|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
257-856 |
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: 780.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 257 APIELGTFSDLGLDLQDESSMPWWRKGKPRAEVPAFDTPVERDAETGVIDRDARDKVTGDLAAVLDQAEQAVERFTGEAP 336
Cdd:COG1674 12 AGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLLLLLLLLGLLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 337 AHPGAVRDDAEPAVLPGFPTGAREKGEAGEFDAPPPIARTAPPYRLPNQAVLAPGTP--PKSRSAANDAVVAAITEVLTQ 414
Cdd:COG1674 92 ALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPkkEKIDEEELEENARLLEETLED 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 415 FQVDARVTGFSRGPSVTRYEVELGPGVKVERFTALTKNIAYAVASNEVSILSPIPGKSAIGVEIPNVDREVVSLGDVLRS 494
Cdd:COG1674 172 FGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 495 SAAAKALHPMTIGVGKDVEGGFVVANLAKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQG 574
Cdd:COG1674 252 DEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 575 VPHLITPIITSPKKAAEALQWVVKEMDMRYDDLASFGFRHIDDFNRAVLADEIELPEGskRQLQPYPYLLVVVDELADLM 654
Cdd:COG1674 332 IPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGEEE--EGLEPLPYIVVIIDELADLM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 655 MVAPRDVEDSIVRITQLARASGIHLVLATQRPSVDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGAEKLIGQGDGLFL 734
Cdd:COG1674 410 MVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 735 PMGASKAVRAQGAWVTEPEIAAVVEHVKKQARPEYRQDVAVEAEKKQIDADIGDDLELLLAAAELIVSTQFGSTSMLQRK 814
Cdd:COG1674 490 PPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRR 569
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2381058128 815 LRVGFAKAGRLMDLLESREIVGPSEGSKARDVLALPDQLPEV 856
Cdd:COG1674 570 LRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
372-850 |
2.56e-117 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 389.44 E-value: 2.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 372 PIARTAPPyrLPNQAVLapgTPPKSRSAANDAV----VAAITEV-LTQFQVDARVTGFSRGPSVTRYEVELGPGVKVERF 446
Cdd:PRK10263 858 PLHKPTTP--LPSLDLL---TPPPSEVEPVDTFaleqMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARI 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 447 TALTKNIAYAVASNEVSILSPIPGKSAIGVEIPNVDREVVSLGDVLRSSAAAKALHPMTIGVGKDVEGGFVVANLAKMPH 526
Cdd:PRK10263 933 SNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPH 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 527 LLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQGVPHLITPIITSPKKAAEALQWVVKEMDMRYDD 606
Cdd:PRK10263 1013 LLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKL 1092
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 607 LASFGFRHIDDFNRAVL-ADEIELP------------EGSKRQLQPYPYLLVVVDELADLMMVAPRDVEDSIVRITQLAR 673
Cdd:PRK10263 1093 MSALGVRNLAGYNEKIAeADRMMRPipdpywkpgdsmDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKAR 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 674 ASGIHLVLATQRPSVDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGAEKLIGQGDGLFLPMGASKAVRAQGAWVTEPE 753
Cdd:PRK10263 1173 AAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQE 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 754 IAAVVEHVKKQARPEYRQDVAVEAEKKQIDA--DIGDDLELLLAAAELIVSTQF-GSTSMLQRKLRVGFAKAGRLMDLLE 830
Cdd:PRK10263 1253 VHAVVQDWKARGRPQYVDGITSDSESEGGAGgfDGAEELDPLFDQAVQFVTEKRkASISGVQRQFRIGYNRAARIIEQME 1332
|
490 500
....*....|....*....|
gi 2381058128 831 SREIVGPSEGSKARDVLALP 850
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
488-687 |
1.21e-59 |
|
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: 202.61 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 488 LGDVLRSSAAAKALHPMTIGVGKDVEGGFVVANLAKMP-HLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKR 566
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 567 VELAAYQGVPHLIT-PIITSPKKAAEALQWVVKEMDMRYDDLASFGFRHIDDFNRAVLADE-------------IELPEG 632
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPldgfgdvflviygVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2381058128 633 SKRQLQPYPYLLVVVDELADLMMVAPRD----VEDSIVRITQLARASGIHLVLATQRPS 687
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
493-731 |
1.55e-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: 110.85 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 493 RSSAAAKALhPMTIGV-GKDvegGFVVANL---AKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVE 568
Cdd:TIGR03928 438 AKNETYKSL-AVPIGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 569 LA-AYQGVPHL---ITPIITSpkKAAEALQWVVKEMDMRYDDLASFGFRHIDDFnravladeIELpegSKRQL--QPYPY 642
Cdd:TIGR03928 514 MAnLFKNLPHLlgtITNLDGA--QSMRALASIKAELKKRQRLFGENNVNHINQY--------QKL---YKQGKakEPMPH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 643 LLVVVDELADLMMVAPrDVEDSIVRITQLARASGIHLVLATQRPSvDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGA 722
Cdd:TIGR03928 581 LFLISDEFAELKSEQP-EFMKELVSTARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
....*....
