|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
323-787 |
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: 845.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 323 PPLTLLNQPAKQKAT-SKAEVQRKGQVLENTLKDFGVNAKVTQIKIGPAVTQYEIQPAQGVKVSKIVNLHNDIALALAAK 401
Cdd:COG1674 138 PPLDLLDPPPPKKEKiDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 402 DVRIEAPIPGRSAVGIEVPNEKISLVSLKEVLD-EKF-PSNNKLEVGLGRDISGDPITVPLNEMPHLLVAGSTGSGKSVC 479
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLEsDEFqNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 480 INGIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHLLIPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYNE 559
Cdd:COG1674 298 INAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 560 LIR--KQNQELDEKQPELPYIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRPSVDVITGIIKNNIPSR 637
Cdd:COG1674 378 KVReaKAKGEEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 638 IAFAVSSQTDSRTIIGTGGAEKLLGKGDMLYVGNGDSSQTRIQGAFLSDQEVQDVVNYVVEQQQANYVKEM--EPDAPVD 715
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIleEEEEEDE 537
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975928 716 KSEMKSEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGSKPRQVLIDLNNDE 787
Cdd:COG1674 538 GGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
322-780 |
1.54e-149 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 472.26 E-value: 1.54e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 322 VPPLTLLNQP-AKQKATSKAEVQRKGQVLENTLKDFGVNAKVTQIKIGPAVTQYEIQPAQGVKVSKIVNLHNDIALALAA 400
Cdd:PRK10263 866 LPSLDLLTPPpSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 401 KDVRIEAPIPGRSAVGIEVPNEKISLVSLKEVLDE-KFPSN-NKLEVGLGRDISGDPITVPLNEMPHLLVAGSTGSGKSV 478
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNaKFRDNpSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 479 CINGIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHLLIPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYN 558
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 559 ELIR--------------KQNQELDEKQP---ELPYIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRP 621
Cdd:PRK10263 1106 EKIAeadrmmrpipdpywKPGDSMDAQHPvlkKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 622 SVDVITGIIKNNIPSRIAFAVSSQTDSRTIIGTGGAEKLLGKGDMLYVGNGDSSQTRIQGAFLSDQEVQDVVNYVVEQQQ 701
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 702 ANYVKEMEPDAP-------VDKSEmkSEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGS 774
Cdd:PRK10263 1266 PQYVDGITSDSEseggaggFDGAE--ELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHN 1343
|
....*.
gi 581975928 775 KPRQVL 780
Cdd:PRK10263 1344 GNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
429-622 |
1.78e-68 |
|
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: 225.33 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 429 LKEVLDEKFPSNNK--LEVGLGRDISGDPITVPLNEMP-HLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPKM 505
Cdd:pfam01580 1 LLEVLESKPFDTDYsrLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 506 VELNVYNGIPHLL-IPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYNELIRKQNQELDEKQ------------ 572
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581975928 573 -----PELPYIVVIVDELADLMMVAGKE----VENAIQRITQMARAAGIHLIVATQRPS 622
Cdd:pfam01580 161 agrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
439-671 |
6.69e-29 |
|
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: 124.33 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 439 SNNKLEVGLGRDISGDPITVPLNEM---PHLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPK---MVelNVYN 512
Cdd:TIGR03928 442 TYKSLAVPIGLRGKDDIVYLNLHEKahgPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 513 GIPHLLiPVVTNPHKA--AQALEKIVAEMERRYDLFQHSSTRNIKGYNELIrKQNQeldEKQPeLPYIVVIVDELADLMm 590
Cdd:TIGR03928 520 NLPHLL-GTITNLDGAqsMRALASIKAELKKRQRLFGENNVNHINQYQKLY-KQGK---AKEP-MPHLFLISDEFAELK- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 591 vagKEVENAIQRITQMA---RAAGIHLIVATQRPSvdvitGIIKNNIPS----RIAFAVSSQTDSRTIIGTGGAEKLL-- 661
Cdd:TIGR03928 593 ---SEQPEFMKELVSTArigRSLGVHLILATQKPS-----GVVDDQIWSnsrfKLALKVQDASDSNEILKTPDAAEITvp 664
|
250
....*....|
gi 581975928 662 GKGdMLYVGN 671
Cdd:TIGR03928 665 GRA-YLQVGN 673
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
721-782 |
8.74e-29 |
|
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: 109.04 E-value: 8.74e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975928 721 SEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGSKPRQVLID 782
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
465-642 |
3.04e-05 |
|
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: 44.52 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 465 HLLVAGSTGSGKSVCINGIITSILlnakPHEVKLMLIDPKM---VELNVYNGIPHLLIPVVTNphkaaqALEKIVAEMER 541
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 542 RydlfqhsstrnikgynelirkQNQELDEKqpelpyIVVIVDELAdlMMVAGKEVENAIQRitqmARAAGIHLIVATQ-- 619
Cdd:cd01127 71 L---------------------SPGRLPRR------VWFILDEFA--NLGRIPNLPNLLAT----GRKRGISVVLILQsl 117
|
170 180
....*....|....*....|....*..
