|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
276-778 |
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: 737.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 276 EVPVINEGGVEKTEPKHYIRDENSDFKNYKLPKLNVLEDMERKSRSnANTITAKEKGEKLIEILHEFGVEANLVQIHIGP 355
Cdd:COG1674 107 ALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEK-IDEEELEENARLLEETLEDFGVEAKVVGVTPGP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 356 SVTKFEIKPELGVRVNKISNLQNDIKMGLAAKDIRIEAPIPGKASVGIEIPNVEKTSVQMKDLMRTiPDSMKDK-KLLFC 434
Cdd:COG1674 186 VVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLES-DEFQNSKsPLPIA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 435 LGKDLMGNNVYGELNRMPHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSPVITDGD 514
Cdd:COG1674 265 LGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 515 LANKALKVIVEMMDRRYDLFGELGVRNITAYNEYVLTHN-----DEHLKVLPRIVIIIDELADLMLVAAKEVEASIQRIT 589
Cdd:COG1674 345 KAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKakgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 590 QLARAAGIHLIVATQRPSVDVITGVIKANIPSRIAFAVSQAVDSRTILDQAGAERLLGNGDMLYLPNGETSPRRIQGVFI 669
Cdd:COG1674 425 QKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 670 KDEEVNNICAFVKSQAMPKYDDAFIQLKDLQNQGNEAQNvtADPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMD 749
Cdd:COG1674 505 SDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDE--DDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLID 582
|
490 500
....*....|....*....|....*....
gi 2427467234 750 VLEANGIIGPSRGSKPREILVQNTLEDDI 778
Cdd:COG1674 583 QMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
226-769 |
1.84e-131 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 423.34 E-value: 1.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 226 ADPVKPVQPDPVVEETKDDEPLIIGDLEPRKPSFMVDVDDEPKEKVVEKNEVPVINEGGVEKTEPK--HYIRDENSDFKN 303
Cdd:PRK10263 779 QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHPLLMRNGDSRP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 304 YK-----LPKLNVLedMERKSRSNANTITAKEKGEKLIEI-LHEFGVEANLVQIHIGPSVTKFEIKPELGVRVNKISNLQ 377
Cdd:PRK10263 859 LHkpttpLPSLDLL--TPPPSEVEPVDTFALEQMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLS 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 378 NDIKMGLAAKDIRIEAPIPGKASVGIEIPNVEKTSVQMKDLMRTIPDSMKDKKLLFCLGKDLMGNNVYGELNRMPHLLIA 457
Cdd:PRK10263 937 RDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVA 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 458 GATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSPVITDGDLANKALKVIVEMMDRRYDLFGEL 537
Cdd:PRK10263 1017 GTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSAL 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 538 GVRNITAYNEYVL------------------THNDEH--LKVLPRIVIIIDELADLMLVAAKEVEASIQRITQLARAAGI 597
Cdd:PRK10263 1097 GVRNLAGYNEKIAeadrmmrpipdpywkpgdSMDAQHpvLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGI 1176
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 598 HLIVATQRPSVDVITGVIKANIPSRIAFAVSQAVDSRTILDQAGAERLLGNGDMLYLPNGETSPRRIQGVFIKDEEVNNI 677
Cdd:PRK10263 1177 HLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAV 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 678 CAFVKSQAMPKYDDAFIQlkDLQNQG-----NEAQNVtaDPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMDVLE 752
Cdd:PRK10263 1257 VQDWKARGRPQYVDGITS--DSESEGgaggfDGAEEL--DPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQME 1332
|
570
....*....|....*..
gi 2427467234 753 ANGIIGPSRGSKPREIL 769
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
435-607 |
1.92e-58 |
|
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: 197.99 E-value: 1.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 435 LGKDLMGNNVYGELNRMP-HLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLS-PVITD 512
Cdd:pfam01580 21 LGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLSvPVATD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 513 GDLANKALKVIVEMMDRRYDLFGELGVRNITAYNEYVLTHNDE--------------------HLKVLPRIVIIIDELAD 572
Cdd:pfam01580 101 PKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDgfgdvflviygvhvmctagrWLEILPYLVVIVDERAE 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 2427467234 573 LMLVAAKE----VEASIQRITQLARAAGIHLIVATQRPS 607
Cdd:pfam01580 181 LRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
712-771 |
4.51e-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: 109.81 E-value: 4.51e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 712 DPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMDVLEANGIIGPSRGSKPREILVQ 771
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
452-637 |
2.08e-23 |
|
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: 106.61 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 452 PHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFT-PYNDVPHLLSpVIT--DGDLANKALKVIVEMMD 528
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 529 RRYDLFGELGVRNITAYNEyvLTHNDEHLKVLPRIVIIIDELADL-------MlvaaKEVeASIQRItqlARAAGIHLIV 601
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQK--LYKQGKAKEPMPHLFLISDEFAELkseqpefM----KEL-VSTARI---GRSLGVHLIL 618
|
170 180 190
....*....|....*....|....*....|....*.
