|
Name |
Accession |
Description |
Interval |
E-value |
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
1-418 |
0e+00 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 877.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 241 SDIAYAFGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKR 400
Cdd:PRK09472 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKR 400
|
410 420
....*....|....*....|
gi 490522983 401 T--SVGSWIKRINSWLRKEF 418
Cdd:PRK09472 401 VtaSVGSWIKRLNSWLRKEF 420
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
5-414 |
0e+00 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 573.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 5 TDRKLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS 84
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 85 GKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
Cdd:COG0849 81 GGHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 165 NDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 245 YAFGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGV 324
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKEL-------KRSGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 325 KHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKRTSvG 404
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKK-G 392
|
410
....*....|
gi 490522983 405 SWIKRINSWL 414
Cdd:COG0849 393 GLFGRIKRWF 402
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
9-385 |
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: 570.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 9 LVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 89 SCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMA 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 169 KNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 249 TPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqLRQQGVKHHL 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQKE------LRKSGFKEEL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522983 329 AAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:TIGR01174 315 NGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-385 |
0e+00 |
|
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: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 8 KLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 88 ISCQNEIGMVPISEE-EVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 167 MAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 247 FGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGVKH 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKEL-------KESGYED 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490522983 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:cd24048 314 LLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
10-196 |
2.82e-83 |
|
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: 252.78 E-value: 2.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 10 VVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 90 CQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAK 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 490522983 170 NIVKAVERCGLKVDQLIFAGLASSYSV 196
Cdd:smart00842 161 NLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-381 |
1.44e-54 |
|
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: 178.29 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 207 CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSLVGKDesvEVPSVGGRPPR 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 287 SLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITG 366
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
170
....*....|....*
gi 490522983 367 ltdyaQEPYYSTAVG 381
Cdd:pfam14450 158 -----RNPAYATALG 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
1-418 |
0e+00 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 877.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 241 SDIAYAFGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKR 400
Cdd:PRK09472 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKR 400
|
410 420
....*....|....*....|
gi 490522983 401 T--SVGSWIKRINSWLRKEF 418
Cdd:PRK09472 401 VtaSVGSWIKRLNSWLRKEF 420
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
5-414 |
0e+00 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 573.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 5 TDRKLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS 84
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 85 GKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
Cdd:COG0849 81 GGHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 165 NDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 245 YAFGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGV 324
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKEL-------KRSGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 325 KHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKRTSvG 404
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKK-G 392
|
410
....*....|
gi 490522983 405 SWIKRINSWL 414
Cdd:COG0849 393 GLFGRIKRWF 402
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
9-385 |
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: 570.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 9 LVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 89 SCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMA 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 169 KNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 249 TPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqLRQQGVKHHL 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQKE------LRKSGFKEEL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522983 329 AAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:TIGR01174 315 NGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-385 |
0e+00 |
|
