|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
816-1273 |
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: 838.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 816 LPSVSLLEEP--QVIEPDEDWITDKKKELNDALFYFNVPAEVQDVTEGPSVTRFELSVEKGVKVSRITALQDDIKMALAA 893
Cdd:COG1674 137 LPPLDLLDPPppKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 894 KDIRIEAPIPGTSRVGIEVPNQNPTTVNLRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTPHALIAGATGSGKSV 973
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 974 CINSILMSLLYKNHPEELRLLLIDPKMVELAPYNGLPHLVAPVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFN 1053
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1054 KKA----------PYDERMPKIVIVIDELADLMMMAPQEVEQSIARIAQKARACGIHMLVATQRPSVNVITGLIKANIPT 1123
Cdd:COG1674 377 EKVreakakgeeeEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1124 RIAFMVSSSVDSRTILDSGGAERLLGYGDMLYLGSGMNKPIRVQGTFVSDDEIDDVVDFIKQQREPDY----LFEEKELL 1199
Cdd:COG1674 457 RIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYieeiLEEEEEED 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612908859 1200 KKTQTQSQDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDVYVTEADLNK 1273
Cdd:COG1674 537 EGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEE 610
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
773-1264 |
1.34e-142 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 467.64 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 773 PSFSNQNEDTANENRPRTNQPDVATNQAVQTS--KPMI-RKG-------PNIKLPSVSLLEEP-QVIEPDEDWITDKKKE 841
Cdd:PRK10263 813 PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHPLLmRNGdsrplhkPTTPLPSLDLLTPPpSEVEPVDTFALEQMAR 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 842 LNDA-LFYFNVPAEVQDVTEGPSVTRFELSVEKGVKVSRITALQDDIKMALAAKDIRIEAPIPGTSRVGIEVPNQNPTTV 920
Cdd:PRK10263 893 LVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTV 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 921 NLRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKM 1000
Cdd:PRK10263 973 YLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKM 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1001 VELAPYNGLPHLVAPVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFNKKA------------------------ 1056
Cdd:PRK10263 1053 LELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIaeadrmmrpipdpywkpgdsmdaq 1132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1057 -PYDERMPKIVIVIDELADLMMMAPQEVEQSIARIAQKARACGIHMLVATQRPSVNVITGLIKANIPTRIAFMVSSSVDS 1135
Cdd:PRK10263 1133 hPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDS 1212
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1136 RTILDSGGAERLLGYGDMLYLGSGMNKPIRVQGTFVSDDEIDDVVDFIKQQREPDYL---------------FEEKELLk 1200
Cdd:PRK10263 1213 RTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVdgitsdseseggaggFDGAEEL- 1291
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612908859 1201 ktqtqsqDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDV 1264
Cdd:PRK10263 1292 -------DPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREV 1348
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
922-1109 |
1.49e-66 |
|
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: 223.79 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 922 LRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTP-HALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKM 1000
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1001 VELAPYNGLPHLVA-PVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFNKKA----------------------- 1056
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612908859 1057 --PYDERMPKIVIVIDELADLMMMAPQE----VEQSIARIAQKARACGIHMLVATQRPS 1109
Cdd:pfam01580 161 agRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
932-1144 |
2.56e-29 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 127.41 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 932 KNAESK-LTVAMGYRINNEPLLMDI---AKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKMVELA-PY 1006
Cdd:TIGR03928 439 KNETYKsLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1007 NGLPHLVApVITDV-----KAATQSLKwavEEMERRYKLFAHYHVRNITAFNKKAPY---DERMPKIVIVIDELADLMMM 1078
Cdd:TIGR03928 519 KNLPHLLG-TITNLdgaqsMRALASIK---AELKKRQRLFGENNVNHINQYQKLYKQgkaKEPMPHLFLISDEFAELKSE 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612908859 1079 APQEVEQ--SIARIaqkARACGIHMLVATQRPSvNVITGLIKANIPTRIAFMVSSSVDSRTILDSGGA 1144
Cdd:TIGR03928 595 QPEFMKElvSTARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1206-1267 |
3.25e-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: 108.27 E-value: 3.25e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612908859 1206 SQDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDVYVT 1267
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
960-1129 |
5.44e-07 |
|
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: 50.30 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 960 HALIAGATGSGKSVCINSILMSLLYKNHpeelRLLLIDPKM---VELAPYNGLPHLVAPVITDVkaatqsLKWAVEEMER 1036
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFNQ------LFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1037 RYKlfahyhvrnitafnkkapyDERMPKIVIVIDELADLMMMapqeveQSIARIAQKARACGIHMLVATQ------RPSV 1110
Cdd:cd01127 71 LSP-------------------GRLPRRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleAVYG 125
|
170
....*....|....*....
