|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-416 |
3.70e-127 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 372.93 E-value: 3.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 2 DEYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAE 81
Cdd:COG0849 3 SNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 82 ICEIILNKGVVAVSsdDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSE 161
Cdd:COG0849 83 HIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 162 STIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDIS 241
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 242 LCLNIPMSEAEKVKLKYG--KINLQKEEDfKIKVNA-SYDNTVEISYNILNEIISFRVEELLSLVKKKLVKNEQMTNISS 318
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGsaLASLADEDE-TIEVPGiGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEKLPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 319 -IVIVGGGiALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVVedvlntlkANPIDEDNKEFNKKREKY 392
Cdd:COG0849 320 gVVLTGGG-SQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLL--------LYAAKNQEERFEPVKEKK 390
|
410 420
....*....|....*....|....
gi 499411894 393 NRneeeifyeeekeGIISKIKEFF 416
Cdd:COG0849 391 KG------------GLFGRIKRWF 402
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
3-366 |
1.48e-118 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 349.91 E-value: 1.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 3 EYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEI 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 83 CEIILNKGVVAVSsDDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSES 162
Cdd:cd24048 81 IRSVNSRGVIAIS-DKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 163 TIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISL 242
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 243 CLNIPMSEAEKVKLKYG---KINLQKEEDFKIKVNASYDNtVEISYNILNEIISFRVEELLSLVKKKLVKNEQMTNISSI 319
Cdd:cd24048 240 GLNTPFEEAERLKIKYGsalSEEADEDEIIEIPGVGGREP-REVSRRELAEIIEARVEEILELVKKELKESGYEDLLPGG 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499411894 320 VIVGGGIALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVV 366
Cdd:cd24048 319 IVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLL 370
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
4-366 |
1.45e-99 |
|
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 301.48 E-value: 1.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 4 YIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEIC 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 84 EIILNKGVVAVSSDdrEIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSEST 163
Cdd:TIGR01174 81 KSQNSIGVVAIKDK--EVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 164 IISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLC 243
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 244 LNIPMSEAEKVKLKYGKINLQ-KEEDFKIKVNASYDNT-VEISYNILNEIISFRVEELLSLVK-KKLVKNEQMTNISSIV 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPlEGPDENIEIPSVGERPpRSLSRKELAEIIEARAEEILEIVKqKELRKSGFKEELNGGI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499411894 321 IVGGGIALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVV 366
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLL 369
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
5-193 |
7.89e-61 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 195.39 E-value: 7.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 5 IVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEICE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 85 IILNKGVVAVssDDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSESTI 164
Cdd:smart00842 81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|....*....
gi 499411894 165 ISNLLKCIKKSGLIVKGMVFQPMANAVSV 193
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
2-366 |
1.74e-53 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 183.83 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 2 DEYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAE 81
Cdd:PRK09472 7 RKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 82 ICEIILNKGVVAVSsdDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSE 161
Cdd:PRK09472 87 HISCQNEIGMVPIS--EEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 162 STIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDIS 241
Cdd:PRK09472 165 NDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 242 LCLNIPMSEAEKVKLKYGkinlqkeedFKIKVNASYDNTVEI-----------SYNILNEIISFRVEELLSLVKKKLVK- 309
Cdd:PRK09472 245 YAFGTPPSDAEAIKVRHG---------CALGSIVGKDESVEVpsvggrpprslQRQTLAEVIEPRYTELLNLVNEEILQl 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 310 NEQMT------NISSIVIVGGGIALLKGVNEIGKDIMDKSTRIGMP-------EYIgtASPLYSSAVGVV 366
Cdd:PRK09472 316 QEQLRqqgvkhHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlnitgltDYA--QEPYYSTAVGLL 383
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
205-364 |
3.46e-35 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 127.83 E-value: 3.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 205 LLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLCLNIPMSEAEKVKLKYGKINLQKEEDFKIKVNASyDNTVEIS 284
Cdd:pfam14450 2 LIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDEVPGVGG-REPREIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 285 YNILNEIISFRVEELLSLVKKKLVKNEQM--------TNISSIVIVGGGiALLKGVNEIGKDIMDKSTRIGMPEYIGTAS 356
Cdd:pfam14450 81 RKELAEIIEARVEEILELVRAELEDREVLpgeyvrleVDVHGIVLTGGG-SALPGLVELAERALGLPVRIGSPDGIGGRN 159
|
....*...
