|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
304-797 |
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: 877.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 304 VEGTLPPISILDPAEKKQLNYSPESLAAVGHLLEIKLKEFGVEVSVDSIHPGPVITRYEIQPAAGVKVSRISNLAKDLAR 383
Cdd:COG1674 133 ALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIAL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 384 SLAVTSVRVVEVIPGKTTVGIEIPNEDRQIVRFSEVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMPHLLVAGTTGS 463
Cdd:COG1674 213 ALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 464 GKSVGVNAMILSILFKSGPDDAKLIMIDPKMLELSIYEGIPHLLCPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNL 543
Cdd:COG1674 293 GKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 544 SGFNAKVKEAQDAGTpltdplykresihdEAPLLTKLPTIVVVVDEFADMMMIVGKKVEELIARIAQKARAAGIHLILAT 623
Cdd:COG1674 373 AGYNEKVREAKAKGE--------------EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILAT 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 624 QRPSVDVITGLIKANIPTRMAFQVSSKIDSRTIIDQGGAEQLLGHGDMLYMPPGTSLPIRVHGAFVSDDEVHRVVEAWKL 703
Cdd:COG1674 439 QRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKS 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 704 RGAPEYNDDILAGVEEAgsgfdggsGGGDDDAETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVV 783
Cdd:COG1674 519 QGEPEYIEEILEEEEEE--------DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....
gi 800911069 784 TAMNTNGSREIIAP 797
Cdd:COG1674 591 GPAEGSKPREVLVS 604
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
308-797 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 699.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 308 LPPISILDPAEKKQLNYSPESLAAVGHLLEIKLKEFGVEVSVDSIHPGPVITRYEIQPAAGVKVSRISNLAKDLARSLAV 387
Cdd:PRK10263 866 LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 388 TSVRVVEVIPGKTTVGIEIPNEDRQIVRFSEVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMPHLLVAGTTGSGKSV 467
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 468 GVNAMILSILFKSGPDDAKLIMIDPKMLELSIYEGIPHLLCPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNLSGFN 547
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 548 AKVKEAQDAGTPLTDPLYKR-ESIHDEAPLLTKLPTIVVVVDEFADMMMIVGKKVEELIARIAQKARAAGIHLILATQRP 626
Cdd:PRK10263 1106 EKIAEADRMMRPIPDPYWKPgDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 627 SVDVITGLIKANIPTRMAFQVSSKIDSRTIIDQGGAEQLLGHGDMLYMPPGTSLPIRVHGAFVSDDEVHRVVEAWKLRGA 706
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 707 PEYNDDILAGVEEagsgfDGGSGGGDDDAETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVVTAM 786
Cdd:PRK10263 1266 PQYVDGITSDSES-----EGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQ 1340
|
490
....*....|.
gi 800911069 787 NTNGSREIIAP 797
Cdd:PRK10263 1341 GHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
418-627 |
5.35e-75 |
|
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: 242.67 E-value: 5.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 418 EVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMP-HLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPKMLE 496
Cdd:pfam01580 3 EVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 497 LSIYEGIPHLL-CPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNLSGFNAKVKEAQDAGTPLTDP-LYKRESIHDEA 574
Cdd:pfam01580 83 LSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLvIYGVHVMCTAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800911069 575 PLLTKLPTIVVVVDEFADMMMIVGKK----VEELIARIAQKARAAGIHLILATQRPS 627
Cdd:pfam01580 163 RWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
23-195 |
3.15e-45 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 160.06 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 23 RLKEGALIAIGALCLFLMMALLTYGKDDPGWSH-NSKIDDVQNFGGPVGSYSADILFMILGYFAYIFPLLLAIKTWQIFR 101
Cdd:pfam13491 3 LLRELLGLALLLLGLFLLLALVSYSPADPSWSTsGSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 102 QRHEPWQWsgwlfsWRLIGLVFLVLSGAALAHIHFHAPT-GLPAGAGGALGESLGDLARRTLNIQGSTLMFIALFLFGLT 180
Cdd:pfam13491 83 RRSLERRW------LRLLGFLLLLLASSALFALRLPSLEfGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLS 156
|
170
....*....|....*
