|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
321-810 |
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: 842.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 321 IPEGEVGDDEFEEFDAEELRELNAYKLPPIDILNDAE-QTAKVSNKEVIQQGKVLEETLKNFGVNAKVSKIRIGPAVTQF 399
Cdd:COG1674 111 LALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPpKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 400 EIQPDIGVKVSKIINLQNDIALSLAAKDIRIEAPIPGKSAVGIEVPNSVVSMVTLREVI---KRRSSDNPLEVALGKDIS 476
Cdd:COG1674 191 EIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLesdEFQNSKSPLPIALGKDIS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 477 GAPIMAELNKMPHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPHLLAPVVTNPQKASDAL 556
Cdd:COG1674 271 GEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 557 NRIVSEMERRYDLFSHSNTRNIEAYNQYLERTADN---PKKVQKLPYIVVIVDELADLMMVASKDVEASITRIAQMARAA 633
Cdd:COG1674 351 KWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 634 GIHLIIATQRPSVDVITGIIKANIPSRIAFAVSSQTDSRTIIDSMGAEKLLGRGDMLFLPSGRSKPLRVQGAFLDDEEVT 713
Cdd:COG1674 431 GIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 714 DIVEFITEQMKANYEKSVI-MNQKQAEKTEVESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVI 792
Cdd:COG1674 511 RVVDFLKSQGEPEYIEEILeEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....*...
gi 1949521445 793 GPASGSKPRSVLIENHED 810
Cdd:COG1674 591 GPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
347-804 |
1.14e-146 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 465.33 E-value: 1.14e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 347 LPPIDILNDA-EQTAKVSNKEVIQQGKVLEETLKNFGVNAKVSKIRIGPAVTQFEIQPDIGVKVSKIINLQNDIALSLAA 425
Cdd:PRK10263 866 LPSLDLLTPPpSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 426 KDIRIEAPIPGKSAVGIEVPNSVVSMVTLREVI---KRRSSDNPLEVALGKDISGAPIMAELNKMPHLLVAGSTGSGKSV 502
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLdnaKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 503 CINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPHLLAPVVTNPQKASDALNRIVSEMERRYDLFSHSNTRNIEAYN 582
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 583 QYLERTADNPKKV------------------QKLPYIVVIVDELADLMMVASKDVEASITRIAQMARAAGIHLIIATQRP 644
Cdd:PRK10263 1106 EKIAEADRMMRPIpdpywkpgdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 645 SVDVITGIIKANIPSRIAFAVSSQTDSRTIIDSMGAEKLLGRGDMLFLPSGRSKPLRVQGAFLDDEEVTDIVEFITEQMK 724
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 725 ANYEKSvIMNQKQAEK-----TEVESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVIGPASGSK 799
Cdd:PRK10263 1266 PQYVDG-ITSDSESEGgaggfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNG 1344
|
....*
gi 1949521445 800 PRSVL 804
Cdd:PRK10263 1345 NREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
454-645 |
1.62e-71 |
|
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: 233.81 E-value: 1.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 454 LREVIKRRSSDN---PLEVALGKDISGAPIMAELNKMP-HLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKM 529
Cdd:pfam01580 1 LLEVLESKPFDTdysRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 530 VELNVYNGIPHLLA-PVVTNPQKASDALNRIVSEMERRYDLFSHSNTRNIEAYNQYLERTADN----------------- 591
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDgfgdvflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949521445 592 -PKKVQKLPYIVVIVDELADLMMVASKD----VEASITRIAQMARAAGIHLIIATQRPS 645
Cdd:pfam01580 161 aGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
744-805 |
1.86e-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: 110.97 E-value: 1.86e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949521445 744 ESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVIGPASGSKPRSVLI 805
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLV 62
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
488-675 |
1.91e-27 |
|
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: 119.71 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 488 PHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPK---MVelNVYNGIPHLLApVVTNPQKASD--ALNRIVSE 562
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLLG-TITNLDGAQSmrALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 563 MERRYDLFSHSNTRNIEAYNQ-YLERTADNPkkvqkLPYIVVIVDELADLmmvASKDVE--ASITRIAQMARAAGIHLII 639
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKlYKQGKAKEP-----MPHLFLISDEFAEL---KSEQPEfmKELVSTARIGRSLGVHLIL 618
|
170 180 190
....*....|....*....|....*....|....*.
