|
Name |
Accession |
Description |
Interval |
E-value |
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
9-386 |
0e+00 |
|
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: 548.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 9 TIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 89 QSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQDWQ 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 169 NNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHACT 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 249 ISRAEAERIKVNYASAFYPArLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDEldklkaELEAKHIKFE 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPL-EGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQK------ELRKSGFKEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357072146 329 LIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY 386
Cdd:TIGR01174 314 LNGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
1-425 |
0e+00 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 519.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 1 MVKGVETKTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVT 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 81 LAITGEHIQSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 161 IACHQDWQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 241 NDIAHACTISRAEAERIKVNYASAFyPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLKAEL 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCAL-GSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 321 EAKHIKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY---NHSNSDDDLIS 397
Cdd:PRK09472 320 RQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYgkeSHLNGEAEVEK 399
|
410 420
....*....|....*....|....*...
gi 1357072146 398 GSDDSEGTFFesiwqgvKKIVNKVRSEF 425
Cdd:PRK09472 400 RVTASVGSWI-------KRLNSWLRKEF 420
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
6-412 |
0e+00 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 511.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 6 ETKTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITG 85
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 86 EHIQSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQ 165
Cdd:COG0849 82 GHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 166 DWQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAH 245
Cdd:COG0849 162 TAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 246 ACTISRAEAERIKVNYASAFyPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLkaeleakHI 325
Cdd:COG0849 242 GLRTPLEEAERLKIKYGSAL-ASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRS-------GY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 326 KFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQYNHSNSDDDLISGSDDSEGT 405
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGG 393
|
....*..
gi 1357072146 406 FFESIWQ 412
Cdd:COG0849 394 LFGRIKR 400
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-386 |
1.40e-163 |
|
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: 464.70 E-value: 1.40e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 8 KTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 88 IQSLNESGFVPIAES-EVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQD 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 167 WQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 247 CTISRAEAERIKVNYASAfYPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLKAEleakhik 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSA-LSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYE------- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 327 FELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY 386
Cdd:cd24048 313 DLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
10-196 |
2.44e-78 |
|
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: 240.46 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 10 IVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEHIQ 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 90 SLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQDWQN 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 1357072146 170 NLKKAIERCGLQVDKVVFSGFAATHSV 196
Cdd:smart00842 161 NLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-382 |
1.20e-47 |
|
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: 160.57 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 207 CLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHACTISRAEAERIKVNYASAFYParlhGDKKIEVASIGGRAP 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALAS----LADEDEVPGVGGREP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 287 RSLTKSDLSLITSARYTELLGVVKDELDKLKAELEAKHIKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNIT 366
Cdd:pfam14450 77 REISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIG 156
|
170
....*....|....*.
gi 1357072146 367 GltdyvNRPQYSTVVG 382
Cdd:pfam14450 157 G-----RNPAYATALG 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
9-386 |
0e+00 |
|
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: 548.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 9 TIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 89 QSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQDWQ 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 169 NNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHACT 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 249 ISRAEAERIKVNYASAFYPArLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDEldklkaELEAKHIKFE 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPL-EGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQK------ELRKSGFKEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1357072146 329 LIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY 386
Cdd:TIGR01174 314 LNGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
1-425 |
0e+00 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 519.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 1 MVKGVETKTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVT 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 81 LAITGEHIQSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 161 IACHQDWQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 241 NDIAHACTISRAEAERIKVNYASAFyPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLKAEL 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCAL-GSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 321 EAKHIKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY---NHSNSDDDLIS 397
Cdd:PRK09472 320 RQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYgkeSHLNGEAEVEK 399
|
410 420
....*....|....*....|....*...
gi 1357072146 398 GSDDSEGTFFesiwqgvKKIVNKVRSEF 425
Cdd:PRK09472 400 RVTASVGSWI-------KRLNSWLRKEF 420
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
6-412 |
0e+00 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 511.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 6 ETKTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITG 85
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 86 EHIQSLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQ 165
Cdd:COG0849 82 GHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 166 DWQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAH 245
Cdd:COG0849 162 TAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 246 ACTISRAEAERIKVNYASAFyPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLkaeleakHI 325
Cdd:COG0849 242 GLRTPLEEAERLKIKYGSAL-ASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRS-------GY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 326 KFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQYNHSNSDDDLISGSDDSEGT 405
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGG 393
|
....*..