gi 581975928 620 ----RPSVDVITGIIKNNIPSRIAFAV 642
Cdd:cd01127 118 aqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
51-180 |
8.87e-04 |
|
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: 41.03 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 51 GIIGRLIDSFFNYLFGYSRYLtYILVLLATGF--ITYSKRIPKTRRTAGSIVLQIALLFVSQLVFHFnsgikaerepvls 128
Cdd:pfam13491 48 GRFGAWLADLLLQLFGYSAWL-LPVALLYWGWrlFRRRSLERRWLRLLGFLLLLLASSALFALRLPS------------- 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 581975928 129 yvyqsyQHSHFPNFGGGVLGFYLLELSVPLISLFGVCIITILLLCSSVILLT 180
Cdd:pfam13491 114 ------LEFGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVT 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
323-787 |
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: 845.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 323 PPLTLLNQPAKQKAT-SKAEVQRKGQVLENTLKDFGVNAKVTQIKIGPAVTQYEIQPAQGVKVSKIVNLHNDIALALAAK 401
Cdd:COG1674 138 PPLDLLDPPPPKKEKiDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 402 DVRIEAPIPGRSAVGIEVPNEKISLVSLKEVLD-EKF-PSNNKLEVGLGRDISGDPITVPLNEMPHLLVAGSTGSGKSVC 479
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLEsDEFqNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 480 INGIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHLLIPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYNE 559
Cdd:COG1674 298 INAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 560 LIR--KQNQELDEKQPELPYIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRPSVDVITGIIKNNIPSR 637
Cdd:COG1674 378 KVReaKAKGEEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 638 IAFAVSSQTDSRTIIGTGGAEKLLGKGDMLYVGNGDSSQTRIQGAFLSDQEVQDVVNYVVEQQQANYVKEM--EPDAPVD 715
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIleEEEEEDE 537
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975928 716 KSEMKSEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGSKPRQVLIDLNNDE 787
Cdd:COG1674 538 GGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
322-780 |
1.54e-149 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 472.26 E-value: 1.54e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 322 VPPLTLLNQP-AKQKATSKAEVQRKGQVLENTLKDFGVNAKVTQIKIGPAVTQYEIQPAQGVKVSKIVNLHNDIALALAA 400
Cdd:PRK10263 866 LPSLDLLTPPpSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 401 KDVRIEAPIPGRSAVGIEVPNEKISLVSLKEVLDE-KFPSN-NKLEVGLGRDISGDPITVPLNEMPHLLVAGSTGSGKSV 478
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNaKFRDNpSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 479 CINGIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHLLIPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYN 558
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 559 ELIR--------------KQNQELDEKQP---ELPYIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRP 621
Cdd:PRK10263 1106 EKIAeadrmmrpipdpywKPGDSMDAQHPvlkKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 622 SVDVITGIIKNNIPSRIAFAVSSQTDSRTIIGTGGAEKLLGKGDMLYVGNGDSSQTRIQGAFLSDQEVQDVVNYVVEQQQ 701
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 702 ANYVKEMEPDAP-------VDKSEmkSEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGS 774
Cdd:PRK10263 1266 PQYVDGITSDSEseggaggFDGAE--ELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHN 1343
|
....*.
