|
Name |
Accession |
Description |
Interval |
E-value |
| HTH_54 |
pfam18607 |
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ... |
13-104 |
9.12e-60 |
|
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.
Pssm-ID: 436616 Cd Length: 92 Bit Score: 188.78 E-value: 9.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 13 AEKMLSALTEQIQLQKEELKENEYFQVYAKAAVAKFPKLTRANVDYAVSEMENGGYVFEKRAAGSSTKYAMTLQNIVDIY 92
Cdd:pfam18607 1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80
|
90
....*....|..
gi 1823954277 93 HHRGVPKYRDRH 104
Cdd:pfam18607 81 KHRGIPKYRDRY 92
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
107-392 |
3.33e-43 |
|
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: 151.16 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 107 AMTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVglVETTSAQAMLQNVSrqel 186
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 187 LNEFIVPSVVPGVDVLPASIDdafiasgWESLCAEHLPGQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAA 266
Cdd:COG1192 69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 267 DLLMTPIPPAQVDFHSTLKYLTRLPElvsIIEASGCPCRLQGNIGFMSKLSNKPDHKVCHSLaKEIFGGDMLDAALPRLD 346
Cdd:COG1192 141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1823954277 347 GFERCGESFDTVISANPSTyvgssealkNARTAAEDFAKAVFDRIE 392
Cdd:COG1192 217 ALAEAPSAGKPVFEYDPKS---------KGAKAYRALAEELLERLE 253
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
108-298 |
8.55e-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: 95.68 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLnhtravglvettsaqamlqnvsrqell 187
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL--------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 188 nefivpsvvpgvdvlpasiddafiasgweslcaehlpgqnphavlreniidklkadYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:cd02042 48 --------------------------------------------------------YDYILIDTPPSLGLLTRNALAAAD 71
|
170 180 190
....*....|....*....|....*....|.
gi 1823954277 268 LLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:cd02042 72 LVLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
112-275 |
8.79e-24 |
|
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: 96.88 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 112 VGNLKGGVSKTVSTVSLAHALRahphllFEDLRVLVIDLDPQSSATMflnhtrAVGL----VETTSAQAMLQNVSrqelL 187
Cdd:pfam13614 6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIdknnVEKTIYELLIGECN----I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 188 NEFIVPSVVPGVDVLPASIDdafiASGWEslcAEHLPGQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:pfam13614 70 EEAIIKTVIENLDLIPSNID----LAGAE---IELIGIENRENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALTASD 141
|
....*...
gi 1823954277 268 LLMTPIPP 275
Cdd:pfam13614 142 SVLIPVQC 149
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
62-301 |
4.41e-18 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 85.06 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 62 EMENGGYVfEKRAAgsstkyaMTLQNIVDIYHHRGVPKYRDRHPEAMTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfe 141
Cdd:PHA02519 69 DFETRGRV-ERRAG-------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 142 dlRVLVID-LDPQSSATMFLNHTRAVGLVETTSAQAMLqnVSRQELLNEFIVPSVVPGVDVLPASIDDAFIASGWESL-C 219
Cdd:PHA02519 137 --RVLLIEgNDPQGTASMYHGYVPDLHIHADDTLLPFY--LGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYhD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 220 AEHLPgQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEA 299
Cdd:PHA02519 213 AGKLP-HPPHLMLRA-AIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDL 290
|
..
gi 1823954277 300 SG 301
Cdd:PHA02519 291 GG 292
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
114-279 |
1.20e-11 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 63.34 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 114 NLKGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDPQSSATMFlnhtravglvettsAQAmlqnvsRQEllnefivp 193
Cdd:NF041546 6 NQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED-------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 194 svvpgvdvlpasiDDAFIASGweslcaehLPGQNPHavlREniIDKLKADYDFIFVDSGPHLDAFLKNAIAAADLLMTPI 273
Cdd:NF041546 52 -------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105
|
....*.
gi 1823954277 274 PPAQVD 279
Cdd:NF041546 106 QPSPYD 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HTH_54 |
pfam18607 |
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful ... |
13-104 |
9.12e-60 |
|
ParA helix turn helix domain; The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region.