gi 1357072146 406 FFESIWQ 412
Cdd:COG0849 394 LFGRIKR 400
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-386 |
1.40e-163 |
|
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: 464.70 E-value: 1.40e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 8 KTIVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 88 IQSLNESGFVPIAES-EVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQD 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 167 WQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 247 CTISRAEAERIKVNYASAfYPARLHGDKKIEVASIGGRAPRSLTKSDLSLITSARYTELLGVVKDELDKLKAEleakhik 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSA-LSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYE------- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 327 FELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYVNRPQYSTVVGLLQY 386
Cdd:cd24048 313 DLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
10-196 |
2.44e-78 |
|
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: 240.46 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 10 IVGLEVGTSKVVAVVGEVFPDGVVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAITGEHIQ 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 90 SLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLIACHQDWQN 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 1357072146 170 NLKKAIERCGLQVDKVVFSGFAATHSV 196
Cdd:smart00842 161 NLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-382 |
1.20e-47 |
|
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: 160.57 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 207 CLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHACTISRAEAERIKVNYASAFYParlhGDKKIEVASIGGRAP 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALAS----LADEDEVPGVGGREP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 287 RSLTKSDLSLITSARYTELLGVVKDELDKLKAELEAKHIKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNIT 366
Cdd:pfam14450 77 REISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIG 156
|
170
....*....|....*.
gi 1357072146 367 GltdyvNRPQYSTVVG 382
Cdd:pfam14450 157 G-----RNPAYATALG 167
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
11-384 |
1.59e-29 |
|
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: 115.85 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 11 VGLEVGTSKVVAVVGEVFPDGVvNVLGVGS--CPSKGIDRGSITDLDAVVGSIQRAIEAAESMADCQIMSVTLAItGEHI 88
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDENI-EVLAFSSeeHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAI-AKVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 89 QSLnesgfvpiaesevtqeeidsalhtassiklpeglsllhvipqeyavdrqmniknplglqgvrlkaqvhliachqdwq 168
Cdd:cd24004 79 ESL----------------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 169 nnlKKAIERCGLQVDKVVFSGFAATHSVLTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHACT 248
Cdd:cd24004 82 ---LNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 249 ISRAEAERIKVNYAsafyparlHGDKKIEVASIGGRaprsLTKSDLSLITSARYTELLGVVKDELDKLKAeleakhiKFE 328
Cdd:cd24004 159 ISFEEAEKIKRTYG--------IFLLIEAKDQLGFT----INKKEVYDIIKPVLEELASGIANAIEEYNG-------KFK 219
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357072146 329 LIAGVVITGGGAQIEDLKECASNVFH------CQVRIASPLNITGLTDYVNRPQYSTVVGLL 384
Cdd:cd24004 220 LPDAVYLVGGGSKLPGLNEALAEKLGlpveriAPRNIGAISDITDETSKAKGPEFVTPLGIA 281
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
90-161 |
5.02e-24 |
|
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: 94.48 E-value: 5.02e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1357072146 90 SLNESGFVPIAESEVTQEEIDSALHTASSIKLPEGLSLLHVIPQEYAVDRQMNIKNPLGLQGVRLKAQVHLI 161
Cdd:pfam02491 1 SQNSSGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVV 72
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
11-383 |
5.94e-23 |
|
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: 98.89 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 11 VGLEVGTSKVVAVVGEVFPDG-VVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAesmaDCQIMSVTLAITGEHIQ 89