gi 2381058128 723 EKLIGQGDG 731
Cdd:TIGR03928 659 AEITVPGRA 667
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
800-848 |
8.34e-19 |
|
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: 80.92 E-value: 8.34e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2381058128 800 IVSTQFGSTSMLQRKLRVGFAKAGRLMDLLESREIVGPSEGSKARDVLA 848
Cdd:smart00843 14 VIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLV 62
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
526-707 |
4.41e-09 |
|
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: 56.07 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 526 HLLVAGSTGSGKSSFINSMITSLLMRakpaEVRMVLIDPKRvELaaYqgvphLITPiitspkkaaealqwvvkEMDMRYD 605
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKG-EL--F-----LVIP-----------------DRDDSFA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 606 DLASFGFRHIDDFNRAVLADeielpEGSKRQLQpypyLLVVVDELADLMMVaprdveDSIVRITQLARASGIHLVLATQ- 684
Cdd:cd01127 52 ALRALFFNQLFRALTELASL-----SPGRLPRR----VWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQs 116
|
170 180
....*....|....*....|....*...
gi 2381058128 685 -----RPSVDVVTGLIKANVPSRLAFAV 707
Cdd:cd01127 117 laqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
257-856 |
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: 780.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 257 APIELGTFSDLGLDLQDESSMPWWRKGKPRAEVPAFDTPVERDAETGVIDRDARDKVTGDLAAVLDQAEQAVERFTGEAP 336
Cdd:COG1674 12 AGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLLLLLLLLGLLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 337 AHPGAVRDDAEPAVLPGFPTGAREKGEAGEFDAPPPIARTAPPYRLPNQAVLAPGTP--PKSRSAANDAVVAAITEVLTQ 414
Cdd:COG1674 92 ALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPkkEKIDEEELEENARLLEETLED 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 415 FQVDARVTGFSRGPSVTRYEVELGPGVKVERFTALTKNIAYAVASNEVSILSPIPGKSAIGVEIPNVDREVVSLGDVLRS 494
Cdd:COG1674 172 FGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 495 SAAAKALHPMTIGVGKDVEGGFVVANLAKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQG 574
Cdd:COG1674 252 DEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 575 VPHLITPIITSPKKAAEALQWVVKEMDMRYDDLASFGFRHIDDFNRAVLADEIELPEGskRQLQPYPYLLVVVDELADLM 654
Cdd:COG1674 332 IPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGEEE--EGLEPLPYIVVIIDELADLM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 655 MVAPRDVEDSIVRITQLARASGIHLVLATQRPSVDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGAEKLIGQGDGLFL 734
Cdd:COG1674 410 MVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 735 PMGASKAVRAQGAWVTEPEIAAVVEHVKKQARPEYRQDVAVEAEKKQIDADIGDDLELLLAAAELIVSTQFGSTSMLQRK 814
Cdd:COG1674 490 PPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRR 569
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2381058128 815 LRVGFAKAGRLMDLLESREIVGPSEGSKARDVLALPDQLPEV 856
Cdd:COG1674 570 LRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
372-850 |
2.56e-117 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 389.44 E-value: 2.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 372 PIARTAPPyrLPNQAVLapgTPPKSRSAANDAV----VAAITEV-LTQFQVDARVTGFSRGPSVTRYEVELGPGVKVERF 446