gi 1949521445 640 ATQRPSvDVITGIIKANIPSRIAFAVSSQTDSRTII 675
Cdd:TIGR03928 619 ATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
39-166 |
2.24e-08 |
|
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: 54.51 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 39 GVVGEYLDAGFNYLFGSSRYFTYFVLLLAAFYLATNLKFPFTK-RMFGYTLMQFGLLFFLHSILYLTNRALTdsyysfqe 117
Cdd:pfam13491 48 GRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRSLERRWlRLLGFLLLLLASSALFALRLPSLEFGLP-------- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1949521445 118 ileltrasgfeFTGGGVIGQTLFNFSSTGISFFGTLLI--SLIFIYLSLII 166
Cdd:pfam13491 120 -----------GGAGGVIGRLLANALVTLLGFTGATLLllALLAIGLSLVT 159
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
489-665 |
1.55e-06 |
|
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: 48.37 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 489 HLLVAGSTGSGKSVcingIIVSILLNAKPHEVKLMMIDPKM---VELNVYNGIPHLLAPVVTNpqkasdalnrivsemer 565
Cdd:cd01127 1 NTLVLGTTGSGKTT----SIVIPLLDQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 566 ryDLFshsntrnieaynQYLERTADNPKKVQKLPyIVVIVDELADLMMVaskdveASITRIAQMARAAGIHLIIATQ--- 642
Cdd:cd01127 60 --QLF------------RALTELASLSPGRLPRR-VWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQsla 118
|
170 180
....*....|....*....|....*.
gi 1949521445 643 ---RPSVDVITGIIKANIPSRIAFAV 665
Cdd:cd01127 119 qleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
321-810 |
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: 842.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 321 IPEGEVGDDEFEEFDAEELRELNAYKLPPIDILNDAE-QTAKVSNKEVIQQGKVLEETLKNFGVNAKVSKIRIGPAVTQF 399
Cdd:COG1674 111 LALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPpKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 400 EIQPDIGVKVSKIINLQNDIALSLAAKDIRIEAPIPGKSAVGIEVPNSVVSMVTLREVI---KRRSSDNPLEVALGKDIS 476
Cdd:COG1674 191 EIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLesdEFQNSKSPLPIALGKDIS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 477 GAPIMAELNKMPHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPHLLAPVVTNPQKASDAL 556
Cdd:COG1674 271 GEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 557 NRIVSEMERRYDLFSHSNTRNIEAYNQYLERTADN---PKKVQKLPYIVVIVDELADLMMVASKDVEASITRIAQMARAA 633
Cdd:COG1674 351 KWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 634 GIHLIIATQRPSVDVITGIIKANIPSRIAFAVSSQTDSRTIIDSMGAEKLLGRGDMLFLPSGRSKPLRVQGAFLDDEEVT 713
Cdd:COG1674 431 GIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 714 DIVEFITEQMKANYEKSVI-MNQKQAEKTEVESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVI 792
Cdd:COG1674 511 RVVDFLKSQGEPEYIEEILeEEEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIV 590
|
490
....*....|....*...