gi 612908859 1111 NVITGLIKANIPTRIAFMV 1129
Cdd:cd01127 126 KDGAQTILGNCNTKLYLGT 144
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
414-602 |
2.73e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.55 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 414 EVTVSDVTSQRQSALQHNVEVNDQDGLknQSRLIADSEEDGATNKEEYSGSQIDdaEFYELNDTE-VDEDTTSNSQDNTN 492
Cdd:PTZ00341 941 EHAEANIEEDAEENVEEDAEENVEENV--EENVEENVEENVEENVEENVEENVE--ENVEENVEEnIEENVEENVEENIE 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 493 RNASEMHVDVPKTQEHAVTESQVNNIDKTVDNDIELAPRHKKDNQTNLSVNSLKTNDVNDGHVVEDSTMNEIEKHSAEVT 572
Cdd:PTZ00341 1017 ENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIE 1096
|
170 180 190
....*....|....*....|....*....|....*..
gi 612908859 573 ENVQNEAAES-EQNGEEKTIENA------NPKKQTEK 602
Cdd:PTZ00341 1097 ENVEENVEENaEENAEENAEENAeeyddeNPEEHNEE 1133
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
538-815 |
7.54e-04 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 43.62 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 538 TNLSVNSLKTNDVNDGHVVEDSTMNEIeKHSAEVTENVQNEAAESEQNGEEKTIENA-NPKKQTEKVSTLSKR------- 609
Cdd:PRK08581 13 TTLVLPTLTSPTAYADDPQKDSTAKTT-SHDSKKSNDDETSKDTSSKDTDKADNNNTsNQDNNDKKFSTIDSStsdsnni 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 610 ---PFNVVMTPSDKKRMMDRKKHSKVNVPELKPIQSKQAVSESKTASQATPSSSTDSQESNTNAYKTNNMTSNNVENDQL 686
Cdd:PRK08581 92 idfIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 687 IGH-GETENDYQNAQQYSDQKPSVDSTQTEIFEESQDDNQLENEQVDQLTSSSVSEVSD-ITEESEETTHLNN----TSG 760
Cdd:PRK08581 172 DNQkAPSSNNTKPSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSDSALDsILDQYSEDAKKTQkdyaSQS 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 612908859 761 QQDNDDQQKDLQPSFSNQNEDTANENRPRTNQPDVATNQAVQTSkpMIRKGPNIK 815
Cdd:PRK08581 252 KKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTS--LFETGPSLS 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
816-1273 |
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: 838.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 816 LPSVSLLEEP--QVIEPDEDWITDKKKELNDALFYFNVPAEVQDVTEGPSVTRFELSVEKGVKVSRITALQDDIKMALAA 893
Cdd:COG1674 137 LPPLDLLDPPppKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 894 KDIRIEAPIPGTSRVGIEVPNQNPTTVNLRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTPHALIAGATGSGKSV 973
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 974 CINSILMSLLYKNHPEELRLLLIDPKMVELAPYNGLPHLVAPVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFN 1053
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1054 KKA----------PYDERMPKIVIVIDELADLMMMAPQEVEQSIARIAQKARACGIHMLVATQRPSVNVITGLIKANIPT 1123
Cdd:COG1674 377 EKVreakakgeeeEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1124 RIAFMVSSSVDSRTILDSGGAERLLGYGDMLYLGSGMNKPIRVQGTFVSDDEIDDVVDFIKQQREPDY----LFEEKELL 1199
Cdd:COG1674 457 RIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYieeiLEEEEEED 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612908859 1200 KKTQTQSQDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDVYVTEADLNK 1273
Cdd:COG1674 537 EGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEE 610
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
773-1264 |
1.34e-142 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 467.64 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 773 PSFSNQNEDTANENRPRTNQPDVATNQAVQTS--KPMI-RKG-------PNIKLPSVSLLEEP-QVIEPDEDWITDKKKE 841
Cdd:PRK10263 813 PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHPLLmRNGdsrplhkPTTPLPSLDLLTPPpSEVEPVDTFALEQMAR 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 842 LNDA-LFYFNVPAEVQDVTEGPSVTRFELSVEKGVKVSRITALQDDIKMALAAKDIRIEAPIPGTSRVGIEVPNQNPTTV 920
Cdd:PRK10263 893 LVEArLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTV 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 921 NLRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKM 1000
Cdd:PRK10263 973 YLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKM 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1001 VELAPYNGLPHLVAPVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFNKKA------------------------ 1056
Cdd:PRK10263 1053 LELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIaeadrmmrpipdpywkpgdsmdaq 1132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1057 -PYDERMPKIVIVIDELADLMMMAPQEVEQSIARIAQKARACGIHMLVATQRPSVNVITGLIKANIPTRIAFMVSSSVDS 1135
Cdd:PRK10263 1133 hPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDS 1212