Cdd:PRK10263 858 PLHKPTTP--LPSLDLL---TPPPSEVEPVDTFaleqMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARI 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 447 TALTKNIAYAVASNEVSILSPIPGKSAIGVEIPNVDREVVSLGDVLRSSAAAKALHPMTIGVGKDVEGGFVVANLAKMPH 526
Cdd:PRK10263 933 SNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPH 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 527 LLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQGVPHLITPIITSPKKAAEALQWVVKEMDMRYDD 606
Cdd:PRK10263 1013 LLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKL 1092
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 607 LASFGFRHIDDFNRAVL-ADEIELP------------EGSKRQLQPYPYLLVVVDELADLMMVAPRDVEDSIVRITQLAR 673
Cdd:PRK10263 1093 MSALGVRNLAGYNEKIAeADRMMRPipdpywkpgdsmDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKAR 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 674 ASGIHLVLATQRPSVDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGAEKLIGQGDGLFLPMGASKAVRAQGAWVTEPE 753
Cdd:PRK10263 1173 AAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQE 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 754 IAAVVEHVKKQARPEYRQDVAVEAEKKQIDA--DIGDDLELLLAAAELIVSTQF-GSTSMLQRKLRVGFAKAGRLMDLLE 830
Cdd:PRK10263 1253 VHAVVQDWKARGRPQYVDGITSDSESEGGAGgfDGAEELDPLFDQAVQFVTEKRkASISGVQRQFRIGYNRAARIIEQME 1332
|
490 500
....*....|....*....|
gi 2381058128 831 SREIVGPSEGSKARDVLALP 850
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
488-687 |
1.21e-59 |
|
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: 202.61 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 488 LGDVLRSSAAAKALHPMTIGVGKDVEGGFVVANLAKMP-HLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKR 566
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 567 VELAAYQGVPHLIT-PIITSPKKAAEALQWVVKEMDMRYDDLASFGFRHIDDFNRAVLADE-------------IELPEG 632
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPldgfgdvflviygVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2381058128 633 SKRQLQPYPYLLVVVDELADLMMVAPRD----VEDSIVRITQLARASGIHLVLATQRPS 687
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
382-480 |
4.51e-28 |
|
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: 108.78 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 382 LPNQAVLAPGTP--PKSRSAANDAVVAAITEVLTQFQVDARVTGFSRGPSVTRYEVELGPGVKVERFTALTKNIAYAVAS 459
Cdd:pfam17854 1 LPPLDLLEPPPTssQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 2381058128 460 NEVSILSPIPGKSAIGVEIPN 480
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
493-731 |
1.55e-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: 110.85 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 493 RSSAAAKALhPMTIGV-GKDvegGFVVANL---AKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVE 568
Cdd:TIGR03928 438 AKNETYKSL-AVPIGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 569 LA-AYQGVPHL---ITPIITSpkKAAEALQWVVKEMDMRYDDLASFGFRHIDDFnravladeIELpegSKRQL--QPYPY 642
Cdd:TIGR03928 514 MAnLFKNLPHLlgtITNLDGA--QSMRALASIKAELKKRQRLFGENNVNHINQY--------QKL---YKQGKakEPMPH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 643 LLVVVDELADLMMVAPrDVEDSIVRITQLARASGIHLVLATQRPSvDVVTGLIKANVPSRLAFAVSSMTDSRVILDQPGA 722
Cdd:TIGR03928 581 LFLISDEFAELKSEQP-EFMKELVSTARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
....*....