gi 2427467234 602 ATQRPSvDVITGVIKANIPSRIAFAVSQAVDSRTIL 637
Cdd:TIGR03928 619 ATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
453-627 |
1.23e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 54.53 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 453 HLLIAGATGSGKSVCVNAIISSILMRtkpdEVKLVLIDPKkveFTPYndvphllsPVITDGDLANKALK-VIVEMMDRRy 531
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPK---GELF--------LVIPDRDDSFAALRaLFFNQLFRA- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 532 dlfgelgvrnitayNEYVLTHNDEHLKvlPRIVIIIDELADLMLVaakeveASIQRITQLARAAGIHLIVATQ------R 605
Cdd:cd01127 65 --------------LTELASLSPGRLP--RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleA 122
|
170 180
....*....|....*....|..
gi 2427467234 606 PSVDVITGVIKANIPSRIAFAV 627
Cdd:cd01127 123 VYGKDGAQTILGNCNTKLYLGT 144
|
|
| SUR7 |
pfam06687 |
SUR7/PalI family; This family consists of several fungal-specific SUR7 proteins. Its activity ... |
30-110 |
8.26e-03 |
|
SUR7/PalI family; This family consists of several fungal-specific SUR7 proteins. Its activity regulates expression of RVS161, a homolog of human endophilin, suggesting a function for both in endocytosis. The protein carries four transmembrane domains and is thus likely to act as an anchoring protein for the eisosome to the plasma membrane. Eisosomes are the immobile protein complexes, that include the proteins Pil1 and Lsp1, which co-localize with sites of protein and lipid endocytosis at the plasma membrane. SUR7 protein may play a role in sporulation. This family also includes PalI which is part of a pH signal transduction cascade. Based on the similarity of PalI to the yeast Rim9 meiotic signal transduction component it has been suggested that PalI might be a membrane sensor for ambient pH.
Pssm-ID: 399580 Cd Length: 201 Bit Score: 38.47 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 30 LCFLICMICISIIAVLeFGIVgAFLKHFFEFL-FGALTNG---LFILNATLCAVLIFHKEQPVIRK--------RYMFGI 97
Cdd:pfam06687 110 FIVHIIALFFTVIALI-LGLL-AIFSHSRRGLlVNLLLSFlafLFTLLAALLDTALFVKARNAFKDygisaslgVKWFAF 187
|
90
....*....|...
gi 2427467234 98 LFLALGLSLISSI 110
Cdd:pfam06687 188 LWLAVAAALLSLI 200
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
276-778 |
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: 737.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 276 EVPVINEGGVEKTEPKHYIRDENSDFKNYKLPKLNVLEDMERKSRSnANTITAKEKGEKLIEILHEFGVEANLVQIHIGP 355
Cdd:COG1674 107 ALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEK-IDEEELEENARLLEETLEDFGVEAKVVGVTPGP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 356 SVTKFEIKPELGVRVNKISNLQNDIKMGLAAKDIRIEAPIPGKASVGIEIPNVEKTSVQMKDLMRTiPDSMKDK-KLLFC 434
Cdd:COG1674 186 VVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLES-DEFQNSKsPLPIA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 435 LGKDLMGNNVYGELNRMPHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSPVITDGD 514
Cdd:COG1674 265 LGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 515 LANKALKVIVEMMDRRYDLFGELGVRNITAYNEYVLTHN-----DEHLKVLPRIVIIIDELADLMLVAAKEVEASIQRIT 589
Cdd:COG1674 345 KAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKakgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 590 QLARAAGIHLIVATQRPSVDVITGVIKANIPSRIAFAVSQAVDSRTILDQAGAERLLGNGDMLYLPNGETSPRRIQGVFI 669
Cdd:COG1674 425 QKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 670 KDEEVNNICAFVKSQAMPKYDDAFIQLKDLQNQGNEAQNvtADPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMD 749
Cdd:COG1674 505 SDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDDDE--DDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLID 582
|
490 500
....*....|....*....|....*....