gi 499411894 357 PLYSSAVG 364
Cdd:pfam14450 160 PAYATALG 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-416 |
3.70e-127 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 372.93 E-value: 3.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 2 DEYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAE 81
Cdd:COG0849 3 SNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 82 ICEIILNKGVVAVSsdDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSE 161
Cdd:COG0849 83 HIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 162 STIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDIS 241
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 242 LCLNIPMSEAEKVKLKYG--KINLQKEEDfKIKVNA-SYDNTVEISYNILNEIISFRVEELLSLVKKKLVKNEQMTNISS 318
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGsaLASLADEDE-TIEVPGiGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEKLPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 319 -IVIVGGGiALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVVedvlntlkANPIDEDNKEFNKKREKY 392
Cdd:COG0849 320 gVVLTGGG-SQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLL--------LYAAKNQEERFEPVKEKK 390
|
410 420
....*....|....*....|....
gi 499411894 393 NRneeeifyeeekeGIISKIKEFF 416
Cdd:COG0849 391 KG------------GLFGRIKRWF 402
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
3-366 |
1.48e-118 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 349.91 E-value: 1.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 3 EYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEI 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 83 CEIILNKGVVAVSsDDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSES 162
Cdd:cd24048 81 IRSVNSRGVIAIS-DKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 163 TIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISL 242
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 243 CLNIPMSEAEKVKLKYG---KINLQKEEDFKIKVNASYDNtVEISYNILNEIISFRVEELLSLVKKKLVKNEQMTNISSI 319
Cdd:cd24048 240 GLNTPFEEAERLKIKYGsalSEEADEDEIIEIPGVGGREP-REVSRRELAEIIEARVEEILELVKKELKESGYEDLLPGG 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499411894 320 VIVGGGIALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVV 366
Cdd:cd24048 319 IVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLL 370
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
4-366 |
1.45e-99 |
|
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 301.48 E-value: 1.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 4 YIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEIC 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 84 EIILNKGVVAVSSDdrEIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSEST 163
Cdd:TIGR01174 81 KSQNSIGVVAIKDK--EVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 164 IISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLC 243
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 244 LNIPMSEAEKVKLKYGKINLQ-KEEDFKIKVNASYDNT-VEISYNILNEIISFRVEELLSLVK-KKLVKNEQMTNISSIV 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPlEGPDENIEIPSVGERPpRSLSRKELAEIIEARAEEILEIVKqKELRKSGFKEELNGGI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499411894 321 IVGGGIALLKGVNEIGKDIMDKSTRIGMPEYIG-----TASPLYSSAVGVV 366
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLL 369
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
5-193 |
7.89e-61 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 195.39 E-value: 7.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 5 IVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEICE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 85 IILNKGVVAVssDDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSESTI 164
Cdd:smart00842 81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|....*....
