|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
842-1305 |
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: 846.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 842 PPLALLSIPQ-QSALDNTEWLDEQKELLDTTFNNFHVGAHVINVSQGPAVTRFEVQPDPGVKVNKITNLSDDIKLSLAAK 920
Cdd:COG1674 138 PPLDLLDPPPpKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 921 DIRIEAPIPGKSAIGIEVPNKESKPVFLREILRSPVFTKSESPLTVALGLDISGDPIVTDIRKMPHGLIAGATGSGKSVC 1000
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1001 INAILTSILYKAKPHEVKLMLIDPKMVELAPYNSVPHLVAPVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYNT 1080
Cdd:COG1674 298 INAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1081 IVSEREIPG------ETLPYIVIVIDELADLMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSVDVITGLIKSNIPTR 1154
Cdd:COG1674 378 KVREAKAKGeeeeglEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1155 IAFTVSSQVDSRTIIDIGGAEKLLGRGDMLFLGNGTSKPVRVQGVYVSDDEIEKTVDHVRKQMKPNYLfkqEDLLAKTEQ 1234
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYI---EEILEEEEE 534
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196975620 1235 A------ESEDELFFEACQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVLISEDEFAAM 1305
Cdd:COG1674 535 EdeggddDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
721-1296 |
8.37e-161 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 518.10 E-value: 8.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 721 VRVENRPMQQVVAEPQveEQPMQQVVAEPQVEEQPmQQVVVESQVEEQPMQQVVVESQvEEQSVQQVVAEPQMEERPVQQ 800
Cdd:PRK10263 749 VEPVQQPQQPVAPQQQ--YQQPQQPVAPQPQYQQP-QQPVAPQPQYQQPQQPVAPQPQ-YQQPQQPVAPQPQYQQPQQPV 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 801 VVEEQVQKPISSTEVQEKAYVVN---QRENDMRNVlhTPPTYTVPPLALLSiPQQSALD--NTEWLDEQKELLDTTFNNF 875
Cdd:PRK10263 825 APQPQYQQPQQPVAPQPQDTLLHpllMRNGDSRPL--HKPTTPLPSLDLLT-PPPSEVEpvDTFALEQMARLVEARLADF 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 876 HVGAHVINVSQGPAVTRFEVQPDPGVKVNKITNLSDDIKLSLAAKDIRIEAPIPGKSAIGIEVPNKESKPVFLREILRSP 955
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 956 VFTKSESPLTVALGLDISGDPIVTDIRKMPHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKMVELAPYNSV 1035
Cdd:PRK10263 982 KFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGI 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1036 PHLVAPVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYNTIVSE-----REIPG----------------ETLPY 1094
Cdd:PRK10263 1062 PHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEadrmmRPIPDpywkpgdsmdaqhpvlKKEPY 1141
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1095 IVIVIDELADLMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSVDVITGLIKSNIPTRIAFTVSSQVDSRTIIDIGGA 1174
Cdd:PRK10263 1142 IVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGA 1221
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1175 EKLLGRGDMLFLGNGTSKPVRVQGVYVSDDEIEKTVDHVRKQMKPNYLfkqEDLLAKTEQ---------AESEDELFFEA 1245
Cdd:PRK10263 1222 ESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYV---DGITSDSESeggaggfdgAEELDPLFDQA 1298
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1196975620 1246 CQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVL 1296
Cdd:PRK10263 1299 VQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
948-1139 |
3.33e-72 |
|
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: 239.97 E-value: 3.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 948 LREILRSPVFTKSESPLTVALGLDISGDPIVTDIRKMP-HGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKM 1026
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1027 VELAPYNSVPHLVA-PVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYN---------------------TIVSE 1084
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNgeiaedpldgfgdvflviygvHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196975620 1085 REIPGETLPYIVIVIDELADLMMVAPGD----VEEAICRIAQKARACGIHLLVATQRPS 1139
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1236-1298 |
9.09e-28 |
|
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: 106.73 E-value: 9.09e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196975620 1236 ESEDELFFEACQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVLIS 1298
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
964-1204 |
1.19e-27 |
|
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: 120.46 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 964 LTVALGLDISGDPIVTDIRK-----M-PHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKM-VELAPYNSVP 1036
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGgATFLGLEGLP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1037 HLVApVITDVkAATAALkwaVE--------EMERRYELFAHAGA-RDLTRYNTiVSEREIPGETLPYIVIVIDELADLMM 1107
Cdd:TIGR03924 489 HVSA-VITNL-ADEAPL---VDrmqdalagEMNRRQELLRAAGNfANVAEYEK-ARAAGADLPPLPALFVVVDEFSELLS 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1108 VAP--GDVEEAICRIaqkARACGIHLLVATQRPSVDVITGLiKSNIPTRIAFTVSSQVDSRTIIDIGGAEKLLGRGDMLF 1185
Cdd:TIGR03924 563 QHPdfADLFVAIGRL---GRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGY 638
|
250
....*....|....*....