gi 2427467234 750 VLEANGIIGPSRGSKPREILVQNTLEDDI 778
Cdd:COG1674 583 QMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
226-769 |
1.84e-131 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 423.34 E-value: 1.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 226 ADPVKPVQPDPVVEETKDDEPLIIGDLEPRKPSFMVDVDDEPKEKVVEKNEVPVINEGGVEKTEPK--HYIRDENSDFKN 303
Cdd:PRK10263 779 QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHPLLMRNGDSRP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 304 YK-----LPKLNVLedMERKSRSNANTITAKEKGEKLIEI-LHEFGVEANLVQIHIGPSVTKFEIKPELGVRVNKISNLQ 377
Cdd:PRK10263 859 LHkpttpLPSLDLL--TPPPSEVEPVDTFALEQMARLVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLS 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 378 NDIKMGLAAKDIRIEAPIPGKASVGIEIPNVEKTSVQMKDLMRTIPDSMKDKKLLFCLGKDLMGNNVYGELNRMPHLLIA 457
Cdd:PRK10263 937 RDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVA 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 458 GATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSPVITDGDLANKALKVIVEMMDRRYDLFGEL 537
Cdd:PRK10263 1017 GTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSAL 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 538 GVRNITAYNEYVL------------------THNDEH--LKVLPRIVIIIDELADLMLVAAKEVEASIQRITQLARAAGI 597
Cdd:PRK10263 1097 GVRNLAGYNEKIAeadrmmrpipdpywkpgdSMDAQHpvLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGI 1176
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 598 HLIVATQRPSVDVITGVIKANIPSRIAFAVSQAVDSRTILDQAGAERLLGNGDMLYLPNGETSPRRIQGVFIKDEEVNNI 677
Cdd:PRK10263 1177 HLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAV 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 678 CAFVKSQAMPKYDDAFIQlkDLQNQG-----NEAQNVtaDPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMDVLE 752
Cdd:PRK10263 1257 VQDWKARGRPQYVDGITS--DSESEGgaggfDGAEEL--DPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQME 1332
|
570
....*....|....*..
gi 2427467234 753 ANGIIGPSRGSKPREIL 769
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
435-607 |
1.92e-58 |
|
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: 197.99 E-value: 1.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 435 LGKDLMGNNVYGELNRMP-HLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLS-PVITD 512
Cdd:pfam01580 21 LGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLSvPVATD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 513 GDLANKALKVIVEMMDRRYDLFGELGVRNITAYNEYVLTHNDE--------------------HLKVLPRIVIIIDELAD 572
Cdd:pfam01580 101 PKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDgfgdvflviygvhvmctagrWLEILPYLVVIVDERAE 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 2427467234 573 LMLVAAKE----VEASIQRITQLARAAGIHLIVATQRPS 607
Cdd:pfam01580 181 LRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
306-407 |
2.21e-34 |
|
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: 126.50 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 306 LPKLNVLEDMErKSRSNANTITAKEKGEKLIEILHEFGVEANLVQIHIGPSVTKFEIKPELGVRVNKISNLQNDIKMGLA 385
Cdd:pfam17854 1 LPPLDLLEPPP-TSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALS 79
|
90 100
....*....|....*....|..
gi 2427467234 386 AKDIRIEAPIPGKASVGIEIPN 407
Cdd:pfam17854 80 APSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
712-771 |
1.12e-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: 114.39 E-value: 1.12e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 712 DPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMDVLEANGIIGPSRGSKPREILVQ 771
Cdd:pfam09397 4 DELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
712-771 |
4.51e-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: 109.81 E-value: 4.51e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 712 DPLYEEVKRFVIASRKASTSLIQRKFSVGYSRAARLMDVLEANGIIGPSRGSKPREILVQ 771
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
452-637 |
2.08e-23 |
|
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: 106.61 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 452 PHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFT-PYNDVPHLLSpVIT--DGDLANKALKVIVEMMD 528
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 529 RRYDLFGELGVRNITAYNEyvLTHNDEHLKVLPRIVIIIDELADL-------MlvaaKEVeASIQRItqlARAAGIHLIV 601
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQK--LYKQGKAKEPMPHLFLISDEFAELkseqpefM----KEL-VSTARI---GRSLGVHLIL 618
|
170 180 190
....*....|....*....|....*....|....*.
