|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
8-407 |
6.92e-135 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 392.57 E-value: 6.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:COG0849 6 IVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGGHIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDApEWVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:COG0849 86 SQNSRGVVAI--SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQ-EGIKDPVGMSGVRLEVDVHIVTGPKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:COG0849 163 AVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIAIG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLYHGVV 325
Cdd:COG0849 243 LRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGrpPREISRKELAEIIEARVEEIFELVRKELKRSGYEEKLPAGVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 326 LTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAEDqnqaALRRSQYATAAGLLMFSQSDTQDTIVEQDDSEPLSMAQRV 405
Cdd:COG0849 323 LTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPE----AVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRI 398
|
..
gi 1577373408 406 KR 407
Cdd:COG0849 399 KR 400
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-381 |
4.10e-118 |
|
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: 348.75 E-value: 4.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:cd24048 3 IVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKHIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVENTDHtITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:cd24048 83 SVNSRGVIAISDKDE-ITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDG-IKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLYHGVV 325
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGrePREVSRRELAEIIEARVEEILELVKKELKESGYEDLLPGGIV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1577373408 326 LTGDAGQIEGMVSFARKILGVSAHLGNPpvqvHAEDQNQAALRRSQYATAAGLLMF 381
Cdd:cd24048 321 LTGGGSQLPGLVELAEEVFGMPVRIGRP----KNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
8-381 |
5.66e-91 |
|
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: 279.52 E-value: 5.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:TIGR01174 2 IVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:TIGR01174 82 SQNSIGVVAI--KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEG-IKNPLGMSGVRLEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRD-VLERNGAIHGLYHGV 324
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGErpPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFKEELNGGI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577373408 325 VLTGDAGQIEGMVSFARKILGVSAHLGNPpvqvhaedQNQAAL----RRSQYATAAGLLMF 381
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLP--------QNIGGLtedvNDPEYSTAVGLLLY 371
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
8-407 |
7.72e-65 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 213.49 E-value: 7.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:PRK09472 10 VVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDdAPEWVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:PRK09472 90 CQNEIGMVPI--SEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAID-YQEGIKNPVGLSGVRMQAKVHLITCHND 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:PRK09472 167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLV-------RDVLERNGAIH 318
Cdd:PRK09472 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGrpPRSLQRQTLAEVIEPRYTELLNLVneeilqlQEQLRQQGVKH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 319 GLYHGVVLTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAEDQNQaalrRSQYATAAGLLMFSQSDTQDTIVEQDDSEP 398
Cdd:PRK09472 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQ----EPYYSTAVGLLHYGKESHLNGEAEVEKRVT 402
|
....*....
gi 1577373408 399 LSMAQRVKR 407
Cdd:PRK09472 403 ASVGSWIKR 411
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
8-196 |
6.45e-54 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 177.67 E-value: 6.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVEntDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:smart00842 81 SVNVSGVVAIP--DKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEG-IKDPIGMSGVRLEVDVHVVTAPKS 157
|
170 180
....*....|....*....|....*....
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEA 196
Cdd:smart00842 158 AIQNLEKCVERAGLEVDGIVLEPLASAEA 186
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
208-377 |
1.69e-42 |
|
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: 147.09 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 208 CLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTEEAERIKLLYGCVDLKVVKPDhMIQFQGIDGPQTI 287
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED-EVPGVGGREPREI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 288 SRIELTEIIIARYDEILGLVRDVLERNGAIHGLY-------HGVVLTGDAGQIEGMVSFARKILGVSAHLGNPpvqvhae 360
Cdd:pfam14450 80 SRKELAEIIEARVEEILELVRAELEDREVLPGEYvrlevdvHGIVLTGGGSALPGLVELAERALGLPVRIGSP------- 152
|
170
....*....|....*..