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: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 8 KLVVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 88 ISCQNEIGMVPISEE-EVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 167 MAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 247 FGTPPSDAEAIKVRHGCALGSLVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGVKH 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKEL-------KESGYED 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490522983 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:cd24048 314 LLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
10-196 |
2.82e-83 |
|
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: 252.78 E-value: 2.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 10 VVGLEIGTAKVAALVGEVLPDGMINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 90 CQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAK 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 490522983 170 NIVKAVERCGLKVDQLIFAGLASSYSV 196
Cdd:smart00842 161 NLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-381 |
1.44e-54 |
|
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: 178.29 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 207 CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSLVGKDesvEVPSVGGRPPR 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 287 SLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITG 366
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
170
....*....|....*
gi 490522983 367 ltdyaQEPYYSTAVG 381
Cdd:pfam14450 158 -----RNPAYATALG 167
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
90-162 |
1.50e-29 |
|
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: 109.50 E-value: 1.50e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490522983 90 CQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLIT 162
Cdd:pfam02491 1 SQNSSGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVVT 73
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
11-383 |
6.74e-28 |
|
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: 111.62 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 11 VGLEIGTAKVAALVGEVLPDGmINIIGVGS--CPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSgKHI 88
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDEN-IEVLAFSSeeHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAIA-KVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 89 scqneigmvpiseeevtqEDVENVVhtaksvrvrdehrvlhvipqeyaidyqegiknpvglsgvrmqakvhlitchndma 168
Cdd:cd24004 79 ------------------ESLLNVL------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 169 knivkavERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:cd24004 86 -------EKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 249 TPPSDAEAIKVRHGCALGSLVGKDESVEVPSVggrpprslqrqTLAEVIEPRYTELLNLVNEEILQLQEqlrqqgvKHHL 328
Cdd:cd24004 159 ISFEEAEKIKRTYGIFLLIEAKDQLGFTINKK-----------EVYDIIKPVLEELASGIANAIEEYNG-------KFKL 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522983 329 AAGIVLTGGAAQIEGLAACAQRVFHTQV------RIGQPLNITGLTDYAQEPYYSTAVGLL 383
Cdd:cd24004 221 PDAVYLVGGGSKLPGLNEALAEKLGLPVeriaprNIGAISDITDETSKAKGPEFVTPLGIA 281
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
11-382 |
3.17e-25 |
|
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: 105.05 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 11 VGLEIGTAKVAALVGEVlPDGMINIIGVGS--CPSRGMDKGGVNDLESVVKCVQRAIDQAELMADcqisSVYLALSGKHI 88
Cdd:cd24049 1 LGIDIGSSSIKAVELKR-SGGGLVLVAFAIipLPEGAIVDGEIADPEALAEALKKLLKENKIKGK----KVVVALPGSDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 89 SCQnEIGMVPISEEEVTQEdvenvvhtaksvrVRDE-HRVLHVIPQEYAIDYQegIKNPVGLSGVRMqaKVHLITCHNDM 167
Cdd:cd24049 76 IVR-TIKLPKMPEKELEEA-------------IRFEaEQYLPFPLEEVVLDYQ--ILGEVEEGGEKL--EVLVVAAPKEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 168 AKNIVKAVERCGLK---VDQLIFAgLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:cd24049 138 VESYLELLKEAGLKpvaIDVESFA-LARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 245 YAFGTPPSDAEAIKVRHGCALGSLVGKDESVevpsvggrpprslqrqtlAEVIEPRYTELLNLVNEEILQLQEQLRQQGV 324
Cdd:cd24049 217 KALGLSFEEAEELKREYGLLLEGEEGELKKV------------------AEALRPVLERLVSEIRRSLDYYRSQNGGEPI 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522983 325 KHhlaagIVLTGGAAQIEGLAACAQRVFHTQVRIGQPLNITGLTDYAQE------PYYSTAVGL 382
Cdd:cd24049 279 DK-----IYLTGGGSLLPGLDEYLSERLGIPVEILNPFSNIESKKSDDEelkedaPLFAVAIGL 337
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
7-233 |
1.33e-11 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 64.88 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 7 RKLVVGLEIGTAKVAALVGEVLPDGM-INIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELmadcQISSVYLALSG 85
Cdd:COG4972 1 KKPLVGIDIGSSSIKLVELSKSGGGYrLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKI----KTKRVAIAVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 86 KHISCQNeIGMVPISEEEVtqedvENVVhtaksvrvrdEHRVLHVIP---QEYAIDYQegIKNPVGLSGVRMQakVHLIT 162
Cdd:COG4972 77 SSVITRK-ITLPALSEKEL-----EEAI----------EFEAEQYIPfplEEVVLDFQ--VLGPSEEGPEKVE--VLLVA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522983 163 CHNDMAKNIVKAVERCGLKVDQL---IFAgLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIP 233
Cdd:COG4972 137 ARKEVVEDYVELLEAAGLKPVVVdvePFA-LLRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIP 209
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
205-344 |
6.61e-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: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA------YAFGTPPSDAEAIKVRHGCALGSlvGKDESVEVp 278
Cdd:cd10225 144 GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrkYNLLIGERTAERIKIEIGSAYPL--DEELSMEV- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 279 sVG-----GRP-PRSLQRQTLAEVIEPRYTELLNLVNE-------EilqlqeqlrqqgvkhhLAA-----GIVLTGGAAQ 340
Cdd:cd10225 221 -RGrdlvtGLPrTIEITSEEVREALEEPVNAIVEAVRStlertppE----------------LAAdivdrGIVLTGGGAL 283
|
....
