|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
4-359 |
1.99e-113 |
|
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: 338.35 E-value: 1.99e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 4 HYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIG 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGeLEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 83 TEVYDESNEIEFYEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARhSLKVDAGVIAIQK 162
Cdd:cd24048 81 IRSVNSRGVIAISDKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGS-RLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 163 SILINMIKCVEACGVDVLDVYSDAY-NYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQ 241
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLaSAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 242 GLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGL-TKVNGGF 320
Cdd:cd24048 240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYeDLLPGGI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488376844 321 VVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:cd24048 320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAY 363
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-359 |
2.95e-101 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 308.22 E-value: 2.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 2 EEHYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPI 80
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGkLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 81 IGTEVYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAI 160
Cdd:COG0849 82 GHIKSQNSRGVVAI-SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEVDVHIVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 161 QKSILINMIKCVEACGVDVLDVYSDAYNYG-SILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDI 239
Cdd:COG0849 160 PKTAVQNLVKCVERAGLEVEDLVLSPLASAeAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 240 AQGLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGL-TKVNG 318
Cdd:COG0849 240 AIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYeEKLPA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488376844 319 GFVVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:COG0849 320 GVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAY 365
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
5-359 |
9.78e-70 |
|
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: 225.98 E-value: 9.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 5 YYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIGT 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 84 EVYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAIQKS 163
Cdd:TIGR01174 81 KSQNSIGVVAI-KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVR-LEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 164 ILINMIKCVEACGVDVLDVYSDAYNYG-SILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQG 242
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAiAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 243 LNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFD-VLQELGL-TKVNGGF 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFkEELNGGI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488376844 321 VVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEY 362
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
6-187 |
5.18e-40 |
|
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: 142.23 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 6 YVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIGTE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGeINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 85 VYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAIQKSI 164
Cdd:smart00842 81 SVNVSGVVAI-PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVR-LEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|...
gi 488376844 165 LINMIKCVEACGVDVLDVYSDAY 187
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPL 181
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
203-359 |
1.81e-33 |
|
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: 123.98 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 203 CVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYDTAEKVKHQYGHAFYDSASDQDVFSvdqVDSDEHV 282
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDEVPG---VGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 283 QYTQKDLSDFIEQRVEDIFFEVFDVLQELG--------LTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRIHTPSQMGI 354
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
....*
gi 488376844 355 RKPEF 359
Cdd:pfam14450 158 RNPAY 162
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
7-349 |
1.74e-30 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 122.20 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 7 VSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPiiGTEV 85
Cdd:PRK09472 11 VGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS--GKHI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 86 YDEsNEIEF--YEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIA-RHSLKVDagVIAIQK 162
Cdd:PRK09472 89 SCQ-NEIGMvpISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGvRMQAKVH--LITCHN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 163 SILINMIKCVEACGVDVLD-VYSDAYNYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQ 241
Cdd:PRK09472 166 DMAKNIVKAVERCGLKVDQlIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 242 GLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQR-------VEDIFFEVFDVLQELGLT 314
Cdd:PRK09472 246 AFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRytellnlVNEEILQLQEQLRQQGVK 325
|
330 340 350
....*....|....*....|....*....|....*.