gi 1577373408 361 dqNQAALRRSQYATAAG 377
Cdd:pfam14450 153 --DGIGGRNPAYATALG 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
8-407 |
6.92e-135 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 392.57 E-value: 6.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:COG0849 6 IVGLDIGTSKVVALVGEVDPDGKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGISGGHIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDApEWVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:COG0849 86 SQNSRGVVAI--SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQ-EGIKDPVGMSGVRLEVDVHIVTGPKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:COG0849 163 AVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITNDIAIG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLYHGVV 325
Cdd:COG0849 243 LRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGrpPREISRKELAEIIEARVEEIFELVRKELKRSGYEEKLPAGVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 326 LTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAEDqnqaALRRSQYATAAGLLMFSQSDTQDTIVEQDDSEPLSMAQRV 405
Cdd:COG0849 323 LTGGGSQLPGLVELAEEILGLPVRIGRPDGIGGLPE----AVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRI 398
|
..
gi 1577373408 406 KR 407
Cdd:COG0849 399 KR 400
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
8-381 |
4.10e-118 |
|
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: 348.75 E-value: 4.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:cd24048 3 IVGLDIGTSKICALVGEVSEDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKHIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVENTDHtITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:cd24048 83 SVNSRGVIAISDKDE-ITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDG-IKDPVGMSGSRLEVDVHVITGSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:cd24048 161 AIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLYHGVV 325
Cdd:cd24048 241 LNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGrePREVSRRELAEIIEARVEEILELVKKELKESGYEDLLPGGIV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1577373408 326 LTGDAGQIEGMVSFARKILGVSAHLGNPpvqvHAEDQNQAALRRSQYATAAGLLMF 381
Cdd:cd24048 321 LTGGGSQLPGLVELAEEVFGMPVRIGRP----KNIGGLPEEVNDPAYATAVGLLLY 372
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
8-381 |
5.66e-91 |
|
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: 279.52 E-value: 5.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:TIGR01174 2 IVGLDIGTSKICAIVAEVLEDGELNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:TIGR01174 82 SQNSIGVVAI--KDKEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEG-IKNPLGMSGVRLEVEVHIITGSST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLVRD-VLERNGAIHGLYHGV 324
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGErpPRSLSRKELAEIIEARAEEILEIVKQkELRKSGFKEELNGGI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577373408 325 VLTGDAGQIEGMVSFARKILGVSAHLGNPpvqvhaedQNQAAL----RRSQYATAAGLLMF 381
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLP--------QNIGGLtedvNDPEYSTAVGLLLY 371
|
|
| ftsA |
PRK09472 |
cell division protein FtsA; Reviewed |
8-407 |
7.72e-65 |
|
cell division protein FtsA; Reviewed
Pssm-ID: 181887 [Multi-domain] Cd Length: 420 Bit Score: 213.49 E-value: 7.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:PRK09472 10 VVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHIS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDdAPEWVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:PRK09472 90 CQNEIGMVPI--SEEEVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAID-YQEGIKNPVGLSGVRMQAKVHLITCHND 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAV 247
Cdd:PRK09472 167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 248 LQTTTEEAERIKLLYGCVDLKVVKPDHMIQFQGIDG--PQTISRIELTEIIIARYDEILGLV-------RDVLERNGAIH 318
Cdd:PRK09472 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGrpPRSLQRQTLAEVIEPRYTELLNLVneeilqlQEQLRQQGVKH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 319 GLYHGVVLTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAEDQNQaalrRSQYATAAGLLMFSQSDTQDTIVEQDDSEP 398
Cdd:PRK09472 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPLNITGLTDYAQ----EPYYSTAVGLLHYGKESHLNGEAEVEKRVT 402
|
....*....
gi 1577373408 399 LSMAQRVKR 407
Cdd:PRK09472 403 ASVGSWIKR 411
|
|
| FtsA |
smart00842 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
8-196 |
6.45e-54 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 177.67 E-value: 6.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 8 VVAIDIGTHKVSVLIGKVHAPDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPSAELK 87
Cdd:smart00842 1 IVGLDIGTSKIKALVAEVDEDGEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 88 SFYASGRTPVEntDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDAPEwVLNPIRMSAHSMTGHYHLMMLPIS 167
Cdd:smart00842 81 SVNVSGVVAIP--DKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEG-IKDPIGMSGVRLEVDVHVVTAPKS 157
|
170 180
....*....|....*....|....*....
