|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-416 |
9.62e-163 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 463.84 E-value: 9.62e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 2 TRNKVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSV 81
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGK-LEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 82 GGAHISSQNSHGVVAVANpeGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHII 161
Cdd:COG0849 80 SGGHIKSQNSRGVVAISG--REITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 162 TGSTTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTN 241
Cdd:COG0849 158 TGPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 242 DLAIGLRLSLDGAEKLKIalseKHEEILAERggNEKGDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQ 321
Cdd:COG0849 238 DIAIGLRTPLEEAERLKI----KYGSALASL--ADEDETIEVPGIGG-RPPREISRKELAE-IIEARVEEIFELVRKELK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 322 KSGFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFHGFKSGGEKSAGVFLP 401
Cdd:COG0849 310 RSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEK 389
|
410
....*....|....*
gi 1278643644 402 RFGGISHKIplKGLF 416
Cdd:COG0849 390 KKGGLFGRI--KRWF 402
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
5-386 |
1.10e-143 |
|
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: 414.24 E-value: 1.10e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 5 KVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGA 84
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGE-LEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 85 HISSQNSHGVVAVANpEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGS 164
Cdd:cd24048 80 HIRSVNSRGVIAISD-KDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 165 TTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLA 244
Cdd:cd24048 159 SSAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 245 IGLRLSLDGAEKLKIALSEKHEEILAERggnekgDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKSG 324
Cdd:cd24048 239 IGLNTPFEEAERLKIKYGSALSEEADED------EIIEIPGVGG-REPREVSRRELAE-IIEARVEEILELVKKELKESG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278643644 325 FAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFH 386
Cdd:cd24048 311 YEDLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
6-384 |
3.34e-129 |
|
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: 377.36 E-value: 3.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 6 VLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGAH 85
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGE-LNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 86 ISSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGST 165
Cdd:TIGR01174 80 IKSQNSIGVVAI--KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 166 TAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAI 245
Cdd:TIGR01174 158 TILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 246 GLRLSLDGAEKLKIALSEKHEEILaerggnEKGDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAV-EIQKSG 324
Cdd:TIGR01174 238 ALRTPLEEAERIKIKYGCASIPLE------GPDENIEIPSVGE-RPPRSLSRKELAE-IIEARAEEILEIVKQkELRKSG 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 325 FAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLL 384
Cdd:TIGR01174 310 FKEELNGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLL 369
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
2-390 |
1.98e-77 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 246.62 E-value: 1.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 2 TRNKVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSV 81
Cdd:PRK09472 5 TDRKLVVGLEIGTAKVAALVGEVLPDGM-VNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 82 GGAHISSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHII 161
Cdd:PRK09472 84 SGKHISCQNEIGMVPI--SEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 162 TGSTTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTN 241
Cdd:PRK09472 162 TCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 242 DLAIGLRLSLDGAEKLKIALSEKHEEILAerggneKGDEIDLAKLGvFEETKTVSQKTLVEgIIRPRLNEIFNMVAVEI- 320
Cdd:PRK09472 242 DIAYAFGTPPSDAEAIKVRHGCALGSIVG------KDESVEVPSVG-GRPPRSLQRQTLAE-VIEPRYTELLNLVNEEIl 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278643644 321 ------QKSGFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFHGFKS 390
Cdd:PRK09472 314 qlqeqlRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKES 389
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
7-196 |
1.93e-69 |
|
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: 217.73 E-value: 1.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 7 LAAIDVGSSKIAVLIGQQNENNeRINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGAHI 86
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDG-EINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 87 SSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGSTT 166
Cdd:smart00842 80 KSVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKS 157
|
170 180 190
....*....|....*....|....*....|
gi 1278643644 167 AVKNLSKCIAEVGADIGDLVFSGIASAGAV 196
Cdd:smart00842 158 AIQNLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-382 |
1.53e-34 |
|
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: 126.29 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 207 ILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIGLRLSLDGAEKLKIalseKHEEILAERGGNEKGDEIDLakl 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKI----KYGSALASLADEDEVPGVGG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 287 gvfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKSGFA-------GLTPSGVVLTGGGALTVGASESCRRNLSLPVRV 359
Cdd:pfam14450 74 ---REPREISRKELAE-IIEARVEEILELVRAELEDREVLpgeyvrlEVDVHGIVLTGGGSALPGLVELAERALGLPVRI 149
|
170 180
....*....|....*....|...