gi 1196975620 1186 LGNGTSKPVRVQGVYVSDD 1204
Cdd:TIGR03924 639 LKVDTAEPVRFRAAYVSGP 657
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
632-797 |
8.06e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.89 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 632 AETEENKR--VVEEAPVAEEQRVVEEAPVAEEQRVVEEAPVAEEQPVVKKEEPKREkkrhvpfnvvmlkQDRTRLMERHA 709
Cdd:PRK10811 853 VQVEEQREaeEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEE-------------VVVVETTHPEV 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 710 ARANAMQHSVNVRVENRPMQQVVAEPQVEEQPMQQVVAEPQVEEQPMQQVVVESQVEEQPMQQVVVESQVEEqsVQQVVA 789
Cdd:PRK10811 920 IAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEV--ETVTAV 997
|
....*...
gi 1196975620 790 EPQMEERP 797
Cdd:PRK10811 998 EPEVAPAQ 1005
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
523-712 |
9.92e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.41 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 523 EAQEEVEVIAETEAQEEVEViaeteepeeveviaeaeelEEVEVIAETEESEEVEVIAEIKAPVVETFVALEEIQQEDEA 602
Cdd:PRK10811 851 QDVQVEEQREAEEVQVQPVV-------------------AEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVV 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 603 IEQKSEFIHVAEADEQTKNDVQSFANVLLAETEENKRVVEEAPVAEEqrvVEEAPVAEEQRVVEEAPVAEEQPVVKKEEP 682
Cdd:PRK10811 912 VETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETAD---IEEAAETAEVVVAEPEVVAQPAAPVVAEVA 988
|
170 180 190
....*....|....*....|....*....|
gi 1196975620 683 KREKKRHVPFNVVMLKQDRTRLMERHAARA 712
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEATVEHNHATA 1018
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
842-1305 |
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: 846.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 842 PPLALLSIPQ-QSALDNTEWLDEQKELLDTTFNNFHVGAHVINVSQGPAVTRFEVQPDPGVKVNKITNLSDDIKLSLAAK 920
Cdd:COG1674 138 PPLDLLDPPPpKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 921 DIRIEAPIPGKSAIGIEVPNKESKPVFLREILRSPVFTKSESPLTVALGLDISGDPIVTDIRKMPHGLIAGATGSGKSVC 1000
Cdd:COG1674 218 SVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1001 INAILTSILYKAKPHEVKLMLIDPKMVELAPYNSVPHLVAPVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYNT 1080
Cdd:COG1674 298 INAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1081 IVSEREIPG------ETLPYIVIVIDELADLMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSVDVITGLIKSNIPTR 1154
Cdd:COG1674 378 KVREAKAKGeeeeglEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1155 IAFTVSSQVDSRTIIDIGGAEKLLGRGDMLFLGNGTSKPVRVQGVYVSDDEIEKTVDHVRKQMKPNYLfkqEDLLAKTEQ 1234
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYI---EEILEEEEE 534
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196975620 1235 A------ESEDELFFEACQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVLISEDEFAAM 1305
Cdd:COG1674 535 EdeggddDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
721-1296 |
8.37e-161 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 518.10 E-value: 8.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 721 VRVENRPMQQVVAEPQveEQPMQQVVAEPQVEEQPmQQVVVESQVEEQPMQQVVVESQvEEQSVQQVVAEPQMEERPVQQ 800
Cdd:PRK10263 749 VEPVQQPQQPVAPQQQ--YQQPQQPVAPQPQYQQP-QQPVAPQPQYQQPQQPVAPQPQ-YQQPQQPVAPQPQYQQPQQPV 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 801 VVEEQVQKPISSTEVQEKAYVVN---QRENDMRNVlhTPPTYTVPPLALLSiPQQSALD--NTEWLDEQKELLDTTFNNF 875
Cdd:PRK10263 825 APQPQYQQPQQPVAPQPQDTLLHpllMRNGDSRPL--HKPTTPLPSLDLLT-PPPSEVEpvDTFALEQMARLVEARLADF 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 876 HVGAHVINVSQGPAVTRFEVQPDPGVKVNKITNLSDDIKLSLAAKDIRIEAPIPGKSAIGIEVPNKESKPVFLREILRSP 955
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 956 VFTKSESPLTVALGLDISGDPIVTDIRKMPHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKMVELAPYNSV 1035