gi 1577373408 168 TMQNLDRALKGANIGVERMVISSLATAEA 196
Cdd:smart00842 158 AIQNLEKCVERAGLEVDGIVLEPLASAEA 186
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
208-377 |
1.69e-42 |
|
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: 147.09 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 208 CLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTEEAERIKLLYGCVDLKVVKPDhMIQFQGIDGPQTI 287
Cdd:pfam14450 1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED-EVPGVGGREPREI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 288 SRIELTEIIIARYDEILGLVRDVLERNGAIHGLY-------HGVVLTGDAGQIEGMVSFARKILGVSAHLGNPpvqvhae 360
Cdd:pfam14450 80 SRKELAEIIEARVEEILELVRAELEDREVLPGEYvrlevdvHGIVLTGGGSALPGLVELAERALGLPVRIGSP------- 152
|
170
....*....|....*..
gi 1577373408 361 dqNQAALRRSQYATAAG 377
Cdd:pfam14450 153 --DGIGGRNPAYATALG 167
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
9-380 |
8.01e-21 |
|
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: 92.73 E-value: 8.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 9 VAIDIGTHKVSVLIGKVHApDNIQVIGMATARN--RGMNKGKIVSLDKVITAIKNAVQEAEdmaeCRVHSAWISIPSAEL 86
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSG-GGLVLVAFAIIPLpeGAIVDGEIADPEALAEALKKLLKENK----IKGKKVVVALPGSDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 87 KSFYAsgRTPVENTDhtittnEVVRALELAKASHLtsdhylvsavplGFELDDApEW---VLNPIRMSAhsmtGHYHLMM 163
Cdd:cd24049 76 IVRTI--KLPKMPEK------ELEEAIRFEAEQYL------------PFPLEEV-VLdyqILGEVEEGG----EKLEVLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 164 L--PISTMQNLDRALKGANIGVERMVISSLATAEA--SLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEH 239
Cdd:cd24049 131 VaaPKEIVESYLELLKEAGLKPVAIDVESFALARAleYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGND 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 240 VTRDIAAVLQTTTEEAERIKLLYGcvdlkvvkpdhmiqFQGIDGPQTISRIEltEIIIARYDEILGLVRDVLE------R 313
Cdd:cd24049 211 ITEAIAKALGLSFEEAEELKREYG--------------LLLEGEEGELKKVA--EALRPVLERLVSEIRRSLDyyrsqnG 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577373408 314 NGAIHGLYhgvvLTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAEDQNQAALRR--SQYATAAGLLM 380
Cdd:cd24049 275 GEPIDKIY----LTGGGSLLPGLDEYLSERLGIPVEILNPFSNIESKKSDDEELKEdaPLFAVAIGLAL 339
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
9-379 |
1.09e-19 |
|
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: 88.50 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 9 VAIDIGTHKVSVLIGKVHApDNIQVIGMA--TARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRVHSAWISIPsael 86
Cdd:cd24004 1 FALDIGTRSIKGLVLEEDD-ENIEVLAFSseEHPERAMGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIAIA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 87 ksfyasgrtpventdhtittnEVVRALElakashltsdhylvsavplgfelddapewvlnpirmsahsmtghyhlmmlpi 166
Cdd:cd24004 76 ---------------------KVVESLL---------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 167 stmqnldRALKGANIGVERMVISSLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAA 246
Cdd:cd24004 83 -------NVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 247 VLQTTTEEAERIKLLYGCVDLKVVKPDHMiqfqgidgpQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLYHGVVL 326
Cdd:cd24004 156 GFLISFEEAEKIKRTYGIFLLIEAKDQLG---------FTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYL 226
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1577373408 327 TGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAED--QNQAALRRSQYATAAGLL 379
Cdd:cd24004 227 VGGGSKLPGLNEALAEKLGLPVERIAPRNIGAISDitDETSKAKGPEFVTPLGIA 281
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
206-350 |
2.01e-08 |
|
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: 55.56 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 206 GVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTT------TEEAERIKLLYGCVdLKVVKPDHMiQFQ 279
Cdd:cd10225 144 GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIINYVRRKynlligERTAERIKIEIGSA-YPLDEELSM-EVR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 280 GID----GPQT--ISRIELTEIIIARYDEILGLVRDVLERN-----GAIHglYHGVVLTGDAGQIEGMVSFARKILGVSA 348
Cdd:cd10225 222 GRDlvtgLPRTieITSEEVREALEEPVNAIVEAVRSTLERTppelaADIV--DRGIVLTGGGALLRGLDELLREETGLPV 299
|
..