gi 1278643644 360 GIPGEISGlvddiLNPAFSVAIG 382
Cdd:pfam14450 150 GSPDGIGG-----RNPAYATALG 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-416 |
9.62e-163 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 463.84 E-value: 9.62e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 2 TRNKVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSV 81
Cdd:COG0849 1 AKSNIIVGLDIGTSKVVALVGEVDPDGK-LEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 82 GGAHISSQNSHGVVAVANpeGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHII 161
Cdd:COG0849 80 SGGHIKSQNSRGVVAISG--REITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 162 TGSTTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTN 241
Cdd:COG0849 158 TGPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 242 DLAIGLRLSLDGAEKLKIalseKHEEILAERggNEKGDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQ 321
Cdd:COG0849 238 DIAIGLRTPLEEAERLKI----KYGSALASL--ADEDETIEVPGIGG-RPPREISRKELAE-IIEARVEEIFELVRKELK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 322 KSGFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFHGFKSGGEKSAGVFLP 401
Cdd:COG0849 310 RSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPEAVRDPAYATAVGLLLYAAKNQEERFEPVKEK 389
|
410
....*....|....*
gi 1278643644 402 RFGGISHKIplKGLF 416
Cdd:COG0849 390 KKGGLFGRI--KRWF 402
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
5-386 |
1.10e-143 |
|
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: 414.24 E-value: 1.10e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 5 KVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGA 84
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGE-LEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 85 HISSQNSHGVVAVANpEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGS 164
Cdd:cd24048 80 HIRSVNSRGVIAISD-KDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 165 TTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLA 244
Cdd:cd24048 159 SSAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 245 IGLRLSLDGAEKLKIALSEKHEEILAERggnekgDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKSG 324
Cdd:cd24048 239 IGLNTPFEEAERLKIKYGSALSEEADED------EIIEIPGVGG-REPREVSRRELAE-IIEARVEEILELVKKELKESG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278643644 325 FAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFH 386
Cdd:cd24048 311 YEDLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
6-384 |
3.34e-129 |
|
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: 377.36 E-value: 3.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 6 VLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGAH 85
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGE-LNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 86 ISSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGST 165
Cdd:TIGR01174 80 IKSQNSIGVVAI--KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 166 TAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAI 245
Cdd:TIGR01174 158 TILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 246 GLRLSLDGAEKLKIALSEKHEEILaerggnEKGDEIDLAKLGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAV-EIQKSG 324
Cdd:TIGR01174 238 ALRTPLEEAERIKIKYGCASIPLE------GPDENIEIPSVGE-RPPRSLSRKELAE-IIEARAEEILEIVKQkELRKSG 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 325 FAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLL 384
Cdd:TIGR01174 310 FKEELNGGIVLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGGLTEDVNDPEYSTAVGLL 369
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
2-390 |
1.98e-77 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 246.62 E-value: 1.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 2 TRNKVLAAIDVGSSKIAVLIGQQNENNErINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSV 81
Cdd:PRK09472 5 TDRKLVVGLEIGTAKVAALVGEVLPDGM-VNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 82 GGAHISSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHII 161
Cdd:PRK09472 84 SGKHISCQNEIGMVPI--SEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 162 TGSTTAVKNLSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTN 241
Cdd:PRK09472 162 TCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 242 DLAIGLRLSLDGAEKLKIALSEKHEEILAerggneKGDEIDLAKLGvFEETKTVSQKTLVEgIIRPRLNEIFNMVAVEI- 320
Cdd:PRK09472 242 DIAYAFGTPPSDAEAIKVRHGCALGSIVG------KDESVEVPSVG-GRPPRSLQRQTLAE-VIEPRYTELLNLVNEEIl 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278643644 321 ------QKSGFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDILNPAFSVAIGLLFHGFKS 390
Cdd:PRK09472 314 qlqeqlRQQGVKHHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQEPYYSTAVGLLHYGKES 389
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
7-196 |
1.93e-69 |
|
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: 217.73 E-value: 1.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 7 LAAIDVGSSKIAVLIGQQNENNeRINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRILVSVGGAHI 86
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDG-EINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 87 SSQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIITGSTT 166
Cdd:smart00842 80 KSVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKS 157
|
170 180 190
....*....|....*....|....*....|
gi 1278643644 167 AVKNLSKCIAEVGADIGDLVFSGIASAGAV 196
Cdd:smart00842 158 AIQNLEKCVERAGLEVDGIVLEPLASAEAV 187
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
207-382 |
1.53e-34 |
|
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: 126.29 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 207 ILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIGLRLSLDGAEKLKIalseKHEEILAERGGNEKGDEIDLakl 286
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKI----KYGSALASLADEDEVPGVGG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 287 gvfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKSGFA-------GLTPSGVVLTGGGALTVGASESCRRNLSLPVRV 359
Cdd:pfam14450 74 ---REPREISRKELAE-IIEARVEEILELVRAELEDREVLpgeyvrlEVDVHGIVLTGGGSALPGLVELAERALGLPVRI 149
|
170 180
....*....|....*....|...
