHrietelMGKfdegklptdphlMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAE 270
Cdd:PHA02518 55 -------PLIPVVR------MGK------------SIRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPS 109
|
170
....*....|....
gi 309400378 271 LFDYTSALQFFDML 284
Cdd:PHA02518 110 PFDIWAAPDLVELI 123
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
101-312 |
7.29e-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: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 101 LRRAEDVFPP----VIGVAAHKGGVYKTSVSVHLAQDLA-LKGLRVLLVEGNDPQGTASMYHGWVPDLHIhAEDTLLPfy 175
Cdd:COG4963 90 LARLLDPGAArrgrVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYLDLEPRRGL-ADALRNP-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 176 lgEKDDVTY--AIKPTCWPGLDIIPSCLALHRIEtelmgkfdegklPTDPHLMLRLaIETVAHDYDVIVIDSAPNLGIGT 253
Cdd:COG4963 167 --DRLDETLldRALTRHSSGLSVLAAPADLERAE------------EVSPEAVERL-LDLLRRHFDYVVVDLPRGLNPWT 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 309400378 254 INVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLkgfepdVRILLTKYSNSNG 312
Cdd:COG4963 232 LAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELGLPDDK------VRLVLNRVPKRGE 284
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
111-309 |
1.97e-05 |
|
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: 45.66 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNdpQGTASMyhgwvpDLHIHAED----TLLPFYLGEKDDVTYAI 186
Cdd:cd02036 2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGLRNL------DLILGLENrivyTLVDVLEGECRLEQALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 187 KPTCWPGLDIIPsclalhrietelmGKFDEGKLPTDPHLMLRLaIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIVP 266
Cdd:cd02036 74 KDKRWENLYLLP-------------ASQTRDKDALTPEKLEEL-VKELKDSFDFILIDSPAGIESGFINAIAPADEAIIV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 309400378 267 TPAELfdytSALQFFDMLRDLLKNVDLKgfepDVRILLTKYSN 309
Cdd:cd02036 140 TNPEI----SSVRDADRVIGLLESKGIV----NIGLIVNRYRP 174
|
|
| TadZ-like |
cd17869 |
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ... |
111-311 |
3.12e-05 |
|
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349778 [Multi-domain] Cd Length: 219 Bit Score: 44.84 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTasmyhgwvpDLHIHAEDTLLPfylgekDDVTYAIKPTC 190
Cdd:cd17869 5 VITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQST---------DVFFGASGRYLM------SDHLYTLKSRK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 191 WPGLDIIPSCLALHRIETELMGKFDEgklptdPHLMLRLAIETV---------AHDYDVIVIDSAPNLGIGTINVVCAAD 261
Cdd:cd17869 70 ANLADKLESCVKQHESGVYYFSPFKS------ALDILEIKKDDIlhmitklveAHAYDYIIMDLSFEFSSTVCKLLQASH 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 309400378 262 VLIVPTpaeLFDYTSALQFFDMLRdLLKNVDLKGFEpdvrILLTKYSNSN 311
Cdd:cd17869 144 NNVVIA---LQDANSSYKLNKFLR-ALEDLFQENFS----YIYNKYSNNV 185
|
|
| eps_fam |
TIGR01007 |
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ... |
111-263 |
3.32e-05 |
|
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273392 [Multi-domain] Cd Length: 204 Bit Score: 44.35 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 111 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwvpdLHIHAEDTLLPFYLGEKDDVTYAIKPTC 190
Cdd:TIGR01007 19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGT------FKSQNKITGLTNFLSGTTDLSDAICDTN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309400378 191 WPGLDIIPSclalhrietelmgkfdeGKLPTDPHLML-----RLAIETVAHDYDVIVIDSAPnlgigtINVVCAADVL 263
Cdd:TIGR01007 93 IENLDVITA-----------------GPVPPNPTELLqssnfKTLIETLRKRFDYIIIDTPP------IGTVTDAAII 147
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
110-148 |
3.68e-05 |
|
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: 42.42 E-value: 3.68e-05
10 20 30
....*....|....*....|....*....|....*....
gi 309400378 110 PVIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGND 148
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD 39
|
|
| MerR |
pfam00376 |
MerR family regulatory protein; |
44-71 |
2.60e-04 |
|
MerR family regulatory protein;
Pssm-ID: 425647 [Multi-domain] Cd Length: 38 Bit Score: 38.17 E-value: 2.60e-04
10 20
....*....|....*....|....*...
