|
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 |
3.54e-116 |
|
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: 345.67 E-value: 3.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 4 HYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIG 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGeLEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 83 TEVYDESNEIDFYEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARhSLKVEAGVIAIQK 162
Cdd:cd24048 81 IRSVNSRGVIAISDKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGS-RLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 163 SILINMIKCVEACGVDVLDVYSDAY-NYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQ 241
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLaSAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 242 GLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGL-TKVNGGF 320
Cdd:cd24048 240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYeDLLPGGI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446313177 321 IVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:cd24048 320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAY 363
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-359 |
2.35e-103 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 313.99 E-value: 2.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 2 EEHYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPI 80
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGkLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 81 IGTEVYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAI 160
Cdd:COG0849 82 GHIKSQNSRGVVAI-SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEVDVHIVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 161 QKSILINMIKCVEACGVDVLDVYSDAYNYG-SILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDI 239
Cdd:COG0849 160 PKTAVQNLVKCVERAGLEVEDLVLSPLASAeAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 240 AQGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGL-TKVNG 318
Cdd:COG0849 240 AIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYeEKLPA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446313177 319 GFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:COG0849 320 GVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAY 365
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
5-359 |
2.43e-73 |
|
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: 235.61 E-value: 2.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 5 YYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGT 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 84 EVYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAIQKS 163
Cdd:TIGR01174 81 KSQNSIGVVAI-KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVR-LEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 164 ILINMIKCVEACGVDVLDVYSDAYNYG-SILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQG 242
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAiAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 243 LNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFD-VLQDLGL-TKVNGGF 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFkEELNGGI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446313177 321 IVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----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 |
6.28e-41 |
|
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: 144.54 E-value: 6.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 6 YVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGTE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGeINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 85 VYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAIQKSI 164
Cdd:smart00842 81 SVNVSGVVAI-PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVR-LEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|...
gi 446313177 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 |
7.32e-36 |
|
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: 130.53 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 203 CVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYETAEKVKHQYGHAFYDSASDQDiftVEQVDSDETV 282
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDE---VPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 283 QYTQKDLSDFIEARVEEIFFEVFDVLQDLG--------LTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMGI 354
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
....*
gi 446313177 355 RKPEF 359
Cdd:pfam14450 158 RNPAY 162
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
7-349 |
1.55e-29 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 119.50 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 7 VSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPiiGTEV 85
Cdd:PRK09472 11 VGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS--GKHI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 86 YDEsNEIDF--YEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPkelIARHSLKVEAGV--IAIQ 161
Cdd:PRK09472 89 SCQ-NEIGMvpISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNP---VGLSGVRMQAKVhlITCH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 162 KSILINMIKCVEACGVDVLD-VYSDAYNYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIA 240
Cdd:PRK09472 165 NDMAKNIVKAVERCGLKVDQlIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 241 QGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEAR-------VEEIFFEVFDVLQDLGL 313
Cdd:PRK09472 245 YAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRytellnlVNEEILQLQEQLRQQGV 324
|
330 340 350
....*....|....*....|....*....|....*..
gi 446313177 314 T-KVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTP 349
Cdd:PRK09472 325 KhHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAP 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 |
3.54e-116 |
|
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: 345.67 E-value: 3.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 4 HYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIG 82
Cdd:cd24048 1 NIIVGLDIGTSKICALVGEVSEDGeLEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 83 TEVYDESNEIDFYEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARhSLKVEAGVIAIQK 162
Cdd:cd24048 81 IRSVNSRGVIAISDKDEITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGS-RLEVDVHVITGSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 163 SILINMIKCVEACGVDVLDVYSDAY-NYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQ 241
Cdd:cd24048 160 SAIQNLIKCVERAGLEVDDIVLSPLaSAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 242 GLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGL-TKVNGGF 320
Cdd:cd24048 240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYeDLLPGGI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446313177 321 IVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:cd24048 320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAY 363
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
2-359 |
2.35e-103 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 313.99 E-value: 2.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 2 EEHYYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPI 80
Cdd:COG0849 2 KSNIIVGLDIGTSKVVALVGEVDPDGkLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 81 IGTEVYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAI 160
Cdd:COG0849 82 GHIKSQNSRGVVAI-SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEVDVHIVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 161 QKSILINMIKCVEACGVDVLDVYSDAYNYG-SILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDI 239
Cdd:COG0849 160 PKTAVQNLVKCVERAGLEVEDLVLSPLASAeAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 240 AQGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGL-TKVNG 318
Cdd:COG0849 240 AIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYeEKLPA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446313177 319 GFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----IRKPEF 359
Cdd:COG0849 320 GVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAY 365
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
5-359 |
2.43e-73 |
|
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: 235.61 E-value: 2.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 5 YYVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGT 83
Cdd:TIGR01174 1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 84 EVYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAIQKS 163
Cdd:TIGR01174 81 KSQNSIGVVAI-KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVR-LEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 164 ILINMIKCVEACGVDVLDVYSDAYNYG-SILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQG 242
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAiAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 243 LNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFD-VLQDLGL-TKVNGGF 320
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFkEELNGGI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446313177 321 IVTGGSANLLGVKELLSDMVSEKVRIHTPSQMG-----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 |
6.28e-41 |
|
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: 144.54 E-value: 6.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 6 YVSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGTE 84
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGeINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 85 VYDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVIAIQKSI 164
Cdd:smart00842 81 SVNVSGVVAI-PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVR-LEVDVHVVTAPKSA 158
|
170 180
....*....|....*....|...