gi 800911069 181 VFTDLSWFKVMDVTG 195
Cdd:pfam13491 157 LVTGFSWLALAERLG 171
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
736-797 |
1.30e-27 |
|
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: 105.96 E-value: 1.30e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800911069 736 ETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVVTAMNTNGSREIIAP 797
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
23-270 |
1.04e-23 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 107.86 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 23 RLKEGALIAIGALCLFLMMALLTYGKDDPGWSHNSKIDDVQNFGGPVGSYSADILFMILGYFAYIFPLLLAIKTWQIFRQ 102
Cdd:PRK10263 21 RLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 103 RHEPWQWSGWLFSWRLIGLVFLVLSGAALAHIhfHAPTGLPAGAGGALGESLGDLARRTLNIQGSTLMFIALFLFGLTVF 182
Cdd:PRK10263 101 QSSDEYIDYFAVSLRIIGVLALILTSCGLAAI--NADDIWYFASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGLTLF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 183 TDLSWFKVMDVTGKITLDLFELfqgAANRwwaarverkqmvaqLREVDTRVNEVVAPSTPDRREQAKVKERLIEREQALS 262
Cdd:PRK10263 179 TGWSWVTIAEKLGGWILNILTF---ASNR--------------TRRDDTWVDEDEYEDDEEYEDENHGKQHESRRARILR 241
|
....*...
gi 800911069 263 KHMSDREK 270
Cdd:PRK10263 242 GALARRKR 249
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
453-657 |
1.49e-22 |
|
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: 103.91 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 453 PHLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPK---MLELsiYEGIPHLLcPVVTDMkDAANALRWSV---A 526
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLL-GTITNL-DGAQSMRALAsikA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 527 EMERRYKLMAKMGVRNLsgfNAKVKeaqdagtpltdpLYKREsIHDEAplltkLPTIVVVVDEFADMmmivgkKVE---- 602
Cdd:TIGR03928 546 ELKKRQRLFGENNVNHI---NQYQK------------LYKQG-KAKEP-----MPHLFLISDEFAEL------KSEqpef 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 800911069 603 --ELI--ARIaqkARAAGIHLILATQRPSvDVITGLIKANIPTRMAFQVSSKIDSRTII 657
Cdd:TIGR03928 599 mkELVstARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
454-647 |
2.21e-10 |
|
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: 59.54 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 454 HLLVAGTTGSGKSVGVNAMILSILfksgPDDAKLIMIDPKMlelsiyegiphLLCPVVTDMKDAANALRwsvaemerryK 533
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-----------ELFLVIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 534 LMakmgvrnlsgFNAKVKEAQDAGTPLTDPLYKResihdeaplltklptIVVVVDEFADMMMIVGkkveelIARIAQKAR 613
Cdd:cd01127 56 LF----------FNQLFRALTELASLSPGRLPRR---------------VWFILDEFANLGRIPN------LPNLLATGR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800911069 614 AAGIHLILATQ------RPSVDVITGLIKANIPTRMAFQV 647
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
304-797 |
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: 877.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 304 VEGTLPPISILDPAEKKQLNYSPESLAAVGHLLEIKLKEFGVEVSVDSIHPGPVITRYEIQPAAGVKVSRISNLAKDLAR 383
Cdd:COG1674 133 ALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIAL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 384 SLAVTSVRVVEVIPGKTTVGIEIPNEDRQIVRFSEVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMPHLLVAGTTGS 463
Cdd:COG1674 213 ALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 464 GKSVGVNAMILSILFKSGPDDAKLIMIDPKMLELSIYEGIPHLLCPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNL 543
Cdd:COG1674 293 GKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 544 SGFNAKVKEAQDAGTpltdplykresihdEAPLLTKLPTIVVVVDEFADMMMIVGKKVEELIARIAQKARAAGIHLILAT 623
Cdd:COG1674 373 AGYNEKVREAKAKGE--------------EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILAT 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 624 QRPSVDVITGLIKANIPTRMAFQVSSKIDSRTIIDQGGAEQLLGHGDMLYMPPGTSLPIRVHGAFVSDDEVHRVVEAWKL 703
Cdd:COG1674 439 QRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKS 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 704 RGAPEYNDDILAGVEEAgsgfdggsGGGDDDAETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVV 783
Cdd:COG1674 519 QGEPEYIEEILEEEEEE--------DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....