gi 2427467234 602 ATQRPSvDVITGVIKANIPSRIAFAVSQAVDSRTIL 637
Cdd:TIGR03928 619 ATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
452-656 |
1.20e-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: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 452 PHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPK-KVEFTPYNDVPHlLSPVITdgDLANKAlkVIVE-M--- 526
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKgGATFLGLEGLPH-VSAVIT--NLADEA--PLVDrMqda 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 527 ----MDRRYDLFGELG-VRNITAYNEYVLThnDEHLKVLPRIVIIIDELADLmLVAAKEVEASIQRITQLARAAGIHLIV 601
Cdd:TIGR03924 511 lageMNRRQELLRAAGnFANVAEYEKARAA--GADLPPLPALFVVVDEFSEL-LSQHPDFADLFVAIGRLGRSLGVHLLL 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2427467234 602 ATQRPSVDVITGvIKANIPSRIAFAVSQAVDSRTIldqagaerlLGNGDMLYLPN 656
Cdd:TIGR03924 588 ASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAV---------LGVPDAYHLPS 632
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
453-637 |
4.70e-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: 76.57 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 453 HLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSPV-ITDGDLANKALKVIVEMMDRRY 531
Cdd:TIGR03928 812 HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFtLDEEEKIEKLIRRIKKEIDRRK 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 532 DLFGELGVRNITAYNEYVlthndehLKVLPRIVIIIDELADLMLVAAKEVEASIqrITQLAR---AAGIHLIV-ATQRPS 607
Cdd:TIGR03928 892 KLFSEYGVASISMYNKAS-------GEKLPQIVIIIDNYDAVKEEPFYEDFEEL--LIQLARegaSLGIYLVMtAGRQNA 962
|
170 180 190
....*....|....*....|....*....|
gi 2427467234 608 VDVitgVIKANIPSRIAFAVSQAVDSRTIL 637
Cdd:TIGR03928 963 VRM---PLMNNIKTKIALYLIDKSEYRSIV 989
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
444-664 |
6.02e-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: 63.08 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 444 VYGELNRMPHLLIAGATGSGKSVCVNAIISSIlmrTKPDEVKLVLIDPKKVEFTPYNDVPHLLSpVITDGDLANKALKVI 523
Cdd:TIGR03928 1089 VYIDLTENPHLLIVGESDDGKTNVLKSLLKTL---AKQEKEKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAEL 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 524 VEMMDRRYDlfgelgvrnitAYNEYVLTHNDEHLKvlPRIVIIIDELADLMLVAAKEVEASIQRITQLARAAGIHLIVAT 603
Cdd:TIGR03928 1165 KEEIELREA-----------AYKEALQNETGEPAF--KPILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAG 1231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427467234 604 QRPSV----DVITGVIKAnipSRIAFAVSQAVDSRTI-LDQAGAERLLGNGDMLYLPNGETSPRRI 664
Cdd:TIGR03928 1232 THSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPGEGYFVVNGKYQKIKI 1294
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
444-602 |
1.65e-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: 61.16 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 444 VYGELNRMPHLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKvefTPYNDVP--HLLSpVITDGDLANKALK 521
Cdd:TIGR03925 356 VYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRR---TLLGAVPedYLAG-YAATSAALTELIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 522 VIVEMMDRRydLFGElgvrNITAyneyvlthndEHLKVL-----PRIVIIIDelaDLMLVAAkeveASIQRITQL----- 591
Cdd:TIGR03925 432 ALAALLERR--LPGP----DVTP----------QQLRARswwsgPEIYVVVD---DYDLVAT----GSGNPLAPLvellp 488
|
170
....*....|..
gi 2427467234 592 -ARAAGIHLIVA 602
Cdd:TIGR03925 489 hARDIGLHVVVA 500
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
453-627 |
1.23e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 54.53 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 453 HLLIAGATGSGKSVCVNAIISSILMRtkpdEVKLVLIDPKkveFTPYndvphllsPVITDGDLANKALK-VIVEMMDRRy 531
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPK---GELF--------LVIPDRDDSFAALRaLFFNQLFRA- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 532 dlfgelgvrnitayNEYVLTHNDEHLKvlPRIVIIIDELADLMLVaakeveASIQRITQLARAAGIHLIVATQ------R 605
Cdd:cd01127 65 --------------LTELASLSPGRLP--RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleA 122
|
170 180
....*....|....*....|..
gi 2427467234 606 PSVDVITGVIKANIPSRIAFAV 627
Cdd:cd01127 123 VYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
453-633 |
1.50e-08 |
|
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: 58.08 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 453 HLLIAGATGSGKSVCVNAIISSILMRTKPDEVKLVLIDPKKVEFTPYNDVPHLLSpVIT--DGDLANKALKVIVEMMDRR 530
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGG-VAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 531 YDLFGELGVRNITAYNEyvlTHNDEHLKVLPR--IVIIIDELADLmlvaAKEVEASIQRITQLAR---AAGIHLIVATQR 605
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRA---RRAAGRLPEDPFgdVFLVIDGWGTL----RQDFEDLEDKVTDLAArglAYGVHVVLTASR 232
|
170 180
....*....|....*....|....*...