gi 488376844 315 -KVNGGFVVTGGSANLLGVKELLQDMVSEKVRIHTP 349
Cdd:PRK09472 326 hHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAP 361
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
4-359 |
1.99e-113 |
|
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: 338.35 E-value: 1.99e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 4 HYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIG 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGeLEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 83 TEVYDESNEIEFYEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARhSLKVDAGVIAIQK 162
Cdd:cd24048 81 IRSVNSRGVIAISDKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGS-RLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 163 SILINMIKCVEACGVDVLDVYSDAY-NYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQ 241
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLaSAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 242 GLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGL-TKVNGGF 320
Cdd:cd24048 240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYeDLLPGGI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488376844 321 VVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:cd24048 320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAY 363
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-359 |
2.95e-101 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 308.22 E-value: 2.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 2 EEHYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPI 80
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGkLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 81 IGTEVYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAI 160
Cdd:COG0849 82 GHIKSQNSRGVVAI-SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEVDVHIVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 161 QKSILINMIKCVEACGVDVLDVYSDAYNYG-SILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDI 239
Cdd:COG0849 160 PKTAVQNLVKCVERAGLEVEDLVLSPLASAeAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 240 AQGLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGL-TKVNG 318
Cdd:COG0849 240 AIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYeEKLPA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488376844 319 GFVVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:COG0849 320 GVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAY 365
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
5-359 |
9.78e-70 |
|
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: 225.98 E-value: 9.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 5 YYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIGT 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 84 EVYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAIQKS 163
Cdd:TIGR01174 81 KSQNSIGVVAI-KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVR-LEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 164 ILINMIKCVEACGVDVLDVYSDAYNYG-SILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQG 242
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAiAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 243 LNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQRVEDIFFEVFD-VLQELGL-TKVNGGF 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFkEELNGGI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488376844 321 VVTGGSANLLGVKELLQDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEY 362
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
6-187 |
5.18e-40 |
|
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: 142.23 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 6 YVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPIIGTE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGeINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 85 VYDESNEIEFyEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVIAIQKSI 164
Cdd:smart00842 81 SVNVSGVVAI-PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVR-LEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|...
gi 488376844 165 LINMIKCVEACGVDVLDVYSDAY 187
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPL 181
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
203-359 |
1.81e-33 |
|
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: 123.98 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 203 CVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYDTAEKVKHQYGHAFYDSASDQDVFSvdqVDSDEHV 282
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDEVPG---VGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 283 QYTQKDLSDFIEQRVEDIFFEVFDVLQELG--------LTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRIHTPSQMGI 354
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
....*
gi 488376844 355 RKPEF 359
Cdd:pfam14450 158 RNPAY 162
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
7-349 |
1.74e-30 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 122.20 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 7 VSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPiiGTEV 85
Cdd:PRK09472 11 VGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS--GKHI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 86 YDEsNEIEF--YEDTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIA-RHSLKVDagVIAIQK 162
Cdd:PRK09472 89 SCQ-NEIGMvpISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGvRMQAKVH--LITCHN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 163 SILINMIKCVEACGVDVLD-VYSDAYNYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQ 241
Cdd:PRK09472 166 DMAKNIVKAVERCGLKVDQlIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 242 GLNTTYDTAEKVKHQYGHAFYDSASDQDVFSVDQVDSDEHVQYTQKDLSDFIEQR-------VEDIFFEVFDVLQELGLT 314