gi 2381058128 723 EKLIGQGDG 731
Cdd:TIGR03928 659 AEITVPGRA 667
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
800-848 |
1.83e-19 |
|
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: 82.80 E-value: 1.83e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2381058128 800 IVSTQFGSTSMLQRKLRVGFAKAGRLMDLLESREIVGPSEGSKARDVLA 848
Cdd:pfam09397 14 VIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLI 62
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
800-848 |
8.34e-19 |
|
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: 80.92 E-value: 8.34e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2381058128 800 IVSTQFGSTSMLQRKLRVGFAKAGRLMDLLESREIVGPSEGSKARDVLA 848
Cdd:smart00843 14 VIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLV 62
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
525-752 |
5.38e-17 |
|
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: 85.79 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 525 PHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPK-RVELAAYQGVPHlITPIITSPKKAA-------EALQwv 596
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKgGATFLGLEGLPH-VSAVITNLADEAplvdrmqDALA-- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 597 vKEMDMRYDDLASFG-FRHIDDFNRAVLADeielpegskRQLQPYPYLLVVVDELADLMMVAPrDVEDSIVRITQLARAS 675
Cdd:TIGR03924 513 -GEMNRRQELLRAAGnFANVAEYEKARAAG---------ADLPPLPALFVVVDEFSELLSQHP-DFADLFVAIGRLGRSL 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2381058128 676 GIHLVLATQRPSVDVVTGLiKANVPSRLAFAVSSMTDSRVILDQPGAEKLIGQGDGLFLPMGASKAVRAQGAWVTEP 752
Cdd:TIGR03924 582 GVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
520-720 |
3.94e-10 |
|
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: 63.85 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 520 NLAKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQGVPHlITPIITS--PKKAAEALQWVV 597
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTLdeEEKIEKLIRRIK 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 598 KEMDMRYDDLASFGFRHIDDFNRAvladeielpegSKRQLqpyPYLLVVVDELaDLMMVAPR--DVEDSIVRITQLARAS 675
Cdd:TIGR03928 885 KEIDRRKKLFSEYGVASISMYNKA-----------SGEKL---PQIVIIIDNY-DAVKEEPFyeDFEELLIQLAREGASL 949
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2381058128 676 GIHLVL-ATQRPSVDVVtglIKANVPSRLAFAVSSMTDSRVILDQP 720
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 ... |
526-707 |
4.41e-09 |
|
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: 56.07 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 526 HLLVAGSTGSGKSSFINSMITSLLMRakpaEVRMVLIDPKRvELaaYqgvphLITPiitspkkaaealqwvvkEMDMRYD 605
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKG-EL--F-----LVIP-----------------DRDDSFA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 606 DLASFGFRHIDDFNRAVLADeielpEGSKRQLQpypyLLVVVDELADLMMVaprdveDSIVRITQLARASGIHLVLATQ- 684
Cdd:cd01127 52 ALRALFFNQLFRALTELASL-----SPGRLPRR----VWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQs 116
|
170 180
....*....|....*....|....*...
gi 2381058128 685 -----RPSVDVVTGLIKANVPSRLAFAV 707
Cdd:cd01127 117 laqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
478-733 |
2.22e-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: 58.46 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 478 IPNVdREVVSLGDVLRSSAAAKALHPMTIGVGKDVEGGFVVA-NLAKMPHLLVAGSTGSGKSSFINSMITSLlmrAKPAE 556
Cdd:TIGR03928 1050 IPMV-PEELSLEEFRERYEVRKILEEGSIPIGLDEETVEPVYiDLTENPHLLIVGESDDGKTNVLKSLLKTL---AKQEK 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 557 VRMVLIDPKRVELAAYQGVPHLITpIITSPKKAAEALQWVVKEMDMRYDDLasfgfrhiddfnravladeIELPEGSKRQ 636
Cdd:TIGR03928 1126 EKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELREAAY-------------------KEALQNETGE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 637 LQPYPYLLvVVDELADLMMVAPRDVEDSIVRITQLARASGIHLVLATQRPSV----DVVTGLIKAnvpSRLAFAVSSMTD 712
Cdd:TIGR03928 1186 PAFKPILL-IIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSD 1261
|
250 260
....*....|....*....|..