Pssm-ID: 436616 Cd Length: 92 Bit Score: 188.78 E-value: 9.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 13 AEKMLSALTEQIQLQKEELKENEYFQVYAKAAVAKFPKLTRANVDYAVSEMENGGYVFEKRAAGSSTKYAMTLQNIVDIY 92
Cdd:pfam18607 1 AERMLQALTEQIQKQKKELDETEYYQTYSKAAVAKLPKLSRAIVDYAVSEMEEAGYVFDKRPAGSTTKYALTIQNIIDIY 80
|
90
....*....|..
gi 1823954277 93 HHRGVPKYRDRH 104
Cdd:pfam18607 81 KHRGIPKYRDRY 92
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
107-392 |
3.33e-43 |
|
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: 151.16 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 107 AMTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVglVETTSAQAMLQNVSrqel 186
Cdd:COG1192 1 MKVIAVANQKGGVGKTTTAVNLAAALARR------GKRVLLIDLDPQGNLTSGLGLDPDD--LDPTLYDLLLDDAP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 187 LNEFIVPSVVPGVDVLPASIDdafiasgWESLCAEHLPGQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAA 266
Cdd:COG1192 69 LEDAIVPTEIPGLDLIPANID-------LAGAEIELVSRPGRELRLKR-ALAPLADDYDYILIDCPPSLGLLTLNALAAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 267 DLLMTPIPPAQVDFHSTLKYLTRLPElvsIIEASGCPCRLQGNIGFMSKLSNKPDHKVCHSLaKEIFGGDMLDAALPRLD 346
Cdd:COG1192 141 DSVLIPVQPEYLSLEGLAQLLETIEE---VREDLNPKLEILGILLTMVDPRTRLSREVLEEL-REEFGDKVLDTVIPRSV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1823954277 347 GFERCGESFDTVISANPSTyvgssealkNARTAAEDFAKAVFDRIE 392
Cdd:COG1192 217 ALAEAPSAGKPVFEYDPKS---------KGAKAYRALAEELLERLE 253
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
108-298 |
8.55e-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: 95.68 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLnhtravglvettsaqamlqnvsrqell 187
Cdd:cd02042 1 KVIAVANQKGGVGKTTLAVNLAAALALR------GKRVLLIDLDPQGSLTSWL--------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 188 nefivpsvvpgvdvlpasiddafiasgweslcaehlpgqnphavlreniidklkadYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:cd02042 48 --------------------------------------------------------YDYILIDTPPSLGLLTRNALAAAD 71
|
170 180 190
....*....|....*....|....*....|.
gi 1823954277 268 LLMTPIPPAQVDFHSTLKYLTRLPELVSIIE 298
Cdd:cd02042 72 LVLIPVQPSPFDLDGLAKLLDTLEELKKQLN 102
|
|
| AAA_31 |
pfam13614 |
AAA domain; This family includes a wide variety of AAA domains including some that have lost ... |
112-275 |
8.79e-24 |
|
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: 96.88 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 112 VGNLKGGVSKTVSTVSLAHALRahphllFEDLRVLVIDLDPQSSATMflnhtrAVGL----VETTSAQAMLQNVSrqelL 187
Cdd:pfam13614 6 IANQKGGVGKTTTSVNLAAALA------KKGKKVLLIDLDPQGNATS------GLGIdknnVEKTIYELLIGECN----I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 188 NEFIVPSVVPGVDVLPASIDdafiASGWEslcAEHLPGQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:pfam13614 70 EEAIIKTVIENLDLIPSNID----LAGAE---IELIGIENRENILKE-ALEPVKDNYDYIIIDCPPSLGLLTINALTASD 141
|
....*...