Cdd:PRK09472 246 AFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRytellnlVNEEILQLQEQLRQQGVK 325
|
330 340 350
....*....|....*....|....*....|....*.
gi 488376844 315 -KVNGGFVVTGGSANLLGVKELLQDMVSEKVRIHTP 349
Cdd:PRK09472 326 hHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAP 361
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
7-349 |
3.18e-23 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 100.05 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 7 VSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSG--IKNGLIDDFDIARQAIKDTIKKASI-----ASGVDIKDVF---L 76
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEgaIVDGEIADPEALAEALKKLLKENKIkgkkvVVALPGSDVIvrtI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 77 KLPIIgtevydESNEIEfyedteidgthiESVLEGIRDKNDVPETEVInvfpIRFVVDKDNEVSDPKeliarhslkVDAG 156
Cdd:cd24049 81 KLPKM------PEKELE------------EAIRFEAEQYLPFPLEEVV----LDYQILGEVEEGGEK---------LEVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 157 VIAIQKSILINMIKCVEACG--VDVLDVYSDA-YNYGSILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGR 233
Cdd:cd24049 130 VVAAPKEIVESYLELLKEAGlkPVAIDVESFAlARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 234 DITDDIAQGLNTTYDTAEKVKHQYGhafydsasdqdvfsvdqvDSDEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQ---- 309
Cdd:cd24049 210 DITEAIAKALGLSFEEAEELKREYG------------------LLLEGEEGELKKVAEALRPVLERLVSEIRRSLDyyrs 271
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 488376844 310 ELGLTKVNgGFVVTGGSANLLGVKELLQDMVSEKVRIHTP 349
Cdd:cd24049 272 QNGGEPID-KIYLTGGGSLLPGLDEYLSERLGIPVEILNP 310
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
7-338 |
2.42e-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: 90.82 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 7 VSIDIGSSSVKTIVGEKFHNGINVIGTGQ--TYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKDVFLKLPiigte 84
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDENIEVLAFSSeeHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAIA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 85 vydesneiefyedteidgTHIESVLEGIRDkndvpetevinvfpirfvvdkdnevsdpkeliarhslkvdAGVIAIqkSI 164
Cdd:cd24004 76 ------------------KVVESLLNVLEK----------------------------------------AGLEPV--GL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 165 LINMIKCVEAcgvdvldvysdaynygsILTPTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLN 244
Cdd:cd24004 96 TLEPFAAANL-----------------LIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 245 TTYDTAEKVKHQYGHAFYDSASDQDVFsvdqvdsdehvQYTQKDLSDFIEQRVEDIFFEVFDVLQEL-GLTKVNGGFVVT 323
Cdd:cd24004 159 ISFEEAEKIKRTYGIFLLIEAKDQLGF-----------TINKKEVYDIIKPVLEELASGIANAIEEYnGKFKLPDAVYLV 227
|
330
....*....|....*
gi 488376844 324 GGSANLLGVKELLQD 338
Cdd:cd24004 228 GGGSKLPGLNEALAE 242
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
204-346 |
5.51e-10 |
|
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: 60.48 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 204 VIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYD------TAEKVKHQYGHAFYDSASDQ-DVFSVDQV 276
Cdd:COG1077 155 VVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIQYVRKKYNlligerTAEEIKIEIGSAYPLEEELTmEVRGRDLV 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488376844 277 DS-DEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQ----ELGLTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRI 346
Cdd:COG1077 235 TGlPKTITITSEEIREALEEPLNAIVEAIKSVLEktppELAADIVDRGIVLTGGGALLRGLDKLLSEETGLPVHV 309
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
204-346 |
7.88e-10 |
|
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: 59.79 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 204 VIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTY------DTAEKVKHQYGHAFYDSASDQ-DVFSVDQV 276
Cdd:cd10225 147 VVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIINYVRRKYnlligeRTAERIKIEIGSAYPLDEELSmEVRGRDLV 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488376844 277 DSDEH-VQYTQKDLSDFIEQRVEDIFFEVFDVLQ----ELGLTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRI 346
Cdd:cd10225 227 TGLPRtIEITSEEVREALEEPVNAIVEAVRSTLErtppELAADIVDRGIVLTGGGALLRGLDELLREETGLPVHV 301
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
6-223 |
3.41e-08 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 54.86 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 6 YVSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSG--IKNGLIDDFDIARQAIKDTIKKasiaSGVDIKDVFLKLPiiGT 83
Cdd:COG4972 4 LVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEgaVVDGNIVDPEAVAEALKELLKR----LKIKTKRVAIAVP--GS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 84 EVYdeSNEIEF--YEDTEIDGT---HIESVLEgirdkndVPETEVInvfpIRFVVDKDNEvsdpkeliaRHSLKVDAGVI 158
Cdd:COG4972 78 SVI--TRKITLpaLSEKELEEAiefEAEQYIP-------FPLEEVV----LDFQVLGPSE---------EGPEKVEVLLV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488376844 159 AIQKSILINMIKCVEACG--VDVLDVYSDA-YNYGSILTPTEKELGACVIDIGEDLTQVAFYERGELV 223
Cdd:COG4972 136 AARKEVVEDYVELLEAAGlkPVVVDVEPFAlLRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPI 203
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
195-346 |
4.47e-08 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 54.91 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 195 PTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYD------TAEKVKHQYGHAFYDSASDQ 268
Cdd:PRK13929 145 PVDEPVANVVVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVSFVRKKYNlligerTAEQVKMEIGYALIEHEPET 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 269 -DVFSVDQVDS-----DEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQELGLTKVNGGFVVTGGSANLLGVKELLQDMVSE 342
Cdd:PRK13929 225 mEVRGRDLVTGlpktiTLESKEIQGAMRESLLHILEAIRATLEDCPPELSGDIVDRGVILTGGGALLNGIKEWLSEEIVV 304
|
....
