|
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: 876.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKR 400
Cdd:PRK09472 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKR 400
|
410 420
....*....|....*....|
gi 556486775 401 V--SVGSWVKRLNNWLRKEF 418
Cdd:PRK09472 401 VtaSVGSWIKRLNSWLRKEF 420
|
|
| 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: 569.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 9 LVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 89 SCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMA 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 169 KNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 249 TPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqLRQQGVKHHL 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQKE------LRKSGFKEEL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 556486775 329 AAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:TIGR01174 315 NGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| 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: 569.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 5 TDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS 84
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 85 GKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
Cdd:COG0849 81 GGHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 165 NDMAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 245 YAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGV 324
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKEL-------KRSGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 325 KHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKRVSvG 404
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKK-G 392
|
410
....*....|
gi 556486775 405 SWVKRLNNWL 414
Cdd:COG0849 393 GLFGRIKRWF 402
|
|
| 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: 543.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 8 KLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 88 ISCQNEIGMVPISEE-EVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 167 MAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGVKH 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKEL-------KESGYED 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 556486775 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHY 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 |
4.38e-82 |
|
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: 250.09 E-value: 4.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 10 VVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 90 CQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAK 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 556486775 170 NIVKAVERCGLKVDQLIFAGLAASYSV 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 |
4.38e-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: 177.14 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 207 CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDesvEVPSVGGRPPR 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 287 SLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITG 366
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
170
....*....|....*
gi 556486775 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: 876.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
Cdd:PRK09472 1 MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
Cdd:PRK09472 81 LALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
Cdd:PRK09472 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
Cdd:PRK09472 241 SDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKR 400
Cdd:PRK09472 321 QQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLNGEAEVEKR 400
|
410 420
....*....|....*....|
gi 556486775 401 V--SVGSWVKRLNNWLRKEF 418
Cdd:PRK09472 401 VtaSVGSWIKRLNSWLRKEF 420
|
|
| 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: 569.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 9 LVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 89 SCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMA 168
Cdd:TIGR01174 81 KSQNSIGVVAIKDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSSTIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 169 KNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:TIGR01174 161 RNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKALR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 249 TPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqLRQQGVKHHL 328
Cdd:TIGR01174 241 TPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQKE------LRKSGFKEEL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 556486775 329 AAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHY 385
Cdd:TIGR01174 315 NGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLLLY 371
|
|
| 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: 569.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 5 TDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS 84
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 85 GKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCH 164
Cdd:COG0849 81 GGHIKSQNSRGVVAISGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 165 NDMAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:COG0849 161 KTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 245 YAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGV 324
Cdd:COG0849 241 IGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKEL-------KRSGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 325 KHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKESHLSGEAEVEKRVSvG 404
Cdd:COG0849 314 EEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEKKK-G 392
|
410
....*....|
gi 556486775 405 SWVKRLNNWL 414
Cdd:COG0849 393 GLFGRIKRWF 402
|
|
| 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: 543.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 8 KLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKH 87
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 88 ISCQNEIGMVPISEE-EVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166
Cdd:cd24048 81 IRSVNSRGVIAISDKdEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 167 MAKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEIlqlqeqlRQQGVKH 326
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKEL-------KESGYED 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 556486775 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHY 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 |
4.38e-82 |
|
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: 250.09 E-value: 4.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 10 VVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 90 CQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAK 169
Cdd:smart00842 81 SVNVSGVVAIPDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSAIQ 160
|
170 180
....*....|....*....|....*..