gi 1278643644 360 GIPGEISGlvddiLNPAFSVAIG 382
Cdd:pfam14450 150 GSPDGIGG-----RNPAYATALG 167
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
88-162 |
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 1278643644 88 SQNSHGVVAVanPEGEIVHEDIKRAIEAARAISLPSSREILHVIPRTYTVDSQQGVADPIGMSGVRLEVDTHIIT 162
Cdd:pfam02491 1 SQNSSGVVAI--SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVVT 73
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
9-383 |
4.21e-20 |
|
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: 90.80 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 9 AIDVGSSKIAVLIGQQNENNERINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAermaGLSIGRILVSVGGAHISS 88
Cdd:cd24049 2 GIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKLLKEN----KIKGKKVVVALPGSDVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 89 QnshgVVAVANPEGEivheDIKRAI--EAARAISLPSSREIL--HVIPRTYTVDSQQGVAdpigMSGVRLEVdthiitgs 164
Cdd:cd24049 78 R----TIKLPKMPEK----ELEEAIrfEAEQYLPFPLEEVVLdyQILGEVEEGGEKLEVL----VVAAPKEI-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 165 ttaVKNLSKCIAEVGADIG--DLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTND 242
Cdd:cd24049 138 ---VESYLELLKEAGLKPVaiDVESFALARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 243 LAIGLRLSLDGAEKLKIalsekheeilaERGGNEKGDEIDLAKlgvfeetktvsqktlVEGIIRPRLNEIFNmvavEIQK 322
Cdd:cd24049 215 IAKALGLSFEEAEELKR-----------EYGLLLEGEEGELKK---------------VAEALRPVLERLVS----EIRR 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278643644 323 S------GFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIP---GEISGLVDDILN---PAFSVAIGL 383
Cdd:cd24049 265 SldyyrsQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPVEILNPfsnIESKKSDDEELKedaPLFAVAIGL 337
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
9-385 |
8.45e-20 |
|
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: 88.89 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 9 AIDVGSSKIAVLIGQqnENNERINVLGASSV--PSLGIRKGQIVNIEEASEVIIKAVEAAERMAGLSIGRIlvsvggahi 86
Cdd:cd24004 2 ALDIGTRSIKGLVLE--EDDENIEVLAFSSEehPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDV--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 87 ssqnshgVVAVANpegeiVHEDIKRAIEAAraislpssreilhviprtytvdsqqgvadpigmsgvrlevdthiitgstt 166
Cdd:cd24004 71 -------VIAIAK-----VVESLLNVLEKA-------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 167 avknlskciaevGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIG 246
Cdd:cd24004 89 ------------GLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 247 LRLSLDGAEKLKIALSEKHEEILAErggnEKGDEIDLAKlgvfeetktvsqktlVEGIIRPRLNEIFNMVAVEIQKSGFA 326
Cdd:cd24004 157 FLISFEEAEKIKRTYGIFLLIEAKD----QLGFTINKKE---------------VYDIIKPVLEELASGIANAIEEYNGK 217
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278643644 327 GLTPSGVVLTGGGALTVGASESCRRNLSLPVRVGIPGEISGLVDDI------LNPAFSVAIGLLF 385
Cdd:cd24004 218 FKLPDAVYLVGGGSKLPGLNEALAEKLGLPVERIAPRNIGAISDITdetskaKGPEFVTPLGIAL 282
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
8-178 |
7.29e-06 |
|
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: 46.17 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 8 AAIDVGSSKIAVLIGQQNeNNERINVLGassVPSLGIRKGqivnieeASEVIIKAVEAAERMAGLSIGRILVSVGGAHIS 87
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDG-ALRHTRVIP---VGGNGITKD-------IAIGLRTAVEEAERLKIKYGSALASLADEDEVP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 88 SQNSHGVVAVANPE-GEIVHEDIKRAIEAARaislpssREIlhvipRTYTVDSQQGVADPIGMSGVrlevdthIITGSTT 166
Cdd:pfam14450 70 GVGGREPREISRKElAEIIEARVEEILELVR-------AEL-----EDREVLPGEYVRLEVDVHGI-------VLTGGGS 130
|
170
....*....|..