gi 490522983 341 IEGL 344
Cdd:cd10225 284 LRGL 287
|
|
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
7-265 |
9.24e-07 |
|
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: 50.55 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 7 RKLVVGLEIGTAKVAALvgEVLPDG---MINIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMAdcqiSSVYLAL 83
Cdd:TIGR01175 2 KSLLVGIDIGSTSVKVA--QLKRSGdryKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINT----KKAATAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 84 SGKHIScqneIGMVPIsEEEVTQEDVENVVhtaksvrvrdEHRVLHVIP---QEYAIDYQEgIKNPVGLSGVRMQakVHL 160
Cdd:TIGR01175 76 PGSAVI----TKVIPV-PAGLDERELEFAV----------YIEASHYIPypiEEVSLDFEK-LGLKANNPESTVQ--VLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 161 ITCHNDMAKNIVKAVERCGLKVDQL---IFAgLASSYSVLTED-----ERELGVCVVDIGGGTMDIAVYTGGALRHTKVI 232
Cdd:TIGR01175 138 AATRKEVVDSRLHALKLAGLEPKVVdveSFA-LLRAWRLLGEQlasrtYRLTDAALVDIGATSSTLNLLHPGRMLFTREV 216
|
250 260 270
....*....|....*....|....*....|...
gi 490522983 233 PYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCAL 265
Cdd:TIGR01175 217 PFGTRQLTSELSRAYGLNPEEAGEAKQQGGLPL 249
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
205-382 |
9.39e-07 |
|
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: 50.46 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA------YAFGTPPSDAEAIKVRhgcaLGSLVGKDESVEVp 278
Cdd:COG1077 152 GNMVVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIqyvrkkYNLLIGERTAEEIKIE----IGSAYPLEEELTM- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 279 SVGGRP-----PRSLQ--RQTLAEVIEPRYTELLNLVNE-------EilqlqeqlrqqgvkhhLAA-----GIVLTGGAA 339
Cdd:COG1077 227 EVRGRDlvtglPKTITitSEEIREALEEPLNAIVEAIKSvlektppE----------------LAAdivdrGIVLTGGGA 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490522983 340 QIEGLAACAQRVFHTQVRIgqplnitgltdyAQEPYYSTAVGL 382
Cdd:COG1077 291 LLRGLDKLLSEETGLPVHV------------AEDPLTCVARGT 321
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
208-358 |
5.35e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 48.21 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 208 VVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA------YAFGTPPSDAEAIKVRHGCALGSlvGKDESVEVP--- 278
Cdd:PRK13930 156 VVDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIVqyvrrkYNLLIGERTAEEIKIEIGSAYPL--DEEESMEVRgrd 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 279 SVGGRpPRSLQ--RQTLAEVIEPRYTELLNLVNEEILQlqeqlrqqgVKHHLAA-----GIVLTGGAAQIEGLAACAQRV 351
Cdd:PRK13930 234 LVTGL-PKTIEisSEEVREALAEPLQQIVEAVKSVLEK---------TPPELAAdiidrGIVLTGGGALLRGLDKLLSEE 303
|
....*..