gi 581975928 775 KPRQVL 780
Cdd:PRK10263 1344 GNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
429-622 |
1.78e-68 |
|
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: 225.33 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 429 LKEVLDEKFPSNNK--LEVGLGRDISGDPITVPLNEMP-HLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPKM 505
Cdd:pfam01580 1 LLEVLESKPFDTDYsrLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 506 VELNVYNGIPHLL-IPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYNELIRKQNQELDEKQ------------ 572
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 581975928 573 -----PELPYIVVIVDELADLMMVAGKE----VENAIQRITQMARAAGIHLIVATQRPS 622
Cdd:pfam01580 161 agrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
323-421 |
6.81e-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: 153.46 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 323 PPLTLLNQP-AKQKATSKAEVQRKGQVLENTLKDFGVNAKVTQIKIGPAVTQYEIQPAQGVKVSKIVNLHNDIALALAAK 401
Cdd:pfam17854 2 PPLDLLEPPpTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAP 81
|
90 100
....*....|....*....|
gi 581975928 402 DVRIEAPIPGRSAVGIEVPN 421
Cdd:pfam17854 82 SIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
721-782 |
4.59e-30 |
|
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: 112.85 E-value: 4.59e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975928 721 SEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGSKPRQVLID 782
Cdd:pfam09397 2 EEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
439-671 |
6.69e-29 |
|
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: 124.33 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 439 SNNKLEVGLGRDISGDPITVPLNEM---PHLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPK---MVelNVYN 512
Cdd:TIGR03928 442 TYKSLAVPIGLRGKDDIVYLNLHEKahgPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 513 GIPHLLiPVVTNPHKA--AQALEKIVAEMERRYDLFQHSSTRNIKGYNELIrKQNQeldEKQPeLPYIVVIVDELADLMm 590
Cdd:TIGR03928 520 NLPHLL-GTITNLDGAqsMRALASIKAELKKRQRLFGENNVNHINQYQKLY-KQGK---AKEP-MPHLFLISDEFAELK- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 591 vagKEVENAIQRITQMA---RAAGIHLIVATQRPSvdvitGIIKNNIPS----RIAFAVSSQTDSRTIIGTGGAEKLL-- 661
Cdd:TIGR03928 593 ---SEQPEFMKELVSTArigRSLGVHLILATQKPS-----GVVDDQIWSnsrfKLALKVQDASDSNEILKTPDAAEITvp 664
|
250
....*....|
gi 581975928 662 GKGdMLYVGN 671
Cdd:TIGR03928 665 GRA-YLQVGN 673
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
721-782 |
8.74e-29 |
|
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: 109.04 E-value: 8.74e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975928 721 SEDALYDEAYLFVVEQQKASTSLLQRQFRIGYNRASRLMDDLERNQVIGPQKGSKPRQVLID 782
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
443-685 |
4.46e-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: 88.88 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 443 LEVGLGRDISGDPITVPLNE-----M-PHLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPK-------MVELn 509
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatflgLEGL- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 510 vyngiPHlLIPVVTN----PHKAAQALEKIVAEMERRYDLFQHS-STRNIKGYNElIRKQNQELdekqPELPYIVVIVDE 584
Cdd:TIGR03924 488 -----PH-VSAVITNladeAPLVDRMQDALAGEMNRRQELLRAAgNFANVAEYEK-ARAAGADL----PPLPALFVVVDE 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 585 LADLMmvAGK----EVENAIQRItqmARAAGIHLIVATQRPSVDVITGiIKNNIPSRIAFAVSSQTDSRTIIGTGGAEKL 660
Cdd:TIGR03924 557 FSELL--SQHpdfaDLFVAIGRL---GRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHL 630
|
250 260
....*....|....*....|....*
gi 581975928 661 LGKGDMLYVGNGDSSQTRIQGAFLS 685
Cdd:TIGR03924 631 PSTPGAGYLKVDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
422-653 |
3.72e-14 |
|
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: 76.95 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 422 EKISLVSLKEV----LDEKFPSNNKLEVGLgRDI----SGDPITVPLNEMPHLLVAGSTGSGKSVCINGIITSILLNAKP 493