gi 1823954277 268 LLMTPIPP 275
Cdd:pfam13614 142 SVLIPVQC 149
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
110-358 |
1.93e-18 |
|
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: 83.55 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 110 LFVGNLKGGVSKTVSTVSLAHALRAHphllfeDLRVLVIDLDPQSSATMFLNHTRAVGLVETTSAQAMLQNVSRQELLne 189
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARR------GLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPIL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 190 FIVPSVVPGVDVLPASIDDAFIASGWESLCAEHLpgqnphavLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAADLL 269
Cdd:pfam01656 73 LKEKSDEGGLDLIPGNIDLEKFEKELLGPRKEER--------LRE-ALEALKEDYDYVIIDGAPGLGELLRNALIAADYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 270 MTPIPPAQVDFHStlkyLTRLPELVSIIEASGCPCRLQgNIGFM-SKLSNKPDHKVCHSLAKEIFGGDMLDAALPRLDGF 348
Cdd:pfam01656 144 IIPLEPEVILVED----AKRLGGVIAALVGGYALLGLK-IIGVVlNKVDGDNHGKLLKEALEELLRGLPVLGVIPRDEAV 218
|
250
....*....|
gi 1823954277 349 ERCGESFDTV 358
Cdd:pfam01656 219 AEAPARGLPV 228
|
|
| PHA02519 |
PHA02519 |
plasmid partition protein SopA; Reviewed |
62-301 |
4.41e-18 |
|
plasmid partition protein SopA; Reviewed
Pssm-ID: 107201 [Multi-domain] Cd Length: 387 Bit Score: 85.06 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 62 EMENGGYVfEKRAAgsstkyaMTLQNIVDIYHHRGVPKYRDRHPEAMTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfe 141
Cdd:PHA02519 69 DFETRGRV-ERRAG-------YTIDQISHMRDHFGNPNQRPDDKNPVVLAVMSHKGGVYKTSSAVHTAQWLALQGH---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 142 dlRVLVID-LDPQSSATMFLNHTRAVGLVETTSAQAMLqnVSRQELLNEFIVPSVVPGVDVLPASIDDAFIASGWESL-C 219
Cdd:PHA02519 137 --RVLLIEgNDPQGTASMYHGYVPDLHIHADDTLLPFY--LGERDNAEYAIKPTCWPGLDIIPSCLALHRIETDLMQYhD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 220 AEHLPgQNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEA 299
Cdd:PHA02519 213 AGKLP-HPPHLMLRA-AIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPAELFDYVSVLQFFTMLLDLLATVDL 290
|
..
gi 1823954277 300 SG 301
Cdd:PHA02519 291 GG 292
|
|
| PRK13705 |
PRK13705 |
plasmid-partitioning protein SopA; Provisional |
87-301 |
1.10e-17 |
|
plasmid-partitioning protein SopA; Provisional
Pssm-ID: 184261 [Multi-domain] Cd Length: 388 Bit Score: 83.87 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 87 NIVDIYHHRGVPKYRDRHPEA---MTLFVGNLKGGVSKTVSTVSLAHalrahpHLLFEDLRVLVID-LDPQSSATMFlnH 162
Cdd:PRK13705 83 TIEQINHMRDVFGTRLRRAEDvfpPVIGVAAHKGGVYKTSVSVHLAQ------DLALKGLRVLLVEgNDPQGTASMY--H 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 163 TRAVGLVETTSAQAMLQNVSRQELLNEFIVPSVVPGVDVLPASIDDAFIASGWESLCAEHLPGQNPHAVLREnIIDKLKA 242
Cdd:PRK13705 155 GWVPDLHIHAEDTLLPFYLGEKDDATYAIKPTCWPGLDIIPSCLALHRIETELMGKFDEGKLPTDPHLMLRL-AIETVAH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1823954277 243 DYDFIFVDSGPHLDAFLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEASG 301
Cdd:PRK13705 234 DYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFDMLRDLLKNVDLKG 292
|
|
| CpaE |
COG4963 |
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ... |
108-290 |
1.02e-13 |
|
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: 71.68 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 108 MTLFVGnLKGGVSKTVSTVSLAHALRAHPhllfeDLRVLVIDLDPQS-SATMFLNHTRAVGLVEttsaqaMLQNVSR--Q 184
Cdd:COG4963 104 VIAVVG-AKGGVGATTLAVNLAWALARES-----GRRVLLVDLDLQFgDVALYLDLEPRRGLAD------ALRNPDRldE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 185 ELLNEFIVPsVVPGVDVLPASIDdafiasgweslcAEHLPGQNPHAVLRenIIDKLKADYDFIFVDSGPHLDAFLKNAIA 264
Cdd:COG4963 172 TLLDRALTR-HSSGLSVLAAPAD------------LERAEEVSPEAVER--LLDLLRRHFDYVVVDLPRGLNPWTLAALE 236
|
170 180
....*....|....*....|....*....