gi 488376844 343 KVRI 346
Cdd:PRK13929 305 PVHV 308
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
195-346 |
3.74e-07 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 51.79 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 195 PTEKELGACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYD------TAEKVKHQYGHAFYDSASDQ 268
Cdd:pfam06723 140 PVEEPTGNMVVDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIIKYIRKKYNlligerTAERIKIEIGSAYPTEEEEK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 269 -DVFSVDQVDSDEH-VQYTQKDLSDFIEQRVEDIFFEVFDVLQ----ELGLTKVNGGFVVTGGSANLLGVKELLQDMVSE 342
Cdd:pfam06723 220 mEIRGRDLVTGLPKtIEISSEEVREALKEPVSAIVEAVKEVLEktppELAADIVDRGIVLTGGGALLRGLDKLLSDETGL 299
|
....
gi 488376844 343 KVRI 346
Cdd:pfam06723 300 PVHI 303
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
201-338 |
3.10e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 46.05 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 201 GACVIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYD------TAEKVKHQYGHAFYDSASDQ-DVFSV 273
Cdd:PRK13928 148 GNMVVDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIRYIRKKYKlligerTAEEIKIKIGTAFPGAREEEmEIRGR 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 274 DQVDS-DEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQ----ELGLTKVNGGFVVTGGSANLLGVKELLQD 338
Cdd:PRK13928 228 DLVTGlPKTITVTSEEIREALKEPVSAIVQAVKSVLErtppELSADIIDRGIIMTGGGALLHGLDKLLAE 297
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
204-346 |
8.81e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 44.31 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 204 VIDIGEDLTQVAFYERGELVDAESIEMAGRDITDDIAQGLNTTYD------TAEKVKHQYGHAF-YDSASDQDVFSVDQV 276
Cdd:PRK13927 152 VVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIINYVRRNYNlligerTAERIKIEIGSAYpGDEVLEMEVRGRDLV 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488376844 277 DS-DEHVQYTQKDLSDFIEQRVEDIFFEVFDVLQ----ELGLTKVNGGFVVTGGSANLLGVKELLQDMVSEKVRI 346
Cdd:PRK13927 232 TGlPKTITISSNEIREALQEPLSAIVEAVKVALEqtppELAADIVDRGIVLTGGGALLRGLDKLLSEETGLPVHV 306
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
97-158 |
1.39e-04 |
|
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: 40.17 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488376844 97 DTEIDGTHIESVLEGIRDKNDVPETEVINVFPIRFVVDKDNEVSDPKELIARHsLKVDAGVI 158
Cdd:pfam02491 12 GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEADVHVV 72
|
|
| ASKHA_NBD_actin-like |
cd10169 |
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ... |
202-350 |
5.54e-03 |
|
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP 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: 466810 [Multi-domain] Cd Length: 258 Bit Score: 38.63 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 202 ACVIDIGEDLTQ-VAFYErGELVD--AESIEMAGRDITDDIAQGLN------TTY---DTAEKVKHQYG---HAFYDsas 266
Cdd:cd10169 97 GLVVDSGEGVTHiVPVYE-GYVLPhaVRRLDIGGRDLTDYLAKLLRekgysfSTSaerEIVRDIKEKLCglhELIYD--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376844 267 dqdvfSVDQVDSDehvqyTQKDLSDFIeqrvediffevfdvlqelgltkvnggfVVTGGSANLLGVKE-LLQDMV----- 340
Cdd:cd10169 173 -----SIMKCDID-----LRKELYSNI---------------------------VLSGGTTLFPGFAErLQKELSklaps 215
|
170
....*....|
gi 488376844 341 SEKVRIHTPS 350
Cdd:cd10169 216 SVKVKVIAPP 225
|
|
| |