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1136 RTILDSGGAERLLGYGDMLYLGSGMNKPIRVQGTFVSDDEIDDVVDFIKQQREPDYL---------------FEEKELLk 1200
Cdd:PRK10263 1213 RTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVdgitsdseseggaggFDGAEEL- 1291
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612908859 1201 ktqtqsqDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDV 1264
Cdd:PRK10263 1292 -------DPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREV 1348
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
922-1109 |
1.49e-66 |
|
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: 223.79 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 922 LRSIIESPSFKNAESKLTVAMGYRINNEPLLMDIAKTP-HALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKM 1000
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1001 VELAPYNGLPHLVA-PVITDVKAATQSLKWAVEEMERRYKLFAHYHVRNITAFNKKA----------------------- 1056
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIaedpldgfgdvflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612908859 1057 --PYDERMPKIVIVIDELADLMMMAPQE----VEQSIARIAQKARACGIHMLVATQRPS 1109
Cdd:pfam01580 161 agRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
816-914 |
3.95e-37 |
|
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: 134.97 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 816 LPSVSLLEEPQVI--EPDEDWITDKKKELNDALFYFNVPAEVQDVTEGPSVTRFELSVEKGVKVSRITALQDDIKMALAA 893
Cdd:pfam17854 1 LPPLDLLEPPPTSsqKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 612908859 894 KDIRIEAPIPGTSRVGIEVPN 914
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
1206-1267 |
2.67e-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: 114.00 E-value: 2.67e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612908859 1206 SQDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDVYVT 1267
Cdd:pfam09397 2 EEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
932-1144 |
2.56e-29 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 127.41 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 932 KNAESK-LTVAMGYRINNEPLLMDI---AKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKMVELA-PY 1006
Cdd:TIGR03928 439 KNETYKsLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1007 NGLPHLVApVITDV-----KAATQSLKwavEEMERRYKLFAHYHVRNITAFNKKAPY---DERMPKIVIVIDELADLMMM 1078
Cdd:TIGR03928 519 KNLPHLLG-TITNLdgaqsMRALASIK---AELKKRQRLFGENNVNHINQYQKLYKQgkaKEPMPHLFLISDEFAELKSE 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612908859 1079 APQEVEQ--SIARIaqkARACGIHMLVATQRPSvNVITGLIKANIPTRIAFMVSSSVDSRTILDSGGA 1144
Cdd:TIGR03928 595 QPEFMKElvSTARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1206-1267 |
3.25e-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: 108.27 E-value: 3.25e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612908859 1206 SQDELFDDVCAFMVNEGHISTSLIQRHFQIGYNRAARIIDQLEQLGYVSSANGSKPRDVYVT 1267
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
938-1174 |
6.16e-24 |
|
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: 108.52 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 938 LTVAMGYRINNEPLLMDIAKT------PHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKM-VELAPYNGLP 1010
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKESaeggmgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGgATFLGLEGLP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1011 HLVApVITDVkAATQSLkwaVE--------EMERRYKLF-AHYHVRNITAFNK----KAPYDErMPKIVIVIDELADLMM 1077
Cdd:TIGR03924 489 HVSA-VITNL-ADEAPL---VDrmqdalagEMNRRQELLrAAGNFANVAEYEKaraaGADLPP-LPALFVVVDEFSELLS 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1078 MAPQEVEqSIARIAQKARACGIHMLVATQRPSVNVITGLiKANIPTRIAFMVSSSVDSRTILDSGGAERLLGYGDMLYLG 1157
Cdd:TIGR03924 563 QHPDFAD-LFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLK 640
|
250
....*....|....*..
gi 612908859 1158 SGMNKPIRVQGTFVSDD 1174
Cdd:TIGR03924 641 VDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
949-1139 |
1.70e-20 |
|
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: 98.52 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 949 EPLLMDIAKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKMVELAPYNGLPHlVAPVIT--DVKAATQS 1026
Cdd:TIGR03928 801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1027 LKWAVEEMERRYKLFAHYHVRNITAFNKKApyDERMPKIVIVIDELaDLMMMAP--QEVEQSIARIAQKARACGIH-MLV 1103
Cdd:TIGR03928 880 IRRIKKEIDRRKKLFSEYGVASISMYNKAS--GEKLPQIVIIIDNY-DAVKEEPfyEDFEELLIQLAREGASLGIYlVMT 956
|
170 180 190
....*....|....*....|....*....|....*.