Cdd:TIGR03928 762 EKIYLDDLHAVefdkLWSKPKEPLQATIGL-LDDpelqSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSP 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 494 HEVKLMLIDPKMVELNVYNGIPHLL-IPVVTNPHKAAQALEKIVAEMERRYDLFQHSSTRNIKGYNELIRKqnqeldekq 572
Cdd:TIGR03928 841 EQLHFYLFDFGTNGLLPLKKLPHVAdYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASGE--------- 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 573 pELPYIVVIVDELADLMMVAGKEVENAIqrITQMAR---AAGIHLIV-ATQRPSVDVitgIIKNNIPSRIAFAVSSQTDS 648
Cdd:TIGR03928 912 -KLPQIVIIIDNYDAVKEEPFYEDFEEL--LIQLARegaSLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEY 985
|
....*
gi 581975928 649 RTIIG 653
Cdd:TIGR03928 986 RSIVG 990
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
410-672 |
2.39e-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: 64.24 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 410 PGRSAVGIEVPNEKISLVSLKEVLDE-KFPSNNKLEVGLGRDiSGDPITVPLNEMPHLLVAGSTGSGKSVCINGIITSIL 488
Cdd:TIGR03928 1043 TGERPKPIPMVPEELSLEEFRERYEVrKILEEGSIPIGLDEE-TVEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLA 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 489 LNAKpheVKLMLIDPKMVELNVYNGIPHLLIpVVTNPHKAAQALEKIVAEMERRYDlfqhsstrnikGYNELIRKQNQEL 568
Cdd:TIGR03928 1122 KQEK---EKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELREA-----------AYKEALQNETGEP 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 569 DEKQpelpyIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRPSV----DVITGIIKNnipSRIAFAVSS 644
Cdd:TIGR03928 1187 AFKP-----ILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMR 1258
|
250 260
....*....|....*....|....*....
gi 581975928 645 QTDSRTI-IGTGGAEKLLGKGDMLYVGNG 672
Cdd:TIGR03928 1259 KSDQSFFkLPFTRSEKELEPGEGYFVVNG 1287
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
389-617 |
7.83e-09 |
|
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: 58.85 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 389 NLHNDIALALAAKDVRIEAPIPGRSAVGIEVPNEKISLVSLKEVLDEKfpsnnKLEVGLGRDISG-DPITVPLNEMPHLL 467
Cdd:TIGR03925 293 GIASVDDLGTRGLVAVIRDVWGGPPAPPVRLLPARLPLSALPAGGGAP-----RLRVPLGLGESDlAPVYVDFAESPHLL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 468 VAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPKMVELNVyngIP--HLLiPVVTNPHKAAQALEKIVAEMERRY-- 543
Cdd:TIGR03925 368 IFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTLLGA---VPedYLA-GYAATSAALTELIAALAALLERRLpg 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581975928 544 -DLFQhsstrnikgynelirkqnQELDEKQP-ELPYIVVIVDelaDLMMVAGKeVENAIQRITQM---ARAAGIHLIVA 617
Cdd:TIGR03925 444 pDVTP------------------QQLRARSWwSGPEIYVVVD---DYDLVATG-SGNPLAPLVELlphARDIGLHVVVA 500
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
430-672 |
1.76e-08 |
|
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: 57.31 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 430 KEVLDEKFPSNNKLEVGLGRDiSGDPITVPLNEM--PHLLVAGSTGSGKSVCINGIITSILLnakpHEVKLMLIDPK--- 504
Cdd:COG0433 13 DEELEELLGDGGGILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSR----AGVPVLVFDPHgey 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 505 ---------MVELNVYN-------GIP------------HLLIPVVTNPHKAAQALEKIVAEMERRY-------DL---- 545
Cdd:COG0433 88 sglaepgaeRADVGVFDpgagrplPINpwdlfataselgPLLLSRLDLNDTQRGVLREALRLADDKGlllldlkDLiall 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 546 ------------FQHSSTRNIKGY------------------NELIRKQNQ-----------------------EL---- 568
Cdd:COG0433 168 eegeelgeeygnVSAASAGALLRRleslesadglfgepgldlEDLLRTDGRvtvidlsglpeelqstfvlwllrELfear 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 569 ----DEKQPELPyIVVIVDELADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRPSvDVITGIIKN-NipSRIAFAVS 643
Cdd:COG0433 248 pevgDADDRKLP-LVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDEDVLSQlG--TQIILRLF 323
|
330 340 350
....*....|....*....|....*....|....*..