gi 499411894 165 ISNLLKCIKKSGLIVKGMVFQPMANAVSV 193
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
2-366 |
1.74e-53 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 183.83 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 2 DEYIVGLNIGSSSVCTAAGKLDKYGKIQIVGINYVPCTGIKKGVVIDIDETSEGIKTSIYQLQTMIDAKVTEVYLSIPAE 81
Cdd:PRK09472 7 RKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 82 ICEIILNKGVVAVSsdDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQIILSE 161
Cdd:PRK09472 87 HISCQNEIGMVPIS--EEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 162 STIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDIS 241
Cdd:PRK09472 165 NDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 242 LCLNIPMSEAEKVKLKYGkinlqkeedFKIKVNASYDNTVEI-----------SYNILNEIISFRVEELLSLVKKKLVK- 309
Cdd:PRK09472 245 YAFGTPPSDAEAIKVRHG---------CALGSIVGKDESVEVpsvggrpprslQRQTLAEVIEPRYTELLNLVNEEILQl 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 310 NEQMT------NISSIVIVGGGIALLKGVNEIGKDIMDKSTRIGMP-------EYIgtASPLYSSAVGVV 366
Cdd:PRK09472 316 QEQLRqqgvkhHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlnitgltDYA--QEPYYSTAVGLL 383
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
205-364 |
3.46e-35 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 127.83 E-value: 3.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 205 LLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLCLNIPMSEAEKVKLKYGKINLQKEEDFKIKVNASyDNTVEIS 284
Cdd:pfam14450 2 LIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDEVPGVGG-REPREIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 285 YNILNEIISFRVEELLSLVKKKLVKNEQM--------TNISSIVIVGGGiALLKGVNEIGKDIMDKSTRIGMPEYIGTAS 356
Cdd:pfam14450 81 RKELAEIIEARVEEILELVRAELEDREVLpgeyvrleVDVHGIVLTGGG-SALPGLVELAERALGLPVRIGSPDGIGGRN 159
|
....*...
gi 499411894 357 PLYSSAVG 364
Cdd:pfam14450 160 PAYATALG 167
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
6-364 |
2.23e-24 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 102.74 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 6 VGLNIGSSSVCTAAGKLDKyGKIQIV--GINYVPCTGIKKGVVIDIDETSEGIKTSIYQlqtmIDAKVTEVYLSIPAEic 83
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSG-GGLVLVafAIIPLPEGAIVDGEIADPEALAEALKKLLKE----NKIKGKKVVVALPGS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 84 EIIlnkgvvavssddreikkndvsralnaSRIITIP--SNKEIIGVIP-----------EEYIVDgYNNIKDPIGMSGvr 150
Cdd:cd24049 74 DVI--------------------------VRTIKLPkmPEKELEEAIRfeaeqylpfplEEVVLD-YQILGEVEEGGE-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 151 lEVDAQIILSESTIISNLLKCIKKSGLIVKGMVFQPMA--NAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDK 228
Cdd:cd24049 125 -KLEVLVVAAPKEIVESYLELLKEAGLKPVAIDVESFAlaRALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 229 ISIGGNMITNDISLCLNIPMSEAEKVKLKYGkINLQKEEDFKIKVNASYDNTVEisyNILNEI---ISFrveellslvkk 305
Cdd:cd24049 204 IPVGGNDITEAIAKALGLSFEEAEELKREYG-LLLEGEEGELKKVAEALRPVLE---RLVSEIrrsLDY----------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 306 kLVKNEQMTNISSIVIVGGGiALLKGVNEIGKDIMDKSTRIGMP-----------EYIGTASPLYSSAVG 364
Cdd:cd24049 269 -YRSQNGGEPIDKIYLTGGG-SLLPGLDEYLSERLGIPVEILNPfsnieskksddEELKEDAPLFAVAIG 336
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
88-158 |
2.42e-22 |
|
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.
Pssm-ID: 460571 [Multi-domain] Cd Length: 73 Bit Score: 89.86 E-value: 2.42e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499411894 88 NKGVVAVSsdDREIKKNDVSRALNASRIITIPSNKEIIGVIPEEYIVDGYNNIKDPIGMSGVRLEVDAQII 158
Cdd:pfam02491 4 SSGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVV 72
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
156-328 |
1.34e-17 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 82.34 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 156 QIILSESTIISNLLKCIKKSGLIVKGMVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNM 235
Cdd:cd24004 69 DVVIAIAKVVESLLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 236 ITNDISLCLNIPMSEAEKVKLKYGKINLQKEEDfkikvnasyDNTVEISYNILNEIISFRVEELLSLVKKKLVK-NEQMT 314
Cdd:cd24004 149 FTKAIAEGFLISFEEAEKIKRTYGIFLLIEAKD---------QLGFTINKKEVYDIIKPVLEELASGIANAIEEyNGKFK 219
|
170
....*....|....