gi 800911069 784 TAMNTNGSREIIAP 797
Cdd:COG1674 591 GPAEGSKPREVLVS 604
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
308-797 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 699.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 308 LPPISILDPAEKKQLNYSPESLAAVGHLLEIKLKEFGVEVSVDSIHPGPVITRYEIQPAAGVKVSRISNLAKDLARSLAV 387
Cdd:PRK10263 866 LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 388 TSVRVVEVIPGKTTVGIEIPNEDRQIVRFSEVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMPHLLVAGTTGSGKSV 467
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 468 GVNAMILSILFKSGPDDAKLIMIDPKMLELSIYEGIPHLLCPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNLSGFN 547
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 548 AKVKEAQDAGTPLTDPLYKR-ESIHDEAPLLTKLPTIVVVVDEFADMMMIVGKKVEELIARIAQKARAAGIHLILATQRP 626
Cdd:PRK10263 1106 EKIAEADRMMRPIPDPYWKPgDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 627 SVDVITGLIKANIPTRMAFQVSSKIDSRTIIDQGGAEQLLGHGDMLYMPPGTSLPIRVHGAFVSDDEVHRVVEAWKLRGA 706
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 707 PEYNDDILAGVEEagsgfDGGSGGGDDDAETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVVTAM 786
Cdd:PRK10263 1266 PQYVDGITSDSES-----EGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQ 1340
|
490
....*....|.
gi 800911069 787 NTNGSREIIAP 797
Cdd:PRK10263 1341 GHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
418-627 |
5.35e-75 |
|
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: 242.67 E-value: 5.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 418 EVLSTPEYDNFKSPVTLALGHDIGGKPVITDLAKMP-HLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPKMLE 496
Cdd:pfam01580 3 EVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 497 LSIYEGIPHLL-CPVVTDMKDAANALRWSVAEMERRYKLMAKMGVRNLSGFNAKVKEAQDAGTPLTDP-LYKRESIHDEA 574
Cdd:pfam01580 83 LSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLvIYGVHVMCTAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 800911069 575 PLLTKLPTIVVVVDEFADMMMIVGKK----VEELIARIAQKARAAGIHLILATQRPS 627
Cdd:pfam01580 163 RWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
23-195 |
3.15e-45 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 160.06 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 23 RLKEGALIAIGALCLFLMMALLTYGKDDPGWSH-NSKIDDVQNFGGPVGSYSADILFMILGYFAYIFPLLLAIKTWQIFR 101
Cdd:pfam13491 3 LLRELLGLALLLLGLFLLLALVSYSPADPSWSTsGSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 102 QRHEPWQWsgwlfsWRLIGLVFLVLSGAALAHIHFHAPT-GLPAGAGGALGESLGDLARRTLNIQGSTLMFIALFLFGLT 180
Cdd:pfam13491 83 RRSLERRW------LRLLGFLLLLLASSALFALRLPSLEfGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLS 156
|
170
....*....|....*
gi 800911069 181 VFTDLSWFKVMDVTG 195
Cdd:pfam13491 157 LVTGFSWLALAERLG 171
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
308-408 |
4.49e-44 |
|
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: 153.84 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 308 LPPISILDPAEKKQLNYSPESLAAVGHLLEIKLKEFGVEVSVDSIHPGPVITRYEIQPAAGVKVSRISNLAKDLARSLAV 387
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 800911069 388 TSVRVVEVIPGKTTVGIEIPN 408
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
736-797 |
1.30e-27 |
|
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: 105.96 E-value: 1.30e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800911069 736 ETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVVTAMNTNGSREIIAP 797
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
736-797 |
3.23e-27 |
|
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: 104.76 E-value: 3.23e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800911069 736 ETDALYDEAVAFVLESRRASISAVQRKLKIGYNRAARMIEAMEHAGVVTAMNTNGSREIIAP 797
Cdd:pfam09397 2 EEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
23-270 |
1.04e-23 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 107.86 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 23 RLKEGALIAIGALCLFLMMALLTYGKDDPGWSHNSKIDDVQNFGGPVGSYSADILFMILGYFAYIFPLLLAIKTWQIFRQ 102
Cdd:PRK10263 21 RLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 103 RHEPWQWSGWLFSWRLIGLVFLVLSGAALAHIhfHAPTGLPAGAGGALGESLGDLARRTLNIQGSTLMFIALFLFGLTVF 182
Cdd:PRK10263 101 QSSDEYIDYFAVSLRIIGVLALILTSCGLAAI--NADDIWYFASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGLTLF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 183 TDLSWFKVMDVTGKITLDLFELfqgAANRwwaarverkqmvaqLREVDTRVNEVVAPSTPDRREQAKVKERLIEREQALS 262
Cdd:PRK10263 179 TGWSWVTIAEKLGGWILNILTF---ASNR--------------TRRDDTWVDEDEYEDDEEYEDENHGKQHESRRARILR 241
|
....*...