gi 1949521445 793 GPASGSKPRSVLIENHED 810
Cdd:COG1674 591 GPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
347-804 |
1.14e-146 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 465.33 E-value: 1.14e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 347 LPPIDILNDA-EQTAKVSNKEVIQQGKVLEETLKNFGVNAKVSKIRIGPAVTQFEIQPDIGVKVSKIINLQNDIALSLAA 425
Cdd:PRK10263 866 LPSLDLLTPPpSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 426 KDIRIEAPIPGKSAVGIEVPNSVVSMVTLREVI---KRRSSDNPLEVALGKDISGAPIMAELNKMPHLLVAGSTGSGKSV 502
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLdnaKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 503 CINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPHLLAPVVTNPQKASDALNRIVSEMERRYDLFSHSNTRNIEAYN 582
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 583 QYLERTADNPKKV------------------QKLPYIVVIVDELADLMMVASKDVEASITRIAQMARAAGIHLIIATQRP 644
Cdd:PRK10263 1106 EKIAEADRMMRPIpdpywkpgdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRP 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 645 SVDVITGIIKANIPSRIAFAVSSQTDSRTIIDSMGAEKLLGRGDMLFLPSGRSKPLRVQGAFLDDEEVTDIVEFITEQMK 724
Cdd:PRK10263 1186 SVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGR 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 725 ANYEKSvIMNQKQAEK-----TEVESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVIGPASGSK 799
Cdd:PRK10263 1266 PQYVDG-ITSDSESEGgaggfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNG 1344
|
....*
gi 1949521445 800 PRSVL 804
Cdd:PRK10263 1345 NREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
454-645 |
1.62e-71 |
|
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: 233.81 E-value: 1.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 454 LREVIKRRSSDN---PLEVALGKDISGAPIMAELNKMP-HLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKM 529
Cdd:pfam01580 1 LLEVLESKPFDTdysRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 530 VELNVYNGIPHLLA-PVVTNPQKASDALNRIVSEMERRYDLFSHSNTRNIEAYNQYLERTADN----------------- 591
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDgfgdvflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949521445 592 -PKKVQKLPYIVVIVDELADLMMVASKD----VEASITRIAQMARAAGIHLIIATQRPS 645
Cdd:pfam01580 161 aGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
347-446 |
1.27e-42 |
|
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: 149.99 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 347 LPPIDILNDAEQTAKVSNKEVIQQ-GKVLEETLKNFGVNAKVSKIRIGPAVTQFEIQPDIGVKVSKIINLQNDIALSLAA 425
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEEtAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1949521445 426 KDIRIEAPIPGKSAVGIEVPN 446
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
744-805 |
1.30e-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: 1.30e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949521445 744 ESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVIGPASGSKPRSVLI 805
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLI 62
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
744-805 |
1.86e-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: 110.97 E-value: 1.86e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949521445 744 ESDDDLYPDAKWFVIEEQRASASLLQRQFRVGYNRAARLVDDLEANGVIGPASGSKPRSVLI 805
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLV 62
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
488-675 |
1.91e-27 |
|
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: 119.71 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 488 PHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPK---MVelNVYNGIPHLLApVVTNPQKASD--ALNRIVSE 562
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLLG-TITNLDGAQSmrALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 563 MERRYDLFSHSNTRNIEAYNQ-YLERTADNPkkvqkLPYIVVIVDELADLmmvASKDVE--ASITRIAQMARAAGIHLII 639
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKlYKQGKAKEP-----MPHLFLISDEFAEL---KSEQPEfmKELVSTARIGRSLGVHLIL 618
|
170 180 190
....*....|....*....|....*....|....*.