gi 612908859 1104 ATQRPSVNVItglIKANIPTRIAFMVSSSVDSRTIL 1139
Cdd:TIGR03928 957 AGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
862-1138 |
1.02e-09 |
|
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: 63.47 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 862 PSVTRFELSVEKGVKVSRITALQDDI-KMALAAKDIRIEaPIPGTsrvgievpnqnPTTVNLRSIIESPSFKNAESKLTV 940
Cdd:TIGR03928 1010 PTLFQTALPVKGEDDLEVIENIKAEIqKMNEAWTGERPK-PIPMV-----------PEELSLEEFRERYEVRKILEEGSI 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 941 AMGYRINN-EPLLMDIAKTPHALIAGATGSGKSVCINSILMSLLYKNHPEelrLLLIDPKMVELAPYNGLPHlVAPVITD 1019
Cdd:TIGR03928 1078 PIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQEKEK---IGLIDSIDRGLLAYRDLKE-VATYIEE 1153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1020 VKAATQSLKWAVEEMERRYKLFAHYHVRNITAFNKKapydermpKIVIVIDELADLMMMAPQEVEQSIARIAQKARACGI 1099
Cdd:TIGR03928 1154 KEDLKEILAELKEEIELREAAYKEALQNETGEPAFK--------PILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGI 1225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 612908859 1100 HMLVATQRPSVN----VITGLIKAnipTRIAFMVSSSVDSRTI 1138
Cdd:TIGR03928 1226 HFIVAGTHSELSksydGVPKEIKQ---LRTGILGMRKSDQSFF 1265
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
944-1184 |
1.17e-07 |
|
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: 55.38 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 944 YRINNEPLLMDIAK--TPHALIAGATGSGKSVCINSIL------------------MSLLYKNHPEELRLLLIDPKMV-- 1001
Cdd:COG0433 31 LLSPGVPVYLDLDKllNRHILILGATGSGKSNTLQVLLeelsragvpvlvfdphgeYSGLAEPGAERADVGVFDPGAGrp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1002 -------------ELAPY------------------------NGLPHL--------------VAPVITDVKAAT-QSLKW 1029
Cdd:COG0433 111 lpinpwdlfatasELGPLllsrldlndtqrgvlrealrladdKGLLLLdlkdlialleegeeLGEEYGNVSAASaGALLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1030 AVEEMERRYKLFAHYHVRNITAFNKKAP-------------------------YDERM---------PKIVIVIDELADL 1075
Cdd:COG0433 191 RLESLESADGLFGEPGLDLEDLLRTDGRvtvidlsglpeelqstfvlwllrelFEARPevgdaddrkLPLVLVIDEAHLL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1076 MMMAPQEVEQSIARIAQKARACGIHMLVATQRPSvNVITGlIKANIPTRIAFMVSSSVDSRTI------LDSGGAERL-- 1147
Cdd:COG0433 271 APAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKAVkaaaetLSEDLLERLps 348
|
330 340 350
....*....|....*....|....*....|....*..
gi 612908859 1148 LGYGDMLYLGSGMNKPIRVQGTFVSDDEIDDVVDFIK 1184
Cdd:COG0433 349 LGTGEALVLGEGIPLPVLVKIRLPESRPGGESPDLVR 385
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
938-1147 |
1.23e-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: 56.15 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 938 LTVAMG-----YRINNEPLLMDIAKTP-HALIAGATGSGKSVCINSILMSLLYKNHPEELRLLLIDPKMVELAPYNGLPH 1011
Cdd:TIGR03925 53 LTVPVGivdrpFEQRQDPLVVDLSGAAgHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1012 lVAPVITdvKAATQSLKWAVEEME----RRYKLFAHYHVRNITAFN----KKAPYDERMPKIVIVIDELADLmMMAPQEV 1083
Cdd:TIGR03925 133 -VGGVAG--RLDPERVRRTVAEVEgllrRRERLFRTHGIDSMAQYRarraAGRLPEDPFGDVFLVIDGWGTL-RQDFEDL 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612908859 1084 EQSIARIAQKARACGIHMLVATQRPSvnVITGLIKANIPTRIAFMVSSSVDSrtILDSGGAERL 1147
Cdd:TIGR03925 209 EDKVTDLAARGLAYGVHVVLTASRWS--EIRPALRDLIGTRIELRLGDPMDS--EIDRRAAARV 268
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
960-1129 |
5.44e-07 |
|
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: 50.30 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 960 HALIAGATGSGKSVCINSILMSLLYKNHpeelRLLLIDPKM---VELAPYNGLPHLVAPVITDVkaatqsLKWAVEEMER 1036
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFNQ------LFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 1037 RYKlfahyhvrnitafnkkapyDERMPKIVIVIDELADLMMMapqeveQSIARIAQKARACGIHMLVATQ------RPSV 1110
Cdd:cd01127 71 LSP-------------------GRLPRRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleAVYG 125
|
170
....*....|....*....
