|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
384-861 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 835.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 384 TLPPTSLLIDGDP--PKKRSSANDAMIEAITEVLDQFKIDAAVTGFTRGPTVTRYEVELGPGVKVEKITALARNIAYAVA 461
Cdd:COG1674 136 VLPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 462 TDNVRLLAPIPGKSAVGIEVPNSDREMVRLADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMPHLLVAGSTGSGKS 541
Cdd:COG1674 216 AKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 542 SFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHLITPIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHIDDF 621
Cdd:COG1674 296 VCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 622 NSKVKSGEITAPlgSERVYRPYPYILAIVDELADLMMTAPRDVEEAIVRITQKARAAGIHLVLATQRPSVDVVTGLIKTN 701
Cdd:COG1674 376 NEKVREAKAKGE--EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKAN 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 702 VPSRLAFATSSLTDSRVILDQPGAEKLIGMGDGLFLPMGAGKPTRLQGAFITDEEISAVVDFSKNQAEPEYTEGVTAAKv 781
Cdd:COG1674 454 IPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEE- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 782 gEKKDVDPDIGDDMDVLLQAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEGSKAREVLIKPDELDGL 861
Cdd:COG1674 533 -EEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
384-855 |
1.80e-138 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 445.30 E-value: 1.80e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 384 TLPPTSLLIDGDPPKK----RSSANDAMIEAITEVLDQFKIDAAVTGFTRGPTVTRYEVELGPGVKVEKITALARNIAYA 459
Cdd:PRK10263 863 TTPLPSLDLLTPPPSEvepvDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARS 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 460 VATDNVRLLAPIPGKSAVGIEVPNSDREMVRLADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMPHLLVAGSTGSG 539
Cdd:PRK10263 943 LSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSG 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 540 KSSFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHLITPIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHID 619
Cdd:PRK10263 1023 KSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLA 1102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 620 DFNSKV-KSGEITAPL------------GSERVYRPYPYILAIVDELADLMMTAPRDVEEAIVRITQKARAAGIHLVLAT 686
Cdd:PRK10263 1103 GYNEKIaEADRMMRPIpdpywkpgdsmdAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLAT 1182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 687 QRPSVDVVTGLIKTNVPSRLAFATSSLTDSRVILDQPGAEKLIGMGDGLFLPMGAGKPTRLQGAFITDEEISAVVDFSKN 766
Cdd:PRK10263 1183 QRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKA 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 767 QAEPEYTEGVTAAKVGEKKDVDPDIGDDMDVLL-QAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEG 845
Cdd:PRK10263 1263 RGRPQYVDGITSDSESEGGAGGFDGAEELDPLFdQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGH 1342
|
490
....*....|
gi 1390033769 846 SKAREVLIKP 855
Cdd:PRK10263 1343 NGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
491-690 |
7.47e-70 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 230.34 E-value: 7.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 491 LADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMP-HLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPKM 569
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 570 VELTPYEGIPHLIT-PIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHIDDFNSKVK-------------SGEITAPLG 635
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflvIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390033769 636 SERVYRPYPYILAIVDELADLMMTAPRD----VEEAIVRITQKARAAGIHLVLATQRPS 690
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
792-854 |
9.72e-26 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 100.57 E-value: 9.72e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390033769 792 GDDMDVLLQAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEGSKAREVLIK 854
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
509-787 |
4.06e-24 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 109.31 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 509 IGL-GKDiegHFVSANL---AKMPHLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPK---MVEltPYEGIPHL 581
Cdd:TIGR03928 450 IGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNLPHL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 582 ITPI--ITQPKKAAAalawLVE---EMEQRYQDMQANRVRHIDDFNSKVKSGEITAPLgservyrpyPYILAIVDELADL 656
Cdd:TIGR03928 525 LGTItnLDGAQSMRA----LASikaELKKRQRLFGENNVNHINQYQKLYKQGKAKEPM---------PHLFLISDEFAEL 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 657 MMTAPRDVEEAI--VRItqkARAAGIHLVLATQRPSvDVVTGLIKTNVPSRLAFATSSLTDSRVILDQPGAEKLIGMGDG 734
Cdd:TIGR03928 592 KSEQPEFMKELVstARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRA 667
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390033769 735 -----------LFLPMGAGKPTRLQGAFITDEEISAVVDFSKNQAEPEYTEGvtaakVGEKKDV 787
Cdd:TIGR03928 668 ylqvgnnevyeLFQSAWSGAPYDPDKDKKEEEDIYMINDLGQYELLNEDLSG-----LKRKKEI 726
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
529-710 |
4.34e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 52.99 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 529 HLLVAGSTGSGKSSFVNSMLVSLLSRATpdevRMILIDPKM---VELTPYEGIPHLITPIITQpkkaaaalaWLVEEMEQ 605
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFN---------QLFRALTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 606 RYQDMQANRVRHiddfnskvksgeitaplgservyrpypyILAIVDELADLMMtaprdvEEAIVRITQKARAAGIHLVLA 685
Cdd:cd01127 68 LASLSPGRLPRR----------------------------VWFILDEFANLGR------IPNLPNLLATGRKRGISVVLI 113
|
170 180 190
....*....|....*....|....*....|.