gi 446313177 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 |
7.32e-36 |
|
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: 130.53 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 203 CVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYETAEKVKHQYGHAFYDSASDQDiftVEQVDSDETV 282
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADEDE---VPGVGGREPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 283 QYTQKDLSDFIEARVEEIFFEVFDVLQDLG--------LTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMGI 354
Cdd:pfam14450 78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157
|
....*
gi 446313177 355 RKPEF 359
Cdd:pfam14450 158 RNPAY 162
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
7-349 |
1.55e-29 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 119.50 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 7 VSIDIGSSSVKTIVGEKFHNG-INVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPiiGTEV 85
Cdd:PRK09472 11 VGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALS--GKHI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 86 YDEsNEIDF--YEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPkelIARHSLKVEAGV--IAIQ 161
Cdd:PRK09472 89 SCQ-NEIGMvpISEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNP---VGLSGVRMQAKVhlITCH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 162 KSILINMIKCVEACGVDVLD-VYSDAYNYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIA 240
Cdd:PRK09472 165 NDMAKNIVKAVERCGLKVDQlIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 241 QGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEAR-------VEEIFFEVFDVLQDLGL 313
Cdd:PRK09472 245 YAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRytellnlVNEEILQLQEQLRQQGV 324
|
330 340 350
....*....|....*....|....*....|....*..
gi 446313177 314 T-KVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTP 349
Cdd:PRK09472 325 KhHLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAP 361
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
7-338 |
2.07e-22 |
|
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: 96.59 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 7 VSIDIGSSSVKTIVGEKFHNGINVIGTGQ--TYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPiigte 84
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDDENIEVLAFSSeeHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAIA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 85 vydesneidfyedteingshieKVLEGIrekndvqetevinvfpirfivdkenevsdpKELIARHSLKVEAGVIAiqksi 164
Cdd:cd24004 76 ----------------------KVVESL------------------------------LNVLEKAGLEPVGLTLE----- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 165 LINMIKCVEacgvdvldvysdaynygsilTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLN 244
Cdd:cd24004 99 PFAAANLLI--------------------PYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGFL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 245 TSYETAEKVKHQYGHAFYDSASDQDIFTveqvdsdetvqYTQKDLSDFIEARVEEIFFEVFDVLQDL-GLTKVNGGFIVT 323
Cdd:cd24004 159 ISFEEAEKIKRTYGIFLLIEAKDQLGFT-----------INKKEVYDIIKPVLEELASGIANAIEEYnGKFKLPDAVYLV 227
|
330
....*....|....*
gi 446313177 324 GGSANLLGVKELLSD 338
Cdd:cd24004 228 GGGSKLPGLNEALAE 242
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
7-349 |
6.67e-22 |
|
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: 96.19 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 7 VSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSG--IKNGLIDDFDIARQAIKDTIKKASIASgvdiKEVFLKLPiiGTE 84
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEgaIVDGEIADPEALAEALKKLLKENKIKG----KKVVVALP--GSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 85 VYDESNEIDFYEDTEINgshiEKVLEGIREKNDVQETEVInvfpIRFIVDKENEVSDPKeliarhslkVEAGVIAIQKSI 164
Cdd:cd24049 75 VIVRTIKLPKMPEKELE----EAIRFEAEQYLPFPLEEVV----LDYQILGEVEEGGEK---------LEVLVVAAPKEI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 165 LINMIKCVEACG--VDVLDVYSDA-YNYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQ 241
Cdd:cd24049 138 VESYLELLKEAGlkPVAIDVESFAlARALEYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 242 GLNTSYETAEKVKHQYGhafydsasdqdiftveqvDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQ----DLGLTKVN 317
Cdd:cd24049 218 ALGLSFEEAEELKREYG------------------LLLEGEEGELKKVAEALRPVLERLVSEIRRSLDyyrsQNGGEPID 279
|
330 340 350
....*....|....*....|....*....|..