gi 612908859 1111 NVITGLIKANIPTRIAFMV 1129
Cdd:cd01127 126 KDGAQTILGNCNTKLYLGT 144
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
917-1104 |
5.99e-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: 53.84 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 917 PTTVNLRSIIESPsfknAESKLTVAMGYRINN-EPLLMDIAKTPHALIAGATGSGKSVCINSILMSLLYKNHPEELRLLL 995
Cdd:TIGR03925 325 PARLPLSALPAGG----GAPRLRVPLGLGESDlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 996 IDPK--MVELAPYNglpHLVApVITDVKAATQSLKWAVEEMERRYKlfahyhVRNITAfnkkapydERM--------PKI 1065
Cdd:TIGR03925 401 VDYRrtLLGAVPED---YLAG-YAATSAALTELIAALAALLERRLP------GPDVTP--------QQLrarswwsgPEI 462
|
170 180 190
....*....|....*....|....*....|....*....
gi 612908859 1066 VIVIDELaDLMMMAPQEVEQSIARIAQKARACGIHMLVA 1104
Cdd:TIGR03925 463 YVVVDDY-DLVATGSGNPLAPLVELLPHARDIGLHVVVA 500
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
414-602 |
2.73e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.55 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 414 EVTVSDVTSQRQSALQHNVEVNDQDGLknQSRLIADSEEDGATNKEEYSGSQIDdaEFYELNDTE-VDEDTTSNSQDNTN 492
Cdd:PTZ00341 941 EHAEANIEEDAEENVEEDAEENVEENV--EENVEENVEENVEENVEENVEENVE--ENVEENVEEnIEENVEENVEENIE 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 493 RNASEMHVDVPKTQEHAVTESQVNNIDKTVDNDIELAPRHKKDNQTNLSVNSLKTNDVNDGHVVEDSTMNEIEKHSAEVT 572
Cdd:PTZ00341 1017 ENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIE 1096
|
170 180 190
....*....|....*....|....*....|....*..
gi 612908859 573 ENVQNEAAES-EQNGEEKTIENA------NPKKQTEK 602
Cdd:PTZ00341 1097 ENVEENVEENaEENAEENAEENAeeyddeNPEEHNEE 1133
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
940-998 |
6.11e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 44.17 E-value: 6.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612908859 940 VAMGYRINNEPLLMDI---AKTPHALIAGATGSGKSVCINSILMSLLYKNHpeelRLLLIDP 998
Cdd:COG3451 183 IYLLNTRSGTPVFFDFhdgLDNGNTLILGPSGSGKSFLLKLLLLQLLRYGA----RIVIFDP 240
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
538-815 |
7.54e-04 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 43.62 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 538 TNLSVNSLKTNDVNDGHVVEDSTMNEIeKHSAEVTENVQNEAAESEQNGEEKTIENA-NPKKQTEKVSTLSKR------- 609
Cdd:PRK08581 13 TTLVLPTLTSPTAYADDPQKDSTAKTT-SHDSKKSNDDETSKDTSSKDTDKADNNNTsNQDNNDKKFSTIDSStsdsnni 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 610 ---PFNVVMTPSDKKRMMDRKKHSKVNVPELKPIQSKQAVSESKTASQATPSSSTDSQESNTNAYKTNNMTSNNVENDQL 686
Cdd:PRK08581 92 idfIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612908859 687 IGH-GETENDYQNAQQYSDQKPSVDSTQTEIFEESQDDNQLENEQVDQLTSSSVSEVSD-ITEESEETTHLNN----TSG 760
Cdd:PRK08581 172 DNQkAPSSNNTKPSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSDSALDsILDQYSEDAKKTQkdyaSQS 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 612908859 761 QQDNDDQQKDLQPSFSNQNEDTANENRPRTNQPDVATNQAVQTSkpMIRKGPNIK 815
Cdd:PRK08581 252 KKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTS--LFETGPSLS 304
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