gi 1577373408 349 HL 350
Cdd:cd10225 300 HV 301
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
6-380 |
2.53e-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: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 6 PSVVAIDIGTHKVSVLIGKvHAPDNIQVIGMATARN-RGM-NKGKIVSLDKVITAIKNAVQEAEdmaeCRVHSAWISIPS 83
Cdd:COG4972 2 KPLVGIDIGSSSIKLVELS-KSGGGYRLERYAEEPLpEGAvVDGNIVDPEAVAEALKELLKRLK----IKTKRVAIAVPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 84 AElksfyasgrtpventdhTITTNEVVRAL---ELAKASHLTSDHYLvsavplGFELDDApEW---VLNPIRMSAHSMtg 157
Cdd:COG4972 77 SS-----------------VITRKITLPALsekELEEAIEFEAEQYI------PFPLEEV-VLdfqVLGPSEEGPEKV-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 158 HYHLMMLPISTMQNLDRALKGANIGVERMVISSLATAEASLLKDEREYG--VCLLDIGAGTTNVAVYLDGRLAMTHTLQR 235
Cdd:COG4972 131 EVLLVAARKEVVEDYVELLEAAGLKPVVVDVEPFALLRALELLPPSGPDetVALVDIGASSTTLSVLSNGKPIFTREIPF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 236 GgehVTRDIAAVLQTtteeaerikllygcvdlkvvkpdhmiqFQGIDGPQTISRIelteiiiarydeilglvrdvlerng 315
Cdd:COG4972 211 G---LAQEIRRSLQF---------------------------YRSQSGGNEVDRI------------------------- 235
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577373408 316 aihglyhgvVLTGDAGQIEGMVSFARKILGVSAHLGNPPVQVH-AEDQNQAALRRSQYATAAGLLM 380
Cdd:COG4972 236 ---------LLAGGGAKLPGLAEYLEERLGIPVEVLNPFAGMAlSVDEEALAEDAPSFAVALGLAL 292
|
|
| PilM_2 |
pfam11104 |
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
175-383 |
1.53e-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: 49.60 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 175 ALKGANIGVERMVISSLATAEAS------LLKDEREYGVCLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVL 248
Cdd:pfam11104 144 LLEAAGLKPKVVDVESYALERAFerivsqLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQEIVRRY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 249 QTTTEEAERIKllygcvdlkvvkpdhmiqfqgIDG--PqtisrIELTEIIIARYDEILglvrdVLERNGAIH-----GLY 321
Cdd:pfam11104 224 GMSYEEAEIAK---------------------RNGdlP-----EDYESEVLEPFVEAL-----AQQISRALQffftsTPY 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1577373408 322 HGV---VLTGDAGQIEGMVSFARKILGVSAHLGNPPVQV-HAEDQNQAALRR--SQYATAAGLLMFSQ 383
Cdd:pfam11104 273 NKVdyiVLAGGCANIPGLAELVTERLGFSTTVANPFRGMeLSPRVRQKQLLRdaPSYMVACGLALRSF 340
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
2-350 |
1.77e-06 |
|
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: 49.69 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 2 NEavPSVVAIDIGTHKV-SV------LIGKvhAPDNIQVIgmatarnRGMNKGKIVSLDkvITA--IKNAVQEAEDMAEC 72
Cdd:COG1077 31 NE--PSVVAIDKKTGKVlAVgeeakeMLGR--TPGNIVAI-------RPLKDGVIADFE--VTEamLKYFIKKVHGRRSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 73 RVHSAWISIPSaelksfyasGRTPVEntdhtitTNEVVRALELAKASHLtsdhYLVsavplgfeldDAPewvlnpirMSA 152
Cdd:COG1077 98 FRPRVVICVPS---------GITEVE-------RRAVRDAAEQAGAREV----YLI----------EEP--------MAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 153 hsmtghyhlmmlpistmqnldrALkGANIGVER----MVIsslataeasllkdereygvcllDIGAGTTNVAVYLDGRLA 228
Cdd:COG1077 140 ----------------------AI-GAGLPIEEptgnMVV----------------------DIGGGTTEVAVISLGGIV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 229 MTHTLQRGGEHVTRDIAAVLQTT------TEEAERIKLLYGCVdLKVVKPDHMiQFQGID---G-PQT--ISRIELTEII 296
Cdd:COG1077 175 VSRSIRVAGDELDEAIIQYVRKKynlligERTAEEIKIEIGSA-YPLEEELTM-EVRGRDlvtGlPKTitITSEEIREAL 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1577373408 297 IARYDEILGLVRDVLERN-----GAIhgLYHGVVLTGDAGQIEGMVSFARKILGVSAHL 350
Cdd:COG1077 253 EEPLNAIVEAIKSVLEKTppelaADI--VDRGIVLTGGGALLRGLDKLLSEETGLPVHV 309