gi 1390033769 686 TQ------RPSVDVVTGLIKTNVPSRLAFAT 710
Cdd:cd01127 114 LQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
384-861 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 835.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 384 TLPPTSLLIDGDP--PKKRSSANDAMIEAITEVLDQFKIDAAVTGFTRGPTVTRYEVELGPGVKVEKITALARNIAYAVA 461
Cdd:COG1674 136 VLPPLDLLDPPPPkkEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 462 TDNVRLLAPIPGKSAVGIEVPNSDREMVRLADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMPHLLVAGSTGSGKS 541
Cdd:COG1674 216 AKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 542 SFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHLITPIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHIDDF 621
Cdd:COG1674 296 VCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 622 NSKVKSGEITAPlgSERVYRPYPYILAIVDELADLMMTAPRDVEEAIVRITQKARAAGIHLVLATQRPSVDVVTGLIKTN 701
Cdd:COG1674 376 NEKVREAKAKGE--EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKAN 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 702 VPSRLAFATSSLTDSRVILDQPGAEKLIGMGDGLFLPMGAGKPTRLQGAFITDEEISAVVDFSKNQAEPEYTEGVTAAKv 781
Cdd:COG1674 454 IPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEE- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 782 gEKKDVDPDIGDDMDVLLQAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEGSKAREVLIKPDELDGL 861
Cdd:COG1674 533 -EEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
384-855 |
1.80e-138 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 445.30 E-value: 1.80e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 384 TLPPTSLLIDGDPPKK----RSSANDAMIEAITEVLDQFKIDAAVTGFTRGPTVTRYEVELGPGVKVEKITALARNIAYA 459
Cdd:PRK10263 863 TTPLPSLDLLTPPPSEvepvDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARS 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 460 VATDNVRLLAPIPGKSAVGIEVPNSDREMVRLADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMPHLLVAGSTGSG 539
Cdd:PRK10263 943 LSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSG 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 540 KSSFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHLITPIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHID 619
Cdd:PRK10263 1023 KSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLA 1102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 620 DFNSKV-KSGEITAPL------------GSERVYRPYPYILAIVDELADLMMTAPRDVEEAIVRITQKARAAGIHLVLAT 686
Cdd:PRK10263 1103 GYNEKIaEADRMMRPIpdpywkpgdsmdAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLAT 1182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 687 QRPSVDVVTGLIKTNVPSRLAFATSSLTDSRVILDQPGAEKLIGMGDGLFLPMGAGKPTRLQGAFITDEEISAVVDFSKN 766
Cdd:PRK10263 1183 QRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKA 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 767 QAEPEYTEGVTAAKVGEKKDVDPDIGDDMDVLL-QAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEG 845
Cdd:PRK10263 1263 RGRPQYVDGITSDSESEGGAGGFDGAEELDPLFdQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGH 1342
|
490
....*....|
gi 1390033769 846 SKAREVLIKP 855
Cdd:PRK10263 1343 NGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
491-690 |
7.47e-70 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 230.34 E-value: 7.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 491 LADVLTAPSTRKDHHPLVIGLGKDIEGHFVSANLAKMP-HLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPKM 569
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 570 VELTPYEGIPHLIT-PIITQPKKAAAALAWLVEEMEQRYQDMQANRVRHIDDFNSKVK-------------SGEITAPLG 635
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflvIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390033769 636 SERVYRPYPYILAIVDELADLMMTAPRD----VEEAIVRITQKARAAGIHLVLATQRPS 690
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
385-483 |
2.73e-35 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 129.19 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 385 LPPTSLLIDGDP--PKKRSSANDAMIEAITEVLDQFKIDAAVTGFTRGPTVTRYEVELGPGVKVEKITALARNIAYAVAT 462
Cdd:pfam17854 1 LPPLDLLEPPPTssQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1390033769 463 DNVRLLAPIPGKSAVGIEVPN 483