gi 1823954277 265 AAD---LLMTPIPPAQVDFHSTLKYLTRL 290
Cdd:COG4963 237 AADevvLVTEPDLPSLRNAKRLLDLLREL 265
|
|
| PRK13869 |
PRK13869 |
plasmid-partitioning protein RepA; Provisional |
110-391 |
3.21e-12 |
|
plasmid-partitioning protein RepA; Provisional
Pssm-ID: 139929 [Multi-domain] Cd Length: 405 Bit Score: 67.39 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 110 LFVGNLKGGVSKTVSTVSLAHalrahpHLLFEDLRVLVIDLDPQSSATMFLNHTRAVGLVETTSAQAMLQNVSRQELLNE 189
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQ------YLALQGYRVLAVDLDPQASLSALLGVLPETDVGANETLYAAIRYDDTRRPLRD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 190 FIVPSVVPGVDVLPASIddafiasgwESLCAEHlpgQNPHAV----LRENI--------IDKLKADYDFIFVDSGPHLDA 257
Cdd:PRK13869 198 VIRPTYFDGLHLVPGNL---------ELMEFEH---TTPKALsdkgTRDGLfftrvaqaFDEVADDYDVVVIDCPPQLGF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 258 FLKNAIAAADLLMTPIPPAQVDFHSTLKYLTRLPELVSIIEASGcpcrlqGNI--GFMSKL------SNKPDHKVChSLA 329
Cdd:PRK13869 266 LTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLGVVKEAG------GNLqyDFIRYLltryepQDAPQTKVA-ALL 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823954277 330 KEIFGGDMLDAALPRLDGFERCGESFDTVI-----SANPSTYVGSSEALKNARTAAEDFAKAVFDRI 391
Cdd:PRK13869 339 RNMFEDHVLTNPMVKSAAVSDAGLTKQTLYeigreNLTRSTYDRAMESLDAVNSEIEALIKMAWGRA 405
|
|
| ParA_partition |
NF041546 |
ParA family partition ATPase; |
114-279 |
1.20e-11 |
|
ParA family partition ATPase;
Pssm-ID: 469431 [Multi-domain] Cd Length: 202 Bit Score: 63.34 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 114 NLKGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDPQSSATMFlnhtravglvettsAQAmlqnvsRQEllnefivp 193
Cdd:NF041546 6 NQKGGVGKTTLATHLAAALAR------RGYRVLLVDADPQGSALDW--------------AAA------RED-------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 194 svvpgvdvlpasiDDAFIASGweslcaehLPGQNPHavlREniIDKLKADYDFIFVDSGPHLDAFLKNAIAAADLLMTPI 273
Cdd:NF041546 52 -------------ERPFPVVG--------LARPTLH---RE--LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPV 105
|
....*.
gi 1823954277 274 PPAQVD 279
Cdd:NF041546 106 QPSPYD 111
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
116-253 |
3.09e-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: 60.59 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 116 KGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDP-QSSATMFLNHTRAVGLVETTSAQAMLQNVsrqellnefIVPS 194
Cdd:COG0489 101 KGGEGKSTVAANLALALAQ------SGKRVLLIDADLrGPSLHRMLGLENRPGLSDVLAGEASLEDV---------IQPT 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823954277 195 VVPGVDVLPASiddafiasgweslcaehLPGQNPHAVLR----ENIIDKLKADYDFIFVDSGP 253
Cdd:COG0489 166 EVEGLDVLPAG-----------------PLPPNPSELLAskrlKQLLEELRGRYDYVIIDTPP 211
|
|
| CpaE-like |
cd03111 |
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ... |
109-272 |
1.09e-09 |
|
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: 58.44 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 109 TLFVGnLKGGVSKTVSTVSLAHALRAHPhllfeDLRVLVIDLD-PQSSATMFLNHTRAVGLVEttsaqaMLQNVSR--QE 185
Cdd:cd03111 3 VAVVG-AKGGVGASTLAVNLAQELAQRA-----KDKVLLIDLDlPFGDLGLYLNLRPDYDLAD------VIQNLDRldRT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 186 LLNEFIVPsVVPGVDVL--PASIDDAfiasgwESLCAEHLpgqnphavlrENIIDKLKADYDFIFVDSGPHLDAFLKNAI 263
Cdd:cd03111 71 LLDSAVTR-HSSGLSLLpaPQELEDL------EALGAEQV----------DKLLQVLRAFYDHIIVDLGHFLDEVTLAVL 133
|
170
....*....|..
gi 1823954277 264 AAAD---LLMTP 272
Cdd:cd03111 134 EAADeilLVTQQ 145
|
|
| FlhG |
COG0455 |
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ... |
125-289 |
4.24e-09 |
|
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: 56.44 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 125 TVSLAHALRAHPHllfedlRVLVIDLDPQSsATMflnHTRaVGLVETTSaqamLQNVSRQEL-LNEFIVPsVVPGVDVLP 203
Cdd:COG0455 3 AVNLAAALARLGK------RVLLVDADLGL-ANL---DVL-LGLEPKAT----LADVLAGEAdLEDAIVQ-GPGGLDVLP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 204 ASIDdafiASGWESLcaehlpgqNPHAVLREnIIDKLKADYDFIFVDSGPHLDAFLKNAIAAAD---LLMTPIPPAQVDF 280
Cdd:COG0455 67 GGSG----PAELAEL--------DPEERLIR-VLEELERFYDVVLVDTGAGISDSVLLFLAAADevvVVTTPEPTSITDA 133
|
....*....