gi 1949521445 640 ATQRPSvDVITGIIKANIPSRIAFAVSSQTDSRTII 675
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 ... |
419-707 |
3.15e-20 |
|
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: 95.81 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 419 IALSLAAKDIRIEAPIPGKSAVGIEVPNSV----VSMVTLREVIKRRSSDNPLEVALGKDISGAPIM------AELNKMP 488
Cdd:TIGR03924 357 LARRLARWRAATAGTVDAPLTGARDLLELLgigdPATLDVDRLWRPRPGRDRLRVPIGVGDDGEPVEldlkesAEGGMGP 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 489 HLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPK-------MVELnvyngiPHLLApVVTN-PQKAS------D 554
Cdd:TIGR03924 437 HGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatflgLEGL------PHVSA-VITNlADEAPlvdrmqD 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 555 ALNrivSEMERRYDLF-SHSNTRNIEAYNQYLERTADNPkkvqKLPYIVVIVDELADLMmvASK----DVEASITRIaqm 629
Cdd:TIGR03924 510 ALA---GEMNRRQELLrAAGNFANVAEYEKARAAGADLP----PLPALFVVVDEFSELL--SQHpdfaDLFVAIGRL--- 577
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949521445 630 ARAAGIHLIIATQRPSVDVITGiIKANIPSRIAFAVSSQTDSRTIIDSMGAEKLLGRGDMLFLPSGRSKPLRVQGAFL 707
Cdd:TIGR03924 578 GRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYV 654
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
466-687 |
2.08e-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: 77.72 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 466 PLEVALG-KDI----SGAPIMAELNKMPHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPH 540
Cdd:TIGR03928 784 PLQATIGlLDDpelqSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 541 LlAPVVTNPQ--KASDALNRIVSEMERRYDLFSHSNTRNIEAYNQYLErtadnpkkvQKLPYIVVIVDELADLMMVASKD 618
Cdd:TIGR03928 864 V-ADYFTLDEeeKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASG---------EKLPQIVIIIDNYDAVKEEPFYE 933
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949521445 619 VEASItrIAQMAR---AAGIHLII-ATQRPSVDVitgIIKANIPSRIAFAVSSQTDSRTIIDS--MGAEKLLGRG 687
Cdd:TIGR03928 934 DFEEL--LIQLARegaSLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIVGRtkFTIEEIPGRG 1003
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
489-687 |
2.06e-10 |
|
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: 64.24 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 489 HLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKMVELNVYNGIPHLlAPVVTnpQKASDALNRIVSEME---- 564
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHV-GGVAG--RLDPERVRRTVAEVEgllr 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 565 RRYDLFShsnTRNIEAYNQYLERTADNPKKVQKLPYIVVIVDELADLMMvASKDVEASITRIAQMARAAGIHLIIATQRP 644
Cdd:TIGR03925 158 RRERLFR---THGIDSMAQYRARRAAGRLPEDPFGDVFLVIDGWGTLRQ-DFEDLEDKVTDLAARGLAYGVHVVLTASRW 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1949521445 645 SvdVITGIIKANIPSRIAFAVSSQTDSrtIIDSMGAEKLL----GRG 687
Cdd:TIGR03925 234 S--EIRPALRDLIGTRIELRLGDPMDS--EIDRRAAARVPagrpGRG 276
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
445-703 |
4.13e-10 |
|
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: 62.70 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 445 PNSVVSMVTLREVIKRRSSDNPLEVALGKDiSGAPIMAELNKM--PHLLVAGSTGSGKSVCINGIIVSILLnakpHEVKL 522
Cdd:COG0433 4 PGSPVYLADDEELEELLGDGGGILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSR----AGVPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 523 MMIDPK------------MVELNVYNGIPHLLAPV--------------------------------------------- 545
Cdd:COG0433 79 LVFDPHgeysglaepgaeRADVGVFDPGAGRPLPInpwdlfataselgplllsrldlndtqrgvlrealrladdkgllll 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 546 ------------------VTNPQKAS-DALNRIVSEMERRYDLFSHSNTR-----------NI----------------- 578