gi 556486775 170 NIVKAVERCGLKVDQLIFAGLAASYSV 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 |
4.38e-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: 177.14 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 207 CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDesvEVPSVGGRPPR 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 287 SLQRQTLAEVIEPRYTELLNLVNEEILQLQEQLRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITG 366
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREVLPGEYVRLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
170
....*....|....*
gi 556486775 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 |
1.77e-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: 109.12 E-value: 1.77e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556486775 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 |
2.78e-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: 112.39 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 11 VGLEIGTAKVAALVGEVLPDGmVNIIGVGS--CPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSgKHI 88
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDEN-IEVLAFSSeeHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAIA-KVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 89 scqneigmvpiseeevtqEDVENVVhtaksvrvrdehrvlhvipqeyaidyqegiknpvglsgvrmqakvhlitchndma 168
Cdd:cd24004 79 ------------------ESLLNVL------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 169 knivkavERCGLKVDQLIFAGLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFG 248
Cdd:cd24004 86 -------EKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 249 TPPSDAEAIKVRHGCALGSIVGKDESVEVPSVggrpprslqrqTLAEVIEPRYTELLNLVNEEILQLQEqlrqqgvKHHL 328
Cdd:cd24004 159 ISFEEAEKIKRTYGIFLLIEAKDQLGFTINKK-----------EVYDIIKPVLEELASGIANAIEEYNG-------KFKL 220
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556486775 329 AAGIVLTGGAAQIEGLAACAQRVFHTQV------RIGAPLNITGLTDYAQEPYYSTAVGLL 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 |
2.62e-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: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 11 VGLEIGTAKVAALVGEVlPDGMVNIIGVGS--CPSRGMDKGGVNDLESVVKCVQRAIDQAELMADcqisSVYLALSGKHI 88
Cdd:cd24049 1 LGIDIGSSSIKAVELKR-SGGGLVLVAFAIipLPEGAIVDGEIADPEALAEALKKLLKENKIKGK----KVVVALPGSDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 89 SCQnEIGMVPISEEEVTQEdvenvvhtaksvrVRDE-HRVLHVIPQEYAIDYQegIKNPVGLSGVRMqaKVHLITCHNDM 167
Cdd:cd24049 76 IVR-TIKLPKMPEKELEEA-------------IRFEaEQYLPFPLEEVVLDYQ--ILGEVEEGGEKL--EVLVVAAPKEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 168 AKNIVKAVERCGLKVDQLIFAGLAAS--YSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY 245
Cdd:cd24049 138 VESYLELLKEAGLKPVAIDVESFALAraLEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 246 AFGTPPSDAEAIKVRHGCALGSIVGKDESVevpsvggrpprslqrqtlAEVIEPRYTELLNLVNEEILQLQEQLRQQGVK 325
Cdd:cd24049 218 ALGLSFEEAEELKREYGLLLEGEEGELKKV------------------AEALRPVLERLVSEIRRSLDYYRSQNGGEPID 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556486775 326 HhlaagIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQE------PYYSTAVGL 382
Cdd:cd24049 280 K-----IYLTGGGSLLPGLDEYLSERLGIPVEILNPFSNIESKKSDDEelkedaPLFAVAIGL 337
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
7-233 |
1.38e-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: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 7 RKLVVGLEIGTAKVAALVGEVLPDGM-VNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELmadcQISSVYLALSG 85
Cdd:COG4972 1 KKPLVGIDIGSSSIKLVELSKSGGGYrLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKI----KTKRVAIAVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 86 KHISCQNeIGMVPISEEEVtqedvENVVhtaksvrvrdEHRVLHVIP---QEYAIDYQegIKNPVGLSGVRMQakVHLIT 162
Cdd:COG4972 77 SSVITRK-ITLPALSEKEL-----EEAI----------EFEAEQYIPfplEEVVLDFQ--VLGPSEEGPEKVE--VLLVA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556486775 163 CHNDMAKNIVKAVERCGLKVDQL---IFAgLAASYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIP 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 ... |
171-344 |
4.69e-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: 57.48 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 171 IVKAVERCGLKVDQLIFAGLAASYSV---LTEDErelGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA--- 244
Cdd:cd10225 110 VKEAAEHAGAREVYLIEEPMAAAIGAglpIEEPR---GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyv 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 245 ---YAFGTPPSDAEAIKVRHGCALGSivGKDESVEVpsVG-----GRP-PRSLQRQTLAEVIEPRYTELLNLVNE----- 310
Cdd:cd10225 187 rrkYNLLIGERTAERIKIEIGSAYPL--DEELSMEV--RGrdlvtGLPrTIEITSEEVREALEEPVNAIVEAVRStlert 262
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556486775 311 --EilqlqeqlrqqgvkhhLAA-----GIVLTGGAAQIEGL 344
Cdd:cd10225 263 ppE----------------LAAdivdrGIVLTGGGALLRGL 287
|
|
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
7-265 |
3.50e-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: 51.71 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 7 RKLVVGLEIGTAKVAALvgEVLPDG---MVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMAdcqiSSVYLAL 83
Cdd:TIGR01175 2 KSLLVGIDIGSTSVKVA--QLKRSGdryKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINT----KKAATAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 84 SGKHIScqneIGMVPIsEEEVTQEDVENVVhtaksvrvrdEHRVLHVIP---QEYAIDYQEgIKNPVGLSGVRMQakVHL 160
Cdd:TIGR01175 76 PGSAVI----TKVIPV-PAGLDERELEFAV----------YIEASHYIPypiEEVSLDFEK-LGLKANNPESTVQ--VLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 161 ITCHNDMAKNIVKAVERCGLKVDQLIFAGLAA--SYSVLTED-----ERELGVCVVDIGGGTMDIAVYTGGALRHTKVIP 233
Cdd:TIGR01175 138 AATRKEVVDSRLHALKLAGLEPKVVDVESFALlrAWRLLGEQlasrtYRLTDAALVDIGATSSTLNLLHPGRMLFTREVP 217
|
250 260 270
....*....|....*....|....*....|..