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
193-353 |
1.90e-06 |
|
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: 48.80 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 193 TAEASLLKDEReyGVcLLDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTEEAERIkllygcvdlkvvKP 272
Cdd:cd24047 102 TAANAVLGIRD--GA-VVDIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLAGNYGISFEEAEII------------KR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 273 DHmiqfqgidgpqtisrielteiiiARYDEILGLVRDVLERNGAI---HGLYHGV---VLTGDAGQIEGMVSFARKILGV 346
Cdd:cd24047 167 DP-----------------------ARHKELLPVVRPVIEKMASIvkrHIKGYKVkdlYLVGGTCCLPGIEEVFEKETGL 223
|
....*...
gi 1577373408 347 SAHL-GNP 353
Cdd:cd24047 224 PVYKpSNP 231
|
|
| pilM |
TIGR01175 |
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
7-378 |
3.72e-05 |
|
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.
Pssm-ID: 273484 [Multi-domain] Cd Length: 348 Bit Score: 45.55 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 7 SVVAIDIGTHKVSVLIGKVH-APDNIQVIGMATARNRGMNKGKIVSLDKVITAIKNAVQEAEDMAecrvHSAWISIPSAE 85
Cdd:TIGR01175 4 LLVGIDIGSTSVKVAQLKRSgDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGINT----KKAATAVPGSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 86 LksfyasgrtpventdhtITTN-EVVRAL---ELAKASHLTSDHYL---VSAVPLGFELDDAPEwvLNPIRMSAhsmtgh 158
Cdd:TIGR01175 80 V-----------------ITKViPVPAGLderELEFAVYIEASHYIpypIEEVSLDFEKLGLKA--NNPESTVQ------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 159 yhlMMLPISTMQNLDR---ALKGANIGVERMVISSLATAEASLLKDE-------REYGVCLLDIGAGTTNVAVYLDGRLA 228
Cdd:TIGR01175 135 ---VLLAATRKEVVDSrlhALKLAGLEPKVVDVESFALLRAWRLLGEqlasrtyRLTDAALVDIGATSSTLNLLHPGRML 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 229 MTHTLQRGGEHVTRDIAAVLQTTTEEAERIKLLYGCVDLKVVkpdhmiqfqgidgpqtisrieltEIIIARYDEILGLVR 308
Cdd:TIGR01175 212 FTREVPFGTRQLTSELSRAYGLNPEEAGEAKQQGGLPLLYDP-----------------------EVLRRFKGELVDEIR 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1577373408 309 DVLERNGAIHGLYH--GVVLTGDAGQIEGMVSFARKILGVSAHLGNPPVQVHAE---DQNQAALRRSQYATAAGL 378
Cdd:TIGR01175 269 RSLQFFTAQSGTNSldGLVLAGGGATLSGLDAAIYQRLGLPTEVANPFALMALDakvDAGRLAVDAPALMTALGL 343
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
151-354 |
1.47e-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: 43.55 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 151 SAHSMTGHYHLMMLPISTMQNLDRALKGANIGV---ERMVIS-SLATAEASLLKDEREYGVCLLDIGAGTTNVAVYLDGR 226
Cdd:TIGR00904 92 SRKSFFKPRIVICVPSGITPVERRAVKESALSAgarEVYLIEePMAAAIGAGLPVEEPTGSMVVDIGGGTTEVAVISLGG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 227 LAMTHTLQRGG--------EHVTRDIAAVLQTTTeeAERIKLLYGCVDLKVVKPDHM-----IQFQGIDGPQTISRIELT 293
Cdd:TIGR00904 172 IVVSRSIRVGGdefdeaiiNYIRRTYNLLIGEQT--AERIKIEIGSAYPLNDEPRKMevrgrDLVTGLPRTIEITSVEVR 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577373408 294 EIIIARYDEILGLVRDVLERNGAIHG---LYHGVVLTGDAGQIEGMVSFARKILGVSAHLGNPP 354
Cdd:TIGR00904 250 EALQEPVNQIVEAVKRTLEKTPPELAadiVERGIVLTGGGALLRNLDKLLSKETGLPVIVADDP 313
|
|
| ASKHA_NBD_AtARP7-like |
cd10209 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ... |
184-348 |
2.50e-04 |
|
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar proteins; Arabidopsis thaliana ARP7 is an essential nuclear protein, ubiquitously expressed in all cell types. It is needed for normal embryogenesis, plant architecture, and floral organ abscission. It may play a role in regulating various phases of plant development through chromatin-mediated gene regulation.