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
793-854 |
1.13e-26 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 103.22 E-value: 1.13e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390033769 793 DDMDVLL-QAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEGSKAREVLIK 854
Cdd:pfam09397 1 EEEDELYeEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
792-854 |
9.72e-26 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 100.57 E-value: 9.72e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390033769 792 GDDMDVLLQAVELVVSSQFGSTSMLQRKLRVGFAKAGRLMDLMETRGVVGPSEGSKAREVLIK 854
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
509-787 |
4.06e-24 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 109.31 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 509 IGL-GKDiegHFVSANL---AKMPHLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPK---MVEltPYEGIPHL 581
Cdd:TIGR03928 450 IGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNLPHL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 582 ITPI--ITQPKKAAAalawLVE---EMEQRYQDMQANRVRHIDDFNSKVKSGEITAPLgservyrpyPYILAIVDELADL 656
Cdd:TIGR03928 525 LGTItnLDGAQSMRA----LASikaELKKRQRLFGENNVNHINQYQKLYKQGKAKEPM---------PHLFLISDEFAEL 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 657 MMTAPRDVEEAI--VRItqkARAAGIHLVLATQRPSvDVVTGLIKTNVPSRLAFATSSLTDSRVILDQPGAEKLIGMGDG 734
Cdd:TIGR03928 592 KSEQPEFMKELVstARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRA 667
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390033769 735 -----------LFLPMGAGKPTRLQGAFITDEEISAVVDFSKNQAEPEYTEGvtaakVGEKKDV 787
Cdd:TIGR03928 668 ylqvgnnevyeLFQSAWSGAPYDPDKDKKEEEDIYMINDLGQYELLNEDLSG-----LKRKKEI 726
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
528-752 |
2.91e-18 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 89.65 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 528 PHLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPKMvELT--PYEGIPHlITPIITQPKKAAAalawLVE---- 601
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKG-GATflGLEGLPH-VSAVITNLADEAP----LVDrmqd 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 602 ----EMEQRYQDM-QANRVRHIDDFNSKVKSGEITAPLgservyrpyPYILAIVDELADLMMTAPrDVEEAIVRITQKAR 676
Cdd:TIGR03924 510 alagEMNRRQELLrAAGNFANVAEYEKARAAGADLPPL---------PALFVVVDEFSELLSQHP-DFADLFVAIGRLGR 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390033769 677 AAGIHLVLATQRPSVDVVTGLiKTNVPSRLAFATSSLTDSRVILDQPGAEKL---IGMGdglFLPMGAGKPTRLQGAFI 752
Cdd:TIGR03924 580 SLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLpstPGAG---YLKVDTAEPVRFRAAYV 654
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
523-723 |
1.61e-13 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 75.02 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 523 NLAKMPHLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHlITPIIT--QPKKAAAALAWLV 600
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLIRRIK 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 601 EEMEQRYQDMQANRVRHIDDFNSkvKSGEitaplgservyrPYPYILAIVDELaDLMMTAPR--DVEEAIVRITQKARAA 678
Cdd:TIGR03928 885 KEIDRRKKLFSEYGVASISMYNK--ASGE------------KLPQIVIIIDNY-DAVKEEPFyeDFEELLIQLAREGASL 949
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390033769 679 GIHLVL-ATQRPSVDVVtglIKTNVPSRLAFATSSLTDSRVILDQP 723
Cdd:TIGR03928 950 GIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIVGRT 992
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
529-710 |
4.34e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 52.99 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 529 HLLVAGSTGSGKSSFVNSMLVSLLSRATpdevRMILIDPKM---VELTPYEGIPHLITPIITQpkkaaaalaWLVEEMEQ 605
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFN---------QLFRALTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 606 RYQDMQANRVRHiddfnskvksgeitaplgservyrpypyILAIVDELADLMMtaprdvEEAIVRITQKARAAGIHLVLA 685
Cdd:cd01127 68 LASLSPGRLPRR----------------------------VWFILDEFANLGR------IPNLPNLLATGRKRGISVVLI 113
|
170 180 190
....*....|....*....|....*....|.