gi 556486775 234 YAGNVVTSDIAYAFGTPPSDAEAIKVRHGCAL 265
Cdd:TIGR01175 218 FGTRQLTSELSRAYGLNPEEAGEAKQQGGLPL 249
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
205-382 |
5.60e-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: 51.23 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA------YAFGTPPSDAEAIKVRHGCALGS-------IVGK 271
Cdd:COG1077 152 GNMVVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIqyvrkkYNLLIGERTAEEIKIEIGSAYPLeeeltmeVRGR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 272 D------ESVEVPSvggrpprslqrQTLAEVIEPRYTELLNLVNE-------EilqlqeqlrqqgvkhhLAA-----GIV 333
Cdd:COG1077 232 DlvtglpKTITITS-----------EEIREALEEPLNAIVEAIKSvlektppE----------------LAAdivdrGIV 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556486775 334 LTGGAAQIEGLAACAQRVFHTQVRIgaplnitgltdyAQEPYYSTAVGL 382
Cdd:COG1077 285 LTGGGALLRGLDKLLSEETGLPVHV------------AEDPLTCVARGT 321
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
208-358 |
6.40e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 47.82 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 208 VVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA------YAFGTPPSDAEAIKVRHGCALGSivGKDESVEV---P 278
Cdd:PRK13930 156 VVDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIVqyvrrkYNLLIGERTAEEIKIEIGSAYPL--DEEESMEVrgrD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 279 SVGGRpPRSLQ--RQTLAEVIEPRYTELLNLVNEEILQlqeqlrqqgVKHHLAA-----GIVLTGGAAQIEGLAACAQRV 351
Cdd:PRK13930 234 LVTGL-PKTIEisSEEVREALAEPLQQIVEAVKSVLEK---------TPPELAAdiidrGIVLTGGGALLRGLDKLLSEE 303
|
....*..
gi 556486775 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 |
7.03e-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: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 172 VKAVERCGLK---VDQLIFAGLAAS---YSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY 245
Cdd:pfam11104 142 VDLLEAAGLKpkvVDVESYALERAFeriVSQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 246 AFGTPPSDAEAIKVrhgcalgsivgkdesvevpsvGGRPPRSLQRqtlaEVIEPRYTELLNLVNEEILQLQEQLRQQGVK 325
Cdd:pfam11104 222 RYGMSYEEAEIAKR---------------------NGDLPEDYES----EVLEPFVEALAQQISRALQFFFTSTPYNKVD 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556486775 326 HhlaagIVLTGGAAQIEGLA-ACAQRV-FHTQV-------RIGAPLNITGLTDYAqePYYSTAVGL 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 ... |
208-344 |
9.42e-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: 44.08 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 208 VVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDI------AYAFGTPPSDAEAIKVRHGCAlgsivGKDESVEVPSVG 281
Cdd:pfam06723 149 VVDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIikyirkKYNLLIGERTAERIKIEIGSA-----YPTEEEEKMEIR 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556486775 282 GRP-----PRSLQ--RQTLAEVIEPRYTELLNLVNEEILQlqeqlrqqgVKHHLAA-----GIVLTGGAAQIEGL 344
Cdd:pfam06723 224 GRDlvtglPKTIEisSEEVREALKEPVSAIVEAVKEVLEK---------TPPELAAdivdrGIVLTGGGALLRGL 289
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
191-358 |
9.82e-05 |
|
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: 44.02 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 191 AASYSVLTEDERELG------VCVVDIGGGTMDIAVYT---GGALRHTKVIPYAGNV-------------VTSDIAYAFG 248
Cdd:cd10170 117 AAALYALEDKGDLLPlkpgdvVLVCDAGGGTVDLSLYEvtsGSPLLLEEVAPGGGALlggtdideafeklLREKLGDKGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 249 TPPSDAEAI--KVRHGC-----ALGSIVGKDESVEVPSVGGRPP-------RSLQRQTLAEVIEPRYTELLNLVNEEILQ 314
Cdd:cd10170 197 DLGRSDADAlaKLLREFeeakkRFSGGEEDERLVPSLLGGGLPElglekgtLLLTEEEIRDLFDPVIDKILELIEEQLEA 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556486775 315 LQEQLrqqgVKHhlaagIVLTGGAAQIEGLAACAQRVFHTQVRI 358
Cdd:cd10170 277 KSGTP----PDA-----VVLVGGFSRSPYLRERLRERFGSAGII 311
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
205-344 |
3.77e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 42.38 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY----AFG------TppsdAEAIKVRHGCALgsivgKDES 274
Cdd:PRK13927 149 GSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIINyvrrNYNlligerT----AERIKIEIGSAY-----PGDE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 275 VEVPSVGGRP-----PRSLQ------RQTLAEVIeprytellnlvnEEIlqlqeqlrQQGVKH-------HLAA-----G 331
Cdd:PRK13927 220 VLEMEVRGRDlvtglPKTITissneiREALQEPL------------SAI--------VEAVKValeqtppELAAdivdrG 279
|
170
....*....|...