gi 2427467234 606 PSvdVITGVIKANIPSRIAFAVSQAVDS 633
Cdd:TIGR03925 233 WS--EIRPALRDLIGTRIELRLGDPMDS 258
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
435-597 |
7.87e-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: 45.75 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 435 LGKDLMGN-NVYGELNRM--PHLLIAGATGSGKSVCVNAIISSiLMRTKpdeVKLVLIDPkKVEFTPYNDVPHLLSPVIT 511
Cdd:COG0433 28 IGKLLSPGvPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEE-LSRAG---VPVLVFDP-HGEYSGLAEPGAERADVGV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 512 DGDLANKALKVIVEMMDRRYDLFGE-LGVRNITAYN-----EYVLTHNDEHLKVLPRIVIIIDELAD-------LMLVAA 578
Cdd:COG0433 103 FDPGAGRPLPINPWDLFATASELGPlLLSRLDLNDTqrgvlREALRLADDKGLLLLDLKDLIALLEEgeelgeeYGNVSA 182
|
170
....*....|....*....
gi 2427467234 579 KEVEASIQRITQLARAAGI 597
Cdd:COG0433 183 ASAGALLRRLESLESADGL 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-625 |
3.85e-04 |
|
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: 41.59 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 450 RMPHLLIAGATGSGKSVCVNAIISSIlmrtKPDEVKLVLIDPkkveftpyndvphllspviTDGDLANKALKVIVEMMDR 529
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL----GPPGGGVIYIDG-------------------EDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 530 RYDLFGELGVRNITAyneyvlthndeHLKVLPRIVIIIDE---LADLMLVAAKEVEASIQRITQLARAAGIHLIVATQRP 606
Cdd:smart00382 58 KASGSGELRLRLALA-----------LARKLKPDVLILDEitsLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
170
....*....|....*....
gi 2427467234 607 SvDVITGVIKANIPSRIAF 625
Cdd:smart00382 127 K-DLGPALLRRRFDRRIVL 144
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
452-491 |
2.27e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.47 E-value: 2.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2427467234 452 PHLLIAGATGSGKSVCVNAIISSILMRtkpdEVKLVLIDP 491
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| AAA_10 |
pfam12846 |
AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
439-493 |
2.92e-03 |
|
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: 40.84 E-value: 2.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2427467234 439 LMGNNVYGELNRMPHLLIAGATGSGKSVCVNAIISSILMRtkpdEVKLVLIDPKK 493
Cdd:pfam12846 9 LANQGVKGSKTNAPHSAIIGDLGGGKSVLNKTLFYYIVLL----GGKALYIDPKK 59
|
|
| SUR7 |
pfam06687 |
SUR7/PalI family; This family consists of several fungal-specific SUR7 proteins. Its activity ... |
30-110 |
8.26e-03 |
|
SUR7/PalI family; This family consists of several fungal-specific SUR7 proteins. Its activity regulates expression of RVS161, a homolog of human endophilin, suggesting a function for both in endocytosis. The protein carries four transmembrane domains and is thus likely to act as an anchoring protein for the eisosome to the plasma membrane. Eisosomes are the immobile protein complexes, that include the proteins Pil1 and Lsp1, which co-localize with sites of protein and lipid endocytosis at the plasma membrane. SUR7 protein may play a role in sporulation. This family also includes PalI which is part of a pH signal transduction cascade. Based on the similarity of PalI to the yeast Rim9 meiotic signal transduction component it has been suggested that PalI might be a membrane sensor for ambient pH.
Pssm-ID: 399580 Cd Length: 201 Bit Score: 38.47 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427467234 30 LCFLICMICISIIAVLeFGIVgAFLKHFFEFL-FGALTNG---LFILNATLCAVLIFHKEQPVIRK--------RYMFGI 97
Cdd:pfam06687 110 FIVHIIALFFTVIALI-LGLL-AIFSHSRRGLlVNLLLSFlafLFTLLAALLDTALFVKARNAFKDygisaslgVKWFAF 187
|
90
....*....|...
gi 2427467234 98 LFLALGLSLISSI 110
Cdd:pfam06687 188 LWLAVAAALLSLI 200
|
|
| |