gi 800911069 263 KHMSDREK 270
Cdd:PRK10263 242 GALARRKR 249
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
453-657 |
1.49e-22 |
|
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: 103.91 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 453 PHLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPK---MLELsiYEGIPHLLcPVVTDMkDAANALRWSV---A 526
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLL-GTITNL-DGAQSMRALAsikA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 527 EMERRYKLMAKMGVRNLsgfNAKVKeaqdagtpltdpLYKREsIHDEAplltkLPTIVVVVDEFADMmmivgkKVE---- 602
Cdd:TIGR03928 546 ELKKRQRLFGENNVNHI---NQYQK------------LYKQG-KAKEP-----MPHLFLISDEFAEL------KSEqpef 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 800911069 603 --ELI--ARIaqkARAAGIHLILATQRPSvDVITGLIKANIPTRMAFQVSSKIDSRTII 657
Cdd:TIGR03928 599 mkELVstARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
436-692 |
1.43e-21 |
|
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: 100.05 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 436 LGHDIGGKPVITDLAK-----M-PHLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPK----MLELsiyEGIPH 505
Cdd:TIGR03924 413 IGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 506 lLCPVVTDMKDAAN-------ALRwsvAEMERRYKLMAKMG-VRNLSGFNakvkEAQDAGTPLtDPlykresihdeapll 577
Cdd:TIGR03924 490 -VSAVITNLADEAPlvdrmqdALA---GEMNRRQELLRAAGnFANVAEYE----KARAAGADL-PP-------------- 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 578 tkLPTIVVVVDEFADMMmivGKKVE--ELIARIAQKARAAGIHLILATQRPSVDVITGLiKANIPTRMAFQVSSKIDSRT 655
Cdd:TIGR03924 547 --LPALFVVVDEFSELL---SQHPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRA 620
|
250 260 270
....*....|....*....|....*....|....*..
gi 800911069 656 IIDQGGAEQLLGHGDMLYMPPGTSLPIRVHGAFVSDD 692
Cdd:TIGR03924 621 VLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
444-657 |
1.50e-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: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 444 PVITDLAKMPHLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPKMLELSIYEGIPHLLCPVVTDMKDA-ANALR 522
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKiEKLIR 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 523 WSVAEMERRYKLMAKMGVRNLSGFNAKVKEaqdagtpltdplykresihdeaplltKLPTIVVVVDEFadmmMIVGK--- 599
Cdd:TIGR03928 882 RIKKEIDRRKKLFSEYGVASISMYNKASGE--------------------------KLPQIVIIIDNY----DAVKEepf 931
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800911069 600 --KVEELIARIAQKARAAGIHLIL-ATQRPSVDVItglIKANIPTRMAFQVSSKIDSRTII 657
Cdd:TIGR03928 932 yeDFEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
454-647 |
2.21e-10 |
|
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: 59.54 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 454 HLLVAGTTGSGKSVGVNAMILSILfksgPDDAKLIMIDPKMlelsiyegiphLLCPVVTDMKDAANALRwsvaemerryK 533
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-----------ELFLVIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 534 LMakmgvrnlsgFNAKVKEAQDAGTPLTDPLYKResihdeaplltklptIVVVVDEFADMMMIVGkkveelIARIAQKAR 613
Cdd:cd01127 56 LF----------FNQLFRALTELASLSPGRLPRR---------------VWFILDEFANLGRIPN------LPNLLATGR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 800911069 614 AAGIHLILATQ------RPSVDVITGLIKANIPTRMAFQV 647
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
444-531 |
1.18e-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: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 444 PVITDLAKMPHLLVAGTTGSGKSVGVNAMILSILFKSGPDDAKLIMIDPKmleLSIYEGIP--HLL--CPVVTDMKDAAN 519
Cdd:TIGR03925 355 PVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR---RTLLGAVPedYLAgyAATSAALTELIA 431
|
90
....*....|..