gi 556486775 332 IVLTGGAAQIEGL 344
Cdd:PRK13927 280 IVLTGGGALLRGL 292
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
205-344 |
4.49e-04 |
|
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: 42.01 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 205 GVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDI------AYAFGTPPSDAEAIKVRHGCAlgsIVGKDESVEVp 278
Cdd:TIGR00904 151 GSMVVDIGGGTTEVAVISLGGIVVSRSIRVGGDEFDEAIinyirrTYNLLIGEQTAERIKIEIGSA---YPLNDEPRKM- 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556486775 279 SVGGRP-----PRSLQ---RQTLAEVIEPrytelLNLVNEEILQLQEQlrqqgVKHHLAA-----GIVLTGGAAQIEGL 344
Cdd:TIGR00904 227 EVRGRDlvtglPRTIEitsVEVREALQEP-----VNQIVEAVKRTLEK-----TPPELAAdiverGIVLTGGGALLRNL 295
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
189-224 |
3.13e-03 |
|
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: 39.18 E-value: 3.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 556486775 189 GLAASYSVLTEDEREL--------GVCVVDIGGGTMDIAVYTGG 224
Cdd:cd24022 151 GVAAYFDYLLDEDGNGtdeeeeegPVAVIDIGGTTTDIAVVSGG 194
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
168-258 |
3.63e-03 |
|
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: 38.79 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 168 AKNIVKAVERCGLKVDQLIFAGLAASYSVLTEDerelGVcVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAF 247
Cdd:cd24047 80 ARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRD----GA-VVDIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLAGNY 154
|
90
....*....|.
gi 556486775 248 GTPPSDAEAIK 258
Cdd:cd24047 155 GISFEEAEIIK 165
|
|
| EutJ |
COG4820 |
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
168-258 |
3.93e-03 |
|
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism];
Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 38.63 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 168 AKNIVKAVERCGLKVDQLIFAGLAASysvltedeRELGV---CVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
Cdd:COG4820 102 VRAIANVVEAAGFEVTNVVDEPTAAA--------AVLGIkdgAVVDIGGGTTGISILKDGEVVYTADEPTGGTHMSLVLA 173
|
90
....*....|....
gi 556486775 245 YAFGTPPSDAEAIK 258
Cdd:COG4820 174 GAYGISFEEAEQLK 187
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
168-233 |
4.30e-03 |
|
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs 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: 466856 [Multi-domain] Cd Length: 294 Bit Score: 38.67 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556486775 168 AKN---IVKAV-ERCGLKVD--------QLIFagLAASYSVLTEDERelgVCVVDIGGGTMDIAVYTGGALRHTKVIP 233
Cdd:cd24006 83 ASNgdeFLERIkRETGIDVEiisgeeeaRLIY--LAVRSGLPLGDGN---ALIVDIGGGSTELTLGDNGEILFSESLP 155
|
|
| ASKHA_NBD_Arp3-like |
cd10221 |
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ... |
184-262 |
6.73e-03 |
|
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.
Pssm-ID: 466822 Cd Length: 404 Bit Score: 38.32 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486775 184 QLIFAgLAASYSVLTEDERELGVCVVDIGGG-TMDIAV---YT-GGALRHtkvIPYAGNVVTSDIAY-----AFGTPPSD 253
Cdd:cd10221 138 QAVLA-LAASWTSRKVGERTLTGTVIDSGDGvTHVIPVaegYViGSCIKH---IPIAGRDITYFIQQllrerEEGIPPED 213
|
90
....*....|...
gi 556486775 254 ----AEAIKVRHG 262
Cdd:cd10221 214 slevAKRIKERYC 226
|
|
| |