Pssm-ID: 466815 [Multi-domain] Cd Length: 354 Bit Score: 42.76 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 184 ERMVISSLATAEASLLKderEYGV-----CLLDIGAGTTNVAVYLDGrlAMTHTLQR----GGEHVTRDIAAVLQTTTE- 253
Cdd:cd10209 106 ETFNVSGLYASEQAVLS---LYAVgrisgCVVDVGHGKIDIAPVWEG--AIQHNAVRrfeiGGRDLTELLAAELGKSNPk 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 254 ------EAERIKLLYGCV------DLKVVKPDHMIQFQGIDGpQTIS----RIELTEII-------IARYDEILGLVRDV 310
Cdd:cd10209 181 vkldrsIVERLKEAVAWSaddeeaYEKKVLTCSPETYTLPDG-RVISvgkeRYCVGEALfrpsilgIEEYGIVEQLVRAV 259
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1577373408 311 LERNGAIH-GLYHGVVLTGDAGQIEGMVS-FARKILGVSA 348
Cdd:cd10209 260 STSPSENRrQLLENIVLCGGTSSVPGLEArLQKEIRLLSS 299
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
138-254 |
3.18e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins 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: 466825 [Multi-domain] Cd Length: 263 Bit Score: 42.12 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 138 DDAPEWVLNPIRMSAHSMTGHYHLMM-LPISTMQNLDRALKGANI---------GVERMV-----------ISSLATAEA 196
Cdd:cd10227 76 EDALLLLLAALALLGDDEEVDVNLVVgLPISEYKEEKKELKKKLLkglheftfnGKERRItindvkvlpegAGAYLDYLL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 197 SLLKDEREYgVCLLDIGAGTTNVAVYLDGRL--AMTHTLQRGGEHVTRDIAAVLQTTTEE 254
Cdd:cd10227 156 DDDELEDGN-VLVIDIGGGTTDILTFENGKPieESSDTLPGGEEALEKYADDILNELLKK 214
|
|
| EutJ |
COG4820 |
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
211-259 |
4.60e-04 |
|
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism];
Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 41.71 E-value: 4.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1577373408 211 DIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTEEAERIK 259
Cdd:COG4820 139 DIGGGTTGISILKDGEVVYTADEPTGGTHMSLVLAGAYGISFEEAEQLK 187
|
|
| SHS2_FTSA |
pfam02491 |
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ... |
88-161 |
5.65e-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: 38.24 E-value: 5.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1577373408 88 SFYASGRTPVenTDHTITTNEVVRALELAKASHLTSDHYLVSAVPLGFELDDApEWVLNPIRMSAHSMTGHYHL 161
Cdd:pfam02491 1 SQNSSGVVAI--SGREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQ-EGIKDPVGMSGVRLEADVHV 71
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
206-380 |
1.09e-03 |
|
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: 40.94 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 206 GVCLLDIGAGTTNVAVY--------LDGRLAMTHTLQRGGEHVTR-------------------DIAAVLQTTTEEAERI 258
Cdd:cd10170 137 VVLVCDAGGGTVDLSLYevtsgsplLLEEVAPGGGALLGGTDIDEafekllreklgdkgkdlgrSDADALAKLLREFEEA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 259 K-LLYGCVDLKVVKPDHMIQFQGIDGPQTISRIELTEIIIARYDEILGLVRDVLERNGAIHGLY--HGVVLTGDAGQIEg 335
Cdd:cd10170 217 KkRFSGGEEDERLVPSLLGGGLPELGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEAKSGTppDAVVLVGGFSRSP- 295