Cdd:COG0433 159 dlkdlialleegeelgeeYGNVSAASaGALLRRLESLESADGLFGEPGLDledllrtdgrvTVidlsglpeelqstfvlw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 579 ---EAYNQYLERTADNPKKVQklpyIVVIVDELADLMMVASKDVEASITRIAQMARAAGIHLIIATQRPSvDVITGIIkA 655
Cdd:COG0433 239 llrELFEARPEVGDADDRKLP----LVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDEDVL-S 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949521445 656 NIPSRIAFAVSSQTDSRTIIDSMGAEKL--------LGRGDMLFLPSGRSKPLRVQ 703
Cdd:COG0433 313 QLGTQIILRLFNPRDQKAVKAAAETLSEdllerlpsLGTGEALVLGEGIPLPVLVK 368
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
39-166 |
2.24e-08 |
|
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: 54.51 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 39 GVVGEYLDAGFNYLFGSSRYFTYFVLLLAAFYLATNLKFPFTK-RMFGYTLMQFGLLFFLHSILYLTNRALTdsyysfqe 117
Cdd:pfam13491 48 GRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRSLERRWlRLLGFLLLLLASSALFALRLPSLEFGLP-------- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1949521445 118 ileltrasgfeFTGGGVIGQTLFNFSSTGISFFGTLLI--SLIFIYLSLII 166
Cdd:pfam13491 120 -----------GGAGGVIGRLLANALVTLLGFTGATLLllALLAIGLSLVT 159
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
394-702 |
2.80e-08 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 57.69 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 394 PAVTQFeIQPDIGVKVSKII-NLQNDIAlslaakdiRIEAPIPGKSAVGIEVPNSVVSMVTLREVIKRRSSDNPLEVALG 472
Cdd:TIGR03928 1010 PTLFQT-ALPVKGEDDLEVIeNIKAEIQ--------KMNEAWTGERPKPIPMVPEELSLEEFRERYEVRKILEEGSIPIG 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 473 KDISGA-PIMAELNKMPHLLVAGSTGSGKSvcinGIIVSILLN-AKPHEVKLMMIDPKMVELNVYNGIPHLlAPVVTNPQ 550
Cdd:TIGR03928 1081 LDEETVePVYIDLTENPHLLIVGESDDGKT----NVLKSLLKTlAKQEKEKIGLIDSIDRGLLAYRDLKEV-ATYIEEKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 551 KASDALNRIVSEMERRYdlfshsntrniEAYNQYLERTADNPKKVQklpyIVVIVDELADLMMVASKDVEASITRIAQMA 630
Cdd:TIGR03928 1156 DLKEILAELKEEIELRE-----------AAYKEALQNETGEPAFKP----ILLIIDDLEDFIQRTDLEIQDILALIMKNG 1220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949521445 631 RAAGIHLIIATQRPSV----DVITGIIKAnipSRIAFAVSSQTDSRTI-IDSMGAEKLLGRGDMLFLPSGRSKPLRV 702
Cdd:TIGR03928 1221 KKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPGEGYFVVNGKYQKIKI 1294
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
489-665 |
1.55e-06 |
|
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: 48.37 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 489 HLLVAGSTGSGKSVcingIIVSILLNAKPHEVKLMMIDPKM---VELNVYNGIPHLLAPVVTNpqkasdalnrivsemer 565
Cdd:cd01127 1 NTLVLGTTGSGKTT----SIVIPLLDQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 566 ryDLFshsntrnieaynQYLERTADNPKKVQKLPyIVVIVDELADLMMVaskdveASITRIAQMARAAGIHLIIATQ--- 642
Cdd:cd01127 60 --QLF------------RALTELASLSPGRLPRR-VWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQsla 118
|
170 180
....*....|....*....|....*.
gi 1949521445 643 ---RPSVDVITGIIKANIPSRIAFAV 665
Cdd:cd01127 119 qleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
466-640 |
7.61e-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: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 466 PLEVALGKDISG-APIMAELNKMPHLLVAGSTGSGKSVCINGIIVSILLNAKPHEVKLMMIDPKMvelnvyngipHLLap 544
Cdd:TIGR03925 341 RLRVPLGLGESDlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRR----------TLL-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949521445 545 vvtnpqkasDAlnrIVSEMERRYDLFSHSNTRNIEAYNQYLERTADNPK-KVQKL--------PYIVVIVDELaDLMMVA 615
Cdd:TIGR03925 409 ---------GA---VPEDYLAGYAATSAALTELIAALAALLERRLPGPDvTPQQLrarswwsgPEIYVVVDDY-DLVATG 475
|
170 180
....*....|....*....|....*
gi 1949521445 616 SKDVEASITRIAQMARAAGIHLIIA 640
Cdd:TIGR03925 476 SGNPLAPLVELLPHARDIGLHVVVA 500
|
|
| |