Cdd:PRK10263 982 KFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGI 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1036 PHLVAPVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYNTIVSE-----REIPG----------------ETLPY 1094
Cdd:PRK10263 1062 PHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEadrmmRPIPDpywkpgdsmdaqhpvlKKEPY 1141
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1095 IVIVIDELADLMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSVDVITGLIKSNIPTRIAFTVSSQVDSRTIIDIGGA 1174
Cdd:PRK10263 1142 IVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGA 1221
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1175 EKLLGRGDMLFLGNGTSKPVRVQGVYVSDDEIEKTVDHVRKQMKPNYLfkqEDLLAKTEQ---------AESEDELFFEA 1245
Cdd:PRK10263 1222 ESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYV---DGITSDSESeggaggfdgAEELDPLFDQA 1298
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1196975620 1246 CQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVL 1296
Cdd:PRK10263 1299 VQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
948-1139 |
3.33e-72 |
|
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: 239.97 E-value: 3.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 948 LREILRSPVFTKSESPLTVALGLDISGDPIVTDIRKMP-HGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKM 1026
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1027 VELAPYNSVPHLVA-PVITDVKAATAALKWAVEEMERRYELFAHAGARDLTRYN---------------------TIVSE 1084
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNgeiaedpldgfgdvflviygvHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196975620 1085 REIPGETLPYIVIVIDELADLMMVAPGD----VEEAICRIAQKARACGIHLLVATQRPS 1139
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
842-940 |
1.06e-38 |
|
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: 139.59 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 842 PPLALLSIPQQSAL-DNTEWLDEQKELLDTTFNNFHVGAHVINVSQGPAVTRFEVQPDPGVKVNKITNLSDDIKLSLAAK 920
Cdd:pfam17854 2 PPLDLLEPPPTSSQkVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAP 81
|
90 100
....*....|....*....|
gi 1196975620 921 DIRIEAPIPGKSAIGIEVPN 940
Cdd:pfam17854 82 SIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
1236-1298 |
1.74e-29 |
|
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: 111.69 E-value: 1.74e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196975620 1236 ESEDELFFEACQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVLIS 1298
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1236-1298 |
9.09e-28 |
|
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: 106.73 E-value: 9.09e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196975620 1236 ESEDELFFEACQFVVEQGGASTSSVQRKFRIGYNRAARLIEEMQSQGIISEARGTKPRDVLIS 1298
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
964-1204 |
1.19e-27 |
|
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: 120.46 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 964 LTVALGLDISGDPIVTDIRK-----M-PHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKM-VELAPYNSVP 1036
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGgATFLGLEGLP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1037 HLVApVITDVkAATAALkwaVE--------EMERRYELFAHAGA-RDLTRYNTiVSEREIPGETLPYIVIVIDELADLMM 1107
Cdd:TIGR03924 489 HVSA-VITNL-ADEAPL---VDrmqdalagEMNRRQELLRAAGNfANVAEYEK-ARAAGADLPPLPALFVVVDEFSELLS 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1108 VAP--GDVEEAICRIaqkARACGIHLLVATQRPSVDVITGLiKSNIPTRIAFTVSSQVDSRTIIDIGGAEKLLGRGDMLF 1185
Cdd:TIGR03924 563 QHPdfADLFVAIGRL---GRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGY 638
|
250
....*....|....*....