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1577373408 336 mvsFARKILgvSAHLGNPPVQVHAEDQNqaalrrSQYATAAGLLM 380
Cdd:cd10170 296 ---YLRERL--RERFGSAGIIIVLRSDD------PDTAVARGAAL 329
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
210-355 |
1.33e-03 |
|
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: 40.62 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 210 LDIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTE------EAERIKLLYGCVdlKVVKPDHMIQFQGID- 282
Cdd:pfam06723 150 VDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIIKYIRKKYNlligerTAERIKIEIGSA--YPTEEEEKMEIRGRDl 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 283 -----GPQTISRIELTEIIIARYDEILGLVRDVLERN-----GAIhgLYHGVVLTGDAGQIEGMVSFARKILGVSAHLGN 352
Cdd:pfam06723 228 vtglpKTIEISSEEVREALKEPVSAIVEAVKEVLEKTppelaADI--VDRGIVLTGGGALLRGLDKLLSDETGLPVHIAE 305
|
...
gi 1577373408 353 PPV 355
Cdd:pfam06723 306 DPL 308
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
211-357 |
1.70e-03 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 39.81 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 211 DIGAGTTNVAVYLDGRLAMTHTLQRGGEHVTRDIAAVLQTTTEEAERIKLlygcvdlkvvKPDHmiqfqgidgpqtisri 290
Cdd:PRK15080 141 DIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAGAYGISFEEAEQYKR----------DPKH---------------- 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577373408 291 elteiiiarYDEILGLVRDVLERNGAI---HGLYHGV---VLTGDAGQIEGMVSFARKILGVSAHLGNPPVQV 357
Cdd:PRK15080 195 ---------HKEIFPVVKPVVEKMASIvarHIEGQDVediYLVGGTCCLPGFEEVFEKQTGLPVHKPQHPLFV 258
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
2-328 |
6.30e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 38.58 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 2 NEavPSVVAIDIGTHKV-SV------LIGKvhAPDNIQVIgmatarnRGMNKGKIVSLDKVITAIKNAVQEAEDMAECRV 74
Cdd:PRK13930 32 NE--PSVVAIDTKTGKVlAVgeeakeMLGR--TPGNIEAI-------RPLKDGVIADFEATEAMLRYFIKKARGRRFFRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 75 HSAWISIPSaelksfyasGRTPVENtdhtittNEVVRALELAKASHLtsdhYLVsavplgfeldDAPewvlnpirMSAhs 154
Cdd:PRK13930 101 PRIVICVPS---------GITEVER-------RAVREAAEHAGAREV----YLI----------EEP--------MAA-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 155 mtghyhlmmlpistmqnldrALkGANIGVER----MVIsslataeasllkdereygvcllDIGAGTTNVAVYLDGRLAMT 230
Cdd:PRK13930 141 --------------------AI-GAGLPVTEpvgnMVV----------------------DIGGGTTEVAVISLGGIVYS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577373408 231 HTLQRGGEHVTRDIAAVLQTTTE------EAERIKLLYGCVdLKVVKPDHMiQFQGID---G-PQT--ISRIELTEIIIA 298
Cdd:PRK13930 178 ESIRVAGDEMDEAIVQYVRRKYNlligerTAEEIKIEIGSA-YPLDEEESM-EVRGRDlvtGlPKTieISSEEVREALAE 255
|
330 340 350
....*....|....*....|....*....|....*
gi 1577373408 299 RYDEILGLVRDVLERN-----GAIhgLYHGVVLTG 328
Cdd:PRK13930 256 PLQQIVEAVKSVLEKTppelaADI--IDRGIVLTG 288
|
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