gi 800911069 520 ALrwsVAEMERR 531
Cdd:TIGR03925 432 AL---AALLERR 440
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
434-492 |
2.13e-05 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 48.02 E-value: 2.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800911069 434 LALGHDIGGKPVITDLAKM---PHLLVAGTTGSGKSVGVNAMILSILFKsgpdDAKLIMIDP 492
Cdd:COG3451 183 IYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
428-685 |
2.65e-05 |
|
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: 47.29 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 428 FKSPVTLALGHDIG-GKPVITDLAKM--PHLLVAGTTGSGKSVGVNAMILSILFKSGPddakLIMIDPK----------- 493
Cdd:COG0433 20 LGDGGGILIGKLLSpGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHgeysglaepga 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 494 -MLELSIYEGIPHLLCPV--------VTDMKDAANA-------------------------------LRWSVAEMERRYK 533
Cdd:COG0433 96 eRADVGVFDPGAGRPLPInpwdlfatASELGPLLLSrldlndtqrgvlrealrladdkglllldlkdLIALLEEGEELGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 534 LMAKMGVRNLSGFNAKVKEAQDA-------GTPLTDPLYKRESIH-------DEAP-------LLTKL------------ 580
Cdd:COG0433 176 EYGNVSAASAGALLRRLESLESAdglfgepGLDLEDLLRTDGRVTvidlsglPEELqstfvlwLLRELfearpevgdadd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 581 --PTIVVVVDE---FADMMmivGKKVEELIARIAQKARAAGIHLILATQRPSvDVITGlIKANIPTRMAFQVSSKIDSRT 655
Cdd:COG0433 256 rkLPLVLVIDEahlLAPAA---PSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKA 330
|
330 340 350
....*....|....*....|....*....|....*...
gi 800911069 656 I------IDQGGAEQL--LGHGDMLYMPPGTSLPIRVH 685
Cdd:COG0433 331 VkaaaetLSEDLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
443-637 |
8.61e-05 |
|
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: 46.13 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 443 KPVITDLAKMPHLLVAGTTGSGKSvGVNAMILSILFKSGPDdaKLIMIDPKMLELSIYEGIPHLLCpVVTDMKDAANALR 522
Cdd:TIGR03928 1087 EPVYIDLTENPHLLIVGESDDGKT-NVLKSLLKTLAKQEKE--KIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILA 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800911069 523 WSVAEMERRyklmakmgvrnlsgfNAKVKEAQDAGTplTDPLYKResihdeaplltklptIVVVVDEFADMMMIVGKKVE 602
Cdd:TIGR03928 1163 ELKEEIELR---------------EAAYKEALQNET--GEPAFKP---------------ILLIIDDLEDFIQRTDLEIQ 1210
|
170 180 190
....*....|....*....|....*....|....*....
gi 800911069 603 ELIARIAQKARAAGIHLILATQRPSV----DVITGLIKA 637
Cdd:TIGR03928 1211 DILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ 1249
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
436-492 |
3.04e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 40.04 E-value: 3.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800911069 436 LGHDIGGK--PVITDLAKM--PHLLVAGTTGSGKSVGVNAMILSILFKsgpDDAKLIMIDP 492
Cdd:pfam01935 3 IGRLLDGSevPVYLDVNKLvsRHFAILGSTGSGKSNTVAVLLEELLEK---KGATVLIFDP 60
|
|
| |