gi 1390033769 686 TQ------RPSVDVVTGLIKTNVPSRLAFAT 710
Cdd:cd01127 114 LQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
487-747 |
8.95e-08 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 56.15 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 487 EMVRLADVLTAPSTRKDHHPLVIGLGKDIEG-HFVSANLAKMPHLLVAGSTGSGKSSFVNSMLVSLlsrATPDEVRMILI 565
Cdd:TIGR03928 1055 EELSLEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTL---AKQEKEKIGLI 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 566 DPKMVELTPYEGIPHlitpIITQPKKAAAALAW---LVEEMEQRYQDMQANRvrhiddfnsKVKSGEItaplgservyrP 642
Cdd:TIGR03928 1132 DSIDRGLLAYRDLKE----VATYIEEKEDLKEIlaeLKEEIELREAAYKEAL---------QNETGEP-----------A 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 643 YPYILAIVDELADLMMTAPRDVEEAIVRITQKARAAGIHLVLATQRPSV----DVVTGLIKTnvpSRLAFATSSLTDSRV 718
Cdd:TIGR03928 1188 FKPILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSF 1264
|
250 260 270
....*....|....*....|....*....|
gi 1390033769 719 I-LDQPGAEKLIGMGDGLFLPMGAGKPTRL 747
Cdd:TIGR03928 1265 FkLPFTRSEKELEPGEGYFVVNGKYQKIKI 1294
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
489-568 |
1.41e-06 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 51.53 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 489 VRLADVLTAPSTRKDHHPLVIGLGKDiEGHFVSANLAKM--PHLLVAGSTGSGKSSFVNSMLVSLLSRatpdEVRMILID 566
Cdd:COG0433 8 VYLADDEELEELLGDGGGILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFD 82
|
..
gi 1390033769 567 PK 568
Cdd:COG0433 83 PH 84
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
520-568 |
1.15e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 48.84 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1390033769 520 VSANLAKMPHLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPK 568
Cdd:TIGR03925 356 VYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
529-724 |
4.05e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 47.29 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 529 HLLVAGSTGSGKSSFVNSMLVSLLSRATPDEVRMILIDPKMVELTPYEGIPHlITPIITQ--PKKAAAALAWLVEEMEQR 606
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGRldPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390033769 607 YQDMQANRVRHIDDFNSKVKSGEITAplgservyRPYPYILAIVDELADLmMTAPRDVEEAIVRITQKARAAGIHLVLAT 686
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRLPE--------DPFGDVFLVIDGWGTL-RQDFEDLEDKVTDLAARGLAYGVHVVLTA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390033769 687 QRPSvDV---VTGLIKTNVPSRLAFATSSLTDSR----VILDQPG 724
Cdd:TIGR03925 231 SRWS-EIrpaLRDLIGTRIELRLGDPMDSEIDRRaaarVPAGRPG 274
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
528-567 |
4.80e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 40.32 E-value: 4.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1390033769 528 PHLLVAGSTGSGKSSFVNSMLVSLLSRatpdEVRMILIDP 567
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| |