gi 1278643644 167 AVKNLSKCIAEV 178
Cdd:pfam14450 131 ALPGLVELAERA 142
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
10-388 |
7.84e-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: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 10 IDVGSSKIAVLIGQQNENNERINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVeaaeRMAGLSIGRILVSVGGAHISSQ 89
Cdd:pfam11104 2 IDISSSAIKLVELSKKKGGYRLERYAIEPLPKGAVVDGNIENIDAVSEALRRAV----KKSGTRLKNVAIAVPGSAVITK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 90 NSHGVVAVANPEGEIVHEdikraIEAARAI-------SL-----------PSSREILHVIPRTYTVDSQQGVADPIGMSG 151
Cdd:pfam11104 78 KIILPAGLSEEELEAQVE-----IEANQYIpfpldevSLdfevlgpnaanPDDVDVLLAAARKEKVEDRVDLLEAAGLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 152 VRLEVDTHIItgsttavknlskciaevgadigDLVFSGIASAgavLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAV 231
Cdd:pfam11104 153 KVVDVESYAL----------------------ERAFERIVSQ---LPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTRE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 232 LPIGSKNVTNDLAIGLRLSLDGAEKLKIA--LSEKHEEILAERGGNEKGDEIDLAkLGVFEetkTVSQKTLVEGIirprl 309
Cdd:pfam11104 208 QAFGGAQLTQEIVRRYGMSYEEAEIAKRNgdLPEDYESEVLEPFVEALAQQISRA-LQFFF---TSTPYNKVDYI----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 310 neifnmvaveiqksgfagltpsgvVLTGGGALTVGASESCRRNLSLPVRVGIPG---EISGLVD--DILN--PAFSVAIG 382
Cdd:pfam11104 279 ------------------------VLAGGCANIPGLAELVTERLGFSTTVANPFrgmELSPRVRqkQLLRdaPSYMVACG 334
|
....*.
gi 1278643644 383 LLFHGF 388
Cdd:pfam11104 335 LALRSF 340
|
|
| eutA |
PRK10719 |
ethanolamine ammonia-lyase reactivating factor EutA; |
160-286 |
2.97e-05 |
|
ethanolamine ammonia-lyase reactivating factor EutA;
Pssm-ID: 236743 [Multi-domain] Cd Length: 475 Bit Score: 46.01 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 160 IITGSTTAVKNLSKCIAEVGADIGDLVfsgIASAGAVL------------TETEKELGVIL-LDIGGGTTSIIVFVENAP 226
Cdd:PRK10719 92 IITGETARKENAREVVMALSGSAGDFV---VATAGPDLesiiagkgagaqTLSEERNTRVLnIDIGGGTANYALFDAGKV 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278643644 227 SYTAVLPIGsknvtndlaiGLRLSLDGAEKLkIALSEKHEEILAERGGN-EKGDEIDLAKL 286
Cdd:PRK10719 169 IDTACLNVG----------GRLIETDSQGRV-TYISPPGQMILDELGLAiTDGRSLTGEQL 218
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
185-359 |
7.75e-05 |
|
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: 44.39 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 185 LVFSGIASA-GAVLTETEKElGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLA------IGLRLSLDGAEKL 257
Cdd:cd10225 124 LIEEPMAAAiGAGLPIEEPR-GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrkYNLLIGERTAERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 258 KI----ALSEKHEEILAERGgnekgdeIDLAKlGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKSG---FAGLTP 330
Cdd:cd10225 203 KIeigsAYPLDEELSMEVRG-------RDLVT-GL-PRTIEITSEEVRE-ALEEPVNAIVEAVRSTLERTPpelAADIVD 272
|
170 180
....*....|....*....|....*....
gi 1278643644 331 SGVVLTGGGALTVGASESCRRNLSLPVRV 359
Cdd:cd10225 273 RGIVLTGGGALLRGLDELLREETGLPVHV 301
|
|
| EutA |
pfam06277 |
Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ... |
160-286 |
4.48e-04 |
|
Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ethanolamine utilization proteins. The EutA protein is thought to protect the lyase (EutBC) from inhibition by CNB12.