gi 309400378 44 RIGEAADLVGVSSQAIRDAEKAGRLPHP 71
Cdd:pfam00376 1 TIGEVAKLLGVSPRTLRYYEKIGLLPPP 28
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
123-251 |
9.87e-04 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 41.29 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 123 KTSVSVHLAQDLALKGLRVLLVEGNdpqgtasMYHGWVPDL-HIHAEDTLLPFYLGeKDDVTYAIKPTCWPGLDIIPscl 201
Cdd:PRK11519 540 KTFVCANLAAVISQTNKRVLLIDCD-------MRKGYTHELlGTNNVNGLSDILIG-QGDITTAAKPTSIANFDLIP--- 608
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 309400378 202 alhrietelmgkfdEGKLPTDPHLML---RLA--IETVAHDYDVIVIDSAPNLGI 251
Cdd:PRK11519 609 --------------RGQVPPNPSELLmseRFAelVNWASKNYDLVLIDTPPILAV 649
|
|
| HTH_MerR-SF |
cd04761 |
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ... |
43-96 |
1.19e-03 |
|
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.
Pssm-ID: 133389 [Multi-domain] Cd Length: 49 Bit Score: 36.42 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 309400378 43 WRIGEAADLVGVSSQAIRDAEKAGRLPhpdmEIRGRVEQRVgYTIEQINHMRDV 96
Cdd:cd04761 1 YTIGELAKLTGVSPSTLRYYERIGLLS----PARTEGGYRL-YSDADLERLRLI 49
|
|
| HTH_MERR |
smart00422 |
helix_turn_helix, mercury resistance; |
43-71 |
1.88e-03 |
|
helix_turn_helix, mercury resistance;
Pssm-ID: 197716 Cd Length: 70 Bit Score: 36.73 E-value: 1.88e-03
10 20
....*....|....*....|....*....
gi 309400378 43 WRIGEAADLVGVSSQAIRDAEKAGRLPHP 71
Cdd:smart00422 1 YTIGEVAKLAGVSVRTLRYYERIGLLPPP 29
|
|
| HTH_HMRTR |
cd04770 |
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ... |
44-90 |
2.08e-03 |
|
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.
Pssm-ID: 133398 [Multi-domain] Cd Length: 123 Bit Score: 37.93 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309400378 44 RIGEAADLVGVSSQAIRDAEKAGRLPHP----------DMEIRGRVE-----QRVGYTIEQI 90
Cdd:cd04770 2 KIGELAKAAGVSPDTIRYYERIGLLPPPqrsengyrlyGEADLARLRfirraQALGFSLAEI 63
|
|
| ArsA |
cd02035 |
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ... |
118-144 |
3.07e-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: 39.03 E-value: 3.07e-03
10 20
....*....|....*....|....*..
gi 309400378 118 KGGVYKTSVSVHLAQDLALKGLRVLLV 144
Cdd:cd02035 8 KGGVGKTTIAAATAVRLAEQGKRVLLV 34
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
118-265 |
3.75e-03 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 38.61 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 118 KGGVYKTSVSVHLAQDLALKGLRVLLVEGnDP-QGTASMyhgwvpdLHIHAEDTLLPfYLGEKDDVT--------YAIKP 188
Cdd:COG3640 8 KGGVGKTTLSALLARYLAEKGKPVLAVDA-DPnANLAEA-------LGLEVEADLIK-PLGEMRELIkertgapgGGMFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309400378 189 TCWPGLDIIPSCLalhrIETE-----LMGKFDEGKL----PtdPHLMLRLAIETVA-HDYDVIVIDS---APNLGIGTIN 255
Cdd:COG3640 79 LNPKVDDIPEEYL----VEGDgvdllVMGTIEEGGSgcycP--ENALLRALLNHLVlGNYEYVVVDMeagIEHLGRGTAE 152
|
170
....*....|
gi 309400378 256 VVcaaDVLIV 265
Cdd:COG3640 153 GV---DLLLV 159
|
|
| HTH_CueR |
cd01108 |
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix ... |
45-107 |
7.13e-03 |
|
Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators; Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.
Pssm-ID: 133383 [Multi-domain] Cd Length: 127 Bit Score: 36.39 E-value: 7.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309400378 45 IGEAADLVGVSSQAIRDAEKAGRLPHPDmeiRGRVEQRVgYTIEQINHMRdvFgtrLRRAEDV 107
Cdd:cd01108 3 IGEAAKLTGLSAKMIRYYEEIGLIPPPS---RSDNGYRV-YNQRDIEELR--F---IRRARDL 56
|
|
| |