gi 446313177 318 gGFIVTGGSANLLGVKELLSDMVSEKVRIHTP 349
Cdd:cd24049 280 -KIYLTGGGSLLPGLDEYLSERLGIPVEILNP 310
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
204-346 |
3.67e-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: 60.95 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 204 VIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQ------GLNTSYETAEKVKHQYGHAFYDSASdqDIFTVEQVD 277
Cdd:cd10225 147 VVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIINyvrrkyNLLIGERTAERIKIEIGSAYPLDEE--LSMEVRGRD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 278 SDE----TVQYTQKDLSDFIEARVEEIFFEVFDVL--------QDLgltkVNGGFIVTGGSANLLGVKELLSDMVSEKVR 345
Cdd:cd10225 225 LVTglprTIEITSEEVREALEEPVNAIVEAVRSTLertppelaADI----VDRGIVLTGGGALLRGLDELLREETGLPVH 300
|
.
gi 446313177 346 I 346
Cdd:cd10225 301 V 301
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
204-346 |
7.81e-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: 60.09 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 204 VIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQ------GLNTSYETAEKVKHQYGHAFYDsaSDQDIFTVEQVD 277
Cdd:COG1077 155 VVDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIIQyvrkkyNLLIGERTAEEIKIEIGSAYPL--EEELTMEVRGRD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 278 SDE----TVQYTQKDLSDFIEARVEEIFFEVFDVL--------QDLgltkVNGGFIVTGGSANLLGVKELLSDMVSEKVR 345
Cdd:COG1077 233 LVTglpkTITITSEEIREALEEPLNAIVEAIKSVLektppelaADI----VDRGIVLTGGGALLRGLDKLLSEETGLPVH 308
|
.
gi 446313177 346 I 346
Cdd:COG1077 309 V 309
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
6-223 |
4.80e-08 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 54.48 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 6 YVSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSG--IKNGLIDDFDIARQAIKDTIKKasiaSGVDIKEVFLKLPiiGT 83
Cdd:COG4972 4 LVGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEgaVVDGNIVDPEAVAEALKELLKR----LKIKTKRVAIAVP--GS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 84 EVYdeSNEIDFyedTEINGSHIEKVLEgirekndvqeTEVINVFPIRF---IVDkeNEVSDPKEliaRHSLKVEAGVIAI 160
Cdd:COG4972 78 SVI--TRKITL---PALSEKELEEAIE----------FEAEQYIPFPLeevVLD--FQVLGPSE---EGPEKVEVLLVAA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446313177 161 QKSILINMIKCVEACG--VDVLDVYSDA-YNYGSILTATEKELGACVIDIGEDVTQVAFYERGELV 223
Cdd:COG4972 138 RKEVVEDYVELLEAAGlkPVVVDVEPFAlLRALELLPPSGPDETVALVDIGASSTTLSVLSNGKPI 203
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
204-346 |
6.67e-07 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 51.06 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 204 VIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSY------ETAEKVKHQYGHAFYDSASDqdifTVEQVD 277
Cdd:PRK13929 154 VVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVSFVRKKYnlligeRTAEQVKMEIGYALIEHEPE----TMEVRG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446313177 278 SD------ETVQYTQKDLSDFIEARVEEIFFEVFDVLQD----LGLTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRI 346
Cdd:PRK13929 230 RDlvtglpKTITLESKEIQGAMRESLLHILEAIRATLEDcppeLSGDIVDRGVILTGGGALLNGIKEWLSEEIVVPVHV 308
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
201-346 |
2.95e-06 |
|
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: 49.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 201 GACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYE------TAEKVKHQYGHAFYDSASDQ-DIFTV 273
Cdd:pfam06723 146 GNMVVDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIIKYIRKKYNlligerTAERIKIEIGSAYPTEEEEKmEIRGR 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446313177 274 EQVDS-DETVQYTQKDLSDFIEARVEEIFFEVFDVLQ----DLGLTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRI 346