Pssm-ID: 377642 Cd Length: 475 Bit Score: 42.23 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 160 IITGSTTAVKNLSKCIAEVGADIGDLVF--------SGIAS--AGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYT 229
Cdd:pfam06277 89 IITGETARKENAREVLHTLSGFAGDFVVatagpdleSIIAGkgAGAAAYSKEHHTRVLNIDIGGGTSNIALFKAGEVIDT 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278643644 230 AVLPIGsknvtndlaiGLRLSLDGAEKLKIALSEKHEEILAERGGN-EKGDEIDLAKL 286
Cdd:pfam06277 169 ACLDVG----------GRLIKIDPDTGRITYISPPARRIIKELGLElEVGEKATLEEL 216
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
191-385 |
4.97e-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: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 191 ASAGAVLTETEKELG------VILLDIGGGTTSIIVF--------VENAPSYTAVLPIGS--------KNVTNDLAIGLR 248
Cdd:cd10170 117 AAALYALEDKGDLLPlkpgdvVLVCDAGGGTVDLSLYevtsgsplLLEEVAPGGGALLGGtdideafeKLLREKLGDKGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 249 LSLDGAEKLKIALSEKHEEILAERGGNEKGDEIDLAKLGVFEETKTVSQKTL------VEGIIRPRLNEIFNmvAVEIQK 322
Cdd:cd10170 197 DLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLEKGTLllteeeIRDLFDPVIDKILE--LIEEQL 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278643644 323 SGFAGLTPSGVVLTGGGALTVGASESCRRnlslpvRVGIPGEISGLVDDilNPAFSVAIGLLF 385
Cdd:cd10170 275 EAKSGTPPDAVVLVGGFSRSPYLRERLRE------RFGSAGIIIVLRSD--DPDTAVARGAAL 329
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
191-383 |
5.46e-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: 41.62 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 191 ASAGAVLTETEKElGVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNV----------TNDLAIGLRLsldgAEKLKIA 260
Cdd:TIGR00904 138 AAIGAGLPVEEPT-GSMVVDIGGGTTEVAVISLGGIVVSRSIRVGGDEFdeaiinyirrTYNLLIGEQT----AERIKIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 261 LSEKHEEILAERGGNEKGDeiDLAKlGVfEETKTVSQKTLVEGIIRPrLNEIFNMVAVEIQKSG---FAGLTPSGVVLTG 337
Cdd:TIGR00904 213 IGSAYPLNDEPRKMEVRGR--DLVT-GL-PRTIEITSVEVREALQEP-VNQIVEAVKRTLEKTPpelAADIVERGIVLTG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278643644 338 GGALTVGASESCRRNLSLPVRVGIpgeisglvddilNPAFSVAIGL 383
Cdd:TIGR00904 288 GGALLRNLDKLLSKETGLPVIVAD------------DPLLCVAKGT 321
|
|
| ASKHA_NBD_ParM_pCBH-like |
cd24025 |
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ... |
197-384 |
1.02e-03 |
|
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments.
Pssm-ID: 466875 [Multi-domain] Cd Length: 326 Bit Score: 41.11 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 197 LTETEKELGVIllDIGGGTTSIIVFVENA---PSYTAVLPIGSKNVTNDLAIGLRlsldgaEKLKIALSEKH-EEILAER 272
Cdd:cd24025 173 KALAKGRVGVI--DIGYRTTDYVVFEDGEflvPELSGSLETGMSTAYRAIANALE------EEYGIDLDLHElDRALREG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 273 GGNEKGDEIDLAKLgvFEETKTVSQKTLVEGIIRpRLNEIFNMVAveiqksgfagltpsGVVLTGGGALTVGASescrrn 352
Cdd:cd24025 245 KIRVRGKEIDLSDL--IDEALKELARQIANEIRS-LWGDGLGDLD--------------AIILAGGGAELLAPY------ 301
|
170 180 190
....*....|....*....|....*....|..