gi 499411894 315 NISSIVIVGGGIAL 328
Cdd:cd24004 220 LPDAVYLVGGGSKL 233
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
5-232 |
9.62e-11 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 62.18 E-value: 9.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 5 IVGLNIGSSSVCTAAGKLDKyGKIQIVGINYVPctgIKKGVVIDID-ETSEGIKTSIYQLQTMIDAKVTEVYLSIPAEic 83
Cdd:COG4972 4 LVGIDIGSSSIKLVELSKSG-GGYRLERYAEEP---LPEGAVVDGNiVDPEAVAEALKELLKRLKIKTKRVAIAVPGS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 84 EIIlnkgvvavssddreikkndvsralnaSRIITIP--SNKEIIGVIP-----------EEYIVDgYNNIKDPIGMSGvr 150
Cdd:COG4972 78 SVI--------------------------TRKITLPalSEKELEEAIEfeaeqyipfplEEVVLD-FQVLGPSEEGPE-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 151 lEVDAQIILSESTIISNLLKCIKKSGLIVKGMVFQPMA--NAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDK 228
Cdd:COG4972 129 -KVEVLLVAARKEVVEDYVELLEAAGLKPVVVDVEPFAllRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTRE 207
|
....
gi 499411894 229 ISIG 232
Cdd:COG4972 208 IPFG 211
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
182-364 |
1.54e-07 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 52.86 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 182 MVFQPMANAVSVLKEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDIS------LCLNIPMSEAEKVK 255
Cdd:cd10225 124 LIEEPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrkYNLLIGERTAERIK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 256 LKYGK-INLQKEEDFKIK-VNASYDN--TVEISYNILNEIISFRVEELLSLVKKKLvknEQMT-NISS------IVIVGG 324
Cdd:cd10225 204 IEIGSaYPLDEELSMEVRgRDLVTGLprTIEITSEEVREALEEPVNAIVEAVRSTL---ERTPpELAAdivdrgIVLTGG 280
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499411894 325 GiALLKGvneigkdiMDK--STRIGMPEYIgTASPLYSSAVG 364
Cdd:cd10225 281 G-ALLRG--------LDEllREETGLPVHV-ADDPLTCVAKG 312
|
|
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
42-259 |
3.90e-06 |
|
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.
Pssm-ID: 273484 [Multi-domain] Cd Length: 348 Bit Score: 48.63 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 42 KKGVVIDIDETSEGIKtsIYQLQTMIDAKVTEVY--LSIPAEICEiilNKGVVAVSSDDREIKKNDVSRALNASRIIT-I 118
Cdd:TIGR01175 1 KKSLLVGIDIGSTSVK--VAQLKRSGDRYKLEHYavEPLPAGIFT---EGHIVEYQAVAEALKELLSELGINTKKAATaV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 119 PSNKEIIGVIP--------------------------EEYIVDgYNNIKDPIGMSGVRLEVdaQIILSESTIISNLLKCI 172
Cdd:TIGR01175 76 PGSAVITKVIPvpaglderelefavyieashyipypiEEVSLD-FEKLGLKANNPESTVQV--LLAATRKEVVDSRLHAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 173 KKSGLIVKGMVFQPMA--NAVSVLKEE-----ETETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLCLN 245
Cdd:TIGR01175 153 KLAGLEPKVVDVESFAllRAWRLLGEQlasrtYRLTDAALVDIGATSSTLNLLHPGRMLFTREVPFGTRQLTSELSRAYG 232
|
250
....*....|....
gi 499411894 246 IPMSEAEKVKLKYG 259
Cdd:TIGR01175 233 LNPEEAGEAKQQGG 246
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
148-255 |
2.73e-05 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 45.33 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 148 GVRLEVDAQ-----IILSESTIISNLLKcikKSGLIVKGMVFQPMAnAVSVLKEEEtetGVLLlDVGAETTNMTVFKEGK 222
Cdd:cd24047 61 GVELTSAATafppgTGERDARAIRNVLE---GAGLEVSNVVDEPTA-ANAVLGIRD---GAVV-DIGGGTTGIAVLKDGK 132
|
90 100 110
....*....|....*....|....*....|...
gi 499411894 223 VIYQDKISIGGNMITNDISLCLNIPMSEAEKVK 255
Cdd:cd24047 133 VVYTADEPTGGTHLSLVLAGNYGISFEEAEIIK 165
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
200-273 |
3.38e-05 |
|
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.