gi 581975928 644 SQTDSRTI------IGTGGAEKL--LGKGDMLYVGNG 672
Cdd:COG0433 324 NPRDQKAVkaaaetLSEDLLERLpsLGTGEALVLGEG 360
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
465-649 |
5.72e-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: 49.61 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 465 HLLVAGSTGSGKSVCINGIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHllIPVVTNPHkAAQALEKIVAEME---- 540
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH--VGGVAGRL-DPERVRRTVAEVEgllr 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 541 RRYDLFQHSSTRNIKGYNELIRKQNqeldekQPELPY--IVVIVDELADLMMvAGKEVENAIQRITQMARAAGIHLIVAT 618
Cdd:TIGR03925 158 RRERLFRTHGIDSMAQYRARRAAGR------LPEDPFgdVFLVIDGWGTLRQ-DFEDLEDKVTDLAARGLAYGVHVVLTA 230
|
170 180 190
....*....|....*....|....*....|....*
gi 581975928 619 QRPSvdVITGIIKNNIPSRIAF----AVSSQTDSR 649
Cdd:TIGR03925 231 SRWS--EIRPALRDLIGTRIELrlgdPMDSEIDRR 263
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
465-642 |
3.04e-05 |
|
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: 44.52 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 465 HLLVAGSTGSGKSVCINGIITSILlnakPHEVKLMLIDPKM---VELNVYNGIPHLLIPVVTNphkaaqALEKIVAEMER 541
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 542 RydlfqhsstrnikgynelirkQNQELDEKqpelpyIVVIVDELAdlMMVAGKEVENAIQRitqmARAAGIHLIVATQ-- 619
Cdd:cd01127 71 L---------------------SPGRLPRR------VWFILDEFA--NLGRIPNLPNLLAT----GRKRGISVVLILQsl 117
|
170 180
....*....|....*....|....*..
gi 581975928 620 ----RPSVDVITGIIKNNIPSRIAFAV 642
Cdd:cd01127 118 aqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
51-180 |
8.87e-04 |
|
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: 41.03 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 51 GIIGRLIDSFFNYLFGYSRYLtYILVLLATGF--ITYSKRIPKTRRTAGSIVLQIALLFVSQLVFHFnsgikaerepvls 128
Cdd:pfam13491 48 GRFGAWLADLLLQLFGYSAWL-LPVALLYWGWrlFRRRSLERRWLRLLGFLLLLLASSALFALRLPS------------- 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 581975928 129 yvyqsyQHSHFPNFGGGVLGFYLLELSVPLISLFGVCIITILLLCSSVILLT 180
Cdd:pfam13491 114 ------LEFGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVT 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
465-640 |
2.78e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 465 HLLVAGSTGSGKSVcingIITSILLNAKPHEVKLMLIDPKMVELNVYNGIPHLLIPVVTNPHKAAQALEKIVAEMERRyd 544
Cdd:smart00382 4 VILIVGPPGSGKTT----LARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975928 545 lfqhsstrnikgynelirkqnqeldekqpelPYIVVIVDE---LADLMMVAGKEVENAIQRITQMARAAGIHLIVATQRP 621
Cdd:smart00382 78 -------------------------------KPDVLILDEitsLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
170
....*....|....*....
gi 581975928 622 SvDVITGIIKNNIPSRIAF 640
Cdd:smart00382 127 K-DLGPALLRRRFDRRIVL 144
|
|
| |