gi 490522983 352 FHTQVRI 358
Cdd:PRK13930 304 TGLPVHI 310
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
172-382 |
6.26e-06 |
|
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: 47.67 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 172 VKAVERCGLK---VDQLIFAGLASS---YSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY 245
Cdd:pfam11104 142 VDLLEAAGLKpkvVDVESYALERAFeriVSQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 246 AFGTPPSDAEAIKvrhgcALGSLvgkdesvevpsvggrpPRSLQRqtlaEVIEPRYTELLNLVNEEILQLQEQLRQQGVK 325
Cdd:pfam11104 222 RYGMSYEEAEIAK-----RNGDL----------------PEDYES----EVLEPFVEALAQQISRALQFFFTSTPYNKVD 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490522983 326 HhlaagIVLTGGAAQIEGLA-ACAQRV-FHTQV-------RIGQPLNITGLTDYAqePYYSTAVGL 382
Cdd:pfam11104 277 Y-----IVLAGGCANIPGLAeLVTERLgFSTTVanpfrgmELSPRVRQKQLLRDA--PSYMVACGL 335
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
208-363 |
6.09e-05 |
|
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: 44.85 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 208 VVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDI------AYAFGTPPSDAEAIKVRHGCAlgslvGKDESVEVPSVG 281
Cdd:pfam06723 149 VVDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIikyirkKYNLLIGERTAERIKIEIGSA-----YPTEEEEKMEIR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 282 GRP-----PRSLQ--RQTLAEVIEPRYTELLNLVNEEILQlqeqlrqqgVKHHLAA-----GIVLTGGAAQIEGLAACAQ 349
Cdd:pfam06723 224 GRDlvtglPKTIEisSEEVREALKEPVSAIVEAVKEVLEK---------TPPELAAdivdrGIVLTGGGALLRGLDKLLS 294
|
170
....*....|....*
gi 490522983 350 RVFHTQVRIG-QPLN 363
Cdd:pfam06723 295 DETGLPVHIAeDPLT 309
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
205-344 |
3.61e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.38 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY----AFG------TppsdAEAIKVRHGCALgslvgKDES 274
Cdd:PRK13927 149 GSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIINyvrrNYNlligerT----AERIKIEIGSAY-----PGDE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 275 VEVPSVGGRP-----PRSLQ------RQTLAEVIeprytellnlvnEEIlqlqeqlrQQGVKH-------HLAA-----G 331
Cdd:PRK13927 220 VLEMEVRGRDlvtglPKTITissneiREALQEPL------------SAI--------VEAVKValeqtppELAAdivdrG 279
|
170
....*....|...
gi 490522983 332 IVLTGGAAQIEGL 344
Cdd:PRK13927 280 IVLTGGGALLRGL 292
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
187-358 |
3.88e-04 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 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: 466811 [Multi-domain] Cd Length: 329 Bit Score: 42.09 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 187 FAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYT---GGALRHTKVIPYAGNV-------------VTSDIAYAFGTP 250
Cdd:cd10170 119 ALYALEDKGDLLPLKPGDVVLVCDAGGGTVDLSLYEvtsGSPLLLEEVAPGGGALlggtdideafeklLREKLGDKGKDL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 251 PSDAEAI--KVRHGC--ALGSLVGKDE-SVEVPSVGGRPPRS---------LQRQTLAEVIEPRYTELLNLVNEEILQLQ 316
Cdd:cd10170 199 GRSDADAlaKLLREFeeAKKRFSGGEEdERLVPSLLGGGLPElglekgtllLTEEEIRDLFDPVIDKILELIEEQLEAKS 278
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490522983 317 EQLrqqgVKHhlaagIVLTGGAAQIEGLAACAQRVFHTQVRI 358
Cdd:cd10170 279 GTP----PDA-----VVLVGGFSRSPYLRERLRERFGSAGII 311
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
205-344 |
1.30e-03 |
|
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129982 [Multi-domain] Cd Length: 333 Bit Score: 40.47 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDI------AYAFGTPPSDAEAIKVRHGCAlgsLVGKDESVEVp 278
Cdd:TIGR00904 151 GSMVVDIGGGTTEVAVISLGGIVVSRSIRVGGDEFDEAIinyirrTYNLLIGEQTAERIKIEIGSA---YPLNDEPRKM- 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490522983 279 SVGGRP-----PRSLQ---RQTLAEVIEPrytelLNLVNEEILQLQEQlrqqgVKHHLAA-----GIVLTGGAAQIEGL 344
Cdd:TIGR00904 227 EVRGRDlvtglPRTIEitsVEVREALQEP-----VNQIVEAVKRTLEK-----TPPELAAdiverGIVLTGGGALLRNL 295
|
|
| EutJ |
COG4820 |
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
168-258 |
3.79e-03 |
|
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism];
Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 39.02 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522983 168 AKNIVKAVERCGLKVDQLIfaglassysvlteDE-----RELGV---CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVV 239
Cdd:COG4820 102 VRAIANVVEAAGFEVTNVV-------------DEptaaaAVLGIkdgAVVDIGGGTTGISILKDGEVVYTADEPTGGTHM 168
|
90
....*....|....*....
gi 490522983 240 TSDIAYAFGTPPSDAEAIK 258
Cdd:COG4820 169 SLVLAGAYGISFEEAEQLK 187
|
|
| |