gi 1823954277 281 HSTLKYLTR 289
Cdd:COG0455 134 YALLKLLRR 142
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
108-299 |
5.28e-09 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 56.01 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 108 MTLFVGNLKGGVSKTVSTVSLAHALRAHPHllfedlRVLVIDLDPQSSATMFLNhTRAVGlVETTSAQAMLQNVSRQell 187
Cdd:PHA02518 1 KIIAVLNQKGGAGKTTVATNLASWLHADGH------KVLLVDLDPQGSSTDWAE-AREEG-EPLIPVVRMGKSIRAD--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 188 nefivpsvvpgvdvlpasiddafiasgweslcaehlpgqnphavlreniIDKLKADYDFIFVDSGPHLDAFLKNAIAAAD 267
Cdd:PHA02518 70 -------------------------------------------------LPKVASGYDYVVVDGAPQDSELARAALRIAD 100
|
170 180 190
....*....|....*....|....*....|..
gi 1823954277 268 LLMTPIPPAQVDFHStlkyltrLPELVSIIEA 299
Cdd:PHA02518 101 MVLIPVQPSPFDIWA-------APDLVELIKA 125
|
|
| FlhG-like |
cd02038 |
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ... |
116-289 |
1.66e-07 |
|
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: 51.80 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 116 KGGVSKTVSTVSLAHALRAhphllfEDLRVLVIDLDpqssatmflnhtraVGL--VET---TSAQAMLQNVSRQELLNEF 190
Cdd:cd02038 9 KGGVGKTNVSANLALALSK------LGKRVLLLDAD--------------LGLanLDIllgLAPKKTLGDVLKGRVSLED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 191 IVPSVVPGVDVLPASIDDafiaSGWESLCAEHLpgqnphAVLRENIiDKLKADYDFIFVDSGPHLDAFLKNAIAAAD--- 267
Cdd:cd02038 69 IIVEGPEGLDIIPGGSGM----EELANLDPEQK------AKLIEEL-SSLESNYDYLLIDTGAGISRNVLDFLLAADevi 137
|
170 180
....*....|....*....|..
gi 1823954277 268 LLMTPIPPAQVDFHSTLKYLTR 289
Cdd:cd02038 138 VVTTPEPTSITDAYALIKVLSR 159
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
121-253 |
3.92e-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: 49.88 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 121 KTVSTVSLAHALRAhphllfEDLRVLVIDLDP-QSSATMFLNHTRAVGLVETtsaqamlqnVSRQELLNEFIVPSVVPGV 199
Cdd:cd05387 33 KSTVAANLAVALAQ------SGKRVLLIDADLrRPSLHRLLGLPNEPGLSEV---------LSGQASLEDVIQSTNIPNL 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1823954277 200 DVLPASiddAFIASGWESLCAEHLpgqnphavlrENIIDKLKADYDFIFVDSGP 253
Cdd:cd05387 98 DVLPAG---TVPPNPSELLSSPRF----------AELLEELKEQYDYVIIDTPP 138
|
|
| MinD |
cd02036 |
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ... |
116-267 |
5.55e-04 |
|
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: 41.03 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 116 KGGVSKTVSTVSLAHALRAHPHllfedlRVLVIDLDpqssatmflnhtraVGLvettsaqamlQNVsrqELLNEFIVPSV 195
Cdd:cd02036 9 KGGVGKTTTTANLGVALAKLGK------KVLLIDAD--------------IGL----------RNL---DLILGLENRIV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823954277 196 VPGVDVLP--ASIDDAFIAS-GWESLCAehLPGQ--------NPHAVlrENIIDKLKADYDFIFVDSGPHLDAFLKNAIA 264
Cdd:cd02036 56 YTLVDVLEgeCRLEQALIKDkRWENLYL--LPASqtrdkdalTPEKL--EELVKELKDSFDFILIDSPAGIESGFINAIA 131
|
...
gi 1823954277 265 AAD 267
Cdd:cd02036 132 PAD 134
|
|
| |