Pssm-ID: 431656 [Multi-domain] Cd Length: 340 Bit Score: 45.74 E-value: 3.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499411894 200 ETGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLCLNIPMSEAEKvklkyGKINLQKEEDFKIKV 273
Cdd:pfam11104 179 DKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVRRYGMSYEEAEI-----AKRNGDLPEDYESEV 247
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
196-330 |
5.19e-05 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 44.95 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 196 EEETETGVLLLDVGAETTNMTVFKEGKVIYQDK---ISIGGNMITNDISLCL-------NIPMSEAEKVkLKYGKINLQ- 264
Cdd:cd24022 169 EEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHARsgtIELGVLDVRDALKDALkkrfglsSISDAELDRA-LRTGKFRLNg 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499411894 265 -KEEDFKIKVNASYDNTVEisyNILNEIisfrveellslvkKKLVKNEQmtNISSIVIVGGGIALLK 330
Cdd:cd24022 248 gKEVDVSDLVNEAIAEVAE---RILNEI-------------KRRLGDAS--DLDRVIFVGGGAELLE 296
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
201-364 |
1.94e-04 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 201 TGVLLLDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDI------SLCLNIPMSEAEKVKLKYGK-INLQKEEDFKIK- 272
Cdd:COG1077 151 TGNMVVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIiqyvrkKYNLLIGERTAEEIKIEIGSaYPLEEELTMEVRg 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 273 --VNASYDNTVEISYNILNEIISFRVEELLSLVKKKLvknEQM-----TNISS--IVIVGGGiALLKGvneigkdiMDK- 342
Cdd:COG1077 231 rdLVTGLPKTITITSEEIREALEEPLNAIVEAIKSVL---EKTppelaADIVDrgIVLTGGG-ALLRG--------LDKl 298
|
170 180
....*....|....*....|...
gi 499411894 343 -STRIGMPEYIGtASPLYSSAVG 364
Cdd:COG1077 299 lSEETGLPVHVA-EDPLTCVARG 320
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
175-255 |
2.84e-04 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 42.51 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 175 SGLIVKGMVFQPMAnAVSVLKeeeTETGVLLlDVGAETTNMTVFKEGKVIYQDKISIGGNMITNDISLCLNIPMSEAEKV 254
Cdd:PRK15080 114 AGLEVTHVLDEPTA-AAAVLG---IDNGAVV-DIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQY 188
|
.
gi 499411894 255 K 255
Cdd:PRK15080 189 K 189
|
|
| ASKHA_NBD_ParM_Alp7A-like |
cd24023 |
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ... |
195-330 |
4.62e-04 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.
Pssm-ID: 466873 [Multi-domain] Cd Length: 368 Bit Score: 41.93 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411894 195 KEEETETGVLLLDVGAETTNMTVFKEGKVIYQDKISI--GGNMITNDISLCLNIpMSEAEKVKLKYGKINLQKEEDFKIK 272
Cdd:cd24023 202 DEDLKEKNILIIDIGGGTTDVAVFEGGKFDPDLSTGIdlGIGTALDEIIKELKK-EYGVEFDRRRLLFELIIKKKEYKDK 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 499411894 273 VNASYDNTVEISYNILNEIIsfrvEELLSLVKKKLVKNEQmtNISSIVIVGGGIALLK 330
Cdd:cd24023 281 NRGKKVDLTDIVEKALEELA----EEILDEIEKKWNKAGN--DIEVIYVYGGGSILLK 332
|
|
| |