Cdd:pfam06723 226 DLVTGlPKTIEISSEEVREALKEPVSAIVEAVKEVLEktppELAADIVDRGIVLTGGGALLRGLDKLLSDETGLPVHI 303
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
86-158 |
1.75e-05 |
|
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: 42.48 E-value: 1.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446313177 86 YDESNEIDFyEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHsLKVEAGVI 158
Cdd:pfam02491 2 QNSSGVVAI-SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVR-LEADVHVV 72
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
9-348 |
3.59e-05 |
|
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: 45.74 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 9 IDIGSSSVKTI-VGEKFHN------GINVIGTGqtytsGIKNGLIDDFDiarqAIKDTIKKASIASGVDIKEVFLKLPii 81
Cdd:pfam11104 2 IDISSSAIKLVeLSKKKGGyrleryAIEPLPKG-----AVVDGNIENID----AVSEALRRAVKKSGTRLKNVAIAVP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 82 GTEVydesneidfyedteingshIEKVL---EGIREKN-DVQ-ETEVINVFPirFIVDkenEVSDPKELI---ARHSLKV 153
Cdd:pfam11104 71 GSAV-------------------ITKKIilpAGLSEEElEAQvEIEANQYIP--FPLD---EVSLDFEVLgpnAANPDDV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 154 EAGVIAIQKSILINMIKCVEACG--VDVLDVYSDAYN-----YGSILTATEKELGACVIDIGEDVTQVAFYERGELVDAD 226
Cdd:pfam11104 127 DVLLAAARKEKVEDRVDLLEAAGlkPKVVDVESYALEraferIVSQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 227 SIEMAGRDITDDIAQGLNTSYETAEKVKhqyghafydsasdqdiftveqVDSDETVQYTQKDLSDFIEARVEEI-----F 301
Cdd:pfam11104 207 EQAFGGAQLTQEIVRRYGMSYEEAEIAK---------------------RNGDLPEDYESEVLEPFVEALAQQIsralqF 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446313177 302 FevFDVLQDLGLTKVnggfIVTGGSANLLGvkelLSDMVSEKVRIHT 348
Cdd:pfam11104 266 F--FTSTPYNKVDYI----VLAGGCANIPG----LAELVTERLGFST 302
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
201-338 |
7.44e-04 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 41.43 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 201 GACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYE------TAEKVKHQYGHAFYDSASDQ-DIFTV 273
Cdd:PRK13928 148 GNMVVDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIRYIRKKYKlligerTAEEIKIKIGTAFPGAREEEmEIRGR 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 274 EQVDS-DETVQYTQKDLSDFIEARVEEIFFEVFDVLQ----DLGLTKVNGGFIVTGGSANLLGVKELLSD 338
Cdd:PRK13928 228 DLVTGlPKTITVTSEEIREALKEPVSAIVQAVKSVLErtppELSADIIDRGIIMTGGGALLHGLDKLLAE 297
|
|
| ASKHA_NBD_Arp3-like |
cd10221 |
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ... |
195-258 |
1.52e-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: 40.63 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446313177 195 ATEKELGACVIDIGEDVTQVAFYERGELVD--ADSIEMAGRDITDDIAQGL---------NTSYETAEKVKHQYG 258
Cdd:cd10221 152 VGERTLTGTVIDSGDGVTHVIPVAEGYVIGscIKHIPIAGRDITYFIQQLLrereegippEDSLEVAKRIKERYC 226
|
|
| ASKHA_NBD_actin-like |
cd10169 |
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ... |
202-270 |
6.35e-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: 38.24 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446313177 202 ACVIDIGEDVTQ-VAFYErGELVD--ADSIEMAGRDITDDIAQGLNTS---------YETAEKVKHQYG---HAFYDS-- 264
Cdd:cd10169 97 GLVVDSGEGVTHiVPVYE-GYVLPhaVRRLDIGGRDLTDYLAKLLREKgysfstsaeREIVRDIKEKLCglhELIYDSim 175
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....*.
gi 446313177 265 ASDQDI 270
Cdd:cd10169 176 KCDIDL 181
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