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGlVLVAFAIIPLPEGAIVDGEIADPEALAEALKKLLKEN----KIKGKKVVVALPGSDVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 90 SLNESgfVPiaesEVTQEEIDSALHTASSIKLPEGLSllhvipqEYAVDRQmniknPLG-LQGVRLKAQVHLIACHQDWQ 168
Cdd:cd24049 77 VRTIK--LP----KMPEKELEEAIRFEAEQYLPFPLE-------EVVLDYQ-----ILGeVEEGGEKLEVLVVAAPKEIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 169 NNLKKAIERCGLQVDKVVFSGFAATHSV--LTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIAHA 246
Cdd:cd24049 139 ESYLELLKEAGLKPVAIDVESFALARALeyLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAKA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 247 CTISRAEAERIKVNYASAFYPArlhgdkkievasiggraprsltksdlslitSARYTELLGVVKDELDKLKAELE----- 321
Cdd:cd24049 219 LGLSFEEAEELKREYGLLLEGE------------------------------EGELKKVAEALRPVLERLVSEIRrsldy 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357072146 322 -AKHIKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASPLNITGLTDYV------NRPQYSTVVGL 383
Cdd:cd24049 269 yRSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPVEILNPFSNIESKKSDdeelkeDAPLFAVAIGL 337
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
8-233 |
4.89e-12 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 66.03 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 8 KTIVGLEVGTSKVVAVVGEVFPDG-VVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESmadcQIMSVTLAITGE 86
Cdd:COG4972 2 KPLVGIDIGSSSIKLVELSKSGGGyRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKI----KTKRVAIAVPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 87 H--IQSLNesgfVPiaesEVTQEEIDSAL--HTASSIKLPeglsllhviPQEYAVDRQmniknPLGL-QGVRLKAQVHLI 161
Cdd:COG4972 78 SviTRKIT----LP----ALSEKELEEAIefEAEQYIPFP---------LEEVVLDFQ-----VLGPsEEGPEKVEVLLV 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1357072146 162 ACHQDWQNNLKKAIERCGLQVDKVVFSGFAATHSV--LTEDEKDLGVCLIDFGAGTMNVMVYTNGALRFSKVIP 233
Cdd:COG4972 136 AARKEVVEDYVELLEAAGLKPVVVDVEPFALLRALelLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIP 209
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
209-363 |
3.20e-09 |
|
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: 58.17 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 209 IDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIA------HACTISRAEAERIKVNYASAFypaRLHGDKKIEVAsig 282
Cdd:COG1077 156 VDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIqyvrkkYNLLIGERTAEEIKIEIGSAY---PLEEELTMEVR--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 283 GR-----APRSLTksdlslITSArytELLGVVKDELDK----LKAELEakHIKFELIA-----GVVITGGGAQIEDLKEC 348
Cdd:COG1077 230 GRdlvtgLPKTIT------ITSE---EIREALEEPLNAiveaIKSVLE--KTPPELAAdivdrGIVLTGGGALLRGLDKL 298
|
170
....*....|....*.
gi 1357072146 349 ASNVFHCQVRIA-SPL 363
Cdd:COG1077 299 LSEETGLPVHVAeDPL 314
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
205-363 |
7.59e-09 |
|
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: 56.71 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 205 GVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIA------HACTISRAEAERIKVNYASAFYparLHGDKKIEV 278
Cdd:cd10225 144 GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrkYNLLIGERTAERIKIEIGSAYP---LDEELSMEV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 279 AsigGR-----APRS--LTKSDLSLITSARYTELLGVVKDELDKLKAELEAKHIKfeliAGVVITGGGAQIEDLKECASN 351
Cdd:cd10225 221 R---GRdlvtgLPRTieITSEEVREALEEPVNAIVEAVRSTLERTPPELAADIVD----RGIVLTGGGALLRGLDELLRE 293
|
170
....*....|...
gi 1357072146 352 VFHCQVRIA-SPL 363
Cdd:cd10225 294 ETGLPVHVAdDPL 306
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
209-364 |
2.53e-08 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 55.14 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 209 IDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIA------HACTISRAEAERIKVNYASAFypaRLHGDKKIEVAsig 282
Cdd:PRK13930 157 VDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIVqyvrrkYNLLIGERTAEEIKIEIGSAY---PLDEEESMEVR--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 283 GR-----APRSLTKSDLSLITSARYT--ELLGVVKDELDKLKAELEAKhikfelIA--GVVITGGGAQIEDLKECASNVF 353
Cdd:PRK13930 231 GRdlvtgLPKTIEISSEEVREALAEPlqQIVEAVKSVLEKTPPELAAD------IIdrGIVLTGGGALLRGLDKLLSEET 304
|
170
....*....|..