gi 1196975620 1186 LGNGTSKPVRVQGVYVSDD 1204
Cdd:TIGR03924 639 LKVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
959-1181 |
3.43e-22 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 104.30 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 959 KSESP--LTVALGLDISGDPIVTDI-RKM--PHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKMVELA-PY 1032
Cdd:TIGR03928 439 KNETYksLAVPIGLRGKDDIVYLNLhEKAhgPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1033 NSVPHLVApVITDV-----KAATAALKwavEEMERRYELFAHAGARDLTRYnTIVSEREIPGETLPYIVIVIDELADLMM 1107
Cdd:TIGR03928 519 KNLPHLLG-TITNLdgaqsMRALASIK---AELKKRQRLFGENNVNHINQY-QKLYKQGKAKEPMPHLFLISDEFAELKS 593
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196975620 1108 VAPGDVEEAIcRIAQKARACGIHLLVATQRPSvDVITGLIKSNIPTRIAFTVSSQVDSRTIIDIGGAEKLL--GRG 1181
Cdd:TIGR03928 594 EQPEFMKELV-STARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITvpGRA 667
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
958-1169 |
8.56e-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: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 958 TKSESPLTVALGL-DI----SGDPIVTDIRKMPHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKMVELAPY 1032
Cdd:TIGR03928 779 SKPKEPLQATIGLlDDpelqSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1033 NSVPHlVAPVIT--DVKAATAALKWAVEEMERRYELFAHAGARDLTRYNtivserEIPGETLPYIVIVIDELaDLMMVAP 1110
Cdd:TIGR03928 859 KKLPH-VADYFTldEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYN------KASGEKLPQIVIIIDNY-DAVKEEP 930
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196975620 1111 G--DVEEAICRIAQKARACGIHLLV-ATQRPSVDVItglIKSNIPTRIAFTVSSQVDSRTII 1169
Cdd:TIGR03928 931 FyeDFEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
954-1197 |
1.05e-11 |
|
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: 68.48 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 954 SPVFTKSESPL--------TVALGLDISGD-PIVTDIRKM--PHGLIAGATGSGKSVCINAILTSI-------------- 1008
Cdd:COG0433 6 SPVYLADDEELeellgdggGILIGKLLSPGvPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELsragvpvlvfdphg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1009 ----LYKAKPHEVKLMLIDPKMVELAPYN----------SVPHL------------------------------------ 1038
Cdd:COG0433 86 eysgLAEPGAERADVGVFDPGAGRPLPINpwdlfataseLGPLLlsrldlndtqrgvlrealrladdkglllldlkdlia 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1039 -------VAPVITDVKAATA-ALKWAVEEMERRYELFAHAGAR--------------DLTR-----YNTIVS-------- 1083
Cdd:COG0433 166 lleegeeLGEEYGNVSAASAgALLRRLESLESADGLFGEPGLDledllrtdgrvtviDLSGlpeelQSTFVLwllrelfe 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1084 ---EREIPGETLPYIVIVIDELADLMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSvDVITGlIKSNIPTRIAFTVS 1160
Cdd:COG0433 246 arpEVGDADDRKLPLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLF 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1196975620 1161 SQVDSRTI------IDIGGAEKL--LGRGDMLFLGNGTSKPVRVQ 1197
Cdd:COG0433 324 NPRDQKAVkaaaetLSEDLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
946-1196 |
1.02e-07 |
|
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: 56.92 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 946 VFLREILRSPVFTKSESPLTVALGLDISG-DPIVTDIRKMPHGLIAGATGSGKSVCINAILTSIlykAKPHEVKLMLIDP 1024
Cdd:TIGR03928 1057 LSLEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTL---AKQEKEKIGLIDS 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1025 KMVELAPYNSVPHlVAPVITDVKAATAALKWAVEEMERRYELFAHAgardltryntIVSEREIPGEtlPYIVIVIDELAD 1104
Cdd:TIGR03928 1134 IDRGLLAYRDLKE-VATYIEEKEDLKEILAELKEEIELREAAYKEA----------LQNETGEPAF--KPILLIIDDLED 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1105 LMMVAPGDVEEAICRIAQKARACGIHLLVATQRPSV----DVITGLIKSnipTRIAFTVSSQVDSrTIIDIG--GAEKLL 1178
Cdd:TIGR03928 1201 FIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQ-SFFKLPftRSEKEL 1276
|
250
....*....|....*...