gi 1278643644 353 lslpVRVGIPGEIsgLVDDilnPAFSVAIGLL 384
Cdd:cd24025 302 ----LKEMFPNAE--VVPD---PQFANARGYL 324
|
|
| EutJ |
COG4820 |
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
210-270 |
1.36e-03 |
|
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism];
Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 40.17 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278643644 210 DIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIGLRLSLDGAEKLKIAlSEKHEEILA 270
Cdd:COG4820 139 DIGGGTTGISILKDGEVVYTADEPTGGTHMSLVLAGAYGISFEEAEQLKRD-PANHREVFP 198
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
4-383 |
2.75e-03 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 39.45 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 4 NKVLAAIDVGSSKIAVLIGQQNENNERINVLGASSVPSLGIRKGQIVNIEEASEVIIKAVEAAermaGLSIGRILVSVGG 83
Cdd:COG4972 1 KKPLVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRL----KIKTKRVAIAVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 84 AHISSQNshgVVAVANPEgeivhEDIKRAI--EAARAISLPSSREIL--HVIPRTYTVDSQQGVadpiGMSGVRLEVdth 159
Cdd:COG4972 77 SSVITRK---ITLPALSE-----KELEEAIefEAEQYIPFPLEEVVLdfQVLGPSEEGPEKVEV----LLVAARKEV--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 160 iitgsttaVKNLSKCIAEVG--ADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFVENAPSYTAVLPIGsk 237
Cdd:COG4972 142 --------VEDYVELLEAAGlkPVVVDVEPFALLRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPFG-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 238 nvtndLAIGLRLSLDgaeklkialsekheeilaerggnekgdeidlaklgvfeetktvsqktlvegiirprlneIFNmva 317
Cdd:COG4972 212 -----LAQEIRRSLQ-----------------------------------------------------------FYR--- 224
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278643644 318 veiqkSGFAGLTPSGVVLTGGGALTVGASESCRRNLSLPVRV-----GIPGEISGLVDDILNPAFSVAIGL 383
Cdd:COG4972 225 -----SQSGGNEVDRILLAGGGAKLPGLAEYLEERLGIPVEVlnpfaGMALSVDEEALAEDAPSFAVALGL 290
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
190-270 |
3.21e-03 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 39.04 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 190 IASAGAVLTETEKE-------LGV---ILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIGLRLSLDGAEKLKI 259
Cdd:PRK15080 111 VESAGLEVTHVLDEptaaaavLGIdngAVVDIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQYKR 190
|
90
....*....|.
gi 1278643644 260 AlSEKHEEILA 270
Cdd:PRK15080 191 D-PKHHKEIFP 200
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
192-270 |
4.30e-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: 38.40 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278643644 192 SAGAVLTETEkelGVILlDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTNDLAIGLRLSLDGAEKLKIALSeKHEEILA 270
Cdd:cd24047 103 AANAVLGIRD---GAVV-DIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLAGNYGISFEEAEIIKRDPA-RHKELLP 176
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
205-383 |
4.90e-03 |
|
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: 38.91 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 205 GVILLDIGGGTTSIIVFVENAPSYTAVLPIGSKNVTND----------LAIGLRLsldgAEKLKI----ALSEKHEEILA 270
Cdd:COG1077 152 GNMVVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAiiqyvrkkynLLIGERT----AEEIKIeigsAYPLEEELTME 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 271 ERGgnekgdeIDLAKlGVfEETKTVSQKTLVEgIIRPRLNEIFNMVAVEIQKsgfaglTP---------SGVVLTGGGAL 341
Cdd:COG1077 228 VRG-------RDLVT-GL-PKTITITSEEIRE-ALEEPLNAIVEAIKSVLEK------TPpelaadivdRGIVLTGGGAL 291
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278643644 342 TVGASESCRRNLSLPVRVgipgeisglVDDilnPAFSVAIGL 383
Cdd:COG1077 292 LRGLDKLLSEETGLPVHV---------AED---PLTCVARGT 321
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
147-382 |
8.60e-03 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 37.96 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 147 IGMSGVRLEVDTHIITGSTTAVKN-LSKCIAEVGADIGDLVFSGIASAGAVLTETEKELGVILLDIGGGTTSIIVFvena 225
Cdd:PRK13929 92 IGMTFRKPNVVVCTPSGSTAVERRaISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAII---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 226 pSYTAVLPIGSKNVTNDlaiglrlSLDgaEKLKIALSEKHEEILAERGGNEKGDEIDLAKLGVFEETKTVSQKTLVEGI- 304
Cdd:PRK13929 168 -SFGGVVSCHSIRIGGD-------QLD--EDIVSFVRKKYNLLIGERTAEQVKMEIGYALIEHEPETMEVRGRDLVTGLp 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278643644 305 -------------IRPRLNEIFNMVAVEIQKS--GFAG-LTPSGVVLTGGGALTVGASESCRRNLSLPVRVGipgeisgl 368
Cdd:PRK13929 238 ktitleskeiqgaMRESLLHILEAIRATLEDCppELSGdIVDRGVILTGGGALLNGIKEWLSEEIVVPVHVA-------- 309
|
250
....*....|....
gi 1278643644 369 vddiLNPAFSVAIG 382
Cdd:PRK13929 310 ----ANPLESVAIG 319
|
|
| |