gi 1357072146 354 HCQVRIA-SPLN 364
Cdd:PRK13930 305 GLPVHIAeDPLT 316
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
209-364 |
6.62e-07 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 51.02 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 209 IDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDI------AHACTISRAEAERIKVNYASAFypaRLHGDKKIEvasIG 282
Cdd:pfam06723 150 VDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIikyirkKYNLLIGERTAERIKIEIGSAY---PTEEEEKME---IR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 283 GR-----APRSLT----------KSDLSLITSArytellgvVKDELDKLKAELEAKHIKfeliAGVVITGGGAQIEDLKE 347
Cdd:pfam06723 224 GRdlvtgLPKTIEisseevrealKEPVSAIVEA--------VKEVLEKTPPELAADIVD----RGIVLTGGGALLRGLDK 291
|
170
....*....|....*...
gi 1357072146 348 CASNVFHCQVRIA-SPLN 364
Cdd:pfam06723 292 LLSDETGLPVHIAeDPLT 309
|
|
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
9-383 |
3.51e-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: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 9 TIVGLEVGTSKVVAVV----GEVFPdgvVNVLGVGSCPSKGIDRGSITDLDAVVGSIQRAIEAAESMADcqimSVTLAIT 84
Cdd:TIGR01175 4 LLVGIDIGSTSVKVAQlkrsGDRYK---LEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINTK----KAATAVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 85 GEHIQSLNesgfVPIaESEVTQEEIDSALHTASSIKLP---EGLSLLHVIPQEYAVDRQMniknplglqgvrlKAQVHLI 161
Cdd:TIGR01175 77 GSAVITKV----IPV-PAGLDERELEFAVYIEASHYIPypiEEVSLDFEKLGLKANNPES-------------TVQVLLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 162 ACHQDWQNNLKKAIERCGLQVDKVVFSGFAATHSVLTEDE-------KDLGVCLIDFGAGTMNVMVYTNGALRFSKVIPY 234
Cdd:TIGR01175 139 ATRKEVVDSRLHALKLAGLEPKVVDVESFALLRAWRLLGEqlasrtyRLTDAALVDIGATSSTLNLLHPGRMLFTREVPF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 235 AGNIVTNDIAHACTISRAEAERIKVNyasafyparlhgdkkievasiGGRAPrsltksdlslitsARYTELLGVVKDEL- 313
Cdd:TIGR01175 219 GTRQLTSELSRAYGLNPEEAGEAKQQ---------------------GGLPL-------------LYDPEVLRRFKGELv 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 314 DKLKAELE---AKHiKFELIAGVVITGGGAQIEDLKECASNVFHCQVRIASP---LNITGLTDY----VNRPQYSTVVGL 383
Cdd:TIGR01175 265 DEIRRSLQfftAQS-GTNSLDGLVLAGGGATLSGLDAAIYQRLGLPTEVANPfalMALDAKVDAgrlaVDAPALMTALGL 343
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
205-364 |
8.89e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 44.31 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 205 GVCLIDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIA------HACTISRAEAERIKVNYASAfYParlhgDKKIEV 278
Cdd:PRK13927 149 GSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIInyvrrnYNLLIGERTAERIKIEIGSA-YP-----GDEVLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 279 ASIGGR-----APRSLTksdlslITSARYTE-LLGVVKDELDKLKAELEAkhIKFELIA-----GVVITGGGAQIEDLKE 347
Cdd:PRK13927 223 MEVRGRdlvtgLPKTIT------ISSNEIREaLQEPLSAIVEAVKVALEQ--TPPELAAdivdrGIVLTGGGALLRGLDK 294
|
170
....*....|....*...
gi 1357072146 348 CASNVFHCQVRIA-SPLN 364
Cdd:PRK13927 295 LLSEETGLPVHVAeDPLT 312
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
209-340 |
1.52e-03 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 40.27 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357072146 209 IDFGAGTMNVMVYTNGALRFSKVIPYAGNIVTNDIA------HACTISRAEAERIKVNYASAFYPARlhgDKKIEvasIG 282
Cdd:PRK13928 152 VDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIryirkkYKLLIGERTAEEIKIKIGTAFPGAR---EEEME---IR 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357072146 283 GRA-----PRSLTksdlslITSARYTELL--------GVVKDELDKLKAELEAKHIKfeliAGVVITGGGA 340
Cdd:PRK13928 226 GRDlvtglPKTIT------VTSEEIREALkepvsaivQAVKSVLERTPPELSADIID----RGIIMTGGGA 286
|
|
| |