gi 1196975620 1179 GRGDMLFLGNGTSKPVRV 1196
Cdd:TIGR03928 1277 EPGEGYFVVNGKYQKIKI 1294
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
963-1166 |
2.33e-07 |
|
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: 55.00 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 963 PLTVALGL-----DISGDPIVTDIRKMP-HGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPKMVELAPYNSVP 1036
Cdd:TIGR03925 52 RLTVPVGIvdrpfEQRQDPLVVDLSGAAgHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1037 HlVAPVITdvKAATAALKWAVEEME----RRYELFAHAGARDLTRYNTIVSEREIPGETLPYIVIVIDELADLMMVAPgD 1112
Cdd:TIGR03925 132 H-VGGVAG--RLDPERVRRTVAEVEgllrRRERLFRTHGIDSMAQYRARRAAGRLPEDPFGDVFLVIDGWGTLRQDFE-D 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1196975620 1113 VEEAICRIAQKARACGIHLLVATQRPSvdVITGLIKSNIPTRIAF----TVSSQVDSR 1166
Cdd:TIGR03925 208 LEDKVTDLAARGLAYGVHVVLTASRWS--EIRPALRDLIGTRIELrlgdPMDSEIDRR 263
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
906-1134 |
4.55e-07 |
|
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: 54.23 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 906 ITNLSDDIKLSLAAKDIRIEAPIPGKSAIGIEV-PNKeskpVFLREILRSPVFTksesPLTVALGLDISG-DPIVTDIRK 983
Cdd:TIGR03925 291 LDGIASVDDLGTRGLVAVIRDVWGGPPAPPVRLlPAR----LPLSALPAGGGAP----RLRVPLGLGESDlAPVYVDFAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 984 MPHGLIAGATGSGKSVCINAILTSILYKAKPHEVKLMLIDPK--MVELAPYNsvpHLVApVITDVKAATAALKWAVEEME 1061
Cdd:TIGR03925 363 SPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRrtLLGAVPED---YLAG-YAATSAALTELIAALAALLE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 1062 RRyelfahagardltryntivsereIPGETL-------------PYIVIVIDELaDLMMVAPGDVEEAICRIAQKARACG 1128
Cdd:TIGR03925 439 RR-----------------------LPGPDVtpqqlrarswwsgPEIYVVVDDY-DLVATGSGNPLAPLVELLPHARDIG 494
|
....*.
gi 1196975620 1129 IHLLVA 1134
Cdd:TIGR03925 495 LHVVVA 500
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
632-797 |
8.06e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.89 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 632 AETEENKR--VVEEAPVAEEQRVVEEAPVAEEQRVVEEAPVAEEQPVVKKEEPKREkkrhvpfnvvmlkQDRTRLMERHA 709
Cdd:PRK10811 853 VQVEEQREaeEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEE-------------VVVVETTHPEV 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 710 ARANAMQHSVNVRVENRPMQQVVAEPQVEEQPMQQVVAEPQVEEQPMQQVVVESQVEEQPMQQVVVESQVEEqsVQQVVA 789
Cdd:PRK10811 920 IAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEV--ETVTAV 997
|
....*...
gi 1196975620 790 EPQMEERP 797
Cdd:PRK10811 998 EPEVAPAQ 1005
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
582-776 |
1.43e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.12 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 582 IKAPVVETFVALEEIQQEDEAIEQKSEfihVAEADEQTKNDVQSFANVLLAETEenkrVVEEAPVAEEQRVVEEAPVAEE 661
Cdd:PRK10811 843 IRYPVVRPQDVQVEEQREAEEVQVQPV---VAEVPVAAAVEPVVSAPVVEAVAE----VVEEPVVVAEPQPEEVVVVETT 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 662 QRVVEEAPVAEEQPVVKKEEPKREKKRHVPFNVVMLKQDRTRLMERHAARANamqhsvnvrvenrpmqQVVAEPQVEEQP 741
Cdd:PRK10811 916 HPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE----------------VVVAEPEVVAQP 979
|
170 180 190
....*....|....*....|....*....|....*
gi 1196975620 742 MQQVVAEPQVEEqpMQQVVVESQVEEQPMQQVVVE 776
Cdd:PRK10811 980 AAPVVAEVAAEV--ETVTAVEPEVAPAQVPEATVE 1012
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
966-1024 |
3.31e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.86 E-value: 3.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196975620 966 VALGLDISGDPIVTDIRKM---PHGLIAGATGSGKSVCINAILTSILYkakpHEVKLMLIDP 1024
Cdd:COG3451 183 IYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLR----YGARIVIFDP 240
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
523-712 |
9.92e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.41 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 523 EAQEEVEVIAETEAQEEVEViaeteepeeveviaeaeelEEVEVIAETEESEEVEVIAEIKAPVVETFVALEEIQQEDEA 602
Cdd:PRK10811 851 QDVQVEEQREAEEVQVQPVV-------------------AEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVV 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196975620 603 IEQKSEFIHVAEADEQTKNDVQSFANVLLAETEENKRVVEEAPVAEEqrvVEEAPVAEEQRVVEEAPVAEEQPVVKKEEP 682
Cdd:PRK10811 912 VETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETAD---IEEAAETAEVVVAEPEVVAQPAAPVVAEVA 988
|
170 180 190
....*....|....*....|....*....|
gi 1196975620 683 KREKKRHVPFNVVMLKQDRTRLMERHAARA 712
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEATVEHNHATA 1018
|
|
| |