gi 2381058128 713 SRVI-LDQPGAEKLIGQGDGLF 733
Cdd:TIGR03928 1262 QSFFkLPFTRSEKELEPGEGYF 1283
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
520-566 |
2.91e-06 |
|
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: 51.15 E-value: 2.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2381058128 520 NLAKMPHLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKR 566
Cdd:TIGR03925 359 DFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRR 405
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
526-721 |
1.04e-04 |
|
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: 46.14 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 526 HLLVAGSTGSGKSSFINSMITSLLMRAKPAEVRMVLIDPKRVELAAYQGVPHlITPIIT--SPKKAAEALQWVVKEMDMR 603
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 604 YDDLASFGFRHIDDFNRAVLAdeIELPEgskrqlQPYPYLLVVVDELADLMmvapRDVEDSIVRITQLAR---ASGIHLV 680
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAA--GRLPE------DPFGDVFLVIDGWGTLR----QDFEDLEDKVTDLAArglAYGVHVV 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2381058128 681 LAT-----QRPSV-DVVTGLIKAnvpsRLAFAVSSMTDSR----VILDQPG 721
Cdd:TIGR03925 228 LTAsrwseIRPALrDLIGTRIEL----RLGDPMDSEIDRRaaarVPAGRPG 274
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
503-677 |
1.29e-04 |
|
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: 45.37 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 503 PMTIGVGKDvEGGFVVANLAKM--PHLLVAGSTGSGKSSFINSMITSLLMrakpAEVRMVLIDPKrVELAAYQGVPHLIT 580
Cdd:COG0433 25 GILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSR----AGVPVLVFDPH-GEYSGLAEPGAERA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 581 PIITSPKKAAEALQWVVKEMDMRYDDLAS--FGFRHIDDFNRAVLADEIELPEGSKRQLQPYPYLLVVVDELADLMMVAP 658
Cdd:COG0433 99 DVGVFDPGAGRPLPINPWDLFATASELGPllLSRLDLNDTQRGVLREALRLADDKGLLLLDLKDLIALLEEGEELGEEYG 178
|
170 180
....*....|....*....|...
gi 2381058128 659 RDVEDSI----VRITQLARASGI 677
Cdd:COG0433 179 NVSAASAgallRRLESLESADGL 201
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
525-566 |
2.81e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 44.55 E-value: 2.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2381058128 525 PHLLVAGSTGSGKSSFINSMITSLLMRakpaEVRMVLIDPKR 566
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDPGG 242
|
|
| AAA_10 |
pfam12846 |
AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
525-681 |
8.25e-04 |
|
AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins, including VirB4 components of the Type IV secretory pathway and conjugal transfer protein TrbE. This entry includes the arcaheal Vir4/HerA homolog CedB, a membrane-bound protein that is highly induced upon UV treatment and essential for DNA transfer between Sulfolobus cells.
Pssm-ID: 315512 [Multi-domain] Cd Length: 362 Bit Score: 42.77 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 525 PHLLVAGSTGSGKSSFINSMITSLLMRAkpaeVRMVLIDPKRVELAAYQGVPHLITPI----ITSPKKAAEALQWVV--- 597
Cdd:pfam12846 22 PHSAIIGDLGGGKSVLNKTLFYYIVLLG----GKALYIDPKKERGQWKETLPEIAHEInfvtLDSETENHGLLDPIVllp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2381058128 598 --KEMDMRYDDLASF--GFRHIDDFNRAVLADEIELPEGSKRqlqpyPYLLVVVDELadlmmvapRDVEDSIVR-----I 668
Cdd:pfam12846 98 reKEAESTAIDILTNltGDSSRDDEKFPALRKAVEAVTEGKQ-----RGLLAVIEEL--------RKEDPKAARniadhL 164
|
170
....*....|...
gi 2381058128 669 TQLARASGIHLVL 681
Cdd:pfam12846 165 ESVVDGSLAHLLF 177
|
|
